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Conserved domains on  [gi|47132591|ref|NP_998725|]
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serine/threonine-protein kinase N1 isoform 1 [Homo sapiens]

Protein Classification

serine/threonine-protein kinase N( domain architecture ID 10184390)

serine/threonine-protein kinase N, a PKC-related protein, catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
621-945 0e+00

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 727.17  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTSAGHPFLVNLFGCFQTPEHVCFV 700
Cdd:cd05589   1 FRCIAVLGRGHFGKVLLAEYKPTGELFAIKALKKGDIIARDEVESLMCEKRIFETVNSARHPFLVNLFACFQTPEHVCFV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGGDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTST 780
Cdd:cd05589  81 MEYAAGGDLMMHIHEDVFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGFGDRTST 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 781 FCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNP 860
Cdd:cd05589 161 FCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSTEAISIMRRLLRKNP 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 861 ERRLGSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFDEEFTGEAPTLSPPRDARPLTAAEQAAFLD 940
Cdd:cd05589 241 ERRLGASERDAEDVKKQPFFRNIDWEALLARKIKPPFVPTIKSPEDVSNFDEEFTSEKPVLTPPKEPRPLTEEEQALFKD 320

                ....*
gi 47132591 941 FDFVA 945
Cdd:cd05589 321 FDYVA 325
HR1_PKN1_2 cd11630
Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
127-202 5.16e-46

Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N1; PKN1, also called PKNalpha or Protein-kinase C-related kinase 1 (PRK1), is a serine/threonine protein kinase that is activated by the Rho family of small GTPases, and by fatty acids such as arachidonic and linoleic acids. It is expressed ubiquitously and is the most abundant PKN isoform in neurons. PKN1 is implicated in a variety of functions including cytoskeletal reorganization, cardiac cell survival, cell adhesion, and glucose transport, among others. PKN1 contains three HR1 domains, a C2 domain, and a kinase domain. This model characterizes the second HR1 domain of PKN1. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; PKN1 binds the GTPases RhoA, RhoB, and RhoC, and can also interact weakly with Rac.


:

Pssm-ID: 212020  Cd Length: 78  Bit Score: 159.03  E-value: 5.16e-46
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47132591 127 SATNLSRVAGLEKQLAIELKVKQGAENMIQTYSNGSTKDRKLLLTAQQMLQDSKTKIDIIRMQLRRALQAGQLENQ 202
Cdd:cd11630   3 SAANQSRIAGLEKQLNIELKVKQGAENMIQTYANGSTKDRKLLQTAQQMLQDSKTKIDIIRMQIRKAMQADELENQ 78
HR1_PKN1_3 cd11636
Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
211-284 6.13e-44

Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N1; PKN1, also called PKNalpha or Protein-kinase C-related kinase 1 (PRK1), is a serine/threonine protein kinase that is activated by the Rho family of small GTPases, and by fatty acids such as arachidonic and linoleic acids. It is expressed ubiquitously and is the most abundant PKN isoform in neurons. PKN1 is implicated in a variety of functions including cytoskeletal reorganization, cardiac cell survival, cell adhesion, and glucose transport, among others. PKN1 contains three HR1 domains, a C2 domain, and a kinase domain. This model characterizes the third HR1 domain of PKN1. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; PKN1 binds the GTPases RhoA, RhoB, and RhoC, and can also interact weakly with Rac.


:

Pssm-ID: 212026  Cd Length: 74  Bit Score: 153.21  E-value: 6.13e-44
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47132591 211 SPDLGAVELRIEELRHHFRVEHAVAEGAKNVLRLLSAAKAPDRKAVSEAQEKLTESNQKLGLLREALERRLGEL 284
Cdd:cd11636   1 KPDLCAVELRIEELRHHFRVEHAVAEGAKNVLRLLGAGKAQDRKAISEAQSKLSESSQKLDLLRVSLEQRLVEL 74
C2_PKN-like cd08687
C2 domain in Protein kinase C-like (PKN) proteins; PKN is a lipid-activated serine/threonine ...
395-482 3.85e-42

C2 domain in Protein kinase C-like (PKN) proteins; PKN is a lipid-activated serine/threonine kinase. It is a member of the protein kinase C (PKC) superfamily, but lacks a C1 domain. There are at least 3 different isoforms of PKN (PRK1/PKNalpha/PAK1; PKNbeta, and PRK2/PAK2/PKNgamma). The C-terminal region contains the Ser/Thr type protein kinase domain, while the N-terminal region of PKN contains three antiparallel coiled-coil (ACC) finger domains which are relatively rich in charged residues and contain a leucine zipper-like sequence. These domains binds to the small GTPase RhoA. Following these domains is a C2-like domain. Its C-terminal part functions as an auto-inhibitory region. PKNs are not activated by classical PKC activators such as diacylglycerol, phorbol ester or Ca2+, but instead are activated by phospholipids and unsaturated fatty acids. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


:

Pssm-ID: 176069  Cd Length: 98  Bit Score: 149.08  E-value: 3.85e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 395 SEVSTVLKLDNTVVGQTSWKPCGPNAWDQSFTLELERARELELAVFWRDQRGLCALKFLKLEDFldneRHEVQLDMEPQG 474
Cdd:cd08687   9 SEVSAVLKLDNTVVGQTQWKPKSNQAWDQSFTLELERSRELEIAVYWRDWRSLCAVKFLKLEDE----RHEVQLDMEPQL 84

                ....*...
gi 47132591 475 CLVAEVTF 482
Cdd:cd08687  85 CLVAELTF 92
HR1_PKN_1 cd11622
First Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
52-104 1.83e-21

First Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N; PKN, also called Protein-kinase C-related kinase (PRK), is a serine/threonine protein kinase that can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytoskeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. In some vertebrates, there are three PKN isoforms from different genes (designated PKN1, PKN2, and PKN3), which show different enzymatic properties, tissue distribution, and varied functions. PKN proteins contain three HR1 domains, a C2 domain, and a kinase domain. This model characterizes the first HR1 domain of PKN. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family.


:

Pssm-ID: 212012  Cd Length: 66  Bit Score: 88.86  E-value: 1.83e-21
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 47132591  52 IRKELKLKEGAENLRRATTDLgRSLGPVELLLRGSSRRLDLLHQQLQELHAHV 104
Cdd:cd11622  15 IRKELKIKEGAENLRKATTDK-KSLAHVESILKKSNRKLEDLHQELQELEAHI 66
 
Name Accession Description Interval E-value
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
621-945 0e+00

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 727.17  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTSAGHPFLVNLFGCFQTPEHVCFV 700
Cdd:cd05589   1 FRCIAVLGRGHFGKVLLAEYKPTGELFAIKALKKGDIIARDEVESLMCEKRIFETVNSARHPFLVNLFACFQTPEHVCFV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGGDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTST 780
Cdd:cd05589  81 MEYAAGGDLMMHIHEDVFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGFGDRTST 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 781 FCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNP 860
Cdd:cd05589 161 FCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSTEAISIMRRLLRKNP 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 861 ERRLGSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFDEEFTGEAPTLSPPRDARPLTAAEQAAFLD 940
Cdd:cd05589 241 ERRLGASERDAEDVKKQPFFRNIDWEALLARKIKPPFVPTIKSPEDVSNFDEEFTSEKPVLTPPKEPRPLTEEEQALFKD 320

                ....*
gi 47132591 941 FDFVA 945
Cdd:cd05589 321 FDYVA 325
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
621-880 8.26e-80

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 259.38  E-value: 8.26e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591    621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIvaRDEVESLMCEKRILAavtSAGHPFLVNLFGCFQTPEHVCFV 700
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKI--KKDRERILREIKILK---KLKHPNIVRLYDVFEDEDKLYLV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591    701 MEYSAGGDLMLHIHSDV-FSEPRAIFYSACVVLGLQFLHEHKIVYRdlkldnllldTEGYVKIADFGLCKEgMGYGDRTS 779
Cdd:smart00220  76 MEYCEGGDLFDLLKKRGrLSEDEARFYLRQILSALEYLHSKGIVHRdlkpenilldEDGHVKLADFGLARQ-LDPGEKLT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591    780 TFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEE-EVFDSIVNDEVRYPRF---LSAEAIGIMRRL 855
Cdd:smart00220 155 TFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLlELFKKIGKPKPPFPPPewdISPEAKDLIRKL 234
                          250       260
                   ....*....|....*....|....*
gi 47132591    856 LRRNPERRLGsserdAEDVKKQPFF 880
Cdd:smart00220 235 LVKDPEKRLT-----AEEALQHPFF 254
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
618-941 7.66e-78

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 257.05  E-value: 7.66e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  618 LEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHV 697
Cdd:PTZ00263  17 LSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELS---HPFIVNMMCSFQDENRV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  698 CFVMEYSAGGDLMLHIHS-DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEgmgYGD 776
Cdd:PTZ00263  94 YFLLEFVVGGELFTHLRKaGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKK---VPD 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  777 RTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLL 856
Cdd:PTZ00263 171 RTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGRARDLVKGLL 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  857 RRNPERRLGSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFDeeftgEAPTlSPPRDARPLTAAEQA 936
Cdd:PTZ00263 251 QTDHTKRLGTLKGGVADVKNHPYFHGANWDKLYARYYPAPIPVRVKSPGDTSNFE-----KYPD-SPVDRLPPLTAAQQA 324

                 ....*
gi 47132591  937 AFLDF 941
Cdd:PTZ00263 325 EFAGF 329
Pkinase pfam00069
Protein kinase domain;
621-880 2.14e-51

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 179.75  E-value: 2.14e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591   621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEvESLMCEKRILAAVtsaGHPFLVNLFGCFQTPEHVCFV 700
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKD-KNILREIKILKKL---NHPNIVRLYDAFEDKDNLYLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591   701 MEYSAGGDLMLHI-HSDVFSEPRAIFYSACVVlglqflhehkivyrdlkldnllldtegyvkiadfglckEGMGYGDRTS 779
Cdd:pfam00069  77 LEYVEGGSLFDLLsEKGAFSEREAKFIMKQIL--------------------------------------EGLESGSSLT 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591   780 TFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRF---LSAEAIGIMRRLL 856
Cdd:pfam00069 119 TFVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELpsnLSEEAKDLLKKLL 198
                         250       260
                  ....*....|....*....|....
gi 47132591   857 RRNPERRLGsserdAEDVKKQPFF 880
Cdd:pfam00069 199 KKDPSKRLT-----ATQALQHPWF 217
HR1_PKN1_2 cd11630
Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
127-202 5.16e-46

Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N1; PKN1, also called PKNalpha or Protein-kinase C-related kinase 1 (PRK1), is a serine/threonine protein kinase that is activated by the Rho family of small GTPases, and by fatty acids such as arachidonic and linoleic acids. It is expressed ubiquitously and is the most abundant PKN isoform in neurons. PKN1 is implicated in a variety of functions including cytoskeletal reorganization, cardiac cell survival, cell adhesion, and glucose transport, among others. PKN1 contains three HR1 domains, a C2 domain, and a kinase domain. This model characterizes the second HR1 domain of PKN1. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; PKN1 binds the GTPases RhoA, RhoB, and RhoC, and can also interact weakly with Rac.


Pssm-ID: 212020  Cd Length: 78  Bit Score: 159.03  E-value: 5.16e-46
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47132591 127 SATNLSRVAGLEKQLAIELKVKQGAENMIQTYSNGSTKDRKLLLTAQQMLQDSKTKIDIIRMQLRRALQAGQLENQ 202
Cdd:cd11630   3 SAANQSRIAGLEKQLNIELKVKQGAENMIQTYANGSTKDRKLLQTAQQMLQDSKTKIDIIRMQIRKAMQADELENQ 78
HR1_PKN1_3 cd11636
Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
211-284 6.13e-44

Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N1; PKN1, also called PKNalpha or Protein-kinase C-related kinase 1 (PRK1), is a serine/threonine protein kinase that is activated by the Rho family of small GTPases, and by fatty acids such as arachidonic and linoleic acids. It is expressed ubiquitously and is the most abundant PKN isoform in neurons. PKN1 is implicated in a variety of functions including cytoskeletal reorganization, cardiac cell survival, cell adhesion, and glucose transport, among others. PKN1 contains three HR1 domains, a C2 domain, and a kinase domain. This model characterizes the third HR1 domain of PKN1. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; PKN1 binds the GTPases RhoA, RhoB, and RhoC, and can also interact weakly with Rac.


Pssm-ID: 212026  Cd Length: 74  Bit Score: 153.21  E-value: 6.13e-44
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47132591 211 SPDLGAVELRIEELRHHFRVEHAVAEGAKNVLRLLSAAKAPDRKAVSEAQEKLTESNQKLGLLREALERRLGEL 284
Cdd:cd11636   1 KPDLCAVELRIEELRHHFRVEHAVAEGAKNVLRLLGAGKAQDRKAISEAQSKLSESSQKLDLLRVSLEQRLVEL 74
C2_PKN-like cd08687
C2 domain in Protein kinase C-like (PKN) proteins; PKN is a lipid-activated serine/threonine ...
395-482 3.85e-42

C2 domain in Protein kinase C-like (PKN) proteins; PKN is a lipid-activated serine/threonine kinase. It is a member of the protein kinase C (PKC) superfamily, but lacks a C1 domain. There are at least 3 different isoforms of PKN (PRK1/PKNalpha/PAK1; PKNbeta, and PRK2/PAK2/PKNgamma). The C-terminal region contains the Ser/Thr type protein kinase domain, while the N-terminal region of PKN contains three antiparallel coiled-coil (ACC) finger domains which are relatively rich in charged residues and contain a leucine zipper-like sequence. These domains binds to the small GTPase RhoA. Following these domains is a C2-like domain. Its C-terminal part functions as an auto-inhibitory region. PKNs are not activated by classical PKC activators such as diacylglycerol, phorbol ester or Ca2+, but instead are activated by phospholipids and unsaturated fatty acids. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176069  Cd Length: 98  Bit Score: 149.08  E-value: 3.85e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 395 SEVSTVLKLDNTVVGQTSWKPCGPNAWDQSFTLELERARELELAVFWRDQRGLCALKFLKLEDFldneRHEVQLDMEPQG 474
Cdd:cd08687   9 SEVSAVLKLDNTVVGQTQWKPKSNQAWDQSFTLELERSRELEIAVYWRDWRSLCAVKFLKLEDE----RHEVQLDMEPQL 84

                ....*...
gi 47132591 475 CLVAEVTF 482
Cdd:cd08687  85 CLVAELTF 92
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
614-937 5.47e-38

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 149.01  E-value: 5.47e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 614 SPLTLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQT 693
Cdd:COG0515   2 SALLLGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERFRREARALARLN---HPNIVRVYDVGEE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 694 PEHVCFVMEYSAGGDLMLHIHSD-VFSEPRAIFYSACVVLGLQFLHEHKIVYR---------DLkldnllldtEGYVKIA 763
Cdd:COG0515  79 DGRPYLVMEYVEGESLADLLRRRgPLPPAEALRILAQLAEALAAAHAAGIVHRdikpanillTP---------DGRVKLI 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 764 DFGLCKE-GMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPR 842
Cdd:COG0515 150 DFGIARAlGGATLTQTGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPS 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 843 ----FLSAEAIGIMRRLLRRNPERRLGSSE---RDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFDEEFT 915
Cdd:COG0515 230 elrpDLPPALDAIVLRALAKDPEERYQSAAelaAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 309
                       330       340
                ....*....|....*....|..
gi 47132591 916 GEAPTLSPPRDARPLTAAEQAA 937
Cdd:COG0515 310 AAAAAAAAAAAAAPAAAAAAAA 331
HR1_PKN_1 cd11622
First Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
52-104 1.83e-21

First Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N; PKN, also called Protein-kinase C-related kinase (PRK), is a serine/threonine protein kinase that can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytoskeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. In some vertebrates, there are three PKN isoforms from different genes (designated PKN1, PKN2, and PKN3), which show different enzymatic properties, tissue distribution, and varied functions. PKN proteins contain three HR1 domains, a C2 domain, and a kinase domain. This model characterizes the first HR1 domain of PKN. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family.


Pssm-ID: 212012  Cd Length: 66  Bit Score: 88.86  E-value: 1.83e-21
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 47132591  52 IRKELKLKEGAENLRRATTDLgRSLGPVELLLRGSSRRLDLLHQQLQELHAHV 104
Cdd:cd11622  15 IRKELKIKEGAENLRKATTDK-KSLAHVESILKKSNRKLEDLHQELQELEAHI 66
HR1 pfam02185
Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of ...
133-202 7.04e-19

Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of the N-terminal non-catalytic part of protein kinase PRK1(PKN). The first two of these repeats were later shown to bind the small G protein rho known to activate PKN in its GTP-bound form. Similar rho-binding domains also occur in a number of other protein kinases and in the rho-binding proteins rhophilin and rhotekin. Recently, the structure of the N-terminal HR1 repeat complexed with RhoA has been determined by X-ray crystallography. It forms an antiparallel coiled-coil fold termed an ACC finger.


Pssm-ID: 460478 [Multi-domain]  Cd Length: 67  Bit Score: 81.41  E-value: 7.04e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591   133 RVAGLEKQLAIELKVKQGAENMIQTYSNgsTKDRKLLLTAQQMLQDSKTKIDIIRMQLRRaLQAGQLENQ 202
Cdd:pfam02185   1 RLQELRKKIEVEKKIKEGAENMLRLLQA--TKDRKVLAEAESELRESNRKIQLLREQLRE-LQARHLPSD 67
HR1 pfam02185
Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of ...
220-279 1.22e-17

Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of the N-terminal non-catalytic part of protein kinase PRK1(PKN). The first two of these repeats were later shown to bind the small G protein rho known to activate PKN in its GTP-bound form. Similar rho-binding domains also occur in a number of other protein kinases and in the rho-binding proteins rhophilin and rhotekin. Recently, the structure of the N-terminal HR1 repeat complexed with RhoA has been determined by X-ray crystallography. It forms an antiparallel coiled-coil fold termed an ACC finger.


Pssm-ID: 460478 [Multi-domain]  Cd Length: 67  Bit Score: 77.95  E-value: 1.22e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591   220 RIEELRHHFRVEHAVAEGAKNVLRLLSAAKapDRKAVSEAQEKLTESNQKLGLLREALER 279
Cdd:pfam02185   1 RLQELRKKIEVEKKIKEGAENMLRLLQATK--DRKVLAEAESELRESNRKIQLLREQLRE 58
Hr1 smart00742
Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical ...
219-279 2.96e-16

Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical domain found in vertebrate PRK1 and yeast PKC1 protein kinases C. The HR1 in rhophilin bind RhoGTP; those in PRK1 bind RhoA and RhoB. Also called RBD - Rho-binding domain


Pssm-ID: 128981  Cd Length: 57  Bit Score: 73.38  E-value: 2.96e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47132591    219 LRIEELRHHFRVEHAVAEGAKNVLRLLSAakapDRKAVSEAQEKLTESNQKLGLLREALER 279
Cdd:smart00742   1 LRLEDLRRKIEKELKVKEGAENMRKLTSN----DRKVLSEAQSMLRESNQKLDLLKEELEK 57
Hr1 smart00742
Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical ...
132-192 5.42e-16

Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical domain found in vertebrate PRK1 and yeast PKC1 protein kinases C. The HR1 in rhophilin bind RhoGTP; those in PRK1 bind RhoA and RhoB. Also called RBD - Rho-binding domain


Pssm-ID: 128981  Cd Length: 57  Bit Score: 72.99  E-value: 5.42e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47132591    132 SRVAGLEKQLAIELKVKQGAENMIQTYSNgstkDRKLLLTAQQMLQDSKTKIDIIRMQLRR 192
Cdd:smart00742   1 LRLEDLRRKIEKELKVKEGAENMRKLTSN----DRKVLSEAQSMLRESNQKLDLLKEELEK 57
Hr1 smart00742
Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical ...
52-99 1.97e-13

Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical domain found in vertebrate PRK1 and yeast PKC1 protein kinases C. The HR1 in rhophilin bind RhoGTP; those in PRK1 bind RhoA and RhoB. Also called RBD - Rho-binding domain


Pssm-ID: 128981  Cd Length: 57  Bit Score: 65.67  E-value: 1.97e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 47132591     52 IRKELKLKEGAENLRRATTDLGRSLGPVELLLRGSSRRLDLLHQQLQE 99
Cdd:smart00742  10 IEKELKVKEGAENMRKLTSNDRKVLSEAQSMLRESNQKLDLLKEELEK 57
HR1 pfam02185
Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of ...
52-108 1.35e-11

Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of the N-terminal non-catalytic part of protein kinase PRK1(PKN). The first two of these repeats were later shown to bind the small G protein rho known to activate PKN in its GTP-bound form. Similar rho-binding domains also occur in a number of other protein kinases and in the rho-binding proteins rhophilin and rhotekin. Recently, the structure of the N-terminal HR1 repeat complexed with RhoA has been determined by X-ray crystallography. It forms an antiparallel coiled-coil fold termed an ACC finger.


Pssm-ID: 460478 [Multi-domain]  Cd Length: 67  Bit Score: 60.61  E-value: 1.35e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591    52 IRKELKLKEGAENLRR---ATTDLgRSLGPVELLLRGSSRRLDLLHQQLQELHAHVVLPD 108
Cdd:pfam02185   9 IEVEKKIKEGAENMLRllqATKDR-KVLAEAESELRESNRKIQLLREQLRELQARHLPSD 67
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
700-863 1.19e-08

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 58.65  E-value: 1.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  700 VMEYSAGGDLMLHIHSD-VFSEPRAIFYSACVVLGLQFLHEHKIVYRdlkldnllldTEGYVKIADFGLCK----EGMGY 774
Cdd:NF033483  85 VMEYVDGRTLKDYIREHgPLSPEEAVEIMIQILSALEHAHRNGIVHRdikpqnilitKDGRVKVTDFGIARalssTTMTQ 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  775 gdrTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDeeEVfdSI----VNDEVRYPRFL------ 844
Cdd:NF033483 165 ---TNSVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFDGDS--PV--SVaykhVQEDPPPPSELnpgipq 237
                        170
                 ....*....|....*....
gi 47132591  845 SAEAIgIMrRLLRRNPERR 863
Cdd:NF033483 238 SLDAV-VL-KATAKDPDDR 254
 
Name Accession Description Interval E-value
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
621-945 0e+00

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 727.17  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTSAGHPFLVNLFGCFQTPEHVCFV 700
Cdd:cd05589   1 FRCIAVLGRGHFGKVLLAEYKPTGELFAIKALKKGDIIARDEVESLMCEKRIFETVNSARHPFLVNLFACFQTPEHVCFV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGGDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTST 780
Cdd:cd05589  81 MEYAAGGDLMMHIHEDVFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGFGDRTST 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 781 FCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNP 860
Cdd:cd05589 161 FCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSTEAISIMRRLLRKNP 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 861 ERRLGSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFDEEFTGEAPTLSPPRDARPLTAAEQAAFLD 940
Cdd:cd05589 241 ERRLGASERDAEDVKKQPFFRNIDWEALLARKIKPPFVPTIKSPEDVSNFDEEFTSEKPVLTPPKEPRPLTEEEQALFKD 320

                ....*
gi 47132591 941 FDFVA 945
Cdd:cd05589 321 FDYVA 325
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
625-944 4.26e-173

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, classical PKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. Novel PKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. Also included in this subfamily are the PKC-like proteins, called PKNs. The PKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 505.60  E-value: 4.26e-173
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 625 AVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAavTSAGHPFLVNLFGCFQTPEHVCFVMEYS 704
Cdd:cd05570   1 KVLGKGSFGKVMLAERKKTDELYAIKVLKKEVIIEDDDVECTMTEKRVLA--LANRHPFLTGLHACFQTEDRLYFVMEYV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 705 AGGDLMLHIHSD-VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCG 783
Cdd:cd05570  79 NGGDLMFHIQRArRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCKEGIWGGNTTSTFCG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 784 TPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNPERR 863
Cdd:cd05570 159 TPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDEVLYPRWLSREAVSILKGLLTKDPARR 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 864 LGSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFDEEFTGEAPTLSPPRDARpLTAAEQAAFLDFDF 943
Cdd:cd05570 239 LGCGPKGEADIKAHPFFRNIDWDKLEKKEVEPPFKPKVKSPRDTSNFDPEFTSESPRLTPVDSDL-LTNIDQEEFRGFSY 317

                .
gi 47132591 944 V 944
Cdd:cd05570 318 I 318
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
626-945 3.56e-131

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of phosphoinositide 3-kinase (PI3K) and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 397.50  E-value: 3.56e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAavtSAGHPFLVNLFGCFQTPEHVCFVMEYSA 705
Cdd:cd05571   2 VLGKGTFGKVILCREKATGELYAIKILKKEVIIAKDEVAHTLTENRVLQ---NTRHPFLTSLKYSFQTNDRLCFVMEYVN 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 706 GGDLMLHIHSD-VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCGT 784
Cdd:cd05571  79 GGELFFHLSRErVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKEEISYGATTKTFCGT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 785 PEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNPERRL 864
Cdd:cd05571 159 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEVRFPSTLSPEAKSLLAGLLKKDPKKRL 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 865 GSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFDEEFTGEAPTLSPPRDARPLT--AAEQAAFLDFD 942
Cdd:cd05571 239 GGGPRDAKEIMEHPFFASINWDDLYQKKIPPPFKPQVTSETDTRYFDEEFTAESVELTPPDRGDLLGleEEERPHFEQFS 318

                ...
gi 47132591 943 FVA 945
Cdd:cd05571 319 YSA 321
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
625-944 8.14e-131

Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 396.37  E-value: 8.14e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 625 AVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTSagHPFLVNLFGCFQTPEHVCFVMEYS 704
Cdd:cd05592   1 KVLGKGSFGKVMLAELKGTNQYFAIKALKKDVVLEDDDVECTMIERRVLALASQ--HPFLTHLFCTFQTESHLFFVMEYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 705 AGGDLMLHIHSD-VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMgYGDR-TSTFC 782
Cdd:cd05592  79 NGGDLMFHIQQSgRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKENI-YGENkASTFC 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 783 GTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNPER 862
Cdd:cd05592 158 GTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDTPHYPRWLTKEAASCLSLLLERNPEK 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 863 RLGSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFDEEFTGEAPTLSPPrDARPLTAAEQAAFLDFD 942
Cdd:cd05592 238 RLGVPECPAGDIRDHPFFKTIDWDKLERREIDPPFKPKVKSANDVSNFDPDFTMEKPVLTPV-DKKLLASMDQEQFKGFS 316

                ..
gi 47132591 943 FV 944
Cdd:cd05592 317 FT 318
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
624-944 2.90e-121

Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 371.72  E-value: 2.90e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 624 LAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAavTSAGHPFLVNLFGCFQTPEHVCFVMEY 703
Cdd:cd05587   1 LMVLGKGSFGKVMLAERKGTDELYAIKILKKDVIIQDDDVECTMVEKRVLA--LSGKPPFLTQLHSCFQTMDRLYFVMEY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 704 SAGGDLMLHI-HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFC 782
Cdd:cd05587  79 VNGGDLMYHIqQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKEGIFGGKTTRTFC 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 783 GTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNPER 862
Cdd:cd05587 159 GTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGLLTKHPAK 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 863 RLGSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFDEEFTGEAPTLSPPrDARPLTAAEQAAFLDFD 942
Cdd:cd05587 239 RLGCGPTGERDIKEHPFFRRIDWEKLERREIQPPFKPKIKSPRDAENFDKEFTKEPPVLTPT-DKLVIMNIDQSEFEGFS 317

                ..
gi 47132591 943 FV 944
Cdd:cd05587 318 FV 319
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
626-944 1.08e-116

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 359.88  E-value: 1.08e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAavTSAGHPFLVNLFGCFQTPEHVCFVMEYSA 705
Cdd:cd05591   2 VLGKGSFGKVMLAERKGTDEVYAIKVLKKDVILQDDDVDCTMTEKRILA--LAAKHPFLTALHSCFQTKDRLFFVMEYVN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 706 GGDLMLHIH-SDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCGT 784
Cdd:cd05591  80 GGDLMFQIQrARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGKTTTTFCGT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 785 PEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNPERRL 864
Cdd:cd05591 160 PDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPAKRL 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 865 G--SSERDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFDEEFTGEAPTLSPPrDARPLTAAEQAAFLDFD 942
Cdd:cd05591 240 GcvASQGGEDAIRQHPFFREIDWEALEQRKVKPPFKPKIKTKRDANNFDQDFTKEEPVLTPV-DPAVIKQINQEEFRGFS 318

                ..
gi 47132591 943 FV 944
Cdd:cd05591 319 FV 320
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
616-944 1.05e-112

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. Although T-cells also express other PKC isoforms, PKC-theta is unique in that upon antigen stimulation, it is translocated to the plasma membrane at the immunological synapse, where it mediates signals essential for T-cell activation. It is essential for TCR-induced proliferation, cytokine production, T-cell survival, and the differentiation and effector function of T-helper (Th) cells, particularly Th2 and Th17. PKC-theta is being developed as a therapeutic target for Th2-mediated allergic inflammation and Th17-mediated autoimmune diseases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 349.61  E-value: 1.05e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 616 LTLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTSagHPFLVNLFGCFQTPE 695
Cdd:cd05619   2 LTIEDFVLHKMLGKGSFGKVFLAELKGTNQFFAIKALKKDVVLMDDDVECTMVEKRVLSLAWE--HPFLTHLFCTFQTKE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 696 HVCFVMEYSAGGDLMLHIHS-DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMgY 774
Cdd:cd05619  80 NLFFVMEYLNGGDLMFHIQScHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKENM-L 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 775 GD-RTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMR 853
Cdd:cd05619 159 GDaKTSTFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIRMDNPFYPRWLEKEAKDILV 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 854 RLLRRNPERRLGSSerdaEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFDEEFTGEAPTLSPPrDARPLTAA 933
Cdd:cd05619 239 KLFVREPERRLGVR----GDIRQHPFFREINWEALEEREIEPPFKPKVKSPFDCSNFDKEFLNEKPRLSFA-DRALINSM 313
                       330
                ....*....|.
gi 47132591 934 EQAAFLDFDFV 944
Cdd:cd05619 314 DQNMFRNFSFV 324
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
626-945 6.64e-110

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-eta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 342.27  E-value: 6.64e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTSagHPFLVNLFGCFQTPEHVCFVMEYSA 705
Cdd:cd05590   2 VLGKGSFGKVMLARLKESGRLYAVKVLKKDVILQDDDVECTMTEKRILSLARN--HPFLTQLYCCFQTPDRLFFVMEFVN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 706 GGDLMLHIH-SDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCGT 784
Cdd:cd05590  80 GGDLMFHIQkSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGIFNGKTTSTFCGT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 785 PEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNPERRL 864
Cdd:cd05590 160 PDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLSQDAVDILKAFMTKNPTMRL 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 865 GSSERDAED-VKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFDEEFTGEAPTLSPPrDARPLTAAEQAAFLDFDF 943
Cdd:cd05590 240 GSLTLGGEEaILRHPFFKELDWEKLNRRQIEPPFRPRIKSREDVSNFDPDFIKEDPVLTPI-EESLLPMINQDEFRNFSY 318

                ..
gi 47132591 944 VA 945
Cdd:cd05590 319 TA 320
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
620-944 6.82e-108

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG, and in most cases, phosphatidylserine (PS) for activation. The cPKC-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 336.97  E-value: 6.82e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAavTSAGHPFLVNLFGCFQTPEHVCF 699
Cdd:cd05616   1 DFNFLMVLGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLA--LSGKPPFLTQLHSCFQTMDRLYF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYSAGGDLMLHIHS-DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRT 778
Cdd:cd05616  79 VMEYVNGGDLMYHIQQvGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 779 STFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRR 858
Cdd:cd05616 159 KTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTK 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 859 NPERRLGSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRtDVSNFDEEFTGEAPTLSPPrDARPLTAAEQAAF 938
Cdd:cd05616 239 HPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKACGR-NAENFDRFFTRHPPVLTPP-DQEVIRNIDQSEF 316

                ....*.
gi 47132591 939 LDFDFV 944
Cdd:cd05616 317 EGFSFV 322
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
626-944 1.50e-106

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 333.06  E-value: 1.50e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAavTSAGHPFLVNLFGCFQTPEHVCFVMEYSA 705
Cdd:cd05620   2 VLGKGSFGKVLLAELKGKGEYFAVKALKKDVVLIDDDVECTMVEKRVLA--LAWENPFLTHLYCTFQTKEHLFFVMEFLN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 706 GGDLMLHIHSD-VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMgYGD-RTSTFCG 783
Cdd:cd05620  80 GGDLMFHIQDKgRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKENV-FGDnRASTFCG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 784 TPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNPERR 863
Cdd:cd05620 159 TPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPRWITKESKDILEKLFERDPTRR 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 864 LGSSerdaEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFDEEFTGEAPTLSPPrDARPLTAAEQAAFLDFDF 943
Cdd:cd05620 239 LGVV----GNIRGHPFFKTINWTALEKRELDPPFKPKVKSPSDYSNFDREFLSEKPRLSYS-DKNLIDSMDQSAFAGFSF 313

                .
gi 47132591 944 V 944
Cdd:cd05620 314 I 314
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
626-944 4.08e-103

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGKs are activated by insulin and growth factors via phosphoinositide 3-kinase and PDK1. They activate ion channels, ion carriers, and the Na-K-ATPase, as well as regulate the activity of enzymes and transcription factors. SGKs play important roles in transport, hormone release, neuroexcitability, cell proliferation, and apoptosis. There are three isoforms of SGK, named SGK1, SGK2, and SGK3 (also called cytokine-independent survival kinase CISK). The SGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 324.27  E-value: 4.08e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILaaVTSAGHPFLVNLFGCFQTPEHVCFVMEYSA 705
Cdd:cd05575   2 VIGKGSFGKVLLARHKAEGKLYAVKVLQKKAILKRNEVKHIMAERNVL--LKNVKHPFLVGLHYSFQTKDKLYFVLDYVN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 706 GGDLMLHIHSD-VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCGT 784
Cdd:cd05575  80 GGELFFHLQRErHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKEGIEPSDTTSTFCGT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 785 PEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNPERRL 864
Cdd:cd05575 160 PEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKPLRLRTNVSPSARDLLEGLLQKDRTKRL 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 865 GSSeRDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFDEEFTGEA--PTLSPPRDARPLTAAEQA---AFL 939
Cdd:cd05575 240 GSG-NDFLEIKNHSFFRPINWDDLEAKKIPPPFNPNVSGPLDLRNIDPEFTREPvpASVGKSADSVAVSASVQEadnAFD 318

                ....*
gi 47132591 940 DFDFV 944
Cdd:cd05575 319 GFSYV 323
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
626-945 5.30e-103

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-beta is the predominant PKB isoform expressed in insulin-responsive tissues. It plays a critical role in the regulation of glucose homeostasis. It is also implicated in muscle cell differentiation. Mice deficient in PKB-beta display normal growth weights but exhibit severe insulin resistance and diabetes, accompanied by lipoatrophy and B-cell failure. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain.The PKB-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 323.88  E-value: 5.30e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILaavTSAGHPFLVNLFGCFQTPEHVCFVMEYSA 705
Cdd:cd05595   2 LLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTESRVL---QNTRHPFLTALKYAFQTHDRLCFVMEYAN 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 706 GGDLMLHIHSD-VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCGT 784
Cdd:cd05595  79 GGELFFHLSRErVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGITDGATMKTFCGT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 785 PEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNPERRL 864
Cdd:cd05595 159 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRL 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 865 GSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFDEEFTGEAPTLSPPRDARPLTAAE---QAAFLDF 941
Cdd:cd05595 239 GGGPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDDEFTAQSITITPPDRYDSLDLLEsdqRTHFPQF 318

                ....
gi 47132591 942 DFVA 945
Cdd:cd05595 319 SYSA 322
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
618-944 9.58e-103

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. The cPKC-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 323.87  E-value: 9.58e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 618 LEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTSAghPFLVNLFGCFQTPEHV 697
Cdd:cd05615   9 LTDFNFLMVLGKGSFGKVMLAERKGSDELYAIKILKKDVVIQDDDVECTMVEKRVLALQDKP--PFLTQLHSCFQTVDRL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 698 CFVMEYSAGGDLMLHIHS-DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGD 776
Cdd:cd05615  87 YFVMEYVNGGDLMYHIQQvGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMVEGV 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 777 RTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLL 856
Cdd:cd05615 167 TTRTFCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGLM 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 857 RRNPERRLGSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRtDVSNFDEEFTGEAPTLSPPrDARPLTAAEQA 936
Cdd:cd05615 247 TKHPAKRLGCGPEGERDIREHAFFRRIDWDKLENREIQPPFKPKVCGK-GAENFDKFFTRGQPVLTPP-DQLVIANIDQA 324

                ....*...
gi 47132591 937 AFLDFDFV 944
Cdd:cd05615 325 DFEGFSYV 332
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
627-880 3.70e-102

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 318.69  E-value: 3.70e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd05123   1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRKEVEHTLNERNILERVN---HPFIVKLHYAFQTEEKLYLVLDYVPG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLMLHIHSD-VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCGTP 785
Cdd:cd05123  78 GELFSHLSKEgRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSDGDRTYTFCGTP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 786 EFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNPERRLG 865
Cdd:cd05123 158 EYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFPEYVSPEAKSLISGLLQKDPTKRLG 237
                       250
                ....*....|....*
gi 47132591 866 SseRDAEDVKKQPFF 880
Cdd:cd05123 238 S--GGAEEIKAHPFF 250
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
619-911 5.63e-102

Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the cAMP-dependent protein kinases, PKA and PRKX, and similar proteins. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. PRKX is also reulated by the R subunit and is is present in many tissues including fetal and adult brain, kidney, and lung. It is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PKA-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 319.91  E-value: 5.63e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVC 698
Cdd:cd05580   1 DDFEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKIIKLKQVEHVLNEKRILSEVR---HPFIVNLLGSFQDDRNLY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGGDLMLHIH-SDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEgmgYGDR 777
Cdd:cd05580  78 MVMEYVPGGELFSLLRrSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKR---VKDR 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 778 TSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLR 857
Cdd:cd05580 155 TYTLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKIRFPSFFDPDAKDLIKRLLV 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 47132591 858 RNPERRLGSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFD 911
Cdd:cd05580 235 VDLTKRLGNLKNGVEDIKNHPWFAGIDWDALLQRKIPAPYVPKVRGPGDTSNFD 288
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
596-924 4.32e-96

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 306.96  E-value: 4.32e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 596 PSETQETPGPALCSPLRKSPLTLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILaa 675
Cdd:cd05594   2 PSDNSGAEEMEVSLTKPKHKVTMNDFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVL-- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 676 vTSAGHPFLVNLFGCFQTPEHVCFVMEYSAGGDLMLHIHSD-VFSEPRAIFYSACVVLGLQFLH-EHKIVYRDLKLDNLL 753
Cdd:cd05594  80 -QNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRErVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLM 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 754 LDTEGYVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSI 833
Cdd:cd05594 159 LDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELI 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 834 VNDEVRYPRFLSAEAIGIMRRLLRRNPERRLGSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFDEE 913
Cdd:cd05594 239 LMEEIRFPRTLSPEAKSLLSGLLKKDPKQRLGGGPDDAKEIMQHKFFAGIVWQDVYEKKLVPPFKPQVTSETDTRYFDEE 318
                       330
                ....*....|.
gi 47132591 914 FTGEAPTLSPP 924
Cdd:cd05594 319 FTAQMITITPP 329
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
624-945 4.47e-94

Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 300.09  E-value: 4.47e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 624 LAVLGRGHFGKVLLSEF---RPSGELFAIKALKKGDIV--ARDEVESlMCEKRILAAVTsagHPFLVNLFGCFQTPEHVC 698
Cdd:cd05584   1 LKVLGKGGYGKVFQVRKttgSDKGKIFAMKVLKKASIVrnQKDTAHT-KAERNILEAVK---HPFIVDLHYAFQTGGKLY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGGDLMLHIHSD-VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDR 777
Cdd:cd05584  77 LILEYLSGGELFMHLEREgIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCKESIHDGTV 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 778 TSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLR 857
Cdd:cd05584 157 THTFCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLNLPPYLTNEARDLLKKLLK 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 858 RNPERRLGSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFDEEFTGEAPTLSPPrDARPLTAAEQaA 937
Cdd:cd05584 237 RNVSSRLGSGPGDAEEIKAHPFFRHINWDDLLAKKVEPPFKPLLQSEEDVSQFDSKFTKQTPVDSPD-DSTLSESANQ-V 314

                ....*...
gi 47132591 938 FLDFDFVA 945
Cdd:cd05584 315 FQGFTYVA 322
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
617-924 1.13e-93

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-gamma is predominantly expressed in neuronal tissues. Mice deficient in PKB-gamma show a reduction in brain weight due to the decreases in cell size and cell number. PKB-gamma has also been shown to be upregulated in estrogen-deficient breast cancer cells, androgen-independent prostate cancer cells, and primary ovarian tumors. It acts as a key mediator in the genesis of ovarian cancer. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 300.07  E-value: 1.13e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 617 TLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILaavTSAGHPFLVNLFGCFQTPEH 696
Cdd:cd05593  13 TMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVL---KNTRHPFLTSLKYSFQTKDR 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 697 VCFVMEYSAGGDLMLHIHSD-VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYG 775
Cdd:cd05593  90 LCFVMEYVNGGELFFHLSRErVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDA 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 776 DRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRL 855
Cdd:cd05593 170 ATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSADAKSLLSGL 249
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47132591 856 LRRNPERRLGSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFDEEFTGEAPTLSPP 924
Cdd:cd05593 250 LIKDPNKRLGGGPDDAKEIMRHSFFTGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPP 318
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
626-944 2.43e-86

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 279.69  E-value: 2.43e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGELFAIKALKKgDIVARDE-VESLMCEKRILAavTSAGHPFLVNLFGCFQTPEHVCFVMEYS 704
Cdd:cd05588   2 VIGRGSYAKVLMVELKKTKRIYAMKVIKK-ELVNDDEdIDWVQTEKHVFE--TASNHPFLVGLHSCFQTESRLFFVIEFV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 705 AGGDLMLHIHSD-VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCG 783
Cdd:cd05588  79 NGGDLMFHMQRQrRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTFCG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 784 TPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPF--------PGDDEEE-VFDSIVNDEVRYPRFLSAEAIGIMRR 854
Cdd:cd05588 159 TPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPFdivgssdnPDQNTEDyLFQVILEKPIRIPRSLSVKAASVLKG 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 855 LLRRNPERRLGSSERDA-EDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFDEEFTGEAPTLSPPrDARPLTAA 933
Cdd:cd05588 239 FLNKNPAERLGCHPQTGfADIQSHPFFRTIDWEQLEQKQVTPPYKPRIESERDLENFDPQFTNEPVQLTPD-DPDVIEKI 317
                       330
                ....*....|.
gi 47132591 934 EQAAFLDFDFV 944
Cdd:cd05588 318 DQSEFEGFEYV 328
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
624-917 6.44e-86

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK3 (also called cytokine-independent survival kinase or CISK) is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. The SGK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 278.77  E-value: 6.44e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 624 LAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILaaVTSAGHPFLVNLFGCFQTPEHVCFVMEY 703
Cdd:cd05604   1 LKVIGKGSFGKVLLAKRKRDGKYYAVKVLQKKVILNRKEQKHIMAERNVL--LKNVKHPFLVGLHYSFQTTDKLYFVLDF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 704 SAGGDLMLHIHSD-VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFC 782
Cdd:cd05604  79 VNGGELFFHLQRErSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEGISNSDTTTTFC 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 783 GTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNPER 862
Cdd:cd05604 159 GTPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENILHKPLVLRPGISLTAWSILEELLEKDRQL 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 47132591 863 RLGSSErDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFDEEFTGE 917
Cdd:cd05604 239 RLGAKE-DFLEIKNHPFFESINWTDLVQKKIPPPFNPNVNGPDDISNFDAEFTEE 292
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
625-944 9.55e-86

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK2 shows a more restricted distribution than SGK1 and is most abundantly expressed in epithelial tissues including kidney, liver, pancreas, and the choroid plexus of the brain. In vitro cellular assays show that SGK2 can stimulate the activity of ion channels, the glutamate transporter EEAT4, and the glutamate receptors, GluR6 and GLUR1. The SGK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 278.01  E-value: 9.55e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 625 AVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILaaVTSAGHPFLVNLFGCFQTPEHVCFVMEYS 704
Cdd:cd05603   1 KVIGKGSFGKVLLAKRKCDGKFYAVKVLQKKTILKKKEQNHIMAERNVL--LKNLKHPFLVGLHYSFQTSEKLYFVLDYV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 705 AGGDLMLHIHSD-VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCG 783
Cdd:cd05603  79 NGGELFFHLQRErCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEGMEPEETTSTFCG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 784 TPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNPERR 863
Cdd:cd05603 159 TPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILHKPLHLPGGKTVAACDLLQGLLHKDQRRR 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 864 LGsSERDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFDEEFTGEAPTLSPPR--DARPLTAAEQAAFLDF 941
Cdd:cd05603 239 LG-AKADFLEIKNHVFFSPINWDDLYHKRITPPYNPNVAGPADLRHFDPEFTQEAVPHSVGRtpDLTASSSSSSSAFLGF 317

                ...
gi 47132591 942 DFV 944
Cdd:cd05603 318 SYA 320
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
626-944 1.76e-82

N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), p90-RSKs, or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 268.88  E-value: 1.76e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEF---RPSGELFAIKALKKGDIVARDEVESLMcEKRILAAVtsaGHPFLVNLFGCFQTPEHVCFVME 702
Cdd:cd05582   2 VLGQGSFGKVFLVRKitgPDAGTLYAMKVLKKATLKVRDRVRTKM-ERDILADV---NHPFIVKLHYAFQTEGKLYLILD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 703 YSAGGDLMLHIHSDV-FSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTF 781
Cdd:cd05582  78 FLRGGDLFTRLSKEVmFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKESIDHEKKAYSF 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 782 CGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNPE 861
Cdd:cd05582 158 CGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRALFKRNPA 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 862 RRLGSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFDEEFTGEAPTLSPprdARPLTAAEQAAFLDF 941
Cdd:cd05582 238 NRLGAGPDGVEEIKRHPFFATIDWNKLYRKEIKPPFKPAVSRPDDTFYFDPEFTSRTPKDSP---GVPPSANAHQLFRGF 314

                ...
gi 47132591 942 DFV 944
Cdd:cd05582 315 SFV 317
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
626-943 1.65e-80

Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal proteins with similarity to the AGC STKs, Saccharomyces cerevisiae YPK1 and Schizosaccharomyces pombe Gad8p. YPK1 is required for cell growth and acts as a downstream kinase in the sphingolipid-mediated signaling pathway of yeast. It also plays a role in efficient endocytosis and in the maintenance of cell wall integrity. Gad8p is a downstream target of Tor1p, the fission yeast homolog of mTOR. It plays a role in cell growth and sexual development. The YPK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 263.66  E-value: 1.65e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTSaghPFLVNLFGCFQTPEHVCFVMEYSA 705
Cdd:cd05585   1 VIGKGSFGKVMQVRKKDTSRIYALKTIRKAHIVSRSEVTHTLAERTVLAQVDC---PFIVPLKFSFQSPEKLYLVLAFIN 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 706 GGDLMLHIHSD-VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCGT 784
Cdd:cd05585  78 GGELFHHLQREgRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKLNMKDDDKTNTFCGT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 785 PEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNPERRL 864
Cdd:cd05585 158 PEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPLRFPDGFDRDAKDLLIGLLNRDPTKRL 237
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47132591 865 GSSerDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFDEEFTGEAPTLSPPRDARpLTAAEQAAFLDFDF 943
Cdd:cd05585 238 GYN--GAQEIKNHPFFDQIDWKRLLMKKIQPPFKPAVENAIDTSNFDEEFTREKPIDSVVDDSH-LSESVQQQFEGWSY 313
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
621-880 8.26e-80

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 259.38  E-value: 8.26e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591    621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIvaRDEVESLMCEKRILAavtSAGHPFLVNLFGCFQTPEHVCFV 700
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKI--KKDRERILREIKILK---KLKHPNIVRLYDVFEDEDKLYLV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591    701 MEYSAGGDLMLHIHSDV-FSEPRAIFYSACVVLGLQFLHEHKIVYRdlkldnllldTEGYVKIADFGLCKEgMGYGDRTS 779
Cdd:smart00220  76 MEYCEGGDLFDLLKKRGrLSEDEARFYLRQILSALEYLHSKGIVHRdlkpenilldEDGHVKLADFGLARQ-LDPGEKLT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591    780 TFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEE-EVFDSIVNDEVRYPRF---LSAEAIGIMRRL 855
Cdd:smart00220 155 TFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLlELFKKIGKPKPPFPPPewdISPEAKDLIRKL 234
                          250       260
                   ....*....|....*....|....*
gi 47132591    856 LRRNPERRLGsserdAEDVKKQPFF 880
Cdd:smart00220 235 LVKDPEKRLT-----AEEALQHPFF 254
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
619-912 2.23e-79

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 259.64  E-value: 2.23e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTSaghPFLVNLFGCFQTPEHVC 698
Cdd:cd14209   1 DDFDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKLKQVEHTLNEKRILQAINF---PFLVKLEYSFKDNSNLY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGGDlMLHIHSDV--FSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGygd 776
Cdd:cd14209  78 MVMEYVPGGE-MFSHLRRIgrFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRVKG--- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 777 RTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLL 856
Cdd:cd14209 154 RTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLL 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 47132591 857 RRNPERRLGSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFDE 912
Cdd:cd14209 234 QVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKLKGPGDTSNFDD 289
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
627-943 1.22e-78

Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Sck1 and similar fungal proteins. Sck1 plays a role in trehalase activation triggered by glucose and a nitrogen source. Trehalase catalyzes the cleavage of the disaccharide trehalose to glucose. Trehalose, as a carbohydrate reserve and stress metabolite, plays an important role in the response of yeast to environmental changes. The Sck1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 259.04  E-value: 1.22e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTSAGHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd05586   1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKEVAHTIGERNILVRTALDESPFIVGLKFSFQTPTDLYLVTDYMSG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLMLHIHSD-VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCGTP 785
Cdd:cd05586  81 GELFWHLQKEgRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSKADLTDNKTTNTFCGTT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 786 EFLAPEVLTD-TSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPR-FLSAEAIGIMRRLLRRNPERR 863
Cdd:cd05586 161 EYLAPEVLLDeKGYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVRFPKdVLSDEGRSFVKGLLNRNPKHR 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 864 LGSSeRDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFDEEFT-----------GEAPTLSPPRDARPLTA 932
Cdd:cd05586 241 LGAH-DDAVELKEHPFFADIDWDLLSKKKITPPFKPIVDSDTDVSNFDPEFTnasllnanivpWAQRPGLPGATSTPLSP 319
                       330
                ....*....|.
gi 47132591 933 AEQAAFLDFDF 943
Cdd:cd05586 320 SVQANFRGFTF 330
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
614-944 6.92e-78

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 258.42  E-value: 6.92e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 614 SPLTLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTSagHPFLVNLFGCFQT 693
Cdd:cd05618  15 SSLGLQDFDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEDIDWVQTEKHVFEQASN--HPFLVGLHSCFQT 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 694 PEHVCFVMEYSAGGDLMLHIHSD-VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGM 772
Cdd:cd05618  93 ESRLFFVIEYVNGGDLMFHMQRQrKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGL 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 773 GYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPF--------PGDDEEE-VFDSIVNDEVRYPRF 843
Cdd:cd05618 173 RPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFdivgssdnPDQNTEDyLFQVILEKQIRIPRS 252
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 844 LSAEAIGIMRRLLRRNPERRLGSSERDA-EDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFDEEFTGEAPTLS 922
Cdd:cd05618 253 LSVKAASVLKSFLNKDPKERLGCHPQTGfADIQGHPFFRNVDWDLMEQKQVVPPFKPNISGEFGLDNFDSQFTNEPVQLT 332
                       330       340
                ....*....|....*....|..
gi 47132591 923 PPrDARPLTAAEQAAFLDFDFV 944
Cdd:cd05618 333 PD-DDDIVRKIDQSEFEGFEYI 353
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
618-941 7.66e-78

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 257.05  E-value: 7.66e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  618 LEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHV 697
Cdd:PTZ00263  17 LSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELS---HPFIVNMMCSFQDENRV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  698 CFVMEYSAGGDLMLHIHS-DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEgmgYGD 776
Cdd:PTZ00263  94 YFLLEFVVGGELFTHLRKaGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKK---VPD 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  777 RTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLL 856
Cdd:PTZ00263 171 RTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGRARDLVKGLL 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  857 RRNPERRLGSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFDeeftgEAPTlSPPRDARPLTAAEQA 936
Cdd:PTZ00263 251 QTDHTKRLGTLKGGVADVKNHPYFHGANWDKLYARYYPAPIPVRVKSPGDTSNFE-----KYPD-SPVDRLPPLTAAQQA 324

                 ....*
gi 47132591  937 AFLDF 941
Cdd:PTZ00263 325 EFAGF 329
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
616-944 1.55e-77

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 257.26  E-value: 1.55e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 616 LTLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTSagHPFLVNLFGCFQTPE 695
Cdd:cd05617  12 LGLQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASS--NPFLVGLHSCFQTTS 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 696 HVCFVMEYSAGGDLMLHIHSD-VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGY 774
Cdd:cd05617  90 RLFLVIEYVNGGDLMFHMQRQrKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGP 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 775 GDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPF-------PGDDEEEVFDSIVNDEVRYPRFLSAE 847
Cdd:cd05617 170 GDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFdiitdnpDMNTEDYLFQVILEKPIRIPRFLSVK 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 848 AIGIMRRLLRRNPERRLGSSERDA-EDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFDEEFTGEaPTLSPPRD 926
Cdd:cd05617 250 ASHVLKGFLNKDPKERLGCQPQTGfSDIKSHTFFRSIDWDLLEKKQVTPPFKPQITDDYGLENFDTQFTSE-PVQLTPDD 328
                       330
                ....*....|....*...
gi 47132591 927 ARPLTAAEQAAFLDFDFV 944
Cdd:cd05617 329 EDVIKRIDQSEFEGFEYI 346
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
627-887 2.32e-77

Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mammals have two cGK isoforms from different genes, cGKI and cGKII. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. cGK consists of an N-terminal regulatory domain containing a dimerization and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. cGKII is a membrane-bound protein that is most abundantly expressed in the intestine. It is also present in the brain nuclei, adrenal cortex, kidney, lung, and prostate. cGKI is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. cGKII plays a role in the regulation of secretion, such as renin secretion by the kidney and aldosterone secretion by the adrenal. It also regulates bone growth and the circadian rhythm. The cGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 253.30  E-value: 2.32e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd05572   1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIVQTRQQEHIFSEKEILEECN---SPFIVKLYRTFKDKKYLYMLMEYCLG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLMLHIHS-DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEgMGYGDRTSTFCGTP 785
Cdd:cd05572  78 GELWTILRDrGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKK-LGSGRKTWTFCGTP 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 786 EFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEE--EVFDSIV--NDEVRYPRFLSAEAIGIMRRLLRRNPE 861
Cdd:cd05572 157 EYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGDDEDpmKIYNIILkgIDKIEFPKYIDKNAKNLIKQLLRRNPE 236
                       250       260
                ....*....|....*....|....*.
gi 47132591 862 RRLGSSERDAEDVKKQPFFRTLGWEA 887
Cdd:cd05572 237 ERLGYLKGGIRDIKKHKWFEGFDWEG 262
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
620-945 1.01e-76

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 254.07  E-value: 1.01e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKFLAVLGRGHFGKVLL---SEFRPSGELFAIKALKKGDIVARDE-VESLMCEKRILAAVTSAghPFLVNLFGCFQTPE 695
Cdd:cd05614   1 NFELLKVLGTGAYGKVFLvrkVSGHDANKLYAMKVLRKAALVQKAKtVEHTRTERNVLEHVRQS--PFLVTLHYAFQTDA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 696 HVCFVMEYSAGGDLMLHIHS-DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGY 774
Cdd:cd05614  79 KLHLILDYVSGGELFTHLYQrDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKEFLTE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 775 -GDRTSTFCGTPEFLAPEVL-TDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEE----EVFDSIVNDEVRYPRFLSAEA 848
Cdd:cd05614 159 eKERTYSFCGTIEYMAPEIIrGKSGHGKAVDWWSLGILMFELLTGASPFTLEGEKntqsEVSRRILKCDPPFPSFIGPVA 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 849 IGIMRRLLRRNPERRLGSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFDEEFTGEAPTLSPPRDAR 928
Cdd:cd05614 239 RDLLQKLLCKDPKKRLGAGPQGAQEIKEHPFFKGLDWEALALRKVNPPFRPSIRSELDVGNFAEEFTNLEPVYSPAGTPP 318
                       330
                ....*....|....*..
gi 47132591 929 PLtaaeQAAFLDFDFVA 945
Cdd:cd05614 319 SG----ARVFQGYSFIA 331
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
620-943 3.22e-76

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK1 is ubiquitously expressed and is under transcriptional control of numerous stimuli including cell stress (cell shrinkage), serum, hormones (gluco- and mineralocorticoids), gonadotropins, growth factors, interleukin-6, and other cytokines. It plays roles in sodium retention and potassium elimination in the kidney, nutrient transport, salt sensitivity, memory consolidation, and cardiac repolarization. A common SGK1 variant is associated with increased blood pressure and body weight. SGK1 may also contribute to tumor growth, neurodegeneration, fibrosing disease, and ischemia. The SGK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 253.02  E-value: 3.22e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILaaVTSAGHPFLVNLFGCFQTPEHVCF 699
Cdd:cd05602   8 DFHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQKKAILKKKEEKHIMSERNVL--LKNVKHPFLVGLHFSFQTTDKLYF 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYSAGGDLMLHIHSD-VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRT 778
Cdd:cd05602  86 VLDYINGGELFYHLQRErCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIEPNGTT 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 779 STFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRR 858
Cdd:cd05602 166 STFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLKPNITNSARHLLEGLLQK 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 859 NPERRLGSSErDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFDEEFTGE-AP-TLSPPRDARPLTAA--E 934
Cdd:cd05602 246 DRTKRLGAKD-DFTEIKNHIFFSPINWDDLINKKITPPFNPNVSGPNDLRHFDPEFTDEpVPnSIGQSPDSILVTASikE 324
                       330
                ....*....|
gi 47132591 935 QA-AFLDFDF 943
Cdd:cd05602 325 AAeAFLGFSY 334
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
619-911 6.34e-76

Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include human PRKX (X chromosome-encoded protein kinase), Drosophila DC2, and similar proteins. PRKX is present in many tissues including fetal and adult brain, kidney, and lung. The PRKX gene is located in the Xp22.3 subregion and has a homolog called PRKY on the Y chromosome. An abnormal interchange between PRKX aand PRKY leads to the sex reversal disorder of XX males and XY females. PRKX is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PRKX-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 250.43  E-value: 6.34e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVC 698
Cdd:cd05612   1 DDFERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEVIRLKQEQHVHNEKRVLKEVS---HPFIIRLFWTEHDQRFLY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGGDLMLHIH-SDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEgmgYGDR 777
Cdd:cd05612  78 MLMEYVPGGELFSYLRnSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKK---LRDR 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 778 TSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLR 857
Cdd:cd05612 155 TWTLCGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKLEFPRHLDLYAKDLIKKLLV 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 47132591 858 RNPERRLGSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFD 911
Cdd:cd05612 235 VDRTRRLGNMKNGADDVKNHRWFKSVDWDDVPQRKLKPPIVPKVSHDGDTSNFD 288
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
619-943 2.30e-75

Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. The ROCK/NDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 251.05  E-value: 2.30e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTSaghPFLVNLFGCFQTPEHVC 698
Cdd:cd05573   1 DDFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSDMLKREQIAHVRAERDILADADS---PWIVRLHYAFQDEDHLY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGGDLM-LHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKeGMGYGDR 777
Cdd:cd05573  78 LVMEYMPGGDLMnLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCT-KMNKSGD 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 778 TS------------------------------TFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEE 827
Cdd:cd05573 157 REsylndsvntlfqdnvlarrrphkqrrvraySAVGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPPFYSDSLV 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 828 EVFDSIVN--DEVRYPR--FLSAEAIGIMRRLLRRnPERRLGSserdAEDVKKQPFFRTLGWEALlaRRLPPPFVPTLSG 903
Cdd:cd05573 237 ETYSKIMNwkESLVFPDdpDVSPEAIDLIRRLLCD-PEDRLGS----AEEIKAHPFFKGIDWENL--RESPPPFVPELSS 309
                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 47132591 904 RTDVSNFDEEFTGEAPTLSPPRDARPLTAAEQAAFLDFDF 943
Cdd:cd05573 310 PTDTSNFDDFEDDLLLSEYLSNGSPLLGKGKQLAFVGFTF 349
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
619-944 4.65e-75

Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also contains fungal NDR-like kinases. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 249.07  E-value: 4.65e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAavtSAGHPFLVNLFGCFQTPEHVC 698
Cdd:cd05599   1 EDFEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEMLEKEQVAHVRAERDILA---EADNPWVVKLYYSFQDEENLY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGGDLM-LHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK----EGMG 773
Cdd:cd05599  78 LIMEFLPGGDMMtLLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCTglkkSHLA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 774 YgdrtSTfCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVN--------DEVRyprfLS 845
Cdd:cd05599 158 Y----ST-VGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIMNwretlvfpPEVP----IS 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 846 AEAIGIMRRLLrRNPERRLGSseRDAEDVKKQPFFRTLGWEALlaRRLPPPFVPTLSGRTDVSNFDEEftgEAPTLSPPR 925
Cdd:cd05599 229 PEAKDLIERLL-CDAEHRLGA--NGVEEIKSHPFFKGVDWDHI--RERPAPILPEVKSILDTSNFDEF---EEVDLQIPS 300
                       330
                ....*....|....*....
gi 47132591 926 DARPLTAAEQAAFLDFDFV 944
Cdd:cd05599 301 SPEAGKDSKELKSKDWVFI 319
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
620-906 6.79e-73

Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phototropins are blue-light receptors that control responses such as phototropism, stromatal opening, and chloroplast movement in order to optimize the photosynthetic efficiency of plants. They are light-activated STKs that contain an N-terminal photosensory domain and a C-terminal catalytic domain. The N-terminal domain contains two LOV (Light, Oxygen or Voltage) domains that binds FMN. Photoexcitation of the LOV domains results in autophosphorylation at multiple sites and activation of the catalytic domain. In addition to plant phototropins, included in this subfamily are predominantly uncharacterized fungal STKs whose catalytic domains resemble the phototropin kinase domain. One protein from Neurospora crassa is called nrc-2, which plays a role in growth and development by controlling entry into the conidiation program. The phototropin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 242.91  E-value: 6.79e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCF 699
Cdd:cd05574   2 HFKKIKLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMIKRNKVKRVLTEREILATLD---HPFLPTLYASFQTSTHLCF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYSAGGDL--MLHIHSD-VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK------- 769
Cdd:cd05574  79 VMDYCPGGELfrLLQKQPGkRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLSKqssvtpp 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 770 ----------EGMGY------------GDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEE 827
Cdd:cd05574 159 pvrkslrkgsRRSSVksieketfvaepSARSNSFVGTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFKGSNRD 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 828 EVFDSIVNDEVRYPR--FLSAEAIGIMRRLLRRNPERRLGsSERDAEDVKKQPFFRTLGWEalLARRLPPPFVPTLSGRT 905
Cdd:cd05574 239 ETFSNILKKELTFPEspPVSSEAKDLIRKLLVKDPSKRLG-SKRGASEIKRHPFFRGVNWA--LIRNMTPPIIPRPDDPI 315

                .
gi 47132591 906 D 906
Cdd:cd05574 316 D 316
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
629-885 8.31e-71

Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAST kinases, MAST-like (MASTL) kinases (also called greatwall kinase or Gwl), and fungal kinases with similarity to Saccharomyces cerevisiae Rim15 and Schizosaccharomyces pombe cek1. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. MASTL kinases carry only a catalytic domain which contains a long insert relative to other kinases. The fungal kinases in this subfamily harbor other domains in addition to a central catalytic domain, which like in MASTL, also contains an insert relative to MAST kinases. Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MASTL/Gwl is involved in the regulation of mitotic entry, mRNA stabilization, and DNA checkpoint recovery. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively. The MAST-like kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 235.57  E-value: 8.31e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 629 RGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTSaghPFLVNLFGCFQTPEHVCFVMEYSAGGD 708
Cdd:cd05579   3 RGAYGRVYLAKKKSTGDLYAIKVIKKRDMIRKNQVDSVLAERNILSQAQN---PFVVKLYYSFQGKKNLYLVMEYLPGGD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 709 L--MLHiHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGM-------------- 772
Cdd:cd05579  80 LysLLE-NVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKVGLvrrqiklsiqkksn 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 773 -GYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRF--LSAEAI 849
Cdd:cd05579 159 gAPEKEDRRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGKIEWPEDpeVSDEAK 238
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 47132591 850 GIMRRLLRRNPERRLGSseRDAEDVKKQPFFRTLGW 885
Cdd:cd05579 239 DLISKLLTPDPEKRLGA--KGIEEIKNHPFFKGIDW 272
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
627-899 8.22e-68

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. GRKs play important roles in the cardiovascular, immune, respiratory, skeletal, and nervous systems. They contain a central catalytic domain, flanked by N- and C-terminal extensions. The N-terminus contains an RGS (regulator of G protein signaling) homology (RH) domain and several motifs. The C-terminus diverges among different groups of GRKs. There are seven types of GRKs, named GRK1 to GRK7, which are subdivided into three main groups: visual (GRK1/7); beta-adrenergic receptor kinases (GRK2/3); and GRK4-like (GRK4/5/6). Expression of GRK2/3/5/6 is widespread while GRK1/4/7 show a limited tissue distribution. The substrate spectrum of the widely expressed GRKs partially overlaps. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 227.80  E-value: 8.22e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTSaghPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd05577   1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKGETMALNEKIILEKVSS---PFIVSLAYAFETKDKLCLVLTLMNG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLMLHIH---SDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEgMGYGDRTSTFCG 783
Cdd:cd05577  78 GDLKYHIYnvgTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVE-FKGGKKIKGRVG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 784 TPEFLAPEVL-TDTSYTRAVDWWGLGVLLYEMLVGESPF----PGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRR 858
Cdd:cd05577 157 THGYMAPEVLqKEVAYDFSVDWFALGCMLYEMIAGRSPFrqrkEKVDKEELKRRTLEMAVEYPDSFSPEARSLCEGLLQK 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 47132591 859 NPERRLGSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVP 899
Cdd:cd05577 237 DPERRLGCRGGSADEVKEHPFFRSLNWQRLEAGMLEPPFVP 277
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
626-883 2.45e-67

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 226.12  E-value: 2.45e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFR---PSGELFAIKALKKGDIVARDEV-ESLMCEKRILAAVTSAghPFLVNLFGCFQTPEHVCFVM 701
Cdd:cd05583   1 VLGTGAYGKVFLVRKVgghDAGKLYAMKVLKKATIVQKAKTaEHTMTERQVLEAVRQS--PFLVTLHYAFQTDAKLHLIL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 702 EYSAGGDLMLHIHS-DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGM-GYGDRTS 779
Cdd:cd05583  79 DYVNGGELFTHLYQrEHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEFLpGENDRAY 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 780 TFCGTPEFLAPEVLT--DTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEE----EVFDSIVNDEVRYPRFLSAEAIGIMR 853
Cdd:cd05583 159 SFCGTIEYMAPEVVRggSDGHDKAVDWWSLGVLTYELLTGASPFTVDGERnsqsEISKRILKSHPPIPKTFSAEAKDFIL 238
                       250       260       270
                ....*....|....*....|....*....|
gi 47132591 854 RLLRRNPERRLGSSERDAEDVKKQPFFRTL 883
Cdd:cd05583 239 KLLEKDPKKRLGAGPRGAHEIKEHPFFKGL 268
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
620-899 3.37e-66

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK1 (also called rhodopsin kinase) belongs to the visual group of GRKs and is expressed in retinal cells. It phosphorylates rhodopsin in rod cells, which leads to termination of the phototransduction cascade. Mutations in GRK1 are associated to a recessively inherited form of stationary nightblindness called Oguchi disease. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 223.61  E-value: 3.37e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKflaVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTSAghpFLVNLFGCFQTPEHVCF 699
Cdd:cd05608   5 DFR---VLGKGGFGEVSACQMRATGKLYACKKLNKKRLKKRKGYEGAMVEKRILAKVHSR---FIVSLAYAFQTKTDLCL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYSAGGDLMLHIHS-----DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGY 774
Cdd:cd05608  79 VMTIMNGGDLRYHIYNvdeenPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVELKDG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 775 GDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDE----EEVFDSIVNDEVRYPRFLSAEAIG 850
Cdd:cd05608 159 QTKTKGYAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFRARGEkvenKELKQRILNDSVTYSEKFSPASKS 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 47132591 851 IMRRLLRRNPERRLGSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVP 899
Cdd:cd05608 239 ICEALLAKDPEKRLGFRDGNCDGLRTHPFFRDINWRKLEAGILPPPFVP 287
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
620-943 8.11e-66

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 224.12  E-value: 8.11e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAavtSAGHPFLVNLFGCFQTPEHVCF 699
Cdd:cd05598   2 MFEKIKTIGVGAFGEVSLVRKKDTNALYAMKTLRKKDVLKRNQVAHVKAERDILA---EADNEWVVKLYYSFQDKENLYF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYSAGGDLM-LHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKeGMGYGDRT 778
Cdd:cd05598  79 VMDYIPGGDLMsLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCT-GFRWTHDS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 779 STFC-----GTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVN--DEVRYPRF--LSAEAI 849
Cdd:cd05598 158 KYYLahslvGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQTPAETQLKVINwrTTLKIPHEanLSPEAK 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 850 GIMRRLLrRNPERRLGSseRDAEDVKKQPFFRTLGWEALlaRRLPPPFVPTLSGRTDVSNFDeEFTGEAPTLSPPRDARP 929
Cdd:cd05598 238 DLILRLC-CDAEDRLGR--NGADEIKAHPFFAGIDWEKL--RKQKAPYIPTIRHPTDTSNFD-PVDPEKLRSSDEEPTTP 311
                       330
                ....*....|....*...
gi 47132591 930 LTAAE----QAAFLDFDF 943
Cdd:cd05598 312 NDPDNgkhpEHAFYEFTF 329
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
620-899 6.42e-64

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 217.56  E-value: 6.42e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKFLAVLGRGHFGKVLLSEF---RPSGELFAIKALKKGDIVARDEV-ESLMCEKRILAAVTSAghPFLVNLFGCFQTPE 695
Cdd:cd05613   1 NFELLKVLGTGAYGKVFLVRKvsgHDAGKLYAMKVLKKATIVQKAKTaEHTRTERQVLEHIRQS--PFLVTLHYAFQTDT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 696 HVCFVMEYSAGGDLMLHIHSDV-FSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMG- 773
Cdd:cd05613  79 KLHLILDYINGGELFTHLSQRErFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEFLLd 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 774 YGDRTSTFCGTPEFLAPEVLT--DTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEE----EVFDSIVNDEVRYPRFLSAE 847
Cdd:cd05613 159 ENERAYSFCGTIEYMAPEIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKnsqaEISRRILKSEPPYPQEMSAL 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 47132591 848 AIGIMRRLLRRNPERRLGSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVP 899
Cdd:cd05613 239 AKDIIQRLLMKDPKKRLGCGPNGADEIKKHPFFQKINWDDLAAKKVPAPFKP 290
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
620-885 1.41e-62

Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine/threonine kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. There are four mammalian MAST kinases, named MAST1-MAST4. MAST1 is also called syntrophin-associated STK (SAST) while MAST2 is also called MAST205. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MAST1, MAST2, and MAST3 bind and phosphorylate the tumor suppressor PTEN, and may contribute to the regulation and stabilization of PTEN. MAST2 is involved in the regulation of the Fc-gamma receptor of the innate immune response in macrophages, and may also be involved in the regulation of the Na+/H+ exchanger NHE3. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 213.42  E-value: 1.41e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILaavTSAGHPFLVNLFGCFQTPEHVCF 699
Cdd:cd05609   1 DFETIKLISNGAYGAVYLVRHRETRQRFAMKKINKQNLILRNQIQQVFVERDIL---TFAENPFVVSMYCSFETKRHLCM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYSAGGD---LMLHIHSdvFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGM---- 772
Cdd:cd05609  78 VMEYVEGGDcatLLKNIGP--LPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSKIGLmslt 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 773 -----GYGDR-TSTF-----CGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYP 841
Cdd:cd05609 156 tnlyeGHIEKdTREFldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIEWP 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 47132591 842 R---FLSAEAIGIMRRLLRRNPERRLGSSerDAEDVKKQPFFRTLGW 885
Cdd:cd05609 236 EgddALPDDAQDLITRLLQQNPLERLGTG--GAEEVKQHPFFQDLDW 280
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
621-899 1.66e-62

Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the GRK4-like group include GRK4, GRK5, GRK6, and similar GRKs. They contain an N-terminal RGS homology (RH) domain and a catalytic domain, but lack a G protein betagamma-subunit binding domain. They are localized to the plasma membrane through post-translational lipid modification or direct binding to PIP2. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 213.37  E-value: 1.66e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARD-EVESLMcEKRILAAVTSaghPFLVNLFGCFQTPEHVCF 699
Cdd:cd05605   2 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKgEAMALN-EKQILEKVNS---RFVVSLAYAYETKDALCL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYSAGGDLMLHIHS---DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEgMGYGD 776
Cdd:cd05605  78 VLTIMNGGDLKFHIYNmgnPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVE-IPEGE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 777 RTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDE----EEVFDSIVNDEVRYPRFLSAEAIGIM 852
Cdd:cd05605 157 TIRGRVGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARKEkvkrEEVDRRVKEDQEEYSEKFSEEAKSIC 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 47132591 853 RRLLRRNPERRLGSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVP 899
Cdd:cd05605 237 SQLLQKDPKTRLGCRGEGAEDVKSHPFFKSINFKRLEAGLLEPPFVP 283
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
619-880 7.77e-62

Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. It is essential for normal embryo development and is important in regulating cell volume. The PDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 211.30  E-value: 7.77e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILaavTSAGHPFLVNLFGCFQTPEHVC 698
Cdd:cd05581   1 NDFKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKRHIIKEKKVKYVTIEKEVL---SRLAHPGIVKLYYTFQDESKLY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGGDLMLHIHSDV-FSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFG----LCKEGM- 772
Cdd:cd05581  78 FVLEYAPNGDLLEYIRKYGsLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGtakvLGPDSSp 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 773 ------------GYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRY 840
Cdd:cd05581 158 estkgdadsqiaYNQARAASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIVKLEYEF 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 47132591 841 PRFLSAEAIGIMRRLLRRNPERRLGSSE-RDAEDVKKQPFF 880
Cdd:cd05581 238 PENFPPDAKDLIQKLLVLDPSKRLGVNEnGGYDELKAHPFF 278
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
621-899 2.36e-60

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK4 has a limited tissue distribution. It is mainly found in the testis, but is also present in the cerebellum and kidney. It is expressed as multiple splice variants with different domain architectures and is post-translationally palmitoylated and localized in the membrane. GRK4 polymorphisms are associated with hypertension and salt sensitivity, as they cause hyperphosphorylation, desensitization, and internalization of the dopamine 1 (D1) receptor while increasing the expression of the angiotensin II type 1 receptor. GRK4 plays a crucial role in the D1 receptor regulation of sodium excretion and blood pressure. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 207.54  E-value: 2.36e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTSAghpFLVNLFGCFQTPEHVCFV 700
Cdd:cd05631   2 FRHYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKRILEKVNSR---FVVSLAYAYETKDALCLV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGGDLMLHIHS---DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEgMGYGDR 777
Cdd:cd05631  79 LTIMNGGDLKFHIYNmgnPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQ-IPEGET 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 778 TSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDE----EEVFDSIVNDEVRYPRFLSAEAIGIMR 853
Cdd:cd05631 158 VRGRVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKErvkrEEVDRRVKEDQEEYSEKFSEDAKSICR 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 47132591 854 RLLRRNPERRLGSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVP 899
Cdd:cd05631 238 MLLTKNPKERLGCRGNGAAGVKQHPIFKNINFKRLEANMLEPPFCP 283
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
621-880 2.55e-59

Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily contains uncharacterized STKs with similarity to the human protein designated as Yank1 or STK32A. The Yank1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 203.64  E-value: 2.55e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILaavTSAGHPFLVNLFGCFQTPEHVCFV 700
Cdd:cd05578   2 FQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNKQKCIEKDSVRNVLNELEIL---QELEHPFLVNLWYSFQDEEDMYMV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGGDLMLHIHSDV-FSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEgMGYGDRTS 779
Cdd:cd05578  79 VDLLLGGDLRYHLQQKVkFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATK-LTDGTLAT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 780 TFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDD---EEEVFDSIVNDEVRYPRFLSAEAIGIMRRLL 856
Cdd:cd05578 158 STSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEIHSrtsIEEIRAKFETASVLYPAGWSEEAIDLINKLL 237
                       250       260
                ....*....|....*....|....
gi 47132591 857 RRNPERRLGSSerdaEDVKKQPFF 880
Cdd:cd05578 238 ERDPQKRLGDL----SDLKNHPYF 257
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
619-944 7.69e-58

Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CRIK (also called citron kinase) is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger, and a pleckstrin homology (PH) domain, in addition to other motifs. The CRIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 201.77  E-value: 7.69e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTSaghPFLVNLFGCFQTPEHVC 698
Cdd:cd05601   1 KDFEVKNVIGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAQEEVSFFEEERDIMAKANS---PWITKLQYAFQDSENLY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGGDLM--LHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGD 776
Cdd:cd05601  78 LVMEYHPGGDLLslLSRYDDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSAAKLSSDKT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 777 RTSTF-CGTPEFLAPEVLT------DTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVN--DEVRYP--RFLS 845
Cdd:cd05601 158 VTSKMpVGTPDYIAPEVLTsmnggsKGTYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIMNfkKFLKFPedPKVS 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 846 AEAIGIMRRLLrRNPERRLGSserdaEDVKKQPFFRTLGWEALlaRRLPPPFVPTLSGRTDVSNFDeEFTGEAPTLSPPR 925
Cdd:cd05601 238 ESAVDLIKGLL-TDAKERLGY-----EGLCCHPFFSGIDWNNL--RQTVPPFVPTLTSDDDTSNFD-EFEPKKTRPSYEN 308
                       330       340
                ....*....|....*....|
gi 47132591 926 DARPL-TAAEQAAFLDFDFV 944
Cdd:cd05601 309 FNKSKgFSGKDLPFVGFTFT 328
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
620-879 3.44e-57

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 197.70  E-value: 3.44e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEvESLMCEKRILAAVtsaGHPFLVNLFGCFQTPEHVCF 699
Cdd:cd05117   1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDE-EMLRREIEILKRL---DHPNIVKLYEVFEDDKNLYL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYSAGGDLMLHIHS-DVFSEPRAIFYSACVVLGLQFLHEHKIVYR---------DLKLDnllldtEGYVKIADFGLCK 769
Cdd:cd05117  77 VMELCTGGELFDRIVKkGSFSEREAAKIMKQILSAVAYLHSQGIVHRdlkpenillASKDP------DSPIKIIDFGLAK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 770 EgMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYP----RFLS 845
Cdd:cd05117 151 I-FEEGEKLKTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDspewKNVS 229
                       250       260       270
                ....*....|....*....|....*....|....
gi 47132591 846 AEAIGIMRRLLRRNPERRLgsserDAEDVKKQPF 879
Cdd:cd05117 230 EEAKDLIKRLLVVDPKKRL-----TAAEALNHPW 258
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
620-881 5.52e-57

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 196.93  E-value: 5.52e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAavtSAGHPFLVNLFGCFQTPEHVCF 699
Cdd:cd14007   1 DFEIGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQLQKSGLEHQLRREIEIQS---HLRHPNILRLYGYFEDKKRIYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYSAGGDLMLHIHSD-VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGygDRT 778
Cdd:cd14007  78 ILEYAPNGELYKELKKQkRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSVHAPS--NRR 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 779 STFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRR 858
Cdd:cd14007 156 KTFCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIKFPSSVSPEAKDLISKLLQK 235
                       250       260
                ....*....|....*....|...
gi 47132591 859 NPERRLgsserDAEDVKKQPFFR 881
Cdd:cd14007 236 DPSKRL-----SLEQVLNHPWIK 253
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
629-886 3.58e-56

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include Saccharomyces cerevisiae Rim15, Schizosaccharomyces pombe cek1, and similar fungal proteins. They contain a central catalytic domain, which contains an insert relative to MAST kinases. In addition, Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. Rim15 (or Rim15p) functions as a regulator of meiosis. It acts as a downstream effector of PKA and regulates entry into stationary phase (G0). Thus, it plays a crucial role in regulating yeast proliferation, differentiation, and aging. Cek1 may facilitate progression of mitotic anaphase. The Rim15-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 195.01  E-value: 3.58e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 629 RGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILaaVTSAGHPFLVNLFGCFQTPEHVCFVMEYSAGGD 708
Cdd:cd05611   6 KGAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKNQVTNVKAERAIM--MIQGESPYVAKLYYSFQSKDYLYLVMEYLNGGD 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 709 LMLHIHS-DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKegMGYGDRTST-FCGTPE 786
Cdd:cd05611  84 CASLIKTlGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSR--NGLEKRHNKkFVGTPD 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 787 FLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPR----FLSAEAIGIMRRLLRRNPER 862
Cdd:cd05611 162 YLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRRINWPEevkeFCSPEAVDLINRLLCMDPAK 241
                       250       260
                ....*....|....*....|....
gi 47132591 863 RLGSSerDAEDVKKQPFFRTLGWE 886
Cdd:cd05611 242 RLGAN--GYQEIKSHPFFKSINWD 263
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
611-925 4.23e-56

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK is also referred to as Rho-associated kinase or simply as Rho kinase. It contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. The ROCK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 197.98  E-value: 4.23e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 611 LRKSPLTLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTSaghPFLVNLFGC 690
Cdd:cd05596  18 ITKLRMNAEDFDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKFEMIKRSDSAFFWEERDIMAHANS---EWIVQLHYA 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 691 FQTPEHVCFVMEYSAGGDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLC-- 768
Cdd:cd05596  95 FQDDKYLYMVMDYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFGTCmk 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 769 --KEGMgygDRTSTFCGTPEFLAPEVLT----DTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVN--DEVRY 840
Cdd:cd05596 175 mdKDGL---VRSDTAVGTPDYISPEVLKsqggDGVYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKIMNhkNSLQF 251
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 841 PR--FLSAEAIGIMRRLLrRNPERRLGssERDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFD--EEFTG 916
Cdd:cd05596 252 PDdvEISKDAKSLICAFL-TDREVRLG--RNGIEEIKAHPFFKNDQWTWDNIRETVPPVVPELSSDIDTSNFDdiEEDET 328

                ....*....
gi 47132591 917 EAPTLSPPR 925
Cdd:cd05596 329 PEETFPVPK 337
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
610-911 6.97e-56

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 196.74  E-value: 6.97e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  610 PLRKSPLTLEDFKFLAVLGRGHFGKVLLSEFRPSG-ELFAIKALKKGDIVARDEVESLMCEKRILAAVTsagHPFLVNLF 688
Cdd:PTZ00426  21 PKRKNKMKYEDFNFIRTLGTGSFGRVILATYKNEDfPPVAIKRFEKSKIIKQKQVDHVFSERKILNYIN---HPFCVNLY 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  689 GCFQTPEHVCFVMEYSAGGDLMLHIHSDV-FSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGL 767
Cdd:PTZ00426  98 GSFKDESYLYLVLEFVIGGEFFTFLRRNKrFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGF 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  768 CKEgmgYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAE 847
Cdd:PTZ00426 178 AKV---VDTRTYTLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYANEPLLIYQKILEGIIYFPKFLDNN 254
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47132591  848 AIGIMRRLLRRNPERRLGSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFD 911
Cdd:PTZ00426 255 CKHLMKKLLSHDLTKRYGNLKKGAQNVKEHPWFGNIDWVSLLHKNVEVPYKPKYKNVFDSSNFE 318
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
620-864 2.07e-55

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 192.35  E-value: 2.07e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVArDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCF 699
Cdd:cd14003   1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKE-EIEEKIKREIEIMKLLN---HPNIIKLYEVIETENKIYL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYSAGGDLMLHIHSDV-FSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEgMGYGDRT 778
Cdd:cd14003  77 VMEYASGGELFDYIVNNGrLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNE-FRGGSLL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 779 STFCGTPEFLAPEVLTDTSY-TRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLR 857
Cdd:cd14003 156 KTFCGTPAYAAPEVLLGRKYdGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPIPSHLSPDARDLIRRMLV 235

                ....*..
gi 47132591 858 RNPERRL 864
Cdd:cd14003 236 VDPSKRI 242
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
612-919 2.47e-55

Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group contains fungal kinases including Schizosaccharomyces pombe Sid2p and Saccharomyces cerevisiae Dbf2p. Group members show similarity to NDR kinases in that they contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Sid2p plays a crucial role in the septum initiation network (SIN) and in the initiation of cytokinesis. Dbf2p is important in regulating the mitotic exit network (MEN) and in cytokinesis. The Sid2p-like group is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 196.79  E-value: 2.47e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 612 RKSPLTLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTSaghPFLVNLFGCF 691
Cdd:cd05600   4 RRTRLKLSDFQILTQVGQGGYGSVFLARKKDTGEICALKIMKKKVLFKLNEVNHVLTERDILTTTNS---PWLVKLLYAF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 692 QTPEHVCFVMEYSAGGDL-MLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKE 770
Cdd:cd05600  81 QDPENVYLAMEYVPGGDFrTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLASG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 771 GMGYG-----------------------DRTSTF--------------CGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYE 813
Cdd:cd05600 161 TLSPKkiesmkirleevkntafleltakERRNIYramrkedqnyansvVGSPDYMAPEVLRGEGYDLTVDYWSLGCILFE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 814 MLVGESPFPGDDEEEVFDSIVN----------DEVRYPRFLSAEAIGIMRRLLrRNPERRLGSSerdaEDVKKQPFFRTL 883
Cdd:cd05600 241 CLVGFPPFSGSTPNETWANLYHwkktlqrpvyTDPDLEFNLSDEAWDLITKLI-TDPQDRLQSP----EQIKNHPFFKNI 315
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 47132591 884 GWEALLArRLPPPFVPTLSGRTDVSNFDeEFTGEAP 919
Cdd:cd05600 316 DWDRLRE-GSKPPFIPELESEIDTSYFD-DFNDEAD 349
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
621-899 6.75e-55

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK5 is widely expressed in many tissues. It associates with the membrane though an N-terminal PIP2 binding domain and also binds phospholipids via its C-terminus. GRK5 deficiency is associated with early Alzheimer's disease in humans and mouse models. GRK5 also plays a crucial role in the pathogenesis of sporadic Parkinson's disease. It participates in the regulation and desensitization of PDGFRbeta, a receptor tyrosine kinase involved in a variety of downstream cellular effects including cell growth, chemotaxis, apoptosis, and angiogenesis. GRK5 also regulates Toll-like receptor 4, which is involved in innate and adaptive immunity. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 193.26  E-value: 6.75e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTSAghpFLVNLFGCFQTPEHVCFV 700
Cdd:cd05632   4 FRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGESMALNEKQILEKVNSQ---FVVNLAYAYETKDALCLV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGGDLMLHIHS---DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEgMGYGDR 777
Cdd:cd05632  81 LTIMNGGDLKFHIYNmgnPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVK-IPEGES 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 778 TSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDE----EEVFDSIVNDEVRYPRFLSAEAIGIMR 853
Cdd:cd05632 160 IRGRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEkvkrEEVDRRVLETEEVYSAKFSEEAKSICK 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 47132591 854 RLLRRNPERRLGSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVP 899
Cdd:cd05632 240 MLLTKDPKQRLGCQEEGAGEVKRHPFFRNMNFKRLEAGMLDPPFVP 285
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
619-943 2.00e-54

Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The DMPK-like subfamily is composed of DMPK and DMPK-related cell division control protein 42 (Cdc42) binding kinase (MRCK). DMPK is expressed in skeletal and cardiac muscles, and in central nervous tissues. The functional role of DMPK is not fully understood. It may play a role in the signal transduction and homeostasis of calcium. The DMPK gene is implicated in myotonic dystrophy 1 (DM1), an inherited multisystemic disorder with symptoms that include muscle hyperexcitability, progressive muscle weakness and wasting, cataract development, testicular atrophy, and cardiac conduction defects. The genetic basis for DM1 is the mutational expansion of a CTG repeat in the 3'-UTR of DMPK. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. The DMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 192.56  E-value: 2.00e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILaavTSAGHPFLVNLFGCFQTPEHVC 698
Cdd:cd05597   1 DDFEILKVIGRGAFGEVAVVKLKSTEKVYAMKILNKWEMLKRAETACFREERDVL---VNGDRRWITKLHYAFQDENYLY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGGDL--MLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLC----KEGM 772
Cdd:cd05597  78 LVMDYYCGGDLltLLSKFEDRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFGSClklrEDGT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 773 GYgdrTSTFCGTPEFLAPEVLTDT-----SYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYpRF---- 843
Cdd:cd05597 158 VQ---SSVAVGTPDYISPEILQAMedgkgRYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKEHF-SFpdde 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 844 --LSAEAIGIMRRLLRRnPERRLGSSerDAEDVKKQPFFRTLGWEALlaRRLPPPFVPTLSGRTDVSNFDEEFTGEAPTL 921
Cdd:cd05597 234 ddVSEEAKDLIRRLICS-RERRLGQN--GIDDFKKHPFFEGIDWDNI--RDSTPPYIPEVTSPTDTSNFDVDDDDLRHTD 308
                       330       340
                ....*....|....*....|..
gi 47132591 922 SPPRDARPLTAAEQAAFLDFDF 943
Cdd:cd05597 309 SLPPPSNAAFSGLHLPFVGFTY 330
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
617-911 1.17e-53

Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like kinase (also called greatwall kinase); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MASTL kinases in this group carry only a catalytic domain, which contains a long insertion relative to MAST kinases. MASTL, also called greatwall kinase (Gwl), is involved in the regulation of mitotic entry, which is controlled by the coordinated activities of protein kinases and opposing protein phosphatases (PPs). The cyclin B/CDK1 complex induces entry into M-phase while PP2A-B55 shows anti-mitotic activity. MASTL/Gwl is activated downstream of cyclin B/CDK1 and indirectly inhibits PP2A-B55 by phosphorylating the small protein alpha-endosulfine (Ensa) or the cAMP-regulated phosphoprotein 19 (Arpp19), resulting in M-phase progression. Gwl kinase may also play roles in mRNA stabilization and DNA checkpoint recovery. The human MASTL gene has also been named FLJ14813; a missense mutation in FLJ14813 is associated with autosomal dominant thrombocytopenia. The MASTL kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 190.86  E-value: 1.17e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 617 TLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTSaghPFLVNLFGCFQTPEH 696
Cdd:cd05610   2 SIEEFVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKADMINKNMVHQVQAERDALALSKS---PFIVHLYYSLQSANN 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 697 VCFVMEYSAGGDL--MLHIHSdVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK----- 769
Cdd:cd05610  79 VYLVMEYLIGGDVksLLHIYG-YFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKvtlnr 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 770 -------------------------------EGMGYGDRT-----------------STFCGTPEFLAPEVLTDTSYTRA 801
Cdd:cd05610 158 elnmmdilttpsmakpkndysrtpgqvlsliSSLGFNTPTpyrtpksvrrgaarvegERILGTPDYLAPELLLGKPHGPA 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 802 VDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYP---RFLSAEAIGIMRRLLRRNPERRLGsserdAEDVKKQP 878
Cdd:cd05610 238 VDWWALGVCLFEFLTGIPPFNDETPQQVFQNILNRDIPWPegeEELSVNAQNAIEILLTMDPTKRAG-----LKELKQHP 312
                       330       340       350
                ....*....|....*....|....*....|...
gi 47132591 879 FFRTLGWEALlaRRLPPPFVPTLSGRTDVSNFD 911
Cdd:cd05610 313 LFHGVDWENL--QNQTMPFIPQPDDETDTSYFE 343
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
626-899 2.73e-53

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK7 (also called iodopsin kinase) belongs to the visual group of GRKs. It is primarily found in the retina and plays a role in the regulation of opsin light receptors. GRK7 is located in retinal cone outer segments and plays an important role in regulating photoresponse of the cones. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 187.80  E-value: 2.73e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTSaghPFLVNLFGCFQTPEHVCFVMEYSA 705
Cdd:cd05607   9 VLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSGEKMALLEKEILEKVNS---PFIVSLAYAFETKTHLCLVMSLMN 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 706 GGDLMLHIH---SDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEgMGYGDRTSTFC 782
Cdd:cd05607  86 GGDLKYHIYnvgERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVE-VKEGKPITQRA 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 783 GTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDE----EEVFDSIVNDEVRY--PRFlSAEAIGIMRRLL 856
Cdd:cd05607 165 GTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRDHKEkvskEELKRRTLEDEVKFehQNF-TEEAKDICRLFL 243
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 47132591 857 RRNPERRLGSSERDaEDVKKQPFFRTLGWEALLARRLPPPFVP 899
Cdd:cd05607 244 AKKPENRLGSRTND-DDPRKHEFFKSINFPRLEAGLIDPPFVP 285
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
621-899 7.11e-53

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK6 is widely expressed in many tissues and is expressed as multiple splice variants with different domain architectures. It is post-translationally palmitoylated and localized in the membrane. GRK6 plays important roles in the regulation of dopamine, M3 muscarinic, opioid, and chemokine receptor signaling. It also plays maladaptive roles in addiction and Parkinson's disease. GRK6-deficient mice exhibit altered dopamine receptor regulation, decreased lymphocyte chemotaxis, and increased acute inflammation and neutrophil chemotaxis. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 186.38  E-value: 7.11e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTSAghpFLVNLFGCFQTPEHVCFV 700
Cdd:cd05630   2 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSR---FVVSLAYAYETKDALCLV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGGDLMLHIH---SDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLC---KEGMGY 774
Cdd:cd05630  79 LTLMNGGDLKFHIYhmgQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAvhvPEGQTI 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 775 GDRTstfcGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDE----EEVFDSIVNDEVRYPRFLSAEAIG 850
Cdd:cd05630 159 KGRV----GTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKkikrEEVERLVKEVPEEYSEKFSPQARS 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 47132591 851 IMRRLLRRNPERRLGSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVP 899
Cdd:cd05630 235 LCSMLLCKDPAERLGCRGGGAREVKEHPLFKKLNFKRLGAGMLEPPFKP 283
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
611-943 1.22e-51

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2 was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 185.97  E-value: 1.22e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 611 LRKSPLTLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTSaghPFLVNLFGC 690
Cdd:cd05621  44 IRELQMKAEDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANS---PWVVQLFCA 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 691 FQTPEHVCFVMEYSAGGDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKE 770
Cdd:cd05621 121 FQDDKYLYMVMEYMPGGDLVNLMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGTCMK 200
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 771 GMGYGD-RTSTFCGTPEFLAPEVLT----DTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVN--DEVRYPR- 842
Cdd:cd05621 201 MDETGMvHCDTAVGTPDYISPEVLKsqggDGYYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMDhkNSLNFPDd 280
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 843 -FLSAEAIGIMRRLLrRNPERRLGSSerDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFD--EEFTGEAP 919
Cdd:cd05621 281 vEISKHAKNLICAFL-TDREVRLGRN--GVEEIKQHPFFRNDQWNWDNIRETAAPVVPELSSDIDTSNFDdiEDDKGDVE 357
                       330       340
                ....*....|....*....|....
gi 47132591 920 TLSPPRdarpLTAAEQAAFLDFDF 943
Cdd:cd05621 358 TFPIPK----AFVGNQLPFVGFTY 377
Pkinase pfam00069
Protein kinase domain;
621-880 2.14e-51

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 179.75  E-value: 2.14e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591   621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEvESLMCEKRILAAVtsaGHPFLVNLFGCFQTPEHVCFV 700
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKD-KNILREIKILKKL---NHPNIVRLYDAFEDKDNLYLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591   701 MEYSAGGDLMLHI-HSDVFSEPRAIFYSACVVlglqflhehkivyrdlkldnllldtegyvkiadfglckEGMGYGDRTS 779
Cdd:pfam00069  77 LEYVEGGSLFDLLsEKGAFSEREAKFIMKQIL--------------------------------------EGLESGSSLT 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591   780 TFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRF---LSAEAIGIMRRLL 856
Cdd:pfam00069 119 TFVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELpsnLSEEAKDLLKKLL 198
                         250       260
                  ....*....|....*....|....
gi 47132591   857 RRNPERRLGsserdAEDVKKQPFF 880
Cdd:pfam00069 199 KKDPSKRLT-----ATQALQHPWF 217
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
626-899 9.08e-51

Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The beta-ARK group is composed of GRK2, GRK3, and similar proteins. GRK2 and GRK3 are both widely expressed in many tissues, although GRK2 is present at higher levels. They contain an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRK2 (also called beta-ARK or beta-ARK1) is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The beta-ARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 180.33  E-value: 9.08e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARdEVESLMCEKRILAAVTSAGH--PFLVNLFGCFQTPEHVCFVMEY 703
Cdd:cd05606   1 IIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMK-QGETLALNERIMLSLVSTGGdcPFIVCMTYAFQTPDKLCFILDL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 704 SAGGDLMLHI-HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEgmgYGDRTSTFC 782
Cdd:cd05606  80 MNGGDLHYHLsQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLACD---FSKKKPHAS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 783 -GTPEFLAPEVLTD-TSYTRAVDWWGLGVLLYEMLVGESPF---PGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLR 857
Cdd:cd05606 157 vGTHGYMAPEVLQKgVAYDSSADWFSLGCMLYKLLKGHSPFrqhKTKDKHEIDRMTLTMNVELPDSFSPELKSLLEGLLQ 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 47132591 858 RNPERRLGSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVP 899
Cdd:cd05606 237 RDVSKRLGCLGRGATEVKEHPFFKGVDWQQVYLQKYPPPLIP 278
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
609-925 6.53e-50

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1 is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 181.74  E-value: 6.53e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 609 SPLRKSPLTLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTSaghPFLVNLF 688
Cdd:cd05622  63 NKIRDLRMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANS---PWVVQLF 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 689 GCFQTPEHVCFVMEYSAGGDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLC 768
Cdd:cd05622 140 YAFQDDRYLYMVMEYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTC 219
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 769 ----KEGMgygDRTSTFCGTPEFLAPEVLT----DTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVN--DEV 838
Cdd:cd05622 220 mkmnKEGM---VRCDTAVGTPDYISPEVLKsqggDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNhkNSL 296
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 839 RYPR--FLSAEAIGIMRRLLrRNPERRLGSSerDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFD--EEF 914
Cdd:cd05622 297 TFPDdnDISKEAKNLICAFL-TDREVRLGRN--GVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFDdlEED 373
                       330
                ....*....|.
gi 47132591 915 TGEAPTLSPPR 925
Cdd:cd05622 374 KGEEETFPIPK 384
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
611-948 1.58e-49

Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-beta is expressed ubiquitously in many tissues. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 180.98  E-value: 1.58e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 611 LRKSPLTLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILaavTSAGHPFLVNLFGC 690
Cdd:cd05624  64 VKEMQLHRDDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETACFREERNVL---VNGDCQWITTLHYA 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 691 FQTPEHVCFVMEYSAGGDLM--LHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLC 768
Cdd:cd05624 141 FQDENYLYLVMDYYVGGDLLtlLSKFEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGSC 220
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 769 KEGMGYGD-RTSTFCGTPEFLAPEVLTDTS-----YTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVR--Y 840
Cdd:cd05624 221 LKMNDDGTvQSSVAVGTPDYISPEILQAMEdgmgkYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHEERfqF 300
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 841 PRFL---SAEAIGIMRRLLRRNpERRLGssERDAEDVKKQPFFRTLGWEALlaRRLPPPFVPTLSGRTDVSNFD-EEFTG 916
Cdd:cd05624 301 PSHVtdvSEEAKDLIQRLICSR-ERRLG--QNGIEDFKKHAFFEGLNWENI--RNLEAPYIPDVSSPSDTSNFDvDDDVL 375
                       330       340       350
                ....*....|....*....|....*....|..
gi 47132591 917 EAPTLSPPRDARPLTaAEQAAFLDFDFVAGGC 948
Cdd:cd05624 376 RNPEILPPSSHTGFS-GLHLPFVGFTYTTESC 406
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
619-943 1.77e-47

Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group is composed of fungal NDR-like proteins including Saccharomyces cerevisiae CBK1 (or CBK1p), Schizosaccharomyces pombe Orb6 (or Orb6p), Ustilago maydis Ukc1 (or Ukc1p), and Neurospora crassa Cot1. Like NDR kinase, group members contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. CBK1 is an essential component in the RAM (regulation of Ace2p activity and cellular morphogenesis) network. CBK1 and Orb6 play similar roles in coordinating cell morphology with cell cycle progression. Ukc1 is involved in morphogenesis, pathogenicity, and pigment formation. Cot1 plays a role in polar tip extension.The fungal NDR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 173.88  E-value: 1.77e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTSaghPFLVNLFGCFQTPEHVC 698
Cdd:cd05629   1 EDFHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMFKKDQLAHVKAERDVLAESDS---PWVVSLYYSFQDAQYLY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGGDLM-LHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK-------- 769
Cdd:cd05629  78 LIMEFLPGGDLMtMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGLSTgfhkqhds 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 770 -------EG---------------------MGYGDRTSTF-----------CGTPEFLAPEVLTDTSYTRAVDWWGLGVL 810
Cdd:cd05629 158 ayyqkllQGksnknridnrnsvavdsinltMSSKDQIATWkknrrlmaystVGTPDYIAPEIFLQQGYGQECDWWSLGAI 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 811 LYEMLVGESPFPGDDEEEVFDSIVN--DEVRYPR--FLSAEAIGIMRRLLrRNPERRLGSSerDAEDVKKQPFFRTLGWE 886
Cdd:cd05629 238 MFECLIGWPPFCSENSHETYRKIINwrETLYFPDdiHLSVEAEDLIRRLI-TNAENRLGRG--GAHEIKSHPFFRGVDWD 314
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47132591 887 ALlaRRLPPPFVPTLSGRTDVSNF---DEEFTGEAPTLSPPRDARPLTAAEQA-AFLDFDF 943
Cdd:cd05629 315 TI--RQIRAPFIPQLKSITDTSYFptdELEQVPEAPALKQAAPAQQEESVELDlAFIGYTY 373
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
626-880 2.88e-47

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 169.62  E-value: 2.88e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGELFAIKALKKGDiVARDEVESLMCEKRILaavTSAGHPFLVNLFGCFQTPEHVCFVMEYSA 705
Cdd:cd06606   7 LLGKGSFGSVYLALNLDTGELMAVKEVELSG-DSEEELEALEREIRIL---SSLKHPNIVRYLGTERTENTLNIFLEYVP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 706 GGDLMLHIHS-DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK--EGMGYGDRTSTFC 782
Cdd:cd06606  83 GGSLASLLKKfGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKrlAEIATGEGTKSLR 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 783 GTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFP--GDDEEEVFDSIVNDEVRY-PRFLSAEAIGIMRRLLRRN 859
Cdd:cd06606 163 GTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWSelGNPVAALFKIGSSGEPPPiPEHLSEEAKDFLRKCLQRD 242
                       250       260
                ....*....|....*....|.
gi 47132591 860 PERRLgsserDAEDVKKQPFF 880
Cdd:cd06606 243 PKKRP-----TADELLQHPFL 258
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
620-915 3.74e-47

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK2, also called beta-adrenergic receptor kinase (beta-ARK) or beta-ARK1, is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRK2 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. TheGRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 171.38  E-value: 3.74e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARdEVESLMCEKRILAAVTSAGH-PFLVNLFGCFQTPEHVC 698
Cdd:cd14223   1 DFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMK-QGETLALNERIMLSLVSTGDcPFIVCMSYAFHTPDKLS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGGDLMLHI-HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDR 777
Cdd:cd14223  80 FILDLMNGGDLHYHLsQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLACDFSKKKPH 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 778 TSTfcGTPEFLAPEVLTD-TSYTRAVDWWGLGVLLYEMLVGESPF---PGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMR 853
Cdd:cd14223 160 ASV--GTHGYMAPEVLQKgVAYDSSADWFSLGCMLFKLLRGHSPFrqhKTKDKHEIDRMTLTMAVELPDSFSPELRSLLE 237
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47132591 854 RLLRRNPERRLGSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVP-----TLSGRTDVSNFDEEFT 915
Cdd:cd14223 238 GLLQRDVNRRLGCMGRGAQEVKEEPFFRGLDWQMVFLQKYPPPLIPprgevNAADAFDIGSFDEEDT 304
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
609-924 3.98e-46

Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-alpha is expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 170.97  E-value: 3.98e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 609 SPLRKSPLTLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILaavTSAGHPFLVNLF 688
Cdd:cd05623  62 SKVKQMRLHKEDFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETACFREERDVL---VNGDSQWITTLH 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 689 GCFQTPEHVCFVMEYSAGGDLM--LHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFG 766
Cdd:cd05623 139 YAFQDDNNLYLVMDYYVGGDLLtlLSKFEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFG 218
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 767 LCKEGMGYGD-RTSTFCGTPEFLAPEVLTDTS-----YTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRY 840
Cdd:cd05623 219 SCLKLMEDGTvQSSVAVGTPDYISPEILQAMEdgkgkYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKERF 298
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 841 pRF------LSAEAIGIMRRLLRRNpERRLGssERDAEDVKKQPFFRTLGWEALlaRRLPPPFVPTLSGRTDVSNF--DE 912
Cdd:cd05623 299 -QFptqvtdVSENAKDLIRRLICSR-EHRLG--QNGIEDFKNHPFFVGIDWDNI--RNCEAPYIPEVSSPTDTSNFdvDD 372
                       330
                ....*....|..
gi 47132591 913 EFTGEAPTLSPP 924
Cdd:cd05623 373 DCLKNCETMPPP 384
HR1_PKN1_2 cd11630
Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
127-202 5.16e-46

Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N1; PKN1, also called PKNalpha or Protein-kinase C-related kinase 1 (PRK1), is a serine/threonine protein kinase that is activated by the Rho family of small GTPases, and by fatty acids such as arachidonic and linoleic acids. It is expressed ubiquitously and is the most abundant PKN isoform in neurons. PKN1 is implicated in a variety of functions including cytoskeletal reorganization, cardiac cell survival, cell adhesion, and glucose transport, among others. PKN1 contains three HR1 domains, a C2 domain, and a kinase domain. This model characterizes the second HR1 domain of PKN1. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; PKN1 binds the GTPases RhoA, RhoB, and RhoC, and can also interact weakly with Rac.


Pssm-ID: 212020  Cd Length: 78  Bit Score: 159.03  E-value: 5.16e-46
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47132591 127 SATNLSRVAGLEKQLAIELKVKQGAENMIQTYSNGSTKDRKLLLTAQQMLQDSKTKIDIIRMQLRRALQAGQLENQ 202
Cdd:cd11630   3 SAANQSRIAGLEKQLNIELKVKQGAENMIQTYANGSTKDRKLLQTAQQMLQDSKTKIDIIRMQIRKAMQADELENQ 78
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
616-915 1.97e-45

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK3, also called beta-adrenergic receptor kinase 2 (beta-ARK2), is widely expressed in many tissues. It is involved in modulating the cholinergic response of airway smooth muscles, and also plays a role in dopamine receptor regulation. GRK3-deficient mice show a lack of olfactory receptor desensitization and altered regulation of the M2 muscarinic airway. GRK3 promoter polymorphisms may also be associated with bipolar disorder. GRK3 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 167.16  E-value: 1.97e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 616 LTLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARdEVESLMCEKRILAAVTSAGH-PFLVNLFGCFQTP 694
Cdd:cd05633   2 LTMNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMK-QGETLALNERIMLSLVSTGDcPFIVCMTYAFHTP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 695 EHVCFVMEYSAGGDLMLHI-HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMG 773
Cdd:cd05633  81 DKLCFILDLMNGGDLHYHLsQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDFSK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 774 YGDRTSTfcGTPEFLAPEVLTD-TSYTRAVDWWGLGVLLYEMLVGESPF---PGDDEEEVFDSIVNDEVRYPRFLSAEAI 849
Cdd:cd05633 161 KKPHASV--GTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFrqhKTKDKHEIDRMTLTVNVELPDSFSPELK 238
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47132591 850 GIMRRLLRRNPERRLGSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVP-----TLSGRTDVSNFDEEFT 915
Cdd:cd05633 239 SLLEGLLQRDVSKRLGCHGRGAQEVKEHSFFKGIDWQQVYLQKYPPPLIPprgevNAADAFDIGSFDEEDT 309
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
621-943 2.84e-45

Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS2 is an essential mitotic regulator responsible for coordinating accurate cytokinesis completion and governing the stabilization of other mitotic regulators. It is also critical in the maintenance of proper chromosome number, genomic stability, mitotic fidelity, and the integrity of centrosome duplication. Downregulation of LATS2 is associated with poor prognosis in acute lymphoblastic leukemia and breast cancer. The LATS2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 167.88  E-value: 2.84e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAavtSAGHPFLVNLFGCFQTPEHVCFV 700
Cdd:cd05626   3 FVKIKTLGIGAFGEVCLACKVDTHALYAMKTLRKKDVLNRNQVAHVKAERDILA---EADNEWVVKLYYSFQDKDNLYFV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGGDLM-LHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLC----------- 768
Cdd:cd05626  80 MDYIPGGDMMsLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLCtgfrwthnsky 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 769 --------KEGMG------------YGDRTST----------------FCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLY 812
Cdd:cd05626 160 yqkgshirQDSMEpsdlwddvsncrCGDRLKTleqratkqhqrclahsLVGTPNYIAPEVLLRKGYTQLCDWWSVGVILF 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 813 EMLVGESPFPGDDEEEVFDSIVNDE--VRYPR--FLSAEAIGIMRRLLrRNPERRLGSSerDAEDVKKQPFFRTLGWEAL 888
Cdd:cd05626 240 EMLVGQPPFLAPTPTETQLKVINWEntLHIPPqvKLSPEAVDLITKLC-CSAEERLGRN--GADDIKAHPFFSEVDFSSD 316
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47132591 889 LaRRLPPPFVPTLSGRTDVSNFD---EEFTGEAPTLSPPRDARPLTAAE----QAAFLDFDF 943
Cdd:cd05626 317 I-RTQPAPYVPKISHPMDTSNFDpveEESPWNDASGDSTRTWDTLCSPNgkhpEHAFYEFTF 377
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
620-880 5.25e-44

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 160.32  E-value: 5.25e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKFLAVLGRGHFGKVLLSEFRPSGELFAIK--ALKKGDivaRDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHV 697
Cdd:cd08215   1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKeiDLSNMS---EKEREEALNEVKLLSKLK---HPNIVKYYESFEENGKL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 698 CFVMEYSAGGDLMLHIH-----SDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGM 772
Cdd:cd08215  75 CIVMEYADGGDLAQKIKkqkkkGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKVLE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 773 GYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVR-YPRFLSAEAIGI 851
Cdd:cd08215 155 STTDLAKTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYPpIPSQYSSELRDL 234
                       250       260
                ....*....|....*....|....*....
gi 47132591 852 MRRLLRRNPERRLgsserDAEDVKKQPFF 880
Cdd:cd08215 235 VNSMLQKDPEKRP-----SANEILSSPFI 258
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
618-943 5.31e-44

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR2 (also called STK38-like) plays a role in proper centrosome duplication. In addition, it is involved in regulating neuronal growth and differentiation, as well as in facilitating neurite outgrowth. NDR2 is also implicated in fear conditioning as it contributes to the coupling of neuronal morphological changes with fear-memory consolidation. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 163.69  E-value: 5.31e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 618 LEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTSAghpFLVNLFGCFQTPEHV 697
Cdd:cd05627   1 LDDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVAHIRAERDILVEADGA---WVVKMFYSFQDKRNL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 698 CFVMEYSAGGDLM-LHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKeGMGYGD 776
Cdd:cd05627  78 YLIMEFLPGGDMMtLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCT-GLKKAH 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 777 RTSTF------------------------------------CGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESP 820
Cdd:cd05627 157 RTEFYrnlthnppsdfsfqnmnskrkaetwkknrrqlaystVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPP 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 821 FPGDDEEEVFDSIVN--DEVRYPRF--LSAEAIGIMRRLLrRNPERRLGSSerDAEDVKKQPFFRTLGWEALlaRRLPPP 896
Cdd:cd05627 237 FCSETPQETYRKVMNwkETLVFPPEvpISEKAKDLILRFC-TDAENRIGSN--GVEEIKSHPFFEGVDWEHI--RERPAA 311
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 47132591 897 FVPTLSGRTDVSNFDEefTGEAPTLSP-PRDARPLTAAEQAAFLDFDF 943
Cdd:cd05627 312 IPIEIKSIDDTSNFDD--FPESDILQPaPNTTEPDYKSKDWVFLNYTY 357
HR1_PKN1_3 cd11636
Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
211-284 6.13e-44

Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N1; PKN1, also called PKNalpha or Protein-kinase C-related kinase 1 (PRK1), is a serine/threonine protein kinase that is activated by the Rho family of small GTPases, and by fatty acids such as arachidonic and linoleic acids. It is expressed ubiquitously and is the most abundant PKN isoform in neurons. PKN1 is implicated in a variety of functions including cytoskeletal reorganization, cardiac cell survival, cell adhesion, and glucose transport, among others. PKN1 contains three HR1 domains, a C2 domain, and a kinase domain. This model characterizes the third HR1 domain of PKN1. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; PKN1 binds the GTPases RhoA, RhoB, and RhoC, and can also interact weakly with Rac.


Pssm-ID: 212026  Cd Length: 74  Bit Score: 153.21  E-value: 6.13e-44
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47132591 211 SPDLGAVELRIEELRHHFRVEHAVAEGAKNVLRLLSAAKAPDRKAVSEAQEKLTESNQKLGLLREALERRLGEL 284
Cdd:cd11636   1 KPDLCAVELRIEELRHHFRVEHAVAEGAKNVLRLLGAGKAQDRKAISEAQSKLSESSQKLDLLRVSLEQRLVEL 74
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
621-911 9.44e-43

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS1 functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. The LATS1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 160.60  E-value: 9.44e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAavtSAGHPFLVNLFGCFQTPEHVCFV 700
Cdd:cd05625   3 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILA---EADNEWVVRLYYSFQDKDNLYFV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGGDLM-LHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLC----------- 768
Cdd:cd05625  80 MDYIPGGDMMsLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdsky 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 769 --------KEGMGY----GDRTSTFC------------------------GTPEFLAPEVLTDTSYTRAVDWWGLGVLLY 812
Cdd:cd05625 160 yqsgdhlrQDSMDFsnewGDPENCRCgdrlkplerraarqhqrclahslvGTPNYIAPEVLLRTGYTQLCDWWSVGVILF 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 813 EMLVGESPF----PGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLrRNPERRLGSSerDAEDVKKQPFFRTLGWEAL 888
Cdd:cd05625 240 EMLVGQPPFlaqtPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLC-RGPEDRLGKN--GADEIKAHPFFKTIDFSSD 316
                       330       340
                ....*....|....*....|...
gi 47132591 889 LaRRLPPPFVPTLSGRTDVSNFD 911
Cdd:cd05625 317 L-RQQSAPYIPKITHPTDTSNFD 338
C2_PKN-like cd08687
C2 domain in Protein kinase C-like (PKN) proteins; PKN is a lipid-activated serine/threonine ...
395-482 3.85e-42

C2 domain in Protein kinase C-like (PKN) proteins; PKN is a lipid-activated serine/threonine kinase. It is a member of the protein kinase C (PKC) superfamily, but lacks a C1 domain. There are at least 3 different isoforms of PKN (PRK1/PKNalpha/PAK1; PKNbeta, and PRK2/PAK2/PKNgamma). The C-terminal region contains the Ser/Thr type protein kinase domain, while the N-terminal region of PKN contains three antiparallel coiled-coil (ACC) finger domains which are relatively rich in charged residues and contain a leucine zipper-like sequence. These domains binds to the small GTPase RhoA. Following these domains is a C2-like domain. Its C-terminal part functions as an auto-inhibitory region. PKNs are not activated by classical PKC activators such as diacylglycerol, phorbol ester or Ca2+, but instead are activated by phospholipids and unsaturated fatty acids. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176069  Cd Length: 98  Bit Score: 149.08  E-value: 3.85e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 395 SEVSTVLKLDNTVVGQTSWKPCGPNAWDQSFTLELERARELELAVFWRDQRGLCALKFLKLEDFldneRHEVQLDMEPQG 474
Cdd:cd08687   9 SEVSAVLKLDNTVVGQTQWKPKSNQAWDQSFTLELERSRELEIAVYWRDWRSLCAVKFLKLEDE----RHEVQLDMEPQL 84

                ....*...
gi 47132591 475 CLVAEVTF 482
Cdd:cd08687  85 CLVAELTF 92
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
627-878 5.95e-42

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 152.81  E-value: 5.95e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKGDIvaRDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd00180   1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKL--KKLLEELLREIEILKKLN---HPNIVKLYDVFETENFLYLVMEYCEG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDL--MLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYR---------DLkldnllldtEGYVKIADFGLCK--EGMG 773
Cdd:cd00180  76 GSLkdLLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRdlkpenillDS---------DGTVKLADFGLAKdlDSDD 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 774 YGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMlvgespfpgddeeevfdsivndevryprflsAEAIGIMR 853
Cdd:cd00180 147 SLLKTTGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL-------------------------------EELKDLIR 195
                       250       260
                ....*....|....*....|....*
gi 47132591 854 RLLRRNPERRLgsserDAEDVKKQP 878
Cdd:cd00180 196 RMLQYDPKKRP-----SAKELLEHL 215
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
627-880 1.24e-41

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 153.48  E-value: 1.24e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKK-------GDIVARDEVESLMCE-KRILAAVTSAGHPFLVNLFGCFQTPE--H 696
Cdd:cd14008   1 LGRGSFGKVKLALDTETGQLYAIKIFNKsrlrkrrEGKNDRGKIKNALDDvRREIAIMKKLDHPNIVRLYEVIDDPEsdK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 697 VCFVMEYSAGGDLM---LHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGlCKEGMG 773
Cdd:cd14008  81 LYLVLEYCEGGPVMeldSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFG-VSEMFE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 774 YGDRTSTFC-GTPEFLAPEVLTDTSYT---RAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIV--NDEVRYPRFLSAE 847
Cdd:cd14008 160 DGNDTLQKTaGTPAFLAPELCDGDSKTysgKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQnqNDEFPIPPELSPE 239
                       250       260       270
                ....*....|....*....|....*....|...
gi 47132591 848 AIGIMRRLLRRNPERRLgsserDAEDVKKQPFF 880
Cdd:cd14008 240 LKDLLRRMLEKDPEKRI-----TLKEIKEHPWV 267
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
619-912 3.45e-40

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR1 (also called STK38) plays a role in proper centrosome duplication. It is highly expressed in thymus, muscle, lung and spleen. It is not an essential protein because mice deficient of NDR1 remain viable and fertile. However, these mice develop T-cell lymphomas and appear to be hypersenstive to carcinogenic treatment. NDR1 appears to also act as a tumor suppressor. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 152.89  E-value: 3.45e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTSAghpFLVNLFGCFQTPEHVC 698
Cdd:cd05628   1 EDFESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQVGHIRAERDILVEADSL---WVVKMFYSFQDKLNLY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGGDLM-LHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKeGMGYGDR 777
Cdd:cd05628  78 LIMEFLPGGDMMtLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCT-GLKKAHR 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 778 TSTF------------------------------------CGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPF 821
Cdd:cd05628 157 TEFYrnlnhslpsdftfqnmnskrkaetwkrnrrqlafstVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPF 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 822 PGDDEEEVFDSIVN--DEVRYPRF--LSAEAIGIMRRLLRRNpERRLGSSerDAEDVKKQPFFRTLGWEALlaRRLPPPF 897
Cdd:cd05628 237 CSETPQETYKKVMNwkETLIFPPEvpISEKAKDLILRFCCEW-EHRIGAP--GVEEIKTNPFFEGVDWEHI--RERPAAI 311
                       330
                ....*....|....*
gi 47132591 898 VPTLSGRTDVSNFDE 912
Cdd:cd05628 312 PIEIKSIDDTSNFDE 326
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
620-880 5.75e-40

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 148.51  E-value: 5.75e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKkgdIVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCF 699
Cdd:cd05122   1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKIN---LESKEKKESILNEIAILKKCK---HPNIVKYYGSYLKKDELWI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYSAGGDL--MLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDR 777
Cdd:cd05122  75 VMEFCSGGSLkdLLKNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSDGKTR 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 778 tSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVND---EVRYPRFLSAEAIGIMRR 854
Cdd:cd05122 155 -NTFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIATNgppGLRNPKKWSKEFKDFLKK 233
                       250       260
                ....*....|....*....|....*.
gi 47132591 855 LLRRNPERRLgsserDAEDVKKQPFF 880
Cdd:cd05122 234 CLQKDPEKRP-----TAEQLLKHPFI 254
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
627-880 1.50e-39

Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest.


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 147.32  E-value: 1.50e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAavtSAGHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd14099   9 LGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLTKPKQREKLKSEIKIHR---SLKHPNIVKFHDCFEDEENVYILLELCSN 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLM-LHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCGTP 785
Cdd:cd14099  86 GSLMeLLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARLEYDGERKKTLCGTP 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 786 EFLAPEVLTDTS-YTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFL--SAEAIGIMRRLLRRNPER 862
Cdd:cd14099 166 NYIAPEVLEKKKgHSFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEYSFPSHLsiSDEAKDLIRSMLQPDPTK 245
                       250
                ....*....|....*...
gi 47132591 863 RLgsserDAEDVKKQPFF 880
Cdd:cd14099 246 RP-----SLDEILSHPFF 258
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
621-863 2.52e-39

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK1, also called ARK5 (AMPK-related protein kinase 5), regulates cell proliferation and displays tumor suppression through direct interaction and phosphorylation of p53. It is also involved in cell senescence and motility. High NUAK1 expression is associated with invasiveness of nonsmall cell lung cancer (NSCLC) and breast cancer cells. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. The NUAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270975 [Multi-domain]  Cd Length: 254  Bit Score: 146.76  E-value: 2.52e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFV 700
Cdd:cd14073   3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIEDEQDMVRIRREIEIMSSLN---HPHIIRIYEVFENKDKIVIV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGGDLMLHI---HSDVFSEPRAIFYSacVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEgmgYGDR 777
Cdd:cd14073  80 MEYASGGELYDYIserRRLPEREARRIFRQ--IVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSNL---YSKD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 778 T--STFCGTPEFLAPEVLTDTSYT-RAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSaEAIGIMRR 854
Cdd:cd14073 155 KllQTFCGSPLYASPEIVNGTPYQgPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSGDYREPTQPS-DASGLIRW 233

                ....*....
gi 47132591 855 LLRRNPERR 863
Cdd:cd14073 234 MLTVNPKRR 242
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
614-937 5.47e-38

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 149.01  E-value: 5.47e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 614 SPLTLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQT 693
Cdd:COG0515   2 SALLLGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERFRREARALARLN---HPNIVRVYDVGEE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 694 PEHVCFVMEYSAGGDLMLHIHSD-VFSEPRAIFYSACVVLGLQFLHEHKIVYR---------DLkldnllldtEGYVKIA 763
Cdd:COG0515  79 DGRPYLVMEYVEGESLADLLRRRgPLPPAEALRILAQLAEALAAAHAAGIVHRdikpanillTP---------DGRVKLI 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 764 DFGLCKE-GMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPR 842
Cdd:COG0515 150 DFGIARAlGGATLTQTGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPS 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 843 ----FLSAEAIGIMRRLLRRNPERRLGSSE---RDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFDEEFT 915
Cdd:COG0515 230 elrpDLPPALDAIVLRALAKDPEERYQSAAelaAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 309
                       330       340
                ....*....|....*....|..
gi 47132591 916 GEAPTLSPPRDARPLTAAEQAA 937
Cdd:COG0515 310 AAAAAAAAAAAAAPAAAAAAAA 331
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
627-865 7.27e-38

Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes yeast ATG1 and metazoan homologs including vertebrate ULK1-3. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. It is involved in nutrient sensing and signaling, the assembly of autophagy factors and the execution of autophagy. In metazoans, ATG1 homologs display additional functions. Unc-51 and ULKs have been implicated in neuronal and axonal development. The ATG1/ULK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 142.36  E-value: 7.27e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARdEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd14009   1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKK-LQENLESEIAILKSIK---HPNIVRLYDVQKTEDFIYLVLEYCAG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLMLHIHS-DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLD---NLLLDTEGYVKIADFGLCK----EGMgygdrT 778
Cdd:cd14009  77 GDLSQYIRKrGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQnllLSTSGDDPVLKIADFGFARslqpASM-----A 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 779 STFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSI----VNDEVRYPRFLSAEAIGIMRR 854
Cdd:cd14009 152 ETLCGSPLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIersdAVIPFPIAAQLSPDCKDLLRR 231
                       250
                ....*....|.
gi 47132591 855 LLRRNPERRLG 865
Cdd:cd14009 232 LLRRDPAERIS 242
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
620-868 2.63e-37

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK3 is represented in this cd. The SnRK3 group contains members also known as CBL-interacting protein kinase, salt overly sensitive 2, SOS3-interacting proteins and protein kinase S. These kinases interact with calcium-binding proteins such as SOS3, SCaBPs, and CBL proteins, and are involved in responses to salt stress and in sugar and ABA signaling. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 141.00  E-value: 2.63e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLmceKRILAAVTSAGHPFLVNLFGCFQTPEHVCF 699
Cdd:cd14663   1 RYELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKEQVAREGMVEQI---KREIAIMKLLRHPNIVELHEVMATKTKIFF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYSAGGDLMLHIHSDV-FSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLC--KEGMGYGD 776
Cdd:cd14663  78 VMELVTGGELFSKIAKNGrLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSalSEQFRQDG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 777 RTSTFCGTPEFLAPEVLTDTSYTRA-VDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRL 855
Cdd:cd14663 158 LLHTTCGTPNYVAPEVLARRGYDGAkADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKGEFEYPRWFSPGAKSLIKRI 237
                       250
                ....*....|...
gi 47132591 856 LRRNPERRLGSSE 868
Cdd:cd14663 238 LDPNPSTRITVEQ 250
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
621-863 1.07e-36

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. NUAK2 is implicated in regulating actin stress fiber assembly through its association with myosin phosphatase Rho-interacting protein (MRIP), which leads to an increase in myosin regulatory light chain (MLC) phosphorylation. It is also associated with tumor growth, migration, and oncogenicity of melanoma cells. The NUAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 138.93  E-value: 1.07e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRpSGELFAIKALKKGDIvaRDEvESLMCEKRILAAVTSAGHPFLVNLFGCFQTPEHVCFV 700
Cdd:cd14161   5 YEFLETLGKGTYGRVKKARDS-SGRLVAIKSIRKDRI--KDE-QDLLHIRREIEIMSSLNHPHIISVYEVFENSSKIVIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGGDLMLHI-HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLckEGMGYGDR-T 778
Cdd:cd14161  81 MEYASRGDLYDYIsERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGL--SNLYNQDKfL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 779 STFCGTPEFLAPEVLTDTSYT-RAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSaEAIGIMRRLLR 857
Cdd:cd14161 159 QTYCGSPLYASPEIVNGRPYIgPEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSGAYREPTKPS-DACGLIRWLLM 237

                ....*.
gi 47132591 858 RNPERR 863
Cdd:cd14161 238 VNPERR 243
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
627-868 1.43e-36

Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This family is composed of MLCKs and related MLCK-like kinase domains from giant STKs such as titin, obscurin, SPEG, Unc-89, Trio, kalirin, and Twitchin. Also included in this family are Death-Associated Protein Kinases (DAPKs) and Death-associated protein kinase-Related Apoptosis-inducing protein Kinase (DRAKs). MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. Titin, obscurin, Twitchin, and SPEG are muscle proteins involved in the contractile apparatus. The giant STKs are multidomain proteins containing immunoglobulin (Ig), fibronectin type III (FN3), SH3, RhoGEF, PH and kinase domains. Titin, obscurin, Twitchin, and SPEG contain many Ig domain repeats at the N-terminus, while Trio and Kalirin contain spectrin-like repeats. The MLCK-like family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 138.55  E-value: 1.43e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKGDivarDEVESLMCEKRILAavtSAGHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd14006   1 LGRGRFGVVKRCIEKATGREFAAKFIPKRD----KKKEAVLREISILN---QLQHPRIIQLHEAYESPTELVLILELCSG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLMLHI-HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGY--VKIADFGLCKEgMGYGDRTSTFCG 783
Cdd:cd14006  74 GELLDRLaERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPSpqIKIIDFGLARK-LNPGEELKEIFG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 784 TPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVR----YPRFLSAEAIGIMRRLLRRN 859
Cdd:cd14006 153 TPEFVAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVDfseeYFSSVSQEAKDFIRKLLVKE 232

                ....*....
gi 47132591 860 PERRLGSSE 868
Cdd:cd14006 233 PRKRPTAQE 241
HR1_PKN_2 cd11623
Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
127-196 2.84e-36

Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N; PKN, also called Protein-kinase C-related kinase (PRK), is a serine/threonine protein kinase that can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytoskeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. In some vertebrates, there are three PKN isoforms from different genes (designated PKN1, PKN2, and PKN3), which show different enzymatic properties, tissue distribution, and varied functions. PKN proteins contain three HR1 domains, a C2 domain, and a kinase domain. This model characterizes the second HR1 domain of PKN. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family.


Pssm-ID: 212013  Cd Length: 71  Bit Score: 131.20  E-value: 2.84e-36
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 127 SATNLSRVAGLEKQLAIELKVKQGAENMIQTYSNGSTKDRKLLLTAQQMLQDSKTKIDIIRMQLRRALQA 196
Cdd:cd11623   1 ENAQNSRLAGLEKQLNIELKVKQGAENMIQMYSNGKSKDRKLLAEAQQMLEDSKAKIEFLRMQILRAKQQ 70
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
627-863 3.68e-36

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 137.28  E-value: 3.68e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRpsGELFAIKALKKGDIVARDEVEsLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd13999   1 IGSGSFGEVYKGKWR--GTDVAIKKLKVEDDNDELLKE-FRREVSILSKLR---HPNIVQFIGACLSPPPLCIVTEYMPG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDL--MLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCGT 784
Cdd:cd13999  75 GSLydLLHKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKMTGVVGT 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 785 PEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVR--YPRFLSAEAIGIMRRLLRRNPER 862
Cdd:cd13999 155 PRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVVQKGLRppIPPDCPPELSKLIKRCWNEDPEK 234

                .
gi 47132591 863 R 863
Cdd:cd13999 235 R 235
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
621-868 3.77e-36

Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIM1 is a widely-expressed kinase belonging to the AMP-activated protein kinase (AMPK) subfamily. Although present in most tissues, NIM1 kinase activity is only observed in the brain and testis. NIM1 is capable of autophosphorylating and activating itself, but may be present in other tissues in the inactive form. The physiological function of NIM1 has yet to be elucidated. The NIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 137.47  E-value: 3.77e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIvarDEVESLMCEKRIlAAVTSAGHPFLVNLFGCFQTPEHVCFV 700
Cdd:cd14075   4 YRIRGELGSGNFSQVKLGIHQLTKEKVAIKILDKTKL---DQKTQRLLSREI-SSMEKLHHPNIIRLYEVVETLSKLHLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGGDLMLHIHSD-VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFG---LCKEgmgyGD 776
Cdd:cd14075  80 MEYASGGELYTKISTEgKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGfstHAKR----GE 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 777 RTSTFCGTPEFLAPEVLTDTSYT-RAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRL 855
Cdd:cd14075 156 TLNTFCGSPPYAAPELFKDEHYIgIYVDIWALGVLLYFMVTGVMPFRAETVAKLKKCILEGTYTIPSYVSEPCQELIRGI 235
                       250
                ....*....|...
gi 47132591 856 LRRNPERRLGSSE 868
Cdd:cd14075 236 LQPVPSDRYSIDE 248
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
621-868 5.23e-36

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 137.07  E-value: 5.23e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDE-VESlmcEKRILAAVTsagHPFLVNLFGCFQTPEHVCF 699
Cdd:cd14095   2 YDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKEHmIEN---EVAILRRVK---HPNIVQLIEEYDTDTELYL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYSAGGDLMLHIHSDV-FSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGY----VKIADFGLCKEgmgY 774
Cdd:cd14095  76 VMELVKGGDLFDAITSSTkFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEDgsksLKLADFGLATE---V 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 775 GDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPF--PGDDEEEVFDSIVNDEVRYPR----FLSAEA 848
Cdd:cd14095 153 KEPLFTVCGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFrsPDRDQEELFDLILAGEFEFLSpywdNISDSA 232
                       250       260
                ....*....|....*....|
gi 47132591 849 IGIMRRLLRRNPERRLGSSE 868
Cdd:cd14095 233 KDLISRMLVVDPEKRYSAGQ 252
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
617-864 8.91e-36

Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 136.63  E-value: 8.91e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 617 TLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIvARDEVESLMceKRILAAVTSAGHPFLVNLFGCFQTPEH 696
Cdd:cd14116   3 ALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQL-EKAGVEHQL--RREVEIQSHLRHPNILRLYGYFHDATR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 697 VCFVMEYSAGGDLMLHIHS-DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGyg 775
Cdd:cd14116  80 VYLILEYAPLGTVYRELQKlSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPS-- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 776 DRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRL 855
Cdd:cd14116 158 SRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRL 237

                ....*....
gi 47132591 856 LRRNPERRL 864
Cdd:cd14116 238 LKHNPSQRP 246
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
619-867 2.40e-35

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK4, also called SAK or STK18, is structurally different from other PLKs in that it contains only one polo box that can form two adjacent polo boxes and a functional PDB by homodimerization. It is required for late mitotic progression, cell survival, and embryonic development. It localizes to centrosomes and is required for centriole duplication and chromosomal stability. Overexpression of PLK4 may be associated with colon tumors. The PLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 135.37  E-value: 2.40e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVC 698
Cdd:cd14186   1 EDFKVLNLLGKGSFACVYRARSLHTGLEVAIKMIDKKAMQKAGMVQRVRNEVEIHCQLK---HPSILELYNYFEDSNYVY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGGDLMLHIHSDV--FSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGD 776
Cdd:cd14186  78 LVLEMCHNGEMSRYLKNRKkpFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKMPHE 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 777 RTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLL 856
Cdd:cd14186 158 KHFTMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLADYEMPAFLSREAQDLIHQLL 237
                       250
                ....*....|.
gi 47132591 857 RRNPERRLGSS 867
Cdd:cd14186 238 RKNPADRLSLS 248
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
619-863 8.18e-35

Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and similar proteins; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include MAPKKs from plants, kinetoplastids, alveolates, and mycetozoa. The MAPKK, LmxPK4, from Leishmania mexicana, is important in differentiation and virulence. Dictyostelium discoideum MEK1 is required for proper chemotaxis; MEK1 null mutants display severe defects in cell polarization and directional movement. Plants contain multiple MAPKKs like other eukaryotes. The Arabidopsis genome encodes for 10 MAPKKs while poplar and rice contain 13 MAPKKs each. The functions of these proteins have not been fully elucidated. There is evidence to suggest that MAPK cascades are involved in plant stress responses. In Arabidopsis, MKK3 plays a role in pathogen signaling; MKK2 is involved in cold and salt stress signaling; MKK4/MKK5 participates in innate immunity; and MKK7 regulates basal and systemic acquired resistance. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 133.87  E-value: 8.18e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKkgdIVARDEVESLMC-EKRILAavtSAGHPFLVNLFGCFQTPEHV 697
Cdd:cd06623   1 SDLERVKVLGQGSSGVVYKVRHKPTGKIYALKKIH---VDGDEEFRKQLLrELKTLR---SCESPYVVKCYGAFYKEGEI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 698 CFVMEYSAGGDLmlhihSDV------FSEP--RAIFYSacVVLGLQFLH-EHKIVYRDLKLDNLLLDTEGYVKIADFGLC 768
Cdd:cd06623  75 SIVLEYMDGGSL-----ADLlkkvgkIPEPvlAYIARQ--ILKGLDYLHtKRHIIHRDIKPSNLLINSKGEVKIADFGIS 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 769 KEGMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFD---SIVNDEVRYPR--F 843
Cdd:cd06623 148 KVLENTLDQCNTFVGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPGQPSFFElmqAICDGPPPSLPaeE 227
                       250       260
                ....*....|....*....|
gi 47132591 844 LSAEAIGIMRRLLRRNPERR 863
Cdd:cd06623 228 FSPEFRDFISACLQKDPKKR 247
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
621-868 1.64e-34

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 132.71  E-value: 1.64e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFV 700
Cdd:cd14014   2 YRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLS---HPNIVRVYDVGEDDGRPYIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGGDLMLHIHSDV-FSEPRAIFYSACVVLGLQFLHEHKIVYR---------DLkldnllldtEGYVKIADFGLCK- 769
Cdd:cd14014  79 MEYVEGGSLADLLRERGpLPPREALRILAQIADALAAAHRAGIVHRdikpanillTE---------DGRVKLTDFGIARa 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 770 EGMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEV----RYPRFLS 845
Cdd:cd14014 150 LGDSGLTQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPpppsPLNPDVP 229
                       250       260
                ....*....|....*....|...
gi 47132591 846 AEAIGIMRRLLRRNPERRLGSSE 868
Cdd:cd14014 230 PALDAIILRALAKDPEERPQSAA 252
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
620-868 2.49e-34

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis. This subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 132.13  E-value: 2.49e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARdEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCF 699
Cdd:cd08530   1 DFKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLGSLSQK-EREDSVNEIRLLASVN---HPNIIRYKEAFLDGNRLCI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYSAGGDLMLHI-----HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFG---LCKEG 771
Cdd:cd08530  77 VMEYAPFGDLSKLIskrkkKRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGiskVLKKN 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 772 MGYgdrtsTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDevRYPRF---LSAEA 848
Cdd:cd08530 157 LAK-----TQIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQELRYKVCRG--KFPPIppvYSQDL 229
                       250       260
                ....*....|....*....|
gi 47132591 849 IGIMRRLLRRNPERRLGSSE 868
Cdd:cd08530 230 QQIIRSLLQVNPKKRPSCDK 249
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
626-864 3.42e-34

Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Checkpoint Kinase 2 (Chk2) plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The Chk2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270986 [Multi-domain]  Cd Length: 275  Bit Score: 132.52  E-value: 3.42e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGELFAIKALKK-----GDIVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFV 700
Cdd:cd14084  13 TLGSGACGEVKLAYDKSTCKKVAIKIINKrkftiGSRREINKPRNIETEIEILKKLS---HPCIIKIEDFFDAEDDYYIV 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGGDLMLHIHSDV-FSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDT---EGYVKIADFGLCKEgMGYGD 776
Cdd:cd14084  90 LELMEGGELFDRVVSNKrLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSqeeECLIKITDFGLSKI-LGETS 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 777 RTSTFCGTPEFLAPEVLT---DTSYTRAVDWWGLGVLLYEMLVGESPFPGD-DEEEVFDSIVNDEVRY----PRFLSAEA 848
Cdd:cd14084 169 LMKTLCGTPTYLAPEVLRsfgTEGYTRAVDCWSLGVILFICLSGYPPFSEEyTQMSLKEQILSGKYTFipkaWKNVSEEA 248
                       250
                ....*....|....*.
gi 47132591 849 IGIMRRLLRRNPERRL 864
Cdd:cd14084 249 KDLVKKMLVVDPSRRP 264
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
621-863 4.21e-34

Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MARKs, also called Partitioning-defective 1 (Par1) proteins, function as regulators of diverse cellular processes in nematodes, Drosophila, yeast, and vertebrates. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. Vertebrates contain four isoforms, namely MARK1 (or Par1c), MARK2 (or Par1b), MARK3 (Par1a), and MARK4 (or MARKL1). Known substrates of MARKs include the cell cycle-regulating phosphatase Cdc25, tyrosine phosphatase PTPH1, MAPK scaffolding protein KSR1, class IIa histone deacetylases, and plakophilin 2. The MARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 131.49  E-value: 4.21e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVArDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFV 700
Cdd:cd14072   2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNP-SSLQKLFREVRIMKILN---HPNIVKLFEVIETEKTLYLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGGDLM--LHIHSDVFS-EPRAIFYSacVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEgMGYGDR 777
Cdd:cd14072  78 MEYASGGEVFdyLVAHGRMKEkEARAKFRQ--IVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNE-FTPGNK 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 778 TSTFCGTPEFLAPEVLTDTSYT-RAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLL 856
Cdd:cd14072 155 LDTFCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFL 234

                ....*..
gi 47132591 857 RRNPERR 863
Cdd:cd14072 235 VLNPSKR 241
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
620-868 6.07e-34

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 131.44  E-value: 6.07e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDE-VESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVC 698
Cdd:cd14098   1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKVAGNDKnLQLFQREINILKSLE---HPGIVRLIDWYEDDQHIY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGGDLMlhihsDVFSEPRAIFYSACVVLGLQFL------HEHKIVYRDLKLDNLLLDTEG--YVKIADFGLCKE 770
Cdd:cd14098  78 LVMEYVEGGDLM-----DFIMAWGAIPEQHARELTKQILeamaytHSMGITHRDLKPENILITQDDpvIVKISDFGLAKV 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 771 gMGYGDRTSTFCGTPEFLAPEVL--TDTS----YTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIvnDEVRYPR-- 842
Cdd:cd14098 153 -IHTGTFLVTFCGTMAYLAPEILmsKEQNlqggYSNLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRI--RKGRYTQpp 229
                       250       260       270
                ....*....|....*....|....*....|
gi 47132591 843 ----FLSAEAIGIMRRLLRRNPERRLGSSE 868
Cdd:cd14098 230 lvdfNISEEAIDFILRLLDVDPEKRMTAAQ 259
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
627-864 7.63e-34

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs, also called STK17, were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. They may play a role in apoptotic signaling. The DRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 131.32  E-value: 7.63e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKgdivaRDEVESlmCEKRIL--AAV--TSAGHPFLVNLFGCFQTPEHVCFVME 702
Cdd:cd14106  16 LGRGKFAVVRKCIHKETGKEYAAKFLRK-----RRRGQD--CRNEILheIAVleLCKDCPRVVNLHEVYETRSELILILE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 703 YSAGGDLMLHIHSD-VFSEPRAIFYSACVVLGLQFLHEHKIVY---RDLKLDNLLLDTEGYVKIADFGLCKEgMGYGDRT 778
Cdd:cd14106  89 LAAGGELQTLLDEEeCLTEADVRRLMRQILEGVQYLHERNIVHldlKPQNILLTSEFPLGDIKLCDFGISRV-IGEGEEI 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 779 STFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFL----SAEAIGIMRR 854
Cdd:cd14106 168 REILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQCNLDFPEELfkdvSPLAIDFIKR 247
                       250
                ....*....|
gi 47132591 855 LLRRNPERRL 864
Cdd:cd14106 248 LLVKDPEKRL 257
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
621-863 1.53e-33

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 130.18  E-value: 1.53e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEveSLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFV 700
Cdd:cd14083   5 YEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGKED--SLENEIAVLRKIK---HPNIVQLLDIYESKSHLYLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGGDLMLHI-HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDT---EGYVKIADFGLCKegMGYGD 776
Cdd:cd14083  80 MELVTGGELFDRIvEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYYSpdeDSKIMISDFGLSK--MEDSG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 777 RTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRY--PRF--LSAEAIGIM 852
Cdd:cd14083 158 VMSTACGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKAEYEFdsPYWddISDSAKDFI 237
                       250
                ....*....|.
gi 47132591 853 RRLLRRNPERR 863
Cdd:cd14083 238 RHLMEKDPNKR 248
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
627-880 2.94e-33

Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BRSK1, also called SAD-B or SAD1 (Synapses of Amphids Defective homolog 1), and BRSK2, also called SAD-A, are highly expressed in mammalian forebrain. They play important roles in establishing neuronal polarity. BRSK1/2 double knock-out mice die soon after birth, showing thin cerebral cortices due to disordered subplate layers and neurons that lack distinct axons and dendrites. BRSK1 regulates presynaptic neurotransmitter release. Its activity fluctuates during cell cysle progression and it acts as a regulator of centrosome duplication. BRSK2 is also abundant in pancreatic islets, where it is involved in the regulation of glucose-stimulated insulin secretion. The BRSK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270983 [Multi-domain]  Cd Length: 255  Bit Score: 128.91  E-value: 2.94e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd14081   9 LGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESVLMKVEREIAIMKLIE---HPNVLKLYDVYENKKYLYLVLEYVSG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLMLHIHSD-VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFG---LCKEGmgygDRTSTFC 782
Cdd:cd14081  86 GELFDYLVKKgRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGmasLQPEG----SLLETSC 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 783 GTPEFLAPEVLTDTSYT-RAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNPE 861
Cdd:cd14081 162 GSPHYACPEVIKGEKYDgRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGVFHIPHFISPDAQDLLRRMLEVNPE 241
                       250
                ....*....|....*....
gi 47132591 862 RRLgsserDAEDVKKQPFF 880
Cdd:cd14081 242 KRI-----TIEEIKKHPWF 255
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
621-880 4.25e-33

Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. TSSK6, also called SSTK, is expressed at the head of elongated sperm. TSSK1/TSSK2 double knock-out and TSSK6 null mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270982 [Multi-domain]  Cd Length: 262  Bit Score: 128.84  E-value: 4.25e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSG--ELFAIKALKKgDIVARDEVESLMceKRILAAVTSAGHPFLVNLFGCFQTPEHVC 698
Cdd:cd14080   2 YRLGKTIGEGSYSKVKLAEYTKSGlkEKVACKIIDK-KKAPKDFLEKFL--PRELEILRKLRHPNIIQVYSIFERGSKVF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGGDLMLHI-HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKE-GMGYGD 776
Cdd:cd14080  79 IFMEYAEHGDLLEYIqKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFARLcPDDDGD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 777 RTS-TFCGTPEFLAPEVLTDTSYT-RAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPR---FLSAEAIGI 851
Cdd:cd14080 159 VLSkTFCGSAAYAAPEILQGIPYDpKKYDIWSLGVILYIMLCGSMPFDDSNIKKMLKDQQNRKVRFPSsvkKLSPECKDL 238
                       250       260
                ....*....|....*....|....*....
gi 47132591 852 MRRLLRRNPERRLGsserdAEDVKKQPFF 880
Cdd:cd14080 239 IDQLLEPDPTKRAT-----IEEILNHPWL 262
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
619-863 4.54e-33

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I gamma; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 129.73  E-value: 4.54e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIvARDEveSLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVC 698
Cdd:cd14166   3 ETFIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPL-SRDS--SLENEIAVLKRIK---HENIVTLEDIYESTTHYY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGGDLMLHI-HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDT---EGYVKIADFGLCKegMGY 774
Cdd:cd14166  77 LVMQLVSGGELFDRIlERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYLTpdeNSKIMITDFGLSK--MEQ 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 775 GDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRY--PRF--LSAEAIG 850
Cdd:cd14166 155 NGIMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYYEFesPFWddISESAKD 234
                       250
                ....*....|...
gi 47132591 851 IMRRLLRRNPERR 863
Cdd:cd14166 235 FIRHLLEKNPSKR 247
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
619-865 9.17e-33

Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK36, also called Fused (or Fu) kinase, is involved in the Hedgehog signaling pathway. It is activated by the Smoothened (SMO) signal transducer, resulting in the stabilization of GLI transcription factors and the phosphorylation of SUFU to facilitate the nuclear accumulation of GLI. In Drosophila, Fused kinase is maternally required for proper segmentation during embryonic development and for the development of legs and wings during the larval stage. In mice, STK36 is not necessary for embryonic development, although mice deficient in STK36 display growth retardation postnatally. The STK36 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270904 [Multi-domain]  Cd Length: 253  Bit Score: 127.75  E-value: 9.17e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIK-ALKKGDivARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHV 697
Cdd:cd14002   1 ENYHVLELIGEGSFGKVYKGRRKYTGQVVALKfIPKRGK--SEKELRNLRQEIEILRKLN---HPNIIEMLDSFETKKEF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 698 CFVMEYsAGGDLmLHIHSDVFSEP----RAIfysAC-VVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEgM 772
Cdd:cd14002  76 VVVTEY-AQGEL-FQILEDDGTLPeeevRSI---AKqLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARA-M 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 773 GYGDRTST-FCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGI 851
Cdd:cd14002 150 SCNTLVLTsIKGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKDPVKWPSNMSPEFKSF 229
                       250
                ....*....|....
gi 47132591 852 MRRLLRRNPERRLG 865
Cdd:cd14002 230 LQGLLNKDPSKRLS 243
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
627-868 1.28e-32

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module. MLCK2, MLCK3, and MLCK4 share a simpler domain architecture of a single kinase domain near the C-terminus and the absence of Ig-like or FN3 domains. The MLCK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 126.96  E-value: 1.28e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFA---IKALKKGDivaRDEVE---SLMCEKRilaavtsagHPFLVNLFGCFQTPEHVCFV 700
Cdd:cd14103   1 LGRGKFGTVYRCVEKATGKELAakfIKCRKAKD---REDVRneiEIMNQLR---------HPRLLQLYDAFETPREMVLV 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGGDLMLHIHSDVF--SEPRAIFYSACVVLGLQFLHEHKIVY------------RdlkldnllldTEGYVKIADFG 766
Cdd:cd14103  69 MEYVAGGELFERVVDDDFelTERDCILFMRQICEGVQYMHKQGILHldlkpenilcvsR----------TGNQIKIIDFG 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 767 LCKEgmgYGDRTST--FCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVN------DEV 838
Cdd:cd14103 139 LARK---YDPDKKLkvLFGTPEFVAPEVVNYEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRakwdfdDEA 215
                       250       260       270
                ....*....|....*....|....*....|..
gi 47132591 839 ryprF--LSAEAIGIMRRLLRRNPERRLGSSE 868
Cdd:cd14103 216 ----FddISDEAKDFISKLLVKDPRKRMSAAQ 243
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
616-896 1.40e-32

Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). This subfamily includes Aurora-B and Aurora-C. Aurora-B is most active at the transition during metaphase to the end of mitosis. It associates with centromeres, relocates to the midzone of the central spindle, and concentrates at the midbody during cell division. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. INCENP participates in the activation of Aurora-B in a two-step process: first by binding to form an intermediate state of activation and the phosphorylation of its C-terminal TSS motif to generate the fully active kinase. The Aurora-B subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 127.67  E-value: 1.40e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 616 LTLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVaRDEVESLMceKRILAAVTSAGHPFLVNLFGCFQTPE 695
Cdd:cd14117   3 FTIDDFDIGRPLGKGKFGNVYLAREKQSKFIVALKVLFKSQIE-KEGVEHQL--RREIEIQSHLRHPNILRLYNYFHDRK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 696 HVCFVMEYSAGGDLMLHIH-SDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGY 774
Cdd:cd14117  80 RIYLILEYAPRGELYKELQkHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWSVHAPSL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 775 gdRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRR 854
Cdd:cd14117 160 --RRRTMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDLKFPPFLSDGSRDLISK 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 47132591 855 LLRRNPERRLGSSErdaedVKKQPffrtlgWEALLARRLPPP 896
Cdd:cd14117 238 LLRYHPSERLPLKG-----VMEHP------WVKANSRRVLPP 268
HR1_PKN_3 cd11625
Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
212-284 1.61e-32

Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N; PKN, also called Protein-kinase C-related kinase (PRK), is a serine/threonine protein kinase that can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytoskeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. In some vertebrates, there are three PKN isoforms from different genes (designated PKN1, PKN2, and PKN3), which show different enzymatic properties, tissue distribution, and varied functions. PKN proteins contain three HR1 domains, a C2 domain, and a kinase domain. This model characterizes the third HR1 domain of PKN. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family.


Pssm-ID: 212015  Cd Length: 74  Bit Score: 120.47  E-value: 1.61e-32
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47132591 212 PDLGAVELRIEELRHHFRVEHAVAEGAKNVLRLLSAAKAPDRKAVSEAQEKLTESNQKLGLLREALERRLGEL 284
Cdd:cd11625   2 PLLLPLELRIEELRHHLRVETAVVEGAKNVIKLLQNAKKDDKKALQEAQKSLSESSQKLDLLRLSLERRLAEL 74
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
627-864 1.97e-32

Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kin4 is a central component of the spindle position checkpoint (SPOC), which monitors spindle position and regulates the mitotic exit network (MEN). Kin4 associates with spindle pole bodies in mother cells to inhibit MEN signaling and delay mitosis until the anaphase nucleus is properly positioned along the mother-bud axis. Kin4 activity is regulated by both the bud neck-associated kinase Elm1 and protein phosphatase 2A. The Kin4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 127.21  E-value: 1.97e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLL-----SEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFVM 701
Cdd:cd14076   9 LGEGEFGKVKLgwplpKANHRSGVQVAIKLIRRDTQQENCQTSKIMREINILKGLT---HPNIVRLLDVLKTKKYIGIVL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 702 EYSAGGDLMLHIHSDVF---SEPRAIFysACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKE-GMGYGDR 777
Cdd:cd14076  86 EFVSGGELFDYILARRRlkdSVACRLF--AQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTfDHFNGDL 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 778 TSTFCGTPEFLAPE-VLTDTSYT-RAVDWWGLGVLLYEMLVGESPF-------PGDDEEEVFDSIVNDEVRYPRFLSAEA 848
Cdd:cd14076 164 MSTSCGSPCYAAPElVVSDSMYAgRKADIWSCGVILYAMLAGYLPFdddphnpNGDNVPRLYRYICNTPLIFPEYVTPKA 243
                       250
                ....*....|....*.
gi 47132591 849 IGIMRRLLRRNPERRL 864
Cdd:cd14076 244 RDLLRRILVPNPRKRI 259
HR1_PKN2_2 cd11631
Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
125-195 2.22e-32

Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N2; PKN2, also called PKNgamma or Protein-kinase C-related kinase 2 (PRK2), is a serine/threonine protein kinase and an effector of the small GTPase Rho/Rac. It regulates G2/M cell cycle progression and the exit from cytokinesis. It also phosphorylates hepatitis C virus (HCV) RNA polymerase and thus, plays a role in HCV RNA replication. PKN2 shares a common domain architecture with other PKNs, containing three HR1 domains, a C2 domain, and a kinase domain. In addition, PKN2 contains a proline-rich region in between its C2 and kinase domains and has been shown to associate with SH3 domain containing proteins like NCK and Grb4. This model characterizes the second HR1 domain of PKN2. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; PKN2 specifically binds to RhoA GTPase in a GTP-dependent manner. The HR1 domains of PKN2, together with its C2 domain, also facilitate the recruitment of PKN2 to primordial junctions at nascent cell-cell contacts, where it promotes junctional maturation.


Pssm-ID: 212021  Cd Length: 74  Bit Score: 120.18  E-value: 2.22e-32
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47132591 125 TCSATNLSRVAGLEKQLAIELKVKQGAENMIQTYSNGSTKDRKLLLTAQQMLQDSKTKIDIIRMQLRRALQ 195
Cdd:cd11631   2 TRMSTNNNRLMALKKQLDIELKVKQGAENMIQMYSNGSSKDRKLLATAQQMLQDSKTKIEVIRMQILQAVQ 72
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
627-863 1.61e-31

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. Its localization changes during mitotic progression; associating first with centrosomes in prophase, with kinetochores in prometaphase and metaphase, at the central spindle in anaphase, and in the midbody during telophase. It carries multiple functions throughout the cell cycle through interactions with differrent substrates at these specific subcellular locations. PLK1 is overexpressed in many human cancers and is associated with poor prognosis. The PLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271089 [Multi-domain]  Cd Length: 265  Bit Score: 124.28  E-value: 1.61e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEkriLAAVTSAGHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd14187  15 LGKGGFAKCYEITDADTKEVFAGKIVPKSLLLKPHQKEKMSME---IAIHRSLAHQHVVGFHGFFEDNDFVYVVLELCRR 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLM-LHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCGTP 785
Cdd:cd14187  92 RSLLeLHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKVEYDGERKKTLCGTP 171
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47132591 786 EFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNPERR 863
Cdd:cd14187 172 NYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTAR 249
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
621-883 1.61e-31

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 124.15  E-value: 1.61e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591   621 FKFLAVLGRGHFGKVLLSEFRPSGELF----AIKALKKGDIvaRDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEH 696
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGEGENTkikvAVKTLKEGAD--EEEREDFLEEASIMKKLD---HPNIVKLLGVCTQGEP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591   697 VCFVMEYSAGGDLM--LHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGM-G 773
Cdd:pfam07714  76 LYIVTEYMPGGDLLdfLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDIYdD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591   774 YGDRTSTFCGTPEF-LAPEVLTDTSYTRAVDWWGLGVLLYEML-VGESPFPGDDEEEVFDSIvndEVRY----PRFLSAE 847
Cdd:pfam07714 156 DYYRKRGGGKLPIKwMAPESLKDGKFTSKSDVWSFGVLLWEIFtLGEQPYPGMSNEEVLEFL---EDGYrlpqPENCPDE 232
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 47132591   848 AIGIMRRLLRRNPERRlgsserdaedvkkqPFFRTL 883
Cdd:pfam07714 233 LYDLMKQCWAYDPEDR--------------PTFSEL 254
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
627-880 2.00e-31

Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. In response to decreased ATP levels, it enhances energy-producing processes and inhibits energy-consuming pathways. Once activated, AMPK phosphorylates a broad range of downstream targets, with effects in carbohydrate metabolism and uptake, lipid and fatty acid biosynthesis, carbon energy storage, and inflammation, among others. Defects in energy homeostasis underlie many human diseases including Type 2 diabetes, obesity, heart disease, and cancer. As a result, AMPK has emerged as a therapeutic target in the treatment of these diseases. The AMPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 123.92  E-value: 2.00e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd14079  10 LGVGSFGKVKLAEHELTGHKVAVKILNRQKIKSLDMEEKIRREIQILKLFR---HPHIIRLYEVIETPTDIFMVMEYVSG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLMLHI-HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLcKEGMGYGDRTSTFCGTP 785
Cdd:cd14079  87 GELFDYIvQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGL-SNIMRDGEFLKTSCGSP 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 786 EFLAPEVLTDTSYTRA-VDWWGLGVLLYEMLVGESPFpgDDEE--EVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNPER 862
Cdd:cd14079 166 NYAAPEVISGKLYAGPeVDVWSCGVILYALLCGSLPF--DDEHipNLFKKIKSGIYTIPSHLSPGARDLIKRMLVVDPLK 243
                       250
                ....*....|....*...
gi 47132591 863 RLgsserDAEDVKKQPFF 880
Cdd:cd14079 244 RI-----TIPEIRQHPWF 256
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
619-863 2.89e-31

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 123.60  E-value: 2.89e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEveSLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVC 698
Cdd:cd14167   3 DIYDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKET--SIENEIAVLHKIK---HPNIVALDDIYESGGHLY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGGDLMLHIHSDVFSEPRAIFYSACVVL-GLQFLHEHKIVYRDLKLDNLLLDT---EGYVKIADFGLCKEgMGY 774
Cdd:cd14167  78 LIMQLVSGGELFDRIVEKGFYTERDASKLIFQILdAVKYLHDMGIVHRDLKPENLLYYSldeDSKIMISDFGLSKI-EGS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 775 GDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRY--PRF--LSAEAIG 850
Cdd:cd14167 157 GSVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYEFdsPYWddISDSAKD 236
                       250
                ....*....|...
gi 47132591 851 IMRRLLRRNPERR 863
Cdd:cd14167 237 FIQHLMEKDPEKR 249
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
627-863 5.04e-31

The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2 (also called STK17B). Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. DRAK2 has been implicated in inducing or enhancing apoptosis in beta cells, fibroblasts, and lymphoid cells, where it is highly expressed. It is involved in regulating many immune processes including the germinal center (GC) reaction, responses to thymus-dependent antigens, activated T cell survival, memory T cell responses. It may be involved in the development of autoimmunity. The DRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 123.11  E-value: 5.04e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKGDiVARDEVESLMCEKRILAAVTSagHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd14198  16 LGRGKFAVVRQCISKSTGQEYAAKFLKKRR-RGQDCRAEILHEIAVLELAKS--NPRVVNLHEVYETTSEIILILEYAAG 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLMLHIHSD---VFSEPRAIFYSACVVLGLQFLHEHKIVY---RDLKLDNLLLDTEGYVKIADFGLCKEgMGYGDRTST 780
Cdd:cd14198  93 GEIFNLCVPDlaeMVSENDIIRLIRQILEGVYYLHQNNIVHldlKPQNILLSSIYPLGDIKIVDFGMSRK-IGHACELRE 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 781 FCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPR----FLSAEAIGIMRRLL 856
Cdd:cd14198 172 IMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQVNVDYSEetfsSVSQLATDFIQKLL 251

                ....*..
gi 47132591 857 RRNPERR 863
Cdd:cd14198 252 VKNPEKR 258
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
621-880 6.34e-31

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. PAK deregulation is associated with tumor development. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). Group II PAKs contain a PBD and a catalytic domain, but lack other motifs found in group I PAKs. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. Group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX; no such binding has been demonstrated for group II PAKs. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 122.32  E-value: 6.34e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKkgdiVARDEVESLMCEKRILaavTSAGHPFLVNLFGCFQTPEHVCFV 700
Cdd:cd06614   2 YKNLEKIGEGASGEVYKATDRATGKEVAIKKMR----LRKQNKELIINEILIM---KECKHPNIVDYYDSYLVGDELWVV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGGDL--MLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRT 778
Cdd:cd06614  75 MEYMDGGSLtdIITQNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQLTKEKSKR 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 779 STFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVND---EVRYPRFLSAEAIGIMRRL 855
Cdd:cd06614 155 NSVVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRALFLITTKgipPLKNPEKWSPEFKDFLNKC 234
                       250       260
                ....*....|....*....|....*
gi 47132591 856 LRRNPERRLgsserDAEDVKKQPFF 880
Cdd:cd06614 235 LVKDPEKRP-----SAEELLQHPFL 254
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
620-868 8.83e-31

Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of yeast Kin1, Kin2, and similar proteins. Fission yeast Kin1 is a membrane-associated kinase that is involved in regulating cell surface cohesiveness during interphase. It also plays a role during mitosis, linking actomyosin ring assembly with septum synthesis and membrane closure to ensure separation of daughter cells. Budding yeast Kin1 and Kin2 act downstream of the Rab-GTPase Sec4 and are associated with the exocytic apparatus; they play roles in the secretory pathway. The Kin1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 122.17  E-value: 8.83e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALK---KGDIVARDEVESLM---CEKRIL--AAVTSA-GHPFLVNLFGC 690
Cdd:cd14077   2 NWEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPrasNAGLKKEREKRLEKeisRDIRTIreAALSSLlNHPHICRLRDF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 691 FQTPEHVCFVMEYSAGGDLMLHIHSD-VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLcK 769
Cdd:cd14077  82 LRTPNHYYMLFEYVDGGQLLDYIISHgKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGL-S 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 770 EGMGYGDRTSTFCGTPEFLAPEVLTDTSYT-RAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEA 848
Cdd:cd14077 161 NLYDPRRLLRTFCGSLYFAAPELLQAQPYTgPEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIKKGKVEYPSYLSSEC 240
                       250       260
                ....*....|....*....|
gi 47132591 849 IGIMRRLLRRNPERRLGSSE 868
Cdd:cd14077 241 KSLISRMLVVDPKKRATLEQ 260
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
622-863 2.31e-30

Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 120.71  E-value: 2.31e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591    622 KFLAVLGRGHFGKVLLSEFRPSG----ELFAIKALKKGDIvaRDEVESLMCEKRILAAVtsaGHPFLVNLFGCFQTPEHV 697
Cdd:smart00219   2 TLGKKLGEGAFGEVYKGKLKGKGgkkkVEVAVKTLKEDAS--EQQIEEFLREARIMRKL---DHPNVVKLLGVCTEEEPL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591    698 CFVMEYSAGGDLM--LHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEgmGYG 775
Cdd:smart00219  77 YIVMEYMEGGDLLsyLRKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRD--LYD 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591    776 DRTSTFCGTPE---FLAPEVLTDTSYTRAVDWWGLGVLLYEML-VGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAI-G 850
Cdd:smart00219 155 DDYYRKRGGKLpirWMAPESLKEGKFTSKSDVWSFGVLLWEIFtLGEQPYPGMSNEEVLEYLKNGYRLPQPPNCPPELyD 234
                          250
                   ....*....|...
gi 47132591    851 IMRRLLRRNPERR 863
Cdd:smart00219 235 LMLQCWAEDPEDR 247
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
627-863 3.24e-30

Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane. The Cdc7-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 120.41  E-value: 3.24e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKGDIvARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd06627   8 IGRGAFGSVYKGLNLNTGEFVAIKQISLEKI-PKSDLKSVMGEIDLLKKLN---HPNIVKYIGSVKTKDSLYIILEYVEN 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLMLHIH-SDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCGTP 785
Cdd:cd06627  84 GSLASIIKkFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATKLNEVEKDENSVVGTP 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 786 EFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFpgddeeevFD--------SIVNDEvrYPRF---LSAEAIGIMRR 854
Cdd:cd06627 164 YWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPY--------YDlqpmaalfRIVQDD--HPPLpenISPELRDFLLQ 233

                ....*....
gi 47132591 855 LLRRNPERR 863
Cdd:cd06627 234 CFQKDPTLR 242
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
626-863 3.98e-30

Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers.The PTK family is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 120.34  E-value: 3.98e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGELF---AIKALKKGDivARDEVESLMCEKRILAAVtsaGHPFLVNLFGCFQTPEHVCFVME 702
Cdd:cd00192   2 KLGEGAFGEVYKGKLKGGDGKTvdvAVKTLKEDA--SESERKDFLKEARVMKKL---GHPNVVRLLGVCTEEEPLYLVME 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 703 YSAGGDL--MLHIHSDVFSEPRAIFYSACVVL--------GLQFLHEHKIVYRdlkldnllldTEGYVKIADFGLCKEGM 772
Cdd:cd00192  77 YMEGGDLldFLRKSRPVFPSPEPSTLSLKDLLsfaiqiakGMEYLASKKFVHRdlaarnclvgEDLVVKISDFGLSRDIY 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 773 GYGDRTSTfCGTPE---FLAPEVLTDTSYTRAVDWWGLGVLLYEMLV-GESPFPGDDEEEVFDSIVNDEvRY--PRFLSA 846
Cdd:cd00192 157 DDDYYRKK-TGGKLpirWMAPESLKDGIFTSKSDVWSFGVLLWEIFTlGATPYPGLSNEEVLEYLRKGY-RLpkPENCPD 234
                       250
                ....*....|....*..
gi 47132591 847 EAIGIMRRLLRRNPERR 863
Cdd:cd00192 235 ELYELMLSCWQLDPEDR 251
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
627-864 6.66e-30

Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MELK is a cell cycle dependent protein which functions in cytokinesis, cell cycle, apoptosis, cell proliferation, and mRNA processing. It is found upregulated in many types of cancer cells, playing an indispensable role in cancer cell survival. It makes an attractive target in the design of inhibitors for use in the treatment of a wide range of human cancer. The MELK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 119.41  E-value: 6.66e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKK---GDIVARDEVEslmcekriLAAVTSAGHPFLVNLFGCFQTPEHVCFVMEY 703
Cdd:cd14078  11 IGSGGFAKVKLATHILTGEKVAIKIMDKkalGDDLPRVKTE--------IEALKNLSHQHICRLYHVIETDNKIFMVLEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 704 SAGGDLMLHIHS-DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLC---KEGMGYgdRTS 779
Cdd:cd14078  83 CPGGELFDYIVAkDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCakpKGGMDH--HLE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 780 TFCGTPEFLAPEVLTDTSYTRA-VDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRR 858
Cdd:cd14078 161 TCCGSPAYAAPELIQGKPYIGSeADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSGKYEEPEWLSPSSKLLLDQMLQV 240

                ....*.
gi 47132591 859 NPERRL 864
Cdd:cd14078 241 DPKKRI 246
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
627-863 8.56e-30

Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNRK is a kinase highly expressed in testis and brain that is found inactive in cells that lack the LKB1 tumour suppressor protein kinase. The regulatory subunits STRAD and MO25 are required for LKB1 to activate SNRK. The SNRK mRNA is increased 3-fold when granule neurons are cultured in low potassium, and may thus play a role in the survival responses in these cells. In some vertebrates, a second SNRK gene (snrkb or snrk-1) has been sequenced and/or identified. Snrk-1 is expressed specifically in embryonic zebrafish vasculature; it plays an essential role in angioblast differentiation, maintenance, and migration. The SNRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 119.05  E-value: 8.56e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKG--DIVARDEvesLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFVMEYS 704
Cdd:cd14074  11 LGRGHFAVVKLARHVFTGEKVAVKVIDKTklDDVSKAH---LFQEVRCMKLVQ---HPNVVRLYEVIDTQTKLYLILELG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 705 AGGDLMLHI--HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLL-LDTEGYVKIADFGLCKEGMGyGDRTSTF 781
Cdd:cd14074  85 DGGDMYDYImkHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKFQP-GEKLETS 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 782 CGTPEFLAPEVLTDTSY-TRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNP 860
Cdd:cd14074 164 CGSLAYSAPEILLGDEYdAPAVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCKYTVPAHVSPECKDLIRRMLIRDP 243

                ...
gi 47132591 861 ERR 863
Cdd:cd14074 244 KKR 246
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
620-901 9.24e-30

C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), 90 kDa ribosomal protein S6 kinases (p90-RSKs), or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 120.05  E-value: 9.24e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMcekRIlaavtsAGHPFLVNLFGCFQTPEHVCF 699
Cdd:cd14091   1 EYEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKSKRDPSEEIEILL---RY------GQHPNIITLRDVYDDGNSVYL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYSAGGDLMLHIHSD-VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEG----YVKIADFGLCKE---- 770
Cdd:cd14091  72 VTELLRGGELLDRILRQkFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESgdpeSLRICDFGFAKQlrae 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 771 -GMgygdrTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPF---PGDDEEEVFDSIvnDEVRYP----- 841
Cdd:cd14091 152 nGL-----LMTPCYTANFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFasgPNDTPEVILARI--GSGKIDlsggn 224
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47132591 842 -RFLSAEAIGIMRRLLRRNPERRLgsserDAEDVKKQPFFRTlgWEALLARRLPPPFVPTL 901
Cdd:cd14091 225 wDHVSDSAKDLVRKMLHVDPSQRP-----TAAQVLQHPWIRN--RDSLPQRQLTDPQDAAL 278
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
620-863 1.23e-29

Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PASK (or PASKIN) is a nutrient and energy sensor and thus, plays an important role in maintaining cellular energy homeostasis. It coordinates the utilization of glucose in response to metabolic demand. It contains an N-terminal PAS domain which directly interacts and inhibits a C-terminal catalytic kinase domain. The PAS domain serves as a sensory module for different environmental signals such as light, redox state, and various metabolites. Binding of ligands to the PAS domain causes structural changes which leads to kinase activation and the phosphorylation of substrates to trigger the appropriate cellular response. The PASK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270906 [Multi-domain]  Cd Length: 256  Bit Score: 118.64  E-value: 1.23e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMC-----EKRILAAVTSAGHPFLVNLFGCFQTP 694
Cdd:cd14004   1 DYTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERILVDTWVRDRKLgtvplEIHILDTLNKRSHPNIVKLLDFFEDD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 695 EHVCFVME-YSAGGDLMLHIHS----DVFsEPRAIFYSacVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFG--- 766
Cdd:cd14004  81 EFYYLVMEkHGSGMDLFDFIERkpnmDEK-EAKYIFRQ--VADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGsaa 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 767 LCKEGmgygdRTSTFCGTPEFLAPEVLTDTSYT-RAVDWWGLGVLLYEMLVGESPFPGDDEeevfdsIVNDEVRYPRFLS 845
Cdd:cd14004 158 YIKSG-----PFDTFVGTIDYAAPEVLRGNPYGgKEQDIWALGVLLYTLVFKENPFYNIEE------ILEADLRIPYAVS 226
                       250
                ....*....|....*...
gi 47132591 846 AEAIGIMRRLLRRNPERR 863
Cdd:cd14004 227 EDLIDLISRMLNRDVGDR 244
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
627-880 1.53e-29

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 (also called STK17A) and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. Rabbit DRAK1 has been shown to induce apoptosis in osteoclasts and overexpressio of human DRAK1 induces apoptosis in cultured fibroblast cells. DRAK1 may be involved in apoptotic signaling. The DRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 118.88  E-value: 1.53e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKgdivaRDEVESlmCEKRILAAVT----SAGHPFLVNLFGCFQTPEHVCFVME 702
Cdd:cd14197  17 LGRGKFAVVRKCVEKDSGKEFAAKFMRK-----RRKGQD--CRMEIIHEIAvlelAQANPWVINLHEVYETASEMILVLE 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 703 YSAGGDLMLHIHSD---VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTE---GYVKIADFGLCKEgMGYGD 776
Cdd:cd14197  90 YAAGGEIFNQCVADreeAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSEsplGDIKIVDFGLSRI-LKNSE 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 777 RTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPR----FLSAEAIGIM 852
Cdd:cd14197 169 ELREIMGTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQMNVSYSEeefeHLSESAIDFI 248
                       250       260
                ....*....|....*....|....*...
gi 47132591 853 RRLLRRNPERRlgsseRDAEDVKKQPFF 880
Cdd:cd14197 249 KTLLIKKPENR-----ATAEDCLKHPWL 271
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
619-880 1.76e-29

Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chk1 is implicated in many major checkpoints of the cell cycle, providing a link between upstream sensors and the cell cycle engine. It plays an important role in DNA damage response and maintaining genomic stability. Chk1 acts as an effector of the sensor kinase, ATR (ATM and Rad3-related), a member of the PI3K family, which is activated upon DNA replication stress. Chk1 delays mitotic entry in response to replication blocks by inhibiting cyclin dependent kinase (Cdk) activity. In addition, Chk1 contributes to the function of centrosome and spindle-based checkpoints, inhibits firing of origins of DNA replication (Ori), and represses transcription of cell cycle proteins including cyclin B and Cdk1. The Chk1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 118.20  E-value: 1.76e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKA--LKKGDIVARDEVESLMCEKRILAavtsagHPFLVNLFGCFQTPEH 696
Cdd:cd14069   1 EDWDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFvdMKRAPGDCPENIKKEVCIQKMLS------HKNVVRFYGHRREGEF 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 697 VCFVMEYSAGGDLMLHIHSDV-FSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLC------- 768
Cdd:cd14069  75 QYLFLEYASGGELFDKIEPDVgMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLAtvfrykg 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 769 KEgmgygdRTST-FCGTPEFLAPEVLTDTSYtRA--VDWWGLGVLLYEMLVGESPF--PGDDEEEVFDSIVNDEVRY-P- 841
Cdd:cd14069 155 KE------RLLNkMCGTLPYVAPELLAKKKY-RAepVDVWSCGIVLFAMLAGELPWdqPSDSCQEYSDWKENKKTYLtPw 227
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 47132591 842 RFLSAEAIGIMRRLLRRNPERRLgsserDAEDVKKQPFF 880
Cdd:cd14069 228 KKIDTAALSLLRKILTENPNKRI-----TIEDIKKHPWY 261
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
627-868 2.75e-29

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 118.23  E-value: 2.75e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKK--------------------GDIVARDEVESLMCEKRILAAVTsagHPFLVN 686
Cdd:cd14118   2 IGKGSYGIVKLAYNEEDNTLYAMKILSKkkllkqagffrrppprrkpgALGKPLDPLDRVYREIAILKKLD---HPNVVK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 687 LFGCFQTP--EHVCFVMEYSAGGDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIAD 764
Cdd:cd14118  79 LVEVLDDPneDNLYMVFELVDKGAVMEVPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIAD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 765 FGLCKEGMGYGDRTSTFCGTPEFLAPEVLTDTSYT---RAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYP 841
Cdd:cd14118 159 FGVSNEFEGDDALLSSTAGTPAFMAPEALSESRKKfsgKALDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIKTDPVVFP 238
                       250       260
                ....*....|....*....|....*....
gi 47132591 842 R--FLSAEAIGIMRRLLRRNPERRLGSSE 868
Cdd:cd14118 239 DdpVVSEQLKDLILRMLDKNPSERITLPE 267
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
619-863 3.19e-29

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-delta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 119.00  E-value: 3.19e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEveSLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVC 698
Cdd:cd14168  10 KIFEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKGKES--SIENEIAVLRKIK---HENIVALEDIYESPNHLY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGGDLMLHI-HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNL---LLDTEGYVKIADFGLCKEgMGY 774
Cdd:cd14168  85 LVMQLVSGGELFDRIvEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLlyfSQDEESKIMISDFGLSKM-EGK 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 775 GDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRY--PRF--LSAEAIG 850
Cdd:cd14168 164 GDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKADYEFdsPYWddISDSAKD 243
                       250
                ....*....|...
gi 47132591 851 IMRRLLRRNPERR 863
Cdd:cd14168 244 FIRNLMEKDPNKR 256
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
622-863 3.53e-29

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 117.26  E-value: 3.53e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591    622 KFLAVLGRGHFGKVLLSEFRPSG----ELFAIKALKKGDivARDEVESLMCEKRILAAVtsaGHPFLVNLFGCFQTPEHV 697
Cdd:smart00221   2 TLGKKLGEGAFGEVYKGTLKGKGdgkeVEVAVKTLKEDA--SEQQIEEFLREARIMRKL---DHPNIVKLLGVCTEEEPL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591    698 CFVMEYSAGGDLM--LHIHSD-VFSEPRAIFYSACVVLGLQFLHEHKIVYR---------DlkldnllldTEGYVKIADF 765
Cdd:smart00221  77 MIVMEYMPGGDLLdyLRKNRPkELSLSDLLSFALQIARGMEYLESKNFIHRdlaarnclvG---------ENLVVKISDF 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591    766 GLCKEgmGYGDRTSTFCGTPE---FLAPEVLTDTSYTRAVDWWGLGVLLYEML-VGESPFPGDDEEEVFDSIVNDEVRYP 841
Cdd:smart00221 148 GLSRD--LYDDDYYKVKGGKLpirWMAPESLKEGKFTSKSDVWSFGVLLWEIFtLGEEPYPGMSNAEVLEYLKKGYRLPK 225
                          250       260
                   ....*....|....*....|...
gi 47132591    842 RFLSAEAI-GIMRRLLRRNPERR 863
Cdd:smart00221 226 PPNCPPELyKLMLQCWAEDPEDR 248
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
621-868 4.64e-29

Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PSKH1 is an autophosphorylating STK that is expressed ubiquitously and exhibits multiple intracellular localizations including the centrosome, Golgi apparatus, and splice factor compartments. It contains a catalytic kinase domain and an N-terminal SH4-like motif that is acylated to facilitate membrane attachment. PSKH1 plays a rile in the maintenance of the Golgi apparatus, an important organelle within the secretory pathway. It may also function as a novel splice factor and a regulator of prostate cancer cell growth. The PSKH1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 117.25  E-value: 4.64e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKkGDIVARDEVESlmcEKRILAAVTsagHPFLVNLFGCFQTPEHVCFV 700
Cdd:cd14087   3 YDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIE-TKCRGREVCES---ELNVLRRVR---HTNIIQLIEVFETKERVYMV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGGDLMLHIHSD-VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDN---LLLDTEGYVKIADFGLCKEGMGYGD 776
Cdd:cd14087  76 MELATGGELFDRIIAKgSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENllyYHPGPDSKIMITDFGLASTRKKGPN 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 777 RT-STFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRY-PRF---LSAEAIGI 851
Cdd:cd14087 156 CLmKTTCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYsGEPwpsVSNLAKDF 235
                       250
                ....*....|....*..
gi 47132591 852 MRRLLRRNPERRLGSSE 868
Cdd:cd14087 236 IDRLLTVNPGERLSATQ 252
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
626-863 5.00e-29

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called Doublecortin-like and CAM kinase-like 3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL3 (or DCAMKL3) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. DCKL3 contains a single DCX domain (instead of a tandem) and a C-terminal kinase domain with similarity to CAMKs. It has been shown to interact with tubulin and JIP1/2. The DCKL3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 116.97  E-value: 5.00e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEveslMCEKRILAaVTSAGHPFLVNLFGCFQTPEHVCFVMEYSA 705
Cdd:cd14185   7 TIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKED----MIESEILI-IKSLSHPNIVKLFEVYETEKEIYLILEYVR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 706 GGDLMLHIHSDV-FSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLD----NLLLDTEGYVKIADFGLCKEGMGygdRTST 780
Cdd:cd14185  82 GGDLFDAIIESVkFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPEnllvQHNPDKSTTLKLADFGLAKYVTG---PIFT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 781 FCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPF--PGDDEEEVFDSIVNDEVRY-PRF---LSAEAIGIMRR 854
Cdd:cd14185 159 VCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFrsPERDQEELFQIIQLGHYEFlPPYwdnISEAAKDLISR 238

                ....*....
gi 47132591 855 LLRRNPERR 863
Cdd:cd14185 239 LLVVDPEKR 247
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
627-864 5.09e-29

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 117.68  E-value: 5.09e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEveslMCEKRIlAAVTSAGHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd14169  11 LGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKEA----MVENEI-AVLRRINHENIVSLEDIYESPTHLYLAMELVTG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLMLHI-HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDT---EGYVKIADFGLCKegMGYGDRTSTFC 782
Cdd:cd14169  86 GELFDRIiERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATpfeDSKIMISDFGLSK--IEAQGMLSTAC 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 783 GTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRY--PRF--LSAEAIGIMRRLLRR 858
Cdd:cd14169 164 GTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILKAEYEFdsPYWddISESAKDFIRHLLER 243

                ....*.
gi 47132591 859 NPERRL 864
Cdd:cd14169 244 DPEKRF 249
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
619-821 8.07e-29

Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 and MEKK1 by acting as a MAPK kinase kinase kinase. Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 116.21  E-value: 8.07e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALK-KGDIvardevESLMCEKRILAAVTSaghPFLVNLFGCFQTPEHV 697
Cdd:cd06612   3 EVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPvEEDL------QEIIKEISILKQCDS---PYIVKYYGSYFKNTDL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 698 CFVMEYSAGG---DLMlHIHSDVFSEPR--AIFYSacVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGM 772
Cdd:cd06612  74 WIVMEYCGAGsvsDIM-KITNKTLTEEEiaAILYQ--TLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLT 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 47132591 773 GYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPF 821
Cdd:cd06612 151 DTMAKRNTVIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPY 199
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
627-863 1.25e-28

Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of plant MAPK kinase kinases (MAPKKKs) including Arabidopsis thaliana MEKK1 and MAPKKK3. Arabidopsis thaliana MEKK1 activates MPK4, a MAPK that regulates systemic acquired resistance. MEKK1 also participates in the regulation of temperature-sensitive and tissue-specific cell death. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The plant MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 115.96  E-value: 1.25e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKG--DIVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFVMEYS 704
Cdd:cd06632   8 LGSGSFGSVYEGFNGDTGDFFAVKEVSLVddDKKSRESVKQLEQEIALLSKLR---HPNIVQYYGTEREEDNLYIFLEYV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 705 AGGDLMLHIHS-DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYgDRTSTFCG 783
Cdd:cd06632  85 PGGSIHKLLQRyGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVEAF-SFAKSFKG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 784 TPEFLAPEVLT--DTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEV--RYPRFLSAEAIGIMRRLLRRN 859
Cdd:cd06632 164 SPYWMAPEVIMqkNSGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGNSGElpPIPDHLSPDAKDFIRLCLQRD 243

                ....
gi 47132591 860 PERR 863
Cdd:cd06632 244 PEDR 247
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
621-868 4.96e-28

Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK33 is highly expressed in the testis and is present in low levels in most tissues. It may be involved in spermatogenesis and organ ontogenesis. It interacts with and phosphorylates vimentin and may be involved in regulating intermediate filament cytoskeletal dynamics. Its role in promoting the cell viability of KRAS-dependent cancer cells is under debate; some studies have found STK33 to promote cancer cell viability, while other studies have found it to be non-essential. KRAS is the most commonly mutated human oncogene, thus, studies on the role of STK33 in KRAS mutant cancer cells are important. The STK33 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 114.18  E-value: 4.96e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKalkkgdIVARDEVESL---MCEKRIlAAVTSAGHPFLVNLFGCFQTPEHV 697
Cdd:cd14097   3 YTFGRKLGQGSFGVVIEATHKETQTKWAIK------KINREKAGSSavkLLEREV-DILKHVNHAHIIHLEEVFETPKRM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 698 CFVMEYSAGGDL-MLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYR-------DLKLDNLLLDTEGYVKIADFGLCK 769
Cdd:cd14097  76 YLVMELCEDGELkELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRdlkleniLVKSSIIDNNDKLNIKVTDFGLSV 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 770 EGMGYG-DRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRF----L 844
Cdd:cd14097 156 QKYGLGeDMLQETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLTFTQSvwqsV 235
                       250       260
                ....*....|....*....|....
gi 47132591 845 SAEAIGIMRRLLRRNPERRLGSSE 868
Cdd:cd14097 236 SDAAKNVLQQLLKVDPAHRMTASE 259
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
627-868 6.33e-28

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 11; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek11 is involved, through direct phosphorylation, in regulating the degradation of Cdc25A (Cell Division Cycle 25 homolog A), which plays a role in cell cycle progression and in activating cyclin dependent kinases. Nek11 is activated by CHK1 (CHeckpoint Kinase 1) and may be involved in the G2/M checkpoint. Nek11 may also play a role in the S-phase checkpoint as well as in DNA replication and genotoxic stress responses. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 113.67  E-value: 6.33e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKK---GDIVARDEVESLMcEKRILAAVTsagHPFLVNLFGCFQTPEHVCFVMEY 703
Cdd:cd08222   8 LGSGNFGTVYLVSDLKATADEELKVLKEisvGELQPDETVDANR-EAKLLSKLD---HPAIVKFHDSFVEKESFCIVTEY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 704 SAGGDLMLHIHS-----DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDtEGYVKIADFGLCKEGMGYGDRT 778
Cdd:cd08222  84 CEGGDLDDKISEykksgTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLK-NNVIKVGDFGISRILMGTSDLA 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 779 STFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEV-RYPRFLSAEAIGIMRRLLR 857
Cdd:cd08222 163 TTFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEGETpSLPDKYSKELNAIYSRMLN 242
                       250
                ....*....|.
gi 47132591 858 RNPERRLGSSE 868
Cdd:cd08222 243 KDPALRPSAAE 253
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
627-880 6.97e-28

Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the subfamily include SLK, STK10 (also called LOK for Lymphocyte-Oriented Kinase), SmSLK (Schistosoma mansoni SLK), and related proteins. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It also plays a role in mediating actin reorganization. STK10 is responsible in regulating the CD28 responsive element in T cells, as well as leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. SmSLK is capable of activating the MAPK Jun N-terminal kinase (JNK) pathway in human embryonic kidney cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions. The SLK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 114.45  E-value: 6.97e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGeLFAikALKKGDIVARDEVESLMCEKRILaavTSAGHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd06611  13 LGDGAFGKVYKAQHKETG-LFA--AAKIIQIESEEELEDFMVEIDIL---SECKHPNIVGLYEAYFYENKLWILIEFCDG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 G---DLMLHIHSdVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCG 783
Cdd:cd06611  87 GaldSIMLELER-GLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKNKSTLQKRDTFIG 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 784 TPEFLAPEVL-----TDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDE---VRYPRFLSAEAIGIMRRL 855
Cdd:cd06611 166 TPYWMAPEVVacetfKDNPYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKSEpptLDQPSKWSSSFNDFLKSC 245
                       250       260
                ....*....|....*....|....*
gi 47132591 856 LRRNPERRLgsserDAEDVKKQPFF 880
Cdd:cd06611 246 LVKDPDDRP-----TAAELLKHPFV 265
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
626-880 1.18e-27

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). Each subunit has tissue-specific isoforms or splice variants. Vertebrates contain two isoforms of the gamma subunit (gamma 1 and gamma 2). The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 113.22  E-value: 1.18e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGELFAIK-----ALKKGDIVARDEVESLMCEKRILAAVtsAGHPFLVNLFGCFQTPEHVCFV 700
Cdd:cd14093  10 ILGRGVSSTVRRCIEKETGQEFAVKiiditGEKSSENEAEELREATRREIEILRQV--SGHPNIIELHDVFESPTFIFLV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGGDLMLHIHSDV-FSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEgMGYGDRTS 779
Cdd:cd14093  88 FELCRKGELFDYLTEVVtLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATR-LDEGEKLR 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 780 TFCGTPEFLAPEVL------TDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRY--PRF--LSAEAI 849
Cdd:cd14093 167 ELCGTPGYLAPEVLkcsmydNAPGYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIMEGKYEFgsPEWddISDTAK 246
                       250       260       270
                ....*....|....*....|....*....|.
gi 47132591 850 GIMRRLLRRNPERRLgsserDAEDVKKQPFF 880
Cdd:cd14093 247 DLISKLLVVDPKKRL-----TAEEALEHPFF 272
HR1_PKN3_2 cd11632
Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
133-197 1.34e-27

Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N3; PKN3, also called PKNbeta, is a serine/threonine protein kinase that is activated by the Rho family of small GTPases, preferentially by RhoC. Both PKN1 and RhoC show limited and barely detectable expression in normal tissues, but are both upregulated in cancer cells, particularly in late-stage malignancies. PKN3 has been implicated to play a role in the metastatic growth and invasiveness of cancer cells, downstream of the oncogenic phosphoinositide 3-kinase signaling network. PKN3 shares a common domain architecture with other PKNs, containing three HR1 domains, a C2 domain, and a kinase domain. In addition, PKN3 contains two proline-rich regions between its C2 and kinase domains, and has been shown to associate with SH3 domain containing proteins like GRAFs, GAP for RhoA, and Cdc42Hs. This model characterizes the second HR1 domain of PKN3. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; PKN3 binds Rho family GTPases, preferentially RhoC.


Pssm-ID: 212022  Cd Length: 74  Bit Score: 106.55  E-value: 1.34e-27
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47132591 133 RVAGLEKQLAIELKVKQGAENMIQTYSNGSTKDRKLLLTAQQMLQDSKTKIDIIRMQLRRALQAG 197
Cdd:cd11632  10 RLEALKRQLHVELKVKQGAENMIQTYSSGTSKERKLLATAQQMLQDSRTKIELLRMQIVKLEQSG 74
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
627-864 5.59e-27

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK3 mRNA is up-regulated in fibroblasts after Ras-induced senescence, and its overexpression induces both autophagy and senescence in a fibroblast cell line. ULK3, through its kinase activity, positively regulates Gli proteins, mediators of the Sonic hedgehog (Shh) signaling pathway that is implicated in tissue homeostasis maintenance and neurogenesis. It is inhibited by binding to Suppressor of Fused (Sufu). The ULK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271023 [Multi-domain]  Cd Length: 252  Bit Score: 110.84  E-value: 5.59e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLlSEFRPSG--ELFAIKALKKgDIVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFVMEYS 704
Cdd:cd14121   3 LGSGTYATVY-KAYRKSGarEVVAVKCVSK-SSLNKASTENLLTEIELLKKLK---HPHIVELKDFQWDEEHIYLIMEYC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 705 AGGDLMLHIHSDvfsepRAIFYSAC------VVLGLQFLHEHKIVYrDLKLDNLLLDTEGY---VKIADFGLCKEgMGYG 775
Cdd:cd14121  78 SGGDLSRFIRSR-----RTLPESTVrrflqqLASALQFLREHNISH-MDLKPQNLLLSSRYnpvLKLADFGFAQH-LKPN 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 776 DRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDE-VRYPRF--LSAEAIGIM 852
Cdd:cd14121 151 DEAHSLRGSPLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFASRSFEELEEKIRSSKpIEIPTRpeLSADCRDLL 230
                       250
                ....*....|..
gi 47132591 853 RRLLRRNPERRL 864
Cdd:cd14121 231 LRLLQRDPDRRI 242
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
620-863 7.72e-27

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii FA2 was discovered in a genetic screen for deflagellation-defective mutants. It is essential for basal-body/centriole-associated microtubule severing, and plays a role in cell cycle progression. No cellular function has yet been ascribed to CNK4. The Chlamydomonas reinhardtii FA2-like subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily contains FA2 and CNK4. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 110.58  E-value: 7.72e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMcEKRILAAVTsagHPFLVNLFGCFQTPEHVCF 699
Cdd:cd08529   1 DFEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDISRMSRKMREEAID-EARVLSKLN---SPYVIKYYDSFVDKGKLNI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYSAGGDLMLHIHSDV---FSEPRA--IFYSACvvLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGY 774
Cdd:cd08529  77 VMEYAENGDLHSLIKSQRgrpLPEDQIwkFFIQTL--LGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKILSDT 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 775 GDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDevRY---PRFLSAEAIGI 851
Cdd:cd08529 155 TNFAQTIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRG--KYppiSASYSQDLSQL 232
                       250
                ....*....|..
gi 47132591 852 MRRLLRRNPERR 863
Cdd:cd08529 233 IDSCLTKDYRQR 244
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
626-863 9.19e-27

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK2, also called Snk (serum-inducible kinase), functions in G1 progression, S-phase arrest, and centriole duplication. Its gene is responsive to both growth factors and cellular stress, is a transcriptional target of p53, and activates a G2-M checkpoint. The PLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 110.49  E-value: 9.19e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVA---RDEVESLMCEKRILAavtsagHPFLVNLFGCFQTPEHVCFVME 702
Cdd:cd14188   8 VLGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVSKphqREKIDKEIELHRILH------HKHVVQFYHYFEDKENIYILLE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 703 YSAGGDlMLHI--HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTST 780
Cdd:cd14188  82 YCSRRS-MAHIlkARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEPLEHRRRT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 781 FCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIvnDEVRY--PRFLSAEAIGIMRRLLRR 858
Cdd:cd14188 161 ICGTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCI--REARYslPSSLLAPAKHLIASMLSK 238

                ....*
gi 47132591 859 NPERR 863
Cdd:cd14188 239 NPEDR 243
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
621-868 1.05e-26

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2, group 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 110.07  E-value: 1.05e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVarDE-VESLMCEKRilaavtSAGHPFLVNLFGCFQTPEHVCF 699
Cdd:cd14665   2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGEKI--DEnVQREIINHR------SLRHPNIVRFKEVILTPTHLAI 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYSAGGDLMLHI-HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLL--DTEGYVKIADFGLCKEGMGYGD 776
Cdd:cd14665  74 VMEYAAGGELFERIcNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLdgSPAPRLKICDFGYSKSSVLHSQ 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 777 RTSTfCGTPEFLAPEVLTDTSYT-RAVDWWGLGVLLYEMLVGESPFPGDDEEEVF----DSIVNDEVRYPRF--LSAEAI 849
Cdd:cd14665 154 PKST-VGTPAYIAPEVLLKKEYDgKIADVWSCGVTLYVMLVGAYPFEDPEEPRNFrktiQRILSVQYSIPDYvhISPECR 232
                       250
                ....*....|....*....
gi 47132591 850 GIMRRLLRRNPERRLGSSE 868
Cdd:cd14665 233 HLISRIFVADPATRITIPE 251
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
621-882 1.49e-26

Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 110.26  E-value: 1.49e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGdiVARDEVESLMCEKRILAAVTSAGHPFLVNLFGCFQTPEHVCFV 700
Cdd:cd06917   3 YRRLELVGRGSYGAVYRGYHVKTGRVVALKVLNLD--TDDDDVSDIQKEVALLSQLKLGQPKNIIKYYGSYLKGPSLWII 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGGDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTST 780
Cdd:cd06917  81 MDYCEGGSIRTLMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQNSSKRST 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 781 FCGTPEFLAPEVLTD-TSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDevRYPRF----LSAEAIGIMRRL 855
Cdd:cd06917 161 FVGTPYWMAPEVITEgKYYDTKADIWSLGITTYEMATGNPPYSDVDALRAVMLIPKS--KPPRLegngYSPLLKEFVAAC 238
                       250       260
                ....*....|....*....|....*..
gi 47132591 856 LRRNPERRLgsserDAEDVKKQPFFRT 882
Cdd:cd06917 239 LDEEPKDRL-----SADELLKSKWIKQ 260
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
627-879 2.24e-26

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ULK4 is a functionally uncharacterized kinase that shows similarity to ATG1/ULKs. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. The ULK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270912 [Multi-domain]  Cd Length: 269  Bit Score: 109.69  E-value: 2.24e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKGDivaRDEVESlmcEKRILAAVTsagHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd14010   8 IGRGKHSVVYKGRRKGTIEFVAIKCVDKSK---RPEVLN---EVRLTHELK---HPNVLKFYEWYETSNHLWLVVEYCTG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLMLHIHSDV-FSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK---------------- 769
Cdd:cd14010  79 GDLETLLRQDGnLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLARregeilkelfgqfsde 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 770 EGMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRF-----L 844
Cdd:cd14010 159 GNVNKVSKKQAKRGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAESFTELVEKILNEDPPPPPPkvsskP 238
                       250       260       270
                ....*....|....*....|....*....|....*
gi 47132591 845 SAEAIGIMRRLLRRNPERRLgsserDAEDVKKQPF 879
Cdd:cd14010 239 SPDFKSLLKGLLEKDPAKRL-----SWDELVKHPF 268
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
627-868 3.43e-26

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 109.82  E-value: 3.43e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDeVESLMCEKRIlaaVTSAGHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd14086   9 LGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARD-HQKLEREARI---CRLLKHPNIVRLHDSISEEGFHYLVFDLVTG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLMLHIHS-DVFSEPRAifySAC---VVLGLQFLHEHKIVYRDLKLDNLLLDTE---GYVKIADFGLCKEGMGYGDRTS 779
Cdd:cd14086  85 GELFEDIVArEFYSEADA---SHCiqqILESVNHCHQNGIVHRDLKPENLLLASKskgAAVKLADFGLAIEVQGDQQAWF 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 780 TFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPR----FLSAEAIGIMRRL 855
Cdd:cd14086 162 GFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSpewdTVTPEAKDLINQM 241
                       250
                ....*....|...
gi 47132591 856 LRRNPERRLGSSE 868
Cdd:cd14086 242 LTVNPAKRITAAE 254
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
619-868 3.64e-26

Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It acts as a MAPK kinase kinase by phosphorylating ASK1, resulting in the phosphorylation of p38. SLK also plays a role in mediating actin reorganization. It is part of a microtubule-associated complex that is targeted at adhesion sites, and is required in focal adhesion turnover and in regulating cell migration. The SLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 109.35  E-value: 3.64e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDF-KFLAVLGRGHFGKVLLSEFRPSGELFAIKALkkgDIVARDEVESLMCEKRILAavtSAGHPFLVNLFGCFQTPEHV 697
Cdd:cd06643   4 EDFwEIVGELGDGAFGKVYKAQNKETGILAAAKVI---DTKSEEELEDYMVEIDILA---SCDHPNIVKLLDAFYYENNL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 698 CFVMEYSAGGDL---MLHIHSDVfSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGY 774
Cdd:cd06643  78 WILIEFCAGGAVdavMLELERPL-TEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTRT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 775 GDRTSTFCGTPEFLAPE-VLTDTSYTRAVDW----WGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDE---VRYPRFLSA 846
Cdd:cd06643 157 LQRRDSFIGTPYWMAPEvVMCETSKDRPYDYkadvWSLGVTLIEMAQIEPPHHELNPMRVLLKIAKSEpptLAQPSRWSP 236
                       250       260
                ....*....|....*....|..
gi 47132591 847 EAIGIMRRLLRRNPERRLGSSE 868
Cdd:cd06643 237 EFKDFLRKCLEKNVDARWTTSQ 258
HR1_PKN2_3 cd11635
Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
212-284 4.40e-26

Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N2; PKN2, also called PKNgamma or Protein-kinase C-related kinase 2 (PRK2), is a serine/threonine protein kinase and an effector of the small GTPase Rho/Rac. It regulates G2/M cell cycle progression and the exit from cytokinesis. It also phosphorylates hepatitis C virus (HCV) RNA polymerase and thus, plays a role in HCV RNA replication. PKN2 shares a common domain architecture with other PKNs, containing three HR1 domains, a C2 domain, and a kinase domain. In addition, PKN2 contains a proline-rich region in between its C2 and kinase domains and has been shown to associate with SH3 domain containing proteins like NCK and Grb4. This model characterizes the third HR1 domain of PKN2. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; PKN2 specifically binds to RhoA GTPase in a GTP-dependent manner. The HR1 domains of PKN2, together with its C2 domain, also facilitate the recruitment of PKN2 to primordial junctions at nascent cell-cell contacts, where it promotes junctional maturation.


Pssm-ID: 212025  Cd Length: 74  Bit Score: 102.04  E-value: 4.40e-26
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47132591 212 PDLGAVELRIEELRHHFRVEHAVAEGAKNVLRLLSAAKAPDRKAVSEAQEKLTESNQKLGLLREALERRLGEL 284
Cdd:cd11635   2 PVISPLELRMEELRHHFRIESAVAEGAKNVMKLLGSGKVTDRKALSEAQARFNESSQKLDLLKYSLEQRLNEL 74
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
620-863 9.05e-26

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek3 is primarily localized in the cytoplasm and shows no cell cycle-dependent changes in its activity. It is present in the axons of neurons and affects morphogenesis and polarity through its regulation of microtubule acetylation. Nek3 modulates the signaling of the prolactin receptor through its activation of Vav2 and contributes to prolactin-mediated motility of breast cancer cells. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 107.37  E-value: 9.05e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGdiVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCF 699
Cdd:cd08219   1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRLP--KSSSAVEDSRKEAVLLAKMK---HPNIVAFKESFEADGHLYI 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYSAGGDLMLHI---HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGD 776
Cdd:cd08219  76 VMEYCDGGDLMQKIklqRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSPGA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 777 RTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVR-YPRFLSAEAIGIMRRL 855
Cdd:cd08219 156 YACTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGSYKpLPSHYSYELRSLIKQM 235

                ....*...
gi 47132591 856 LRRNPERR 863
Cdd:cd08219 236 FKRNPRSR 243
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
627-868 1.05e-25

Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase (also called MAK-V); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HUNK/MAK-V was identified from a mammary tumor in an MMTV-neu transgenic mouse. It is required for the metastasis of c-myc-induced mammary tumors, but is not necessary for c-myc-induced primary tumor formation or normal development. It is required for HER2/neu-induced tumor formation and maintenance of the cells' tumorigenic phenotype. It is over-expressed in aggressive subsets of ovary, colon, and breast carcinomas. HUNK interacts with synaptopodin, and may also play a role in synaptic plasticity. The HUNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 107.60  E-value: 1.05e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKGDivARDE---VESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFVMEY 703
Cdd:cd14070  10 LGEGSFAKVREGLHAVTGEKVAIKVIDKKK--AKKDsyvTKNLRREGRIQQMIR---HPNITQLLDILETENSYYLVMEL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 704 SAGGDLMLHIHSDV-FSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGL--CKEGMGYGDRTST 780
Cdd:cd14070  85 CPGGNLMHRIYDKKrLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLsnCAGILGYSDPFST 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 781 FCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGD--DEEEVFDSIVNDEVR-YPRFLSAEAIGIMRRLLR 857
Cdd:cd14070 165 QCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFTVEpfSLRALHQKMVDKEMNpLPTDLSPGAISFLRSLLE 244
                       250
                ....*....|.
gi 47132591 858 RNPERRLGSSE 868
Cdd:cd14070 245 PDPLKRPNIKQ 255
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
619-863 1.06e-25

Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal STKs including Saccharomyces cerevisiae RCK1 and RCK2, Schizosaccharomyces pombe Sty1-regulated kinase 1 (Srk1), and similar proteins. RCK1, RCK2 (or Rck2p), and Srk1 are MAPK-activated protein kinases. RCK1 and RCK2 are involved in oxidative and metal stress resistance in budding yeast. RCK2 also regulates rapamycin sensitivity in both S. cerevisiae and Candida albicans. Srk1 is activated by Sty1/Spc1 and is involved in negatively regulating cell cycle progression by inhibiting Cdc25. The RCK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 108.29  E-value: 1.06e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRP-SGELFAIKALKKGDIvaRDEVESLMCEKRILAAVT---SAGHPFLVNLFGCFQTP 694
Cdd:cd14096   1 ENYRLINKIGEGAFSNVYKAVPLRnTGKPVAIKVVRKADL--SSDNLKGSSRANILKEVQimkRLSHPNIVKLLDFQESD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 695 EHVCFVMEYSAGGDLMLHI-HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYR------------------DLKLDNLLLD 755
Cdd:cd14096  79 EYYYIVLELADGGEIFHQIvRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRdikpenllfepipfipsiVKLRKADDDE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 756 TE---------------GYVKIADFGLCKegMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESP 820
Cdd:cd14096 159 TKvdegefipgvggggiGIVKLADFGLSK--QVWDSNTKTPCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFPP 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 47132591 821 FPGDDEEEVFDSIVNDEVRY--PRF--LSAEAIGIMRRLLRRNPERR 863
Cdd:cd14096 237 FYDESIETLTEKISRGDYTFlsPWWdeISKSAKDLISHLLTVDPAKR 283
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
627-863 1.08e-25

Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase or LOK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK10/LOK is also called polo-like kinase kinase 1 in Xenopus (xPlkk1). It is highly expressed in lymphocytes and is responsible in regulating leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. It plays a role in regulating the CD28 responsive element in T cells, and may also function as a regulator of polo-like kinase 1 (Plk1), a protein which is overexpressed in multiple tumor types. The STK10 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 108.20  E-value: 1.08e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALkkgDIVARDEVESLMCEKRILAavtSAGHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd06644  20 LGDGAFGKVYKAKNKETGALAAAKVI---ETKSEEELEDYMVEIEILA---TCNHPYIVKLLGAFYWDGKLWIMIEFCPG 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GD---LMLHIHSDVfSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCG 783
Cdd:cd06644  94 GAvdaIMLELDRGL-TEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSAKNVKTLQRRDSFIG 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 784 TPEFLAPEV-----LTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDE---VRYPRFLSAEAIGIMRRL 855
Cdd:cd06644 173 TPYWMAPEVvmcetMKDTPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEpptLSQPSKWSMEFRDFLKTA 252

                ....*...
gi 47132591 856 LRRNPERR 863
Cdd:cd06644 253 LDKHPETR 260
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
627-879 2.32e-25

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 106.39  E-value: 2.32e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKrilaavtSAGHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd14662   8 IGSGNFGVARLMRNKETKELVAVKYIERGLKIDENVQREIINHR-------SLRHPNIIRFKEVVLTPTHLAIVMEYAAG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLMLHIHS-DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLL--DTEGYVKIADFGLCKEGMGYGDRTSTfCG 783
Cdd:cd14662  81 GELFERICNaGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLdgSPAPRLKICDFGYSKSSVLHSQPKST-VG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 784 TPEFLAPEVLTDTSYT-RAVDWWGLGVLLYEMLVGESPFPGDDEEEVF----DSIVNDEVRYPRF--LSAEAIGIMRRLL 856
Cdd:cd14662 160 TPAYIAPEVLSRKEYDgKVADVWSCGVTLYVMLVGAYPFEDPDDPKNFrktiQRIMSVQYKIPDYvrVSQDCRHLLSRIF 239
                       250       260
                ....*....|....*....|...
gi 47132591 857 RRNPERRLGSSErdaedVKKQPF 879
Cdd:cd14662 240 VANPAKRITIPE-----IKNHPW 257
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
627-863 5.05e-25

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek1 is associated with centrosomes throughout the cell cycle. It is involved in the formation of primary cilium and in the maintenance of centrosomes. It cycles through the nucleus and may be capable of relaying signals between the cilium and the nucleus. Nek1 is implicated in the development of polycystic kidney disease, which is characterized by benign polycystic tumors formed by abnormal overgrowth of renal epithelial cells. It appears also to be involved in DNA damage response, and may be important for both correct DNA damage checkpoint activation and DNA repair. Nek1 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 105.28  E-value: 5.05e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESlmceKRILAAVTSAGHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd08218   8 IGEGSFGKALLVKSKEDGKQYVIKEINISKMSPKEREES----RKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDYCDG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLMLHIHSD---VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCG 783
Cdd:cd08218  84 GDLYKRINAQrgvLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVLNSTVELARTCIG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 784 TPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPF-PGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNPER 862
Cdd:cd08218 164 TPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFeAGNMKNLVLKIIRGSYPPVPSRYSYDLRSLVSQLFKRNPRD 243

                .
gi 47132591 863 R 863
Cdd:cd08218 244 R 244
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
621-863 6.09e-25

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The specific function of Nek5 is unknown. Nek5 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 105.04  E-value: 6.09e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARdEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFV 700
Cdd:cd08225   2 YEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVK-EKEASKKEVILLAKMK---HPNIVTFFASFQENGRLFIV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGGDLMLHI---HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYV-KIADFGLCKEGMGYGD 776
Cdd:cd08225  78 MEYCDGGDLMKRInrqRGVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGIARQLNDSME 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 777 RTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVR--YPRFlSAEAIGIMRR 854
Cdd:cd08225 158 LAYTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQGYFApiSPNF-SRDLRSLISQ 236

                ....*....
gi 47132591 855 LLRRNPERR 863
Cdd:cd08225 237 LFKVSPRDR 245
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
626-825 8.34e-25

Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Mammals have four MLKs (MLK1-4), mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 104.78  E-value: 8.34e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRpsGELFAIKALKK-GDIVARDEVESLMCEKRILAAVTsagHPFLVNLFG-CFQTPeHVCFVMEY 703
Cdd:cd14061   1 VIGVGGFGKVYRGIWR--GEEVAVKAARQdPDEDISVTLENVRQEARLFWMLR---HPNIIALRGvCLQPP-NLCLVMEY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 704 SAGGDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHK---IVYRD--------LKLDNLLLDTEGYVKIADFGLCKEgM 772
Cdd:cd14061  75 ARGGALNRVLAGRKIPPHVLVDWAIQIARGMNYLHNEApvpIIHRDlkssniliLEAIENEDLENKTLKITDFGLARE-W 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 47132591 773 GYGDRTSTfCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDD 825
Cdd:cd14061 154 HKTTRMSA-AGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPYKGID 205
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
626-868 8.75e-25

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK3 (or MYLK3) phosphorylates myosin regulatory light chain 2 and controls the contraction of cardiac muscles. It is expressed specifically in both the atrium and ventricle of the heart and its expression is regulated by the cardiac protein Nkx2-5. MLCK3 plays an important role in cardiogenesis by regulating the assembly of cardiac sarcomeres, the repeating contractile unit of striated muscle. MLCK3 contains a single kinase domain near the C-terminus and a unique N-terminal half, and unlike MLCK1/2, it does not appear to be regulated by Ca2+/calmodulin. The MLCK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 104.66  E-value: 8.75e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVeslmceKRILAAVTSAGHPFLVNLFGCFQTPEHVCFVMEYSA 705
Cdd:cd14192  11 VLGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKEREEV------KNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVD 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 706 GGDLMLHIHSDVF--SEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNL--LLDTEGYVKIADFGLCKEGMGYGDRTSTF 781
Cdd:cd14192  85 GGELFDRITDESYqlTELDAILFTRQICEGVHYLHQHYILHLDLKPENIlcVNSTGNQIKIIDFGLARRYKPREKLKVNF 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 782 cGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYP----RFLSAEAIGIMRRLLR 857
Cdd:cd14192 165 -GTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNCKWDFDaeafENLSEEAKDFISRLLV 243
                       250
                ....*....|.
gi 47132591 858 RNPERRLGSSE 868
Cdd:cd14192 244 KEKSCRMSATQ 254
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
619-820 9.95e-25

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 105.02  E-value: 9.95e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALkkgDI-VARDEVESLMCEKRILAAVTSaghPFLVNLFGCFQTPEHV 697
Cdd:cd06609   1 ELFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVI---DLeEAEDEIEDIQQEIQFLSQCDS---PYITKYYGSFLKGSKL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 698 CFVMEYSAGG---DLMLhihSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGY 774
Cdd:cd06609  75 WIIMEYCGGGsvlDLLK---PGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGQLTST 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 47132591 775 GDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESP 820
Cdd:cd06609 152 MSKRNTFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPP 197
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
625-879 1.06e-24

Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Schizosaccharomyces pombe Byr2, Saccharomyces cerevisiae and Cryptococcus neoformans Ste11, and related proteins. They contain an N-terminal SAM (sterile alpha-motif) domain, which mediates protein-protein interaction, and a C-terminal catalytic domain. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Byr2 is regulated by Ras1. It responds to pheromone signaling and controls mating through the MAPK pathway. Budding yeast Ste11 functions in MAPK cascades that regulate mating, high osmolarity glycerol, and filamentous growth responses. The Byr2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 104.54  E-value: 1.06e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 625 AVLGRGHFGKVLLSEFRPSGELFAIKALK------KGDIVARDEVESLmceKRILAAVTSAGHPFLVNLFGCFQTPEHVC 698
Cdd:cd06628   6 ALIGSGSFGSVYLGMNASSGELMAVKQVElpsvsaENKDRKKSMLDAL---QREIALLRELQHENIVQYLGSSSDANHLN 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGGDL--MLHIHSDvFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKE------ 770
Cdd:cd06628  83 IFLEYVPGGSVatLLNNYGA-FEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKKleansl 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 771 GMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDE-EEVFDSIVNDEVRYPRFLSAEAI 849
Cdd:cd06628 162 STKNNGARPSLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFPDCTQmQAIFKIGENASPTIPSNISSEAR 241
                       250       260       270
                ....*....|....*....|....*....|
gi 47132591 850 GIMRRLLRRNPERRlgsseRDAEDVKKQPF 879
Cdd:cd06628 242 DFLEKTFEIDHNKR-----PTADELLKHPF 266
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
621-880 1.17e-24

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 103.85  E-value: 1.17e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDI---VARDEVESLmceKRILAAVtsaGHPFLVNLFGCFQTPE-- 695
Cdd:cd05118   1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFRhpkAALREIKLL---KHLNDVE---GHPNIVKLLDVFEHRGgn 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 696 HVCFVMEYsAGGDL--MLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYR-DLKLDNLLLDTEGYVKIADFGLCKEgm 772
Cdd:cd05118  75 HLCLVFEL-MGMNLyeLIKDYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRdLKPENILINLELGQLKLADFGLARS-- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 773 gYGDRTST-FCGTPEFLAPEV-LTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVndEVRYPRflsaEAIG 850
Cdd:cd05118 152 -FTSPPYTpYVATRWYRAPEVlLGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIV--RLLGTP----EALD 224
                       250       260       270
                ....*....|....*....|....*....|
gi 47132591 851 IMRRLLRRNPERRLgsserDAEDVKKQPFF 880
Cdd:cd05118 225 LLSKMLKYDPAKRI-----TASQALAHPYF 249
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
630-880 1.22e-24

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 104.55  E-value: 1.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  630 GHFGKVLLSEFRPSGELFAIKALKKgDIVARDE--VESLMcekrilaavtsAGHPFLVNLFGCFQTPEHVCFVMEYSAGG 707
Cdd:PHA03390  27 GKFGKVSVLKHKPTQKLFVQKIIKA-KNFNAIEpmVHQLM-----------KDNPNFIKLYYSVTTLKGHVLIMDYIKDG 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  708 DL--MLHiHSDVFSEPRAIFYSACVVLGLQFLHEHKIV----------YRDLKLDnllldtegyVKIADFGLCK-EGMgy 774
Cdd:PHA03390  95 DLfdLLK-KEGKLSEAEVKKIIRQLVEALNDLHKHNIIhndiklenvlYDRAKDR---------IYLCDYGLCKiIGT-- 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  775 gdrTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEV-FDSIvndEVRY------PRFLSAE 847
Cdd:PHA03390 163 ---PSCYDGTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKEDEDEELdLESL---LKRQqkklpfIKNVSKN 236
                        250       260       270
                 ....*....|....*....|....*....|...
gi 47132591  848 AIGIMRRLLRRNPERRLgsseRDAEDVKKQPFF 880
Cdd:PHA03390 237 ANDFVQSMLKYNINYRL----TNYNEIIKHPFL 265
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
626-865 1.44e-24

Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SIKs are part of a complex network that regulates Na,K-ATPase to maintain sodium homeostasis and blood pressure. Vertebrates contain three forms of SIKs (SIK1-3) from three distinct genes, which display tissue-specific effects. SIK1, also called SNF1LK, controls steroidogenic enzyme production in adrenocortical cells. In the brain, both SIK1 and SIK2 regulate energy metabolism. SIK2, also called QIK or SNF1LK2, is involved in the regulation of gluconeogenesis in the liver and lipogenesis in adipose tissues, where it phosphorylates the insulin receptor substrate-1. In the liver, SIK3 (also called QSK) regulates cholesterol and bile acid metabolism. In addition, SIK2 plays an important role in the initiation of mitosis and regulates the localization of C-Nap1, a centrosome linker protein. The SIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 104.01  E-value: 1.44e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGELFAIKALKKGDIvARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFVMEYSA 705
Cdd:cd14071   7 TIGKGNFAVVKLARHRITKTEVAIKIIDKSQL-DEENLKKIYREVQIMKMLN---HPHIIKLYQVMETKDMLYLVTEYAS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 706 GGDLMLHIHSD-VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLckeGMGY--GDRTSTFC 782
Cdd:cd14071  83 NGEIFDYLAQHgRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGF---SNFFkpGELLKTWC 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 783 GTPEFLAPEVLTDTSYT-RAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNPE 861
Cdd:cd14071 160 GSPPYAAPEVFEGKEYEgPQLDIWSLGVVLYVLVCGALPFDGSTLQTLRDRVLSGRFRIPFFMSTDCEHLIRRMLVLDPS 239

                ....
gi 47132591 862 RRLG 865
Cdd:cd14071 240 KRLT 243
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
627-841 2.15e-24

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinases 12 and 13; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K12 is also called MAPK upstream kinase (MUK), dual leucine zipper-bearing kinase (DLK) or leucine-zipper protein kinase (ZPK). It is involved in the c-Jun N-terminal kinase (JNK) pathway that directly regulates axonal regulation through the phosphorylation of microtubule-associated protein 1B (MAP1B). It also regulates the differentiation of many cell types including adipocytes and may play a role in adipogenesis. MAP3K13, also called leucine zipper-bearing kinase (LZK), directly phosphorylates and activates MKK7, which in turn activates the JNK pathway. It also activates NF-kB through IKK activation and this activity is enhanced by antioxidant protein-1 (AOP-1). MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAP2Ks (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K12/13 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270961 [Multi-domain]  Cd Length: 237  Bit Score: 102.96  E-value: 2.15e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRpsGELFAIKALkkgdivaRDEVESLMCEKRILaavtsaGHPFLVNLFG-CFQTPEHvCFVMEYSA 705
Cdd:cd14059   1 LGSGAQGAVFLGKFR--GEEVAVKKV-------RDEKETDIKHLRKL------NHPNIIKFKGvCTQAPCY-CILMEYCP 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 706 GGDLMLHIHSDVFSEPRAIF-YSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEgmgYGDRTS--TFC 782
Cdd:cd14059  65 YGQLYEVLRAGREITPSLLVdWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKE---LSEKSTkmSFA 141
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 47132591 783 GTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYP 841
Cdd:cd14059 142 GTVAWMAPEVIRNEPCSEKVDIWSFGVVLWELLTGEIPYKDVDSSAIIWGVGSNSLQLP 200
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
626-863 2.57e-24

Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They contain N-terminal cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. The PKD subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 103.26  E-value: 2.57e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEvESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFVMEySA 705
Cdd:cd14082  10 VLGSGQFGIVYGGKHRKTGRDVAIKVIDKLRFPTKQE-SQLRNEVAILQQLS---HPGVVNLECMFETPERVFVVME-KL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 706 GGDLMLHIHSDV---FSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEG---YVKIADFGLCKEgMGYGDRTS 779
Cdd:cd14082  85 HGDMLEMILSSEkgrLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEpfpQVKLCDFGFARI-IGEKSFRR 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 780 TFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFpgDDEEEVFDSIVNDEVRYPR----FLSAEAIGIMRRL 855
Cdd:cd14082 164 SVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF--NEDEDINDQIQNAAFMYPPnpwkEISPDAIDLINNL 241

                ....*...
gi 47132591 856 LRRNPERR 863
Cdd:cd14082 242 LQVKMRKR 249
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
621-863 2.76e-24

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 103.02  E-value: 2.76e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKalkkgdIVARDEVESLMCEK---RILAAVTSAGHPFLVNLFGCFQ-TPEH 696
Cdd:cd14164   2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIK------IVDRRRASPDFVQKflpRELSILRRVNHPNIVQMFECIEvANGR 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 697 VCFVMEySAGGDLMLHIHSDVF---SEPRAIFysACVVLGLQFLHEHKIVYRDLKLDNLLLDTEG-YVKIADFGLCKEGM 772
Cdd:cd14164  76 LYIVME-AAATDLLQKIQEVHHipkDLARDMF--AQMVGAVNYLHDMNIVHRDLKCENILLSADDrKIKIADFGFARFVE 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 773 GYGDRTSTFCGTPEFLAPEVLTDTSY-TRAVDWWGLGVLLYEMLVGESPFPGDDEEEVfdSIVNDEVRYPRFLSAE--AI 849
Cdd:cd14164 153 DYPELSTTFCGSRAYTPPEVILGTPYdPKKYDVWSLGVVLYVMVTGTMPFDETNVRRL--RLQQRGVLYPSGVALEepCR 230
                       250
                ....*....|....
gi 47132591 850 GIMRRLLRRNPERR 863
Cdd:cd14164 231 ALIRTLLQFNPSTR 244
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
618-864 3.87e-24

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. DAPK2 is also called DAPK-related protein 1 (DRP-1), while DAPK3 has also been named DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk). These proteins are ubiquitously expressed in adult tissues, are capable of cross talk with each other, and may act synergistically in regulating cell death. The DAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 102.95  E-value: 3.87e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 618 LEDF-KFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDI------VARDEVESlmcEKRILAAVTsagHPFLVNLFGC 690
Cdd:cd14105   3 VEDFyDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSkasrrgVSREDIER---EVSILRQVL---HPNIITLHDV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 691 FQTPEHVCFVMEYSAGGDLMLHI-HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEG----YVKIADF 765
Cdd:cd14105  77 FENKTDVVLILELVAGGELFDFLaEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNvpipRIKLIDF 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 766 GLCKEgMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVN-----DEvRY 840
Cdd:cd14105 157 GLAHK-IEDGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAvnydfDD-EY 234
                       250       260
                ....*....|....*....|....
gi 47132591 841 PRFLSAEAIGIMRRLLRRNPERRL 864
Cdd:cd14105 235 FSNTSELAKDFIRQLLVKDPRKRM 258
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
621-868 4.20e-24

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK1, also called CaMKK alpha, is involved in the regulation of glucose uptake in skeletal muscles, independently of AMPK and PKB activation. It also play roles in learning and memory. Studies on CaMKK1 knockout mice reveal deficits in fear conditioning. The CaMKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 103.49  E-value: 4.20e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVAR-----------------DEVESLMCEKRI---LAAVTSAG 680
Cdd:cd14200   2 YKLQSEIGKGSYGVVKLAYNESDDKYYAMKVLSKKKLLKQygfprrppprgskaaqgEQAKPLAPLERVyqeIAILKKLD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 681 HPFLVNLFGCFQTP--EHVCFVMEYSAGGDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEG 758
Cdd:cd14200  82 HVNIVKLIEVLDDPaeDNLYMVFDLLRKGPVMEVPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDDG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 759 YVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTDTSYT---RAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVN 835
Cdd:cd14200 162 HVKIADFGVSNQFEGNDALLSSTAGTPAFMAPETLSDSGQSfsgKALDVWAMGVTLYCFVYGKCPFIDEFILALHNKIKN 241
                       250       260       270
                ....*....|....*....|....*....|....*
gi 47132591 836 DEVRYPR--FLSAEAIGIMRRLLRRNPERRLGSSE 868
Cdd:cd14200 242 KPVEFPEepEISEELKDLILKMLDKNPETRITVPE 276
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
625-863 5.41e-24

Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MEKK3, MEKK2, and related proteins; all contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKK) that activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270795 [Multi-domain]  Cd Length: 260  Bit Score: 102.43  E-value: 5.41e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 625 AVLGRGHFGKVLLSEFRPSGELFAIKALKKGDI--VARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFVME 702
Cdd:cd06625   6 KLLGQGAFGQVYLCYDADTGRELAVKQVEIDPIntEASKEVKALECEIQLLKNLQ---HERIVQYYGCLQDEKSLSIFME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 703 YSAGGDLMLHIHS-DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK--EGMGYGDRTS 779
Cdd:cd06625  83 YMPGGSVKDEIKAyGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASKrlQTICSSTGMK 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 780 TFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRY--PRFLSAEAIGIMRRLLR 857
Cdd:cd06625 163 SVTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWAEFEPMAAIFKIATQPTNPqlPPHVSEDARDFLSLIFV 242

                ....*.
gi 47132591 858 RNPERR 863
Cdd:cd06625 243 RNKKQR 248
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
627-881 9.21e-24

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 101.75  E-value: 9.21e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKalkKGDIVARDEVESLMCEKRILaavTSAGHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd06648  15 IGEGSTGIVCIATDKSTGRQVAVK---KMDLRKQQRRELLFNEVVIM---RDYQHPNIVEMYSSYLVGDELWVVMEFLEG 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCGTPE 786
Cdd:cd06648  89 GALTDIVTHTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQVSKEVPRRKSLVGTPY 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 787 FLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDE---VRYPRFLSAEAIGIMRRLLRRNPERR 863
Cdd:cd06648 169 WMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIRDNEppkLKNLHKVSPRLRSFLDRMLVRDPAQR 248
                       250
                ....*....|....*...
gi 47132591 864 LgsserDAEDVKKQPFFR 881
Cdd:cd06648 249 A-----TAAELLNHPFLA 261
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
619-880 1.05e-23

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAPK, which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPKK kinase (MAPKKK or MKKK or MAP3K). There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 101.65  E-value: 1.05e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGdiVARDEVESLMCEKRILAAVTSaghPFLVNLFGCFQTPEHVC 698
Cdd:cd06605   1 DDLEYLGELGEGNGGVVSKVRHRPSGQIMAVKVIRLE--IDEALQKQILRELDVLHKCNS---PYIVGFYGAFYSEGDIS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGGDL-MLHIHSDVFSEPRAIFYSACVVLGLQFLHE-HKIVYRDLKLDNLLLDTEGYVKIADFGLckEGMGYGD 776
Cdd:cd06605  76 ICMEYMDGGSLdKILKEVGRIPERILGKIAVAVVKGLIYLHEkHKIIHRDVKPSNILVNSRGQVKLCDFGV--SGQLVDS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 777 RTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEE------EVFDSIVNDEVryPRF----LSA 846
Cdd:cd06605 154 LAKTFVGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYPPPNAKpsmmifELLSYIVDEPP--PLLpsgkFSP 231
                       250       260       270
                ....*....|....*....|....*....|....
gi 47132591 847 EAIGIMRRLLRRNPERRlgsseRDAEDVKKQPFF 880
Cdd:cd06605 232 DFQDFVSQCLQKDPTER-----PSYKELMEHPFI 260
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
626-868 1.26e-23

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. MLCK4 (or MYLK4 or SgK085) contains a single kinase domain near the C-terminus. The MLCK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 101.53  E-value: 1.26e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVEslmCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFVMEYSA 705
Cdd:cd14193  11 ILGGGRFGQVHKCEEKSSGLKLAAKIIKARSQKEKEEVK---NEIEVMNQLN---HANLIQLYDAFESRNDIVLVMEYVD 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 706 GGDLMLHIHSDVF--SEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLL--LDTEGYVKIADFGLCKEgmgYGDRTS-- 779
Cdd:cd14193  85 GGELFDRIIDENYnlTELDTILFIKQICEGIQYMHQMYILHLDLKPENILcvSREANQVKIIDFGLARR---YKPREKlr 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 780 TFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIV----NDEVRYPRFLSAEAIGIMRRL 855
Cdd:cd14193 162 VNFGTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILacqwDFEDEEFADISEEAKDFISKL 241
                       250
                ....*....|...
gi 47132591 856 LRRNPERRLGSSE 868
Cdd:cd14193 242 LIKEKSWRMSASE 254
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
619-821 1.45e-23

Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates. The OSR1 and SPAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 101.28  E-value: 1.45e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKA--LKKGDIvardEVESLMCEkriLAAVTSAGHPFLVNLFGCFQTPEH 696
Cdd:cd06610   1 DDYELIEVIGSGATAVVYAAYCLPKKEKVAIKRidLEKCQT----SMDELRKE---IQAMSQCNHPNVVSYYTSFVVGDE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 697 VCFVMEYSAGG---DLMLHIHS-DVFSEPraifySACVVL-----GLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGL 767
Cdd:cd06610  74 LWLVMPLLSGGsllDIMKSSYPrGGLDEA-----IIATVLkevlkGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGV 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 47132591 768 CKEGMGYGDRTS----TFCGTPEFLAPEVLT-DTSYTRAVDWWGLGVLLYEMLVGESPF 821
Cdd:cd06610 149 SASLATGGDRTRkvrkTFVGTPCWMAPEVMEqVRGYDFKADIWSFGITAIELATGAAPY 207
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
669-863 1.75e-23

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 105.10  E-value: 1.75e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  669 EKRILAAVTSAGhpfLVNLFGCFQTPEHVCFVMEYSAGGDLMLHIHSDV-----FSEPRA--IFYSacVVLGLQFLHEHK 741
Cdd:PTZ00267 115 ELHCLAACDHFG---IVKHFDDFKSDDKLLLIMEYGSGGDLNKQIKQRLkehlpFQEYEVglLFYQ--IVLALDEVHSRK 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  742 IVYRDLKLDNLLLDTEGYVKIADFGLCKEgmgYGDRTS-----TFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLV 816
Cdd:PTZ00267 190 MMHRDLKSANIFLMPTGIIKLGDFGFSKQ---YSDSVSldvasSFCGTPYYLAPELWERKRYSKKADMWSLGVILYELLT 266
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 47132591  817 GESPFPGDDEEEVFDSIVNDEVR-YPRFLSAEAIGIMRRLLRRNPERR 863
Cdd:PTZ00267 267 LHRPFKGPSQREIMQQVLYGKYDpFPCPVSSGMKALLDPLLSKNPALR 314
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
618-868 2.40e-23

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK2, also called CaMKK beta, is one of the most versatile CaMKs. It is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. CaMKK2 contains unique N- and C-terminal domains and a central catalytic kinase domain that is followed by a regulatory domain that bears overlapping autoinhibitory and CaM-binding regions. It can be activated by signaling through G-coupled receptors, IP3 receptors, plasma membrane ion channels, and Toll-like receptors. Thus, CaMKK2 acts as a molecular hub that is capable of receiving and decoding signals from diverse pathways. The CaMKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 101.20  E-value: 2.40e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 618 LEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKK-----------------------GDIVARDEVESLMCEKRILA 674
Cdd:cd14199   1 LNQYKLKDEIGKGSYGVVKLAYNEDDNTYYAMKVLSKkklmrqagfprrppprgaraapeGCTQPRGPIERVYQEIAILK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 675 AVTsagHPFLVNLFGCFQTP--EHVCFVMEYSAGGDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNL 752
Cdd:cd14199  81 KLD---HPNVVKLVEVLDDPseDHLYMVFELVKQGPVMEVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 753 LLDTEGYVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTDTSYT---RAVDWWGLGVLLYEMLVGESPFPGDDEEEV 829
Cdd:cd14199 158 LVGEDGHIKIADFGVSNEFEGSDALLTNTVGTPAFMAPETLSETRKIfsgKALDVWAMGVTLYCFVFGQCPFMDERILSL 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 47132591 830 FDSIVNDEVRYPRF--LSAEAIGIMRRLLRRNPERRLGSSE 868
Cdd:cd14199 238 HSKIKTQPLEFPDQpdISDDLKDLLFRMLDKNPESRISVPE 278
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
618-864 5.56e-23

The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. Twitchin and Projectin are both associated with thick filaments. Twitchin is localized in the outer parts of A-bands and is involved in regulating muscle contraction. It interacts with the myofibrillar proteins myosin and actin in a phosphorylation-dependent manner, and may be involved in regulating the myosin cross-bridge cycle. The kinase activity of Twitchen is activated by Ca2+ and the Ca2+ binding protein S100A1. Projectin is associated with the end of thick filaments and is a component of flight muscle connecting filaments. The kinase domain of Projectin may play roles in autophosphorylation and transphosphorylation, which impact the formation of myosin filaments. The Twitchin-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 99.58  E-value: 5.56e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 618 LEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVeslmceKRILAAVTSAGHPFLVNLFGCFQTPEHV 697
Cdd:cd14114   1 YDHYDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKETV------RKEIQIMNQLHHPKLINLHDAFEDDNEM 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 698 CFVMEYSAGGDLMLHIHSD--VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTE--GYVKIADFGLCKEgMG 773
Cdd:cd14114  75 VLILEFLSGGELFERIAAEhyKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKrsNEVKLIDFGLATH-LD 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 774 YGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVN-----DEVRYpRFLSAEA 848
Cdd:cd14114 154 PKESVKVTTGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKScdwnfDDSAF-SGISEEA 232
                       250
                ....*....|....*.
gi 47132591 849 IGIMRRLLRRNPERRL 864
Cdd:cd14114 233 KDFIRKLLLADPNKRM 248
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
621-880 5.72e-23

Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of human MAK and MAK-related kinase (MRK), Saccharomyces cerevisiae Ime2p, Schizosaccharomyces pombe Mei4-dependent protein 3 (Mde3) and Pit1, Caenorhabditis elegans dyf-5, Arabidopsis thaliana MHK, and similar proteins. These proteins play important roles during meiosis. MAK is highly expressed in testicular cells specifically in the meiotic phase, but is not essential for spermatogenesis and fertility. It functions as a coactivator of the androgen receptor in prostate cells. MRK, also called Intestinal Cell Kinase (ICK), is expressed ubiquitously, with highest expression in the ovary and uterus. A missense mutation in MRK causes endocrine-cerebro-osteodysplasia, suggesting that this protein plays an important role in the development of many organs. MAK and MRK may be involved in regulating cell cycle and cell fate. Ime2p is a meiosis-specific kinase that is important during meiotic initiation and during the later stages of meiosis. Mde3 functions downstream of the transcription factor Mei-4 which is essential for meiotic prophase I. The MAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 99.92  E-value: 5.72e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKK-----GDIVARDEVESLMcekrilaAVTSagHPFLVNLFGCFQTPE 695
Cdd:cd07830   1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKMKKkfyswEECMNLREVKSLR-------KLNE--HPNIVKLKEVFREND 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 696 HVCFVMEYSAGG--DLMLHIHSDVFSEP--RAIFYSacVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEG 771
Cdd:cd07830  72 ELYFVFEYMEGNlyQLMKDRKGKPFSESviRSIIYQ--ILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLAREI 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 772 MGYGDRTsTFCGTPEFLAPEV-LTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIV-------NDE------ 837
Cdd:cd07830 150 RSRPPYT-DYVSTRWYRAPEIlLRSTSYSSPVDIWALGCIMAELYTLRPLFPGSSEIDQLYKICsvlgtptKQDwpegyk 228
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 838 ------VRYPRFL-----------SAEAIGIMRRLLRRNPERRLgsserDAEDVKKQPFF 880
Cdd:cd07830 229 lasklgFRFPQFAptslhqlipnaSPEAIDLIKDMLRWDPKKRP-----TASQALQHPYF 283
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
627-864 7.45e-23

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. It is Ca2+/calmodulin (CaM)-regulated and actin-associated protein that contains an N-terminal kinase domain followed by an autoinhibitory CaM binding region and a large C-terminal extension with multiple functional domains including ankyrin (ANK) repeats, a cytoskeletal binding domain, a Death domain, and a serine-rich tail. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. The DAPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 99.32  E-value: 7.45e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKGDI------VARDEVESlmcEKRILAAVTsagHPFLVNLFGCFQTPEHVCFV 700
Cdd:cd14194  13 LGSGQFAVVKKCREKSTGLQYAAKFIKKRRTkssrrgVSREDIER---EVSILKEIQ---HPNVITLHEVYENKTDVILI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGGDLMLHI-HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGY----VKIADFGLCKEgMGYG 775
Cdd:cd14194  87 LELVAGGELFDFLaEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVpkprIKIIDFGLAHK-IDFG 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 776 DRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSI--VNDEVRYPRFLSAEAIG--I 851
Cdd:cd14194 166 NEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVsaVNYEFEDEYFSNTSALAkdF 245
                       250
                ....*....|...
gi 47132591 852 MRRLLRRNPERRL 864
Cdd:cd14194 246 IRRLLVKDPKKRM 258
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
626-879 1.28e-22

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase signal-integrating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 99.03  E-value: 1.28e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVAR----DEVESL-MCekrilaavtsAGHPFLVNLFGCFQTPEHVCFV 700
Cdd:cd14090   9 LLGEGAYASVQTCINLYTGKEYAVKIIEKHPGHSRsrvfREVETLhQC----------QGHPNILQLIEYFEDDERFYLV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGGDLMLHIHSDV-FSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYV---KIADFGL---CKEGMG 773
Cdd:cd14090  79 FEKMRGGPLLSHIEKRVhFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKVspvKICDFDLgsgIKLSST 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 774 YGD-----RTSTFCGTPEFLAPEVL-----TDTSYTRAVDWWGLGVLLYEMLVGESPFPG---------------DDEEE 828
Cdd:cd14090 159 SMTpvttpELLTPVGSAEYMAPEVVdafvgEALSYDKRCDLWSLGVILYIMLCGYPPFYGrcgedcgwdrgeacqDCQEL 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 47132591 829 VFDSIVNDEVRYPR----FLSAEAIGIMRRLLRRNPERRLgsserDAEDVKKQPF 879
Cdd:cd14090 239 LFHSIQEGEYEFPEkewsHISAEAKDLISHLLVRDASQRY-----TAEQVLQHPW 288
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
619-879 1.67e-22

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 98.18  E-value: 1.67e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVesLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVC 698
Cdd:cd14184   1 EKYKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEHL--IENEVSILRRVK---HPNIIMLIEEMDTPAELY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGGDLMLHIHSDV-FSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDN----LLLDTEGYVKIADFGLCK--EG 771
Cdd:cd14184  76 LVMELVKGGDLFDAITSSTkYTERDASAMVYNLASALKYLHGLCIVHRDIKPENllvcEYPDGTKSLKLGDFGLATvvEG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 772 MGYgdrtsTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDD--EEEVFDSIVNDEVRYPR----FLS 845
Cdd:cd14184 156 PLY-----TVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENnlQEDLFDQILLGKLEFPSpywdNIT 230
                       250       260       270
                ....*....|....*....|....*....|....
gi 47132591 846 AEAIGIMRRLLRRNPERRLgsserDAEDVKKQPF 879
Cdd:cd14184 231 DSAKELISHMLQVNVEARY-----TAEQILSHPW 259
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
619-821 1.78e-22

N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class III myosins are motor proteins with an N-terminal kinase catalytic domain and a C-terminal actin-binding motor domain. Class III myosins are present in the photoreceptors of invertebrates and vertebrates and in the auditory hair cells of mammals. The kinase domain of myosin III can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, and can autophosphorylate the C-terminal motor domain. Myosin III may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. It may also function as a cargo carrier during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The Drosophila class III myosin, called NinaC (Neither inactivation nor afterpotential protein C), is critical in normal adaptation and termination of photoresponse. Vertebrates contain two isoforms of class III myosin, IIIA and IIIB. This subfamily also includes mammalian NIK-like embryo-specific kinase (NESK), Traf2- and Nck-interacting kinase (TNIK), and mitogen-activated protein kinase (MAPK) kinase kinase kinase 4/6. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The class III myosin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 98.53  E-value: 1.78e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALkkgDIVArDEVESLMCEKRILAAVTSagHPFLVNLFGCFQTPEHVC 698
Cdd:cd06608   6 GIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIM---DIIE-DEEEEIKLEINILRKFSN--HPNIATFYGAFIKKDPPG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 ------FVMEYSAGG---DLM--LHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGL 767
Cdd:cd06608  80 gddqlwLVMEYCGGGsvtDLVkgLRKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGV 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 47132591 768 CKEGMGYGDRTSTFCGTPEFLAPEVLT-----DTSYTRAVDWWGLGVLLYEMLVGESPF 821
Cdd:cd06608 160 SAQLDSTLGRRNTFIGTPYWMAPEVIAcdqqpDASYDARCDVWSLGITAIELADGKPPL 218
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
620-880 1.87e-22

Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CCRK was previously called p42. It is a Cyclin-Dependent Kinase (CDK)-Activating Kinase (CAK) which is essential for the activation of CDK2. It is indispensable for cell growth and has been implicated in the progression of glioblastoma multiforme. In the heart, a splice variant of CCRK with a different C-terminal half is expressed; this variant promotes cardiac cell growth and survival and is significantly down-regulated during the development of heart failure. The CCRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 98.56  E-value: 1.87e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKFLAVLGRGHFGKVLLSEFRPSGELFAIK--ALKKGDivarDEVE-SLMCEKRILAAVTsaGHPFLVNLFGCFQTPEH 696
Cdd:cd07832   1 RYKILGRIGEGAHGIVFKAKDRETGETVALKkvALRKLE----GGIPnQALREIKALQACQ--GHPYVVKLRDVFPHGTG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 697 VCFVMEYsaggdlMLHIHSDV-------FSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK 769
Cdd:cd07832  75 FVLVFEY------MLSSLSEVlrdeerpLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLAR 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 770 EGMGYGDRT-STFCGTPEFLAPEVLTDT-SYTRAVDWWGLGVLLYEMLVGESPFPGDDEEE----VFDSI-VNDEVRYPR 842
Cdd:cd07832 149 LFSEEDPRLySHQVATRWYRAPELLYGSrKYDEGVDLWAVGCIFAELLNGSPLFPGENDIEqlaiVLRTLgTPNEKTWPE 228
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47132591 843 F-------------------------LSAEAIGIMRRLLRRNPERRLGsserdAEDVKKQPFF 880
Cdd:cd07832 229 LtslpdynkitfpeskgirleeifpdCSPEAIDLLKGLLVYNPKKRLS-----AEEALRHPYF 286
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
626-868 1.88e-22

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK2 (or MYLK2) phosphorylates myosin regulatory light chain and controls the contraction of skeletal muscles. MLCK2 contains a single kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site. The MLCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 98.07  E-value: 1.88e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVeslMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFVMEYSA 705
Cdd:cd14190  11 VLGGGKFGKVHTCTEKRTGLKLAAKVINKQNSKDKEMV---LLEIQVMNQLN---HRNLIQLYEAIETPNEIVLFMEYVE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 706 GGDLMLHIHSDVF--SEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDN--LLLDTEGYVKIADFGLCKEGMGYGDRTSTF 781
Cdd:cd14190  85 GGELFERIVDEDYhlTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENilCVNRTGHQVKIIDFGLARRYNPREKLKVNF 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 782 cGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVN-----DEVRYPRfLSAEAIGIMRRLL 856
Cdd:cd14190 165 -GTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVLMgnwyfDEETFEH-VSDEAKDFVSNLI 242
                       250
                ....*....|..
gi 47132591 857 RRNPERRLGSSE 868
Cdd:cd14190 243 IKERSARMSATQ 254
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
619-868 1.96e-22

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 98.77  E-value: 1.96e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARD--EVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEH 696
Cdd:cd14094   3 DVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSSPglSTEDLKREASICHMLK---HPHIVELLETYSSDGM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 697 VCFVMEYSAGGDLMLHI-----HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLK---LDNLLLDTEGYVKIADFGLC 768
Cdd:cd14094  80 LYMVFEFMDGADLCFEIvkradAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKphcVLLASKENSAPVKLGGFGVA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 769 KEGMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGdDEEEVFDSIVNDEV----RYPRFL 844
Cdd:cd14094 160 IQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYkmnpRQWSHI 238
                       250       260
                ....*....|....*....|....
gi 47132591 845 SAEAIGIMRRLLRRNPERRLGSSE 868
Cdd:cd14094 239 SESAKDLVRRMLMLDPAERITVYE 262
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
621-868 2.09e-22

Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 98.39  E-value: 2.09e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALK-KGdivardeVESLMCEKRIlAAVTSAGHPFLVNLFGCFQTPEHVCF 699
Cdd:cd14104   2 YMIAEELGRGQFGIVHRCVETSSKKTYMAKFVKvKG-------ADQVLVKKEI-SILNIARHRNILRLHESFESHEELVM 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYSAGGDL--MLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTE--GYVKIADFGLCKEgMGYG 775
Cdd:cd14104  74 IFEFISGVDIfeRITTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRrgSYIKIIEFGQSRQ-LKPG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 776 DRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYP----RFLSAEAIGI 851
Cdd:cd14104 153 DKFRLQYTSAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEYAFDdeafKNISIEALDF 232
                       250
                ....*....|....*..
gi 47132591 852 MRRLLRRNPERRLGSSE 868
Cdd:cd14104 233 VDRLLVKERKSRMTAQE 249
HR1_PKN3_3 cd11637
Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
214-284 2.12e-22

Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N3; PKN3, also called PKNbeta, is a serine/threonine protein kinase that is activated by the Rho family of small GTPases, preferentially by RhoC. Both PKN1 and RhoC show limited and barely detectable expression in normal tissues, but are both upregulated in cancer cells, particularly in late-stage malignancies. PKN3 has been implicated to play a role in the metastatic growth and invasiveness of cancer cells, downstream of the oncogenic phosphoinositide 3-kinase signaling network. PKN3 shares a common domain architecture with other PKNs, containing three HR1 domains, a C2 domain, and a kinase domain. In addition, PKN3 contains two proline-rich regions between its C2 and kinase domains, and has been shown to associate with SH3 domain containing proteins like GRAFs, GAP for RhoA, and Cdc42Hs. This model characterizes the third HR1 domain of PKN3. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; PKN3 binds Rho family GTPases, preferentially RhoC.


Pssm-ID: 212027  Cd Length: 74  Bit Score: 91.84  E-value: 2.12e-22
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47132591 214 LGAVELRIEELRHHFRVEHAVAEGAKNVLRLLSAAKAPDRKAVSEAQEKLTESNQKLGLLREALERRLGEL 284
Cdd:cd11637   4 MSAPELRVEELRHHLRIEAAVAEGAKNVVKLLGGRRFQDRKILAEAQARLQESSQKIDLLRLSLERCLAAL 74
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
681-881 2.20e-22

Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group I PAKs, also called conventional PAKs, include PAK1, PAK2, and PAK3. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). They interact with the SH3 domain containing proteins Nck, Grb2 and PIX. Binding of group I PAKs to activated GTPases leads to conformational changes that destabilize the AID, allowing autophosphorylation and full activation of the kinase domain. Known group I PAK substrates include MLCK, Bad, Raf, MEK1, LIMK, Merlin, Vimentin, Myc, Stat5a, and Aurora A, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 97.69  E-value: 2.20e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 681 HPFLVNLFGCFQTPEHVCFVMEYSAGGDLmlhihSDVFSEP---RAIFYSAC--VVLGLQFLHEHKIVYRDLKLDNLLLD 755
Cdd:cd06647  63 NPNIVNYLDSYLVGDELWVVMEYLAGGSL-----TDVVTETcmdEGQIAAVCreCLQALEFLHSNQVIHRDIKSDNILLG 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 756 TEGYVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVN 835
Cdd:cd06647 138 MDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIAT 217
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 47132591 836 D---EVRYPRFLSAEAIGIMRRLLRRNPERRlGSserdAEDVKKQPFFR 881
Cdd:cd06647 218 NgtpELQNPEKLSAIFRDFLNRCLEMDVEKR-GS----AKELLQHPFLK 261
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
621-873 2.95e-22

Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Pat1 (also called Ran1), Saccharomyces cerevisiae VHS1 and KSP1, and similar fungal STKs. Pat1 blocks Mei2, an RNA-binding protein which is indispensable in the initiation of meiosis. Pat1 is inactivated and Mei2 activated, which initiates meiosis, under nutrient-deprived conditions through a signaling cascade involving Ste11. Meiosis induced by Pat1 inactivation may show different characteristics than normal meiosis including aberrant positioning of centromeres. VHS1 was identified in a screen for suppressors of cell cycle arrest at the G1/S transition, while KSP1 may be involved in regulating PRP20, which is required for mRNA export and maintenance of nuclear structure. The Pat1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 97.42  E-value: 2.95e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESL----MCEKRILAAVtsAGHPFLVNLFGCFQTPEH 696
Cdd:cd13993   2 YQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLYKSGPNSKDGNDFQklpqLREIDLHRRV--SRHPNIITLHDVFETEVA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 697 VCFVMEYSAGGDLMLHIHSDVFSEP-----RAIFYSacVVLGLQFLHEHKIVYRDLKLDNLLLDT-EGYVKIADFGL-CK 769
Cdd:cd13993  80 IYIVLEYCPNGDLFEAITENRIYVGkteliKNVFLQ--LIDAVKHCHSLGIYHRDIKPENILLSQdEGTVKLCDFGLaTT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 770 EGMGYGDRtstfCGTPEFLAPEVLTDTS------YTRAVDWWGLGVLLYEMLVGESPFPGDDEEE--VFDSIVNDEVRYP 841
Cdd:cd13993 158 EKISMDFG----VGSEFYMAPECFDEVGrslkgyPCAAGDIWSLGIILLNLTFGRNPWKIASESDpiFYDYYLNSPNLFD 233
                       250       260       270
                ....*....|....*....|....*....|....
gi 47132591 842 RFL--SAEAIGIMRRLLRRNPERRlgSSERDAED 873
Cdd:cd13993 234 VILpmSDDFYNLLRQIFTVNPNNR--ILLPELQL 265
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
620-820 3.77e-22

Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAP4K3, MAP4K1, MAP4K2, MAP4K5, and related proteins. Vertebrate members contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K1, also called haematopoietic progenitor kinase 1 (HPK1), is a hematopoietic-specific STK involved in many cellular signaling cascades including MAPK, antigen receptor, apoptosis, growth factor, and cytokine signaling. It participates in the regulation of T cell receptor signaling and T cell-mediated immune responses. MAP4K2 was referred to as germinal center (GC) kinase because of its preferred location in GC B cells. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. It is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). The MAP4K3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 96.99  E-value: 3.77e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKkgdIVARDEVESLMCEKRILAavtSAGHPFLVNLFGCFQTPEHVCF 699
Cdd:cd06613   1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVIK---LEPGDDFEIIQQEISMLK---ECRHPNIVAYFGSYLRRDKLWI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYSAGGDL-MLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRT 778
Cdd:cd06613  75 VMEYCGGGSLqDIYQVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQLTATIAKR 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 47132591 779 STFCGTPEFLAPEVLT---DTSYTRAVDWWGLGVLLYEMLVGESP 820
Cdd:cd06613 155 KSFIGTPYWMAPEVAAverKGGYDGKCDIWALGITAIELAELQPP 199
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
620-863 7.53e-22

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily includes Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants prevented from entering mitosis. NIMA is essential for mitotic entry and progression through mitosis, and its degradation is essential for mitotic exit. NIMA is involved in nuclear membrane fission. Vertebrate Nek2 is a cell cycle-regulated STK, localized in centrosomes and kinetochores, that regulates centrosome splitting at the G2/M phase. It also interacts with other mitotic kinases such as Polo-like kinase 1 and may play a role in spindle checkpoint. An increase in the expression of the human NEK2 gene is strongly associated with the progression of non-Hodgkin lymphoma. Nek2 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. It The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 96.07  E-value: 7.53e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARdEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPE-HVC 698
Cdd:cd08217   1 DYEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYGKMSEK-EKQQLVSEVNILRELK---HPNIVRYYDRIVDRAnTTL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 F-VMEYSAGGDLMLHI-----HSDVFSEPRAIFYSACVVLGLQFLH-----EHKIVYRDLKLDNLLLDTEGYVKIADFGL 767
Cdd:cd08217  77 YiVMEYCEGGDLAQLIkkckkENQYIPEEFIWKIFTQLLLALYECHnrsvgGGKILHRDLKPANIFLDSDNNVKLGDFGL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 768 CKEgMGYGDR-TSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEV-RYPRFLS 845
Cdd:cd08217 157 ARV-LSHDSSfAKTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANQLELAKKIKEGKFpRIPSRYS 235
                       250
                ....*....|....*...
gi 47132591 846 AEAIGIMRRLLRRNPERR 863
Cdd:cd08217 236 SELNEVIKSMLNVDPDKR 253
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
627-868 1.34e-21

Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 95.34  E-value: 1.34e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKkgdIVARDEVESLMcEKRILAAVTsagHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd14107  10 IGRGTFGFVKRVTHKGNGECCAAKFIP---LRSSTRARAFQ-ERDILARLS---HRRLTCLLDQFETRKTLILILELCSS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLMLHIH-SDVFSEPRAIFYSACVVLGLQFLHEHKIVYR--DLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFcG 783
Cdd:cd14107  83 EELLDRLFlKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLdiKPDNILMVSPTREDIKICDFGFAQEITPSEHQFSKY-G 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 784 TPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRY--PRF--LSAEAIGIMRRLLRRN 859
Cdd:cd14107 162 SPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVVSWdtPEIthLSEDAKDFIKRVLQPD 241

                ....*....
gi 47132591 860 PERRLGSSE 868
Cdd:cd14107 242 PEKRPSASE 250
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
627-864 1.83e-21

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type IV; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKIV is found predominantly in neurons and immune cells. It is activated by the binding of calcium/CaM and phosphorylation by CaMKK (alpha or beta). The CaMKK-CaMKIV cascade participates in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors. It also is implicated in T-cell development and signaling, cytokine secretion, and signaling through Toll-like receptors, and is thus, pivotal in immune response and inflammation. The CaMKIV subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 96.05  E-value: 1.83e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKK--GDIVARDEVESLMcekrilaavtSAGHPFLVNLFGCFQTPEHVCFVMEYS 704
Cdd:cd14085  11 LGRGATSVVYRCRQKGTQKPYAVKKLKKtvDKKIVRTEIGVLL----------RLSHPNIIKLKEIFETPTEISLVLELV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 705 AGGDLMLHI-HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGY---VKIADFGLCKEgMGYGDRTST 780
Cdd:cd14085  81 TGGELFDRIvEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPdapLKIADFGLSKI-VDQQVTMKT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 781 FCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDD-EEEVFDSIVNDEVRY--PRF--LSAEAIGIMRRL 855
Cdd:cd14085 160 VCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDERgDQYMFKRILNCDYDFvsPWWddVSLNAKDLVKKL 239

                ....*....
gi 47132591 856 LRRNPERRL 864
Cdd:cd14085 240 IVLDPKKRL 248
HR1_PKN_1 cd11622
First Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
52-104 1.83e-21

First Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N; PKN, also called Protein-kinase C-related kinase (PRK), is a serine/threonine protein kinase that can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytoskeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. In some vertebrates, there are three PKN isoforms from different genes (designated PKN1, PKN2, and PKN3), which show different enzymatic properties, tissue distribution, and varied functions. PKN proteins contain three HR1 domains, a C2 domain, and a kinase domain. This model characterizes the first HR1 domain of PKN. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family.


Pssm-ID: 212012  Cd Length: 66  Bit Score: 88.86  E-value: 1.83e-21
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 47132591  52 IRKELKLKEGAENLRRATTDLgRSLGPVELLLRGSSRRLDLLHQQLQELHAHV 104
Cdd:cd11622  15 IRKELKIKEGAENLRKATTDK-KSLAHVESILKKSNRKLEDLHQELQELEAHI 66
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
619-868 2.28e-21

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL2, also called p56 KKIAMRE, is expressed in testis, kidney, lung, and brain. It functions mainly in mature neurons and plays an important role in learning and memory. Inactivation of CDKL3, also called NKIAMRE (NKIATRE in rat), by translocation is associated with mild mental retardation. It has been reported that CDKL3 is lost in leukemic cells having a chromosome arm 5q deletion, and may contribute to the transformed phenotype. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 95.57  E-value: 2.28e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDivARDEVESL-MCEKRILAAVTsagHPFLVNLFGCFQTPEHV 697
Cdd:cd07846   1 EKYENLGLVGEGSYGMVMKCRHKETGQIVAIKKFLESE--DDKMVKKIaMREIKMLKQLR---HENLVNLIEVFRRKKRW 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 698 CFVMEY---SAGGDLMLHIHSDVFSEPRAIFYSacVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGY 774
Cdd:cd07846  76 YLVFEFvdhTVLDDLEKYPNGLDESRVRKYLFQ--ILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 775 GDRTSTFCGTPEFLAPEVLT-DTSYTRAVDWWGLGVLLYEMLVGESPFPGDDE------------------EEVF----- 830
Cdd:cd07846 154 GEVYTDYVATRWYRAPELLVgDTKYGKAVDVWAVGCLVTEMLTGEPLFPGDSDidqlyhiikclgnliprhQELFqknpl 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 47132591 831 ---------DSIVNDEVRYPRfLSAEAIGIMRRLLRRNPERRLGSSE 868
Cdd:cd07846 234 fagvrlpevKEVEPLERRYPK-LSGVVIDLAKKCLHIDPDKRPSCSE 279
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
681-879 3.53e-21

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 93.97  E-value: 3.53e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 681 HPFLVNLFGCFQTPEHVCFVMEYSAGGDLMLHIHSD-VFSEPRAIFYSACVVLGLQFLHEHKIVYR---------DLKLD 750
Cdd:cd14120  51 HENVVALLDCQETSSSVYLVMEYCNGGDLADYLQAKgTLSEDTIRVFLQQIAAAMKALHSKGIVHRdlkpqnillSHNSG 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 751 NLLLDTEGYVKIADFGLCKEGMGyGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEV- 829
Cdd:cd14120 131 RKPSPNDIRLKIADFGFARFLQD-GMMAATLCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTPQELk 209
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 47132591 830 --FDSIVNDEVRYPRFLSAEAIGIMRRLLRRNPERRLgsserDAEDVKKQPF 879
Cdd:cd14120 210 afYEKNANLRPNIPSGTSPALKDLLLGLLKRNPKDRI-----DFEDFFSHPF 256
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
627-881 3.63e-21

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK2 plays a role in pro-apoptotic signaling. It is cleaved and activated by caspases leading to morphological changes during apoptosis. PAK2 is also activated in response to a variety of stresses including DNA damage, hyperosmolarity, serum starvation, and contact inhibition, and may play a role in coordinating the stress response. PAK2 also contributes to cancer cell invasion through a mechanism distinct from that of PAK1. It belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 95.18  E-value: 3.63e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALkkgDIVARDEVESLMCEKRILAAVTSaghPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd06655  27 IGQGASGTVFTAIDVATGQEVAIKQI---NLQKQPKKELIINEILVMKELKN---PNIVNFLDSFLVGDELFVVMEYLAG 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCGTPE 786
Cdd:cd06655 101 GSLTDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPY 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 787 FLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVND---EVRYPRFLSAEAIGIMRRLLRRNPERR 863
Cdd:cd06655 181 WMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNgtpELQNPEKLSPIFRDFLNRCLEMDVEKR 260
                       250
                ....*....|....*...
gi 47132591 864 lGSserdAEDVKKQPFFR 881
Cdd:cd06655 261 -GS----AKELLQHPFLK 273
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
627-880 4.30e-21

Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 93.91  E-value: 4.30e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFG--KVLLSEFRPSGELFAIKALKKGDI--VARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEH-VCFVM 701
Cdd:cd13994   1 IGKGATSvvRIVTKKNPRSGVLYAVKEYRRRDDesKRKDYVKRLTSEYIISSKLH---HPNIVKVLDLCQDLHGkWCLVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 702 EYSAGGDLMLHIHSDV---FSEPRAIFYSacVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRT 778
Cdd:cd13994  78 EYCPGGDLFTLIEKADslsLEEKDCFFKQ--ILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAEVFGMPAEKE 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 779 STF----CGTPEFLAPEVLTDTSYT-RAVDWWGLGVLLYEMLVGESPF----PGDDEEEVFDSIVNDEVRYPRFLSAEAI 849
Cdd:cd13994 156 SPMsaglCGSEPYMAPEVFTSGSYDgRAVDVWSCGIVLFALFTGRFPWrsakKSDSAYKAYEKSGDFTNGPYEPIENLLP 235
                       250       260       270
                ....*....|....*....|....*....|....*
gi 47132591 850 GIMRRLLRR----NPERRLgsserDAEDVKKQPFF 880
Cdd:cd13994 236 SECRRLIYRmlhpDPEKRI-----TIDEALNDPWV 265
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
619-881 6.21e-21

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 and MEK2 are MAPK kinases (MAPKKs or MKKs), and are dual-specificity PKs that phosphorylate and activate the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1/2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. This cascade has also been implicated in synaptic plasticity, migration, morphological determination, and stress response immunological reactions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1/2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 94.42  E-value: 6.21e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFA-------IKALKKGDIVArdeveslmcEKRILAAVTSaghPFLVNLFGCF 691
Cdd:cd06615   1 DDFEKLGELGAGNGGVVTKVLHRPSGLIMArklihleIKPAIRNQIIR---------ELKVLHECNS---PYIVGFYGAF 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 692 QTPEHVCFVMEYSAGG--DLML----HIHSDVFSEpraifYSACVVLGLQFLHE-HKIVYRDLKLDNLLLDTEGYVKIAD 764
Cdd:cd06615  69 YSDGEISICMEHMDGGslDQVLkkagRIPENILGK-----ISIAVLRGLTYLREkHKIMHRDVKPSNILVNSRGEIKLCD 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 765 FGLckEGMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEE----------------- 827
Cdd:cd06615 144 FGV--SGQLIDSMANSFVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGRYPIPPPDAKeleamfgrpvsegeake 221
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47132591 828 -------------------EVFDSIVNDEV-RYP-RFLSAEAIGIMRRLLRRNPERRLgsserDAEDVKKQPFFR 881
Cdd:cd06615 222 shrpvsghppdsprpmaifELLDYIVNEPPpKLPsGAFSDEFQDFVDKCLKKNPKERA-----DLKELTKHPFIK 291
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
627-863 8.93e-21

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP kinases serve as essential sensors of cellular stress. They are involved in regulating NF-kappaB and MAPK signaling, and are implicated in mediating cellular processes such as apoptosis, necroptosis, differentiation, and survival. RIP kinases contain a homologous N-terminal kinase domain and varying C-terminal domains. Higher vertebrates contain multiple RIP kinases, with mammals harboring at least five members. RIP1 and RIP2 harbor C-terminal domains from the Death domain (DD) superfamily while RIP4 contains ankyrin (ANK) repeats. RIP3 contain a RIP homotypic interaction motif (RHIM) that facilitates binding to RIP1. RIP1 and RIP3 are important in apoptosis and necroptosis, while RIP2 and RIP4 play roles in keratinocyte differentiation and inflammatory immune responses. The RIP subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 92.90  E-value: 8.93e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKGDiVARDEVESLMCEKRILaavTSAGHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd13978   1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSP-NCIEERKALLKEAEKM---ERARHSYVLPLLGVCVERRSLGLVMEYMEN 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLMLHIHSDVFSEPRAIFYSAC--VVLGLQFLH--EHKIVYRDLKLDNLLLDTEGYVKIADFGLCK-----EGMGYGDR 777
Cdd:cd13978  77 GSLKSLLEREIQDVPWSLRFRIIheIALGMNFLHnmDPPLLHHDLKPENILLDNHFHVKISDFGLSKlgmksISANRRRG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 778 TSTFCGTPEFLAPEVLTDTSY--TRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIV--------NDEVRY-PRFLSA 846
Cdd:cd13978 157 TENLGGTPIYMAPEAFDDFNKkpTSKSDVYSFAIVIWAVLTRKEPFENAINPLLIMQIVskgdrpslDDIGRLkQIENVQ 236
                       250
                ....*....|....*..
gi 47132591 847 EAIGIMRRLLRRNPERR 863
Cdd:cd13978 237 ELISLMIRCWDGNPDAR 253
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
626-880 8.96e-21

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 2 subunit (PhKG2) is also referred to as the testis/liver gamma isoform. Mutations in its gene cause autosomal-recessive glycogenosis of the liver. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 93.50  E-value: 8.96e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGELFAIKALK----KGDIVARDEV-ESLMCEKRILAAVtsAGHPFLVNLFGCFQTPEHVCFV 700
Cdd:cd14181  17 VIGRGVSSVVRRCVHRHTGQEFAVKIIEvtaeRLSPEQLEEVrSSTLKEIHILRQV--SGHPSIITLIDSYESSTFIFLV 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGGDLMLHIHSDVF---SEPRAIFYSacVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGL-CKegMGYGD 776
Cdd:cd14181  95 FDLMRRGELFDYLTEKVTlseKETRSIMRS--LLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFsCH--LEPGE 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 777 RTSTFCGTPEFLAPEVL------TDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRY--PRF--LSA 846
Cdd:cd14181 171 KLRELCGTPGYLAPEILkcsmdeTHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIMEGRYQFssPEWddRSS 250
                       250       260       270
                ....*....|....*....|....*....|....
gi 47132591 847 EAIGIMRRLLRRNPERRLgsserDAEDVKKQPFF 880
Cdd:cd14181 251 TVKDLISRLLVVDPEIRL-----TAEQALQHPFF 279
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
626-880 9.63e-21

Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. It phosphorylates Cre-Responsive Element Binding protein (CREB), facilitating the binding of CREB to the specific cis cAMP responsive element (CRE), which is important in activating genes related to germ cell differentiation. Mutations in the human TSSK4 gene is associated with infertile Chinese men with impaired spermatogenesis. The TSSK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 92.75  E-value: 9.63e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGELFAIKALKKGDivARDEVESlMCEKRILAAVTSAGHPFLVNLFGCFQTPEHVCFVMEYSA 705
Cdd:cd14162   7 TLGHGSYAVVKKAYSTKHKCKVAIKIVSKKK--APEDYLQ-KFLPREIEVIKGLKHPNLICFYEAIETTSRVYIIMELAE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 706 GGDLMLHIHSDVF-SEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGM----GYGDRTST 780
Cdd:cd14162  84 NGDLLDYIRKNGAlPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFARGVMktkdGKPKLSET 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 781 FCGTPEFLAPEVLTDTSYT-RAVDWWGLGVLLYEMLVGESPFpGDDEEEVFDSIVNDEVRYPR--FLSAEAIGIMRRLLR 857
Cdd:cd14162 164 YCGSYAYASPEILRGIPYDpFLSDIWSMGVVLYTMVYGRLPF-DDSNLKVLLKQVQRRVVFPKnpTVSEECKDLILRMLS 242
                       250       260
                ....*....|....*....|...
gi 47132591 858 RNPERrlgsseRDAEDVKKQPFF 880
Cdd:cd14162 243 PVKKR------ITIEEIKRDPWF 259
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
627-881 1.02e-20

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 3, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. PAK3 belongs to group I. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAK3 is highly expressed in the brain. It is implicated in neuronal plasticity, synapse formation, dendritic spine morphogenesis, cell cycle progression, neuronal migration, and apoptosis. Inactivating mutations in the PAK3 gene cause X-linked non-syndromic mental retardation, the severity of which depends on the site of the mutation.


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 93.63  E-value: 1.02e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALkkgDIVARDEVESLMCEkriLAAVTSAGHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd06656  27 IGQGASGTVYTAIDIATGQEVAIKQM---NLQQQPKKELIINE---ILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCGTPE 786
Cdd:cd06656 101 GSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPY 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 787 FLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVND---EVRYPRFLSAEAIGIMRRLLRRNPERR 863
Cdd:cd06656 181 WMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNgtpELQNPERLSAVFRDFLNRCLEMDVDRR 260
                       250
                ....*....|....*...
gi 47132591 864 lGSserdAEDVKKQPFFR 881
Cdd:cd06656 261 -GS----AKELLQHPFLK 273
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
617-825 1.07e-20

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK3 is a mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK3 activates multiple MAPK pathways and plays a role in apoptosis, proliferation, migration, and differentiation, depending on the cellular context. It is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. MLK3 also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and consequently, it also impacts inflammation and immunity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 93.17  E-value: 1.07e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 617 TLEDFKFLAVLGRGHFGKVLLSEFRpsGELFAIKALKKG---DIVArdEVESLMCEKRILAAVTsagHPFLVNLFG-CFQ 692
Cdd:cd14147   1 SFQELRLEEVIGIGGFGKVYRGSWR--GELVAVKAARQDpdeDISV--TAESVRQEARLFAMLA---HPNIIALKAvCLE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 693 TPeHVCFVMEYSAGGDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIV---YRDLKLDNLLLDTEGY--------VK 761
Cdd:cd14147  74 EP-NLCLVMEYAAGGPLSRALAGRRVPPHVLVNWAVQIARGMHYLHCEALVpviHRDLKSNNILLLQPIEnddmehktLK 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47132591 762 IADFGLCKEGmgYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDD 825
Cdd:cd14147 153 ITDFGLAREW--HKTTQMSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRGID 214
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
621-880 1.07e-20

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. CDKs are partly regulated by their subcellular localization, which defines substrate phosphorylation and the resulting specific function. CDK1, CDK2, CDK4, and CDK6 have well-defined functions in the cell cycle, such as the regulation of the early G1 phase by CDK4 or CDK6, the G1/S phase transition by CDK2, or the entry of mitosis by CDK1. They also exhibit overlapping cyclin specificity and functions in certain conditions. Knockout mice with a single CDK deleted remain viable with specific phenotypes, showing that some CDKs can compensate for each other. For example, CDK4 can compensate for the loss of CDK6, however, double knockout mice with both CDK4 and CDK6 deleted die in utero. CDK8 and CDK9 are mainly involved in transcription while CDK5 is implicated in neuronal function. CDK7 plays essential roles in both the cell cycle as a CDK-Activating Kinase (CAK) and in transcription as a component of the general transcription factor TFIIH. The CDK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270823 [Multi-domain]  Cd Length: 282  Bit Score: 93.32  E-value: 1.07e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKkgdIVARDE--VESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVC 698
Cdd:cd07829   1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIR---LDNEEEgiPSTALREISLLKELK---HPNIVKLLDVIHTENKLY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGgDL--MLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEgmgYGD 776
Cdd:cd07829  75 LVFEYCDQ-DLkkYLDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLARA---FGI 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 777 RTSTFcgTPE-----FLAPEVL-TDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDE---------------EEV---FDS 832
Cdd:cd07829 151 PLRTY--THEvvtlwYRAPEILlGSKHYSTAVDIWSVGCIFAELITGKPLFPGDSEidqlfkifqilgtptEESwpgVTK 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 47132591 833 IVNDEVRYPRF-----------LSAEAIGIMRRLLRRNPERRLgsserDAEDVKKQPFF 880
Cdd:cd07829 229 LPDYKPTFPKWpkndlekvlprLDPEGIDLLSKMLQYNPAKRI-----SAKEALKHPYF 282
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
627-880 1.18e-20

Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LKB1, also called STK11, was first identified as a tumor suppressor responsible for Peutz-Jeghers syndrome, a disorder that leads to an increased risk of spontaneous epithelial cancer. It serves as a master upstream kinase that activates AMP-activated protein kinase (AMPK) and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. To be activated, LKB1 requires the adaptor proteins STe20-Related ADaptor (STRAD) and mouse protein 25 (MO25). The LKB1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271021 [Multi-domain]  Cd Length: 255  Bit Score: 92.32  E-value: 1.18e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKV---LLSEfrpSGELFAIKALKKGDIV----ARDEVESlmcEKRILAAVTsagHPFLVNLFGCFQTPE--HV 697
Cdd:cd14119   1 LGEGSYGKVkevLDTE---TLCRRAVKILKKRKLRripnGEANVKR---EIQILRRLN---HRNVIKLVDVLYNEEkqKL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 698 CFVMEYSAGG-DLMLHihsdvfSEPRAIF-------YSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK 769
Cdd:cd14119  72 YMVMEYCVGGlQEMLD------SAPDKRLpiwqahgYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAE 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 770 EGMGY--GDRTSTFCGTPEFLAPEVL--TDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLS 845
Cdd:cd14119 146 ALDLFaeDDTCTTSQGSPAFQPPEIAngQDSFSGFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGEYTIPDDVD 225
                       250       260       270
                ....*....|....*....|....*....|....*
gi 47132591 846 AEAIGIMRRLLRRNPERRLgsserDAEDVKKQPFF 880
Cdd:cd14119 226 PDLQDLLRGMLEKDPEKRF-----TIEQIRQHPWF 255
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
626-867 1.51e-20

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 96.09  E-value: 1.51e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  626 VLGRGHFGKVLLSEFRPSGELFAIK-----ALKKGDIV-ARDEVESLM-CEkrilaavtsaghpfLVNLFGCF------- 691
Cdd:PTZ00283  39 VLGSGATGTVLCAKRVSDGEPFAVKvvdmeGMSEADKNrAQAEVCCLLnCD--------------FFSIVKCHedfakkd 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  692 -QTPEHV---CFVMEYSAGGDLMLHIHSDV-----FSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKI 762
Cdd:PTZ00283 105 pRNPENVlmiALVLDYANAGDLRQEIKSRAktnrtFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKL 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  763 ADFGLCK--EGMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDevRY 840
Cdd:PTZ00283 185 GDFGFSKmyAATVSDDVGRTFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENMEEVMHKTLAG--RY 262
                        250       260       270
                 ....*....|....*....|....*....|
gi 47132591  841 ---PRFLSAEAIGIMRRLLRRNPERRLGSS 867
Cdd:PTZ00283 263 dplPPSISPEMQEIVTALLSSDPKRRPSSS 292
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
626-864 1.65e-20

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK3, also called Prk or Fnk (FGF-inducible kinase), regulates angiogenesis and responses to DNA damage. Activated PLK3 mediates Chk2 phosphorylation by ATM and the resulting checkpoint activation. PLK3 phosphorylates DNA polymerase delta and may be involved in DNA repair. It also inhibits Cdc25c, thereby regulating the onset of mitosis. The PLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 92.30  E-value: 1.65e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFVMEYSA 705
Cdd:cd14189   8 LLGKGGFARCYEMTDLATNKTYAVKVIPHSRVAKPHQREKIVNEIELHRDLH---HKHVVKFSHHFEDAENIYIFLELCS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 706 GGDLMlHI----HSdvFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTF 781
Cdd:cd14189  85 RKSLA-HIwkarHT--LLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARLEPPEQRKKTI 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 782 CGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIvnDEVRY--PRFLSAEAIGIMRRLLRRN 859
Cdd:cd14189 162 CGTPNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCI--KQVKYtlPASLSLPARHLLAGILKRN 239

                ....*
gi 47132591 860 PERRL 864
Cdd:cd14189 240 PGDRL 244
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
619-863 1.94e-20

Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lyn subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 92.41  E-value: 1.94e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELfAIKALKKGDIvardEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVC 698
Cdd:cd05072   7 ESIKLVKKLGAGQFGEVWMGYYNNSTKV-AVKTLKPGTM----SVQAFLEEANLMKTLQ---HDKLVRLYAVVTKEEPIY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGGDLMLHIHSDVFSE---PRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK--EGMG 773
Cdd:cd05072  79 IITEYMAKGSLLDFLKSDEGGKvllPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARviEDNE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 774 YGDRTSTfcGTP-EFLAPEVLTDTSYTRAVDWWGLGVLLYEMLV-GESPFPGDDEEEVFdSIVNDEVRYPRFLS--AEAI 849
Cdd:cd05072 159 YTAREGA--KFPiKWTAPEAINFGSFTIKSDVWSFGILLYEIVTyGKIPYPGMSNSDVM-SALQRGYRMPRMENcpDELY 235
                       250
                ....*....|....
gi 47132591 850 GIMRRLLRRNPERR 863
Cdd:cd05072 236 DIMKTCWKEKAEER 249
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
627-879 2.43e-20

Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Saccharomyces cerevisiae Bck1 and Schizosaccharomyces pombe Mkh1, and related proteins. Budding yeast Bck1 is part of the cell integrity MAPK pathway, which is activated by stresses and aggressions to the cell wall. The MAPKKK Bck1, MAPKKs Mkk1 and Mkk2, and the MAPK Slt2 make up the cascade that is important in the maintenance of cell wall homeostasis. Fission yeast Mkh1 is involved in MAPK cascades regulating cell morphology, cell wall integrity, salt resistance, and filamentous growth in response to stress. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The Bck1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270799 [Multi-domain]  Cd Length: 270  Bit Score: 92.06  E-value: 2.43e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIK--ALKKGDIVARDE-----VESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCF 699
Cdd:cd06629   9 IGKGTYGRVYLAMNATTGEMLAVKqvELPKTSSDRADSrqktvVDALKSEIDTLKDLD---HPNIVQYLGFEETEDYFSI 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYSAGGDLM--LHIHSDvFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMG-YG- 775
Cdd:cd06629  86 FLEYVPGGSIGscLRKYGK-FEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISKKSDDiYGn 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 776 DRTSTFCGTPEFLAPEVLTD--TSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYP----RFLSAEAI 849
Cdd:cd06629 165 NGATSMQGSVFWMAPEVIHSqgQGYSAKVDIWSLGCVVLEMLAGRRPWSDDEAIAAMFKLGNKRSAPPvpedVNLSPEAL 244
                       250       260       270
                ....*....|....*....|....*....|
gi 47132591 850 GIMRRLLRRNPERRlgsseRDAEDVKKQPF 879
Cdd:cd06629 245 DFLNACFAIDPRDR-----PTAAELLSHPF 269
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
622-815 2.90e-20

Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are PTKs, catalyzing the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jaks are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 92.06  E-value: 2.90e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 622 KFLAVLGRGHFGKVLLSEFRP----SGELFAIKALK--KGDIVARD---EVESLmcekRILAavtsagHPFLVNLFGCFQ 692
Cdd:cd05038   7 KFIKQLGEGHFGSVELCRYDPlgdnTGEQVAVKSLQpsGEEQHMSDfkrEIEIL----RTLD------HEYIVKYKGVCE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 693 TPEH--VCFVMEYSAGGDL--MLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLC 768
Cdd:cd05038  77 SPGRrsLRLIMEYLPSGSLrdYLQRHRDQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLA 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 47132591 769 K---EGMGY----GDRTStfcgtPEF-LAPEVLTDTSYTRAVDWWGLGVLLYEML 815
Cdd:cd05038 157 KvlpEDKEYyyvkEPGES-----PIFwYAPECLRESRFSSASDVWSFGVTLYELF 206
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
627-868 3.30e-20

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK1 is important in the regulation of many cellular processes including cytoskeletal dynamics, cell motility, growth, and proliferation. Although PAK1 has been regarded mainly as a cytosolic protein, recent reports indicate that PAK1 also exists in significant amounts in the nucleus, where it is involved in transcription modulation and in cell cycle regulatory events. PAK1 is also involved in transformation and tumorigenesis. Its overexpression, hyperactivation and increased nuclear accumulation is correlated to breast cancer invasiveness and progression. Nuclear accumulation is also linked to tamoxifen resistance in breast cancer cells. PAK1 belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 92.09  E-value: 3.30e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALkkgDIVARDEVESLMCEkriLAAVTSAGHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd06654  28 IGQGASGTVYTAMDVATGQEVAIRQM---NLQQQPKKELIINE---ILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCGTPE 786
Cdd:cd06654 102 GSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPY 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 787 FLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVND---EVRYPRFLSAEAIGIMRRLLRRNPERR 863
Cdd:cd06654 182 WMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNgtpELQNPEKLSAIFRDFLNRCLEMDVEKR 261

                ....*
gi 47132591 864 LGSSE 868
Cdd:cd06654 262 GSAKE 266
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
627-868 3.32e-20

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK1 (or MYLK1) phosphorylates myosin regulatory light chain and controls the contraction of smooth muscles. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module which results in the expression of telokin in phasic smooth muscles, leading to Ca2+ desensitization by cyclic nucleotides of smooth muscle force. MLCK1 is also responsible for myosin regulatory light chain phosphorylation in nonmuscle cells and may play a role in regulating myosin II ATPase activity. The MLCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 91.22  E-value: 3.32e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKgdiVARDEVESLMCEkriLAAVTSAGHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd14191  10 LGSGKFGQVFRLVEKKTKKVWAGKFFKA---YSAKEKENIRQE---ISIMNCLHHPKLVQCVDAFEEKANIVMVLEMVSG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLMLHIHSDVF--SEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLL--LDTEGYVKIADFGLCKEGMGYGDRTSTFc 782
Cdd:cd14191  84 GELFERIIDEDFelTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcvNKTGTKIKLIDFGLARRLENAGSLKVLF- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 783 GTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEV----------FDSIVNDEVryprflSAEAIGIM 852
Cdd:cd14191 163 GTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETlanvtsatwdFDDEAFDEI------SDDAKDFI 236
                       250
                ....*....|....*.
gi 47132591 853 RRLLRRNPERRLGSSE 868
Cdd:cd14191 237 SNLLKKDMKARLTCTQ 252
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
627-868 3.46e-20

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 92.36  E-value: 3.46e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKalkkgdIVARD-----EVESL-MCEkrilaavtsaGHPFLVNLFGCFQTPEHVCFV 700
Cdd:cd14092  14 LGDGSFSVCRKCVHKKTGQEFAVK------IVSRRldtsrEVQLLrLCQ----------GHPNIVKLHEVFQDELHTYLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGGDLMLHIHS-DVFSEPRA--IFYSacVVLGLQFLHEHKIVYRDLKLDNLLLDTEG---YVKIADFGLC--KEGM 772
Cdd:cd14092  78 MELLRGGELLERIRKkKRFTESEAsrIMRQ--LVSAVSFMHSKGVVHRDLKPENLLFTDEDddaEIKIVDFGFArlKPEN 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 773 gygDRTSTFCGTPEFLAPEVL----TDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVnDEVRYPRF----- 843
Cdd:cd14092 156 ---QPLKTPCFTLPYAAPEVLkqalSTQGYDESCDLWSLGVILYTMLSGQVPFQSPSRNESAAEIM-KRIKSGDFsfdge 231
                       250       260
                ....*....|....*....|....*....
gi 47132591 844 ----LSAEAIGIMRRLLRRNPERRLGSSE 868
Cdd:cd14092 232 ewknVSSEAKSLIQGLLTVDPSKRLTMSE 260
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
625-881 3.46e-20

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK1 is a MAPK kinase kinase (MAPKKK or MKKK) that phosphorylates and activates activates the ERK1/2 and c-Jun N-terminal kinase (JNK) pathways by activating their respective MAPKKs, MEK1/2 and MKK4/MKK7, respectively. MEKK1 is important in regulating cell survival and apoptosis. MEKK1 also plays a role in cell migration, tissue maintenance and homeostasis, and wound healing. The MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270800 [Multi-domain]  Cd Length: 268  Bit Score: 91.34  E-value: 3.46e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 625 AVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDE---VESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFVM 701
Cdd:cd06630   6 PLLGTGAFSSCYQARDVKTGTLMAVKQVSFCRNSSSEQeevVEAIREEIRMMARLN---HPNIVRMLGATQHKSHFNIFV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 702 EYSAGGDL--MLHIHSdVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEG-YVKIADFG----LCKEGMGY 774
Cdd:cd06630  83 EWMAGGSVasLLSKYG-AFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGqRLRIADFGaaarLASKGTGA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 775 GDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSI-----VNDEVRYPRFLSAEAI 849
Cdd:cd06630 162 GEFQGQLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLALIfkiasATTPPPIPEHLSPGLR 241
                       250       260       270
                ....*....|....*....|....*....|..
gi 47132591 850 GIMRRLLRRNPERRLGsserdAEDVKKQPFFR 881
Cdd:cd06630 242 DVTLRCLELQPEDRPP-----ARELLKHPVFT 268
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
615-841 3.49e-20

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called Doublecortin-like and CAM kinase-like 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL1 (or DCAMKL1) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL1 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL1 interacts with tubulin, glucocorticoid receptor, dynein, JIP1/2, caspases (3 and 8), and calpain, among others. It plays roles in neurogenesis, neuronal migration, retrograde transport, and neuronal apoptosis. The DCKL1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 91.59  E-value: 3.49e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 615 PLTLED-FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDivARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQT 693
Cdd:cd14183   1 PASISErYKVGRTIGDGNFAVVKECVERSTGREYALKIINKSK--CRGKEHMIQNEVSILRRVK---HPNIVLLIEEMDM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 694 PEHVCFVMEYSAGGDLMLHIHS-DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDN----LLLDTEGYVKIADFGLC 768
Cdd:cd14183  76 PTELYLVMELVKGGDLFDAITStNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENllvyEHQDGSKSLKLGDFGLA 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47132591 769 K--EGMGYgdrtsTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPG--DDEEEVFDSIVNDEVRYP 841
Cdd:cd14183 156 TvvDGPLY-----TVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGsgDDQEVLFDQILMGQVDFP 227
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
620-863 3.98e-20

Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity kinase Myt1, the protein tyrosine kinase Wee1, and similar proteins. These proteins are cell cycle checkpoint kinases that are involved in the regulation of cyclin-dependent kinase CDK1, the master engine for mitosis. CDK1 is kept inactivated through phosphorylation of N-terminal thr (T14 by Myt1) and tyr (Y15 by Myt1 and Wee1) residues. Mitosis progression is ensured through activation of CDK1 by dephoshorylation and inactivation of Myt1/Wee1. The Wee1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 90.91  E-value: 3.98e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKgDIVARDEVESLMCEKRILAAVtsAGHPFLVNLFGCFQTPEHVCF 699
Cdd:cd13997   1 HFHELEQIGSGSFSEVFKVRSKVDGCLYAVKKSKK-PFRGPKERARALREVEAHAAL--GQHPNIVRYYSSWEEGGHLYI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYSAGGDLMLHIHSDV----FSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYG 775
Cdd:cd13997  78 QMELCENGSLQDALEELSpiskLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRLETSG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 776 DRTStfcGTPEFLAPEVLTD-TSYTRAVDWWGLGVLLYEMlVGESPFP--GDDEEEVFDSIVNDEVRYPrfLSAEAIGIM 852
Cdd:cd13997 158 DVEE---GDSRYLAPELLNEnYTHLPKADIFSLGVTVYEA-ATGEPLPrnGQQWQQLRQGKLPLPPGLV--LSQELTRLL 231
                       250
                ....*....|.
gi 47132591 853 RRLLRRNPERR 863
Cdd:cd13997 232 KVMLDPDPTRR 242
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
627-864 4.24e-20

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK3, also called DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk), contains an N-terminal kinase domain and a C-terminal region with nuclear localization signals (NLS) and a leucine zipper motif that mediates homodimerization and interaction with other leucine zipper proteins. It interacts with Par-4, a protein that contains a death domain and interacts with actin filaments. DAPK3 is present in both the cytoplasm and nucleus. Its co-expression with Par-4 results in the co-localization of the two proteins to actin filaments. In addition to cell death, DAPK3 is also implicated in mediating cell motility and the contraction of smooth muscles. The DAPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 91.22  E-value: 4.24e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKGDI------VARDEVESlmcEKRILAAVTsagHPFLVNLFGCFQTPEHVCFV 700
Cdd:cd14195  13 LGSGQFAIVRKCREKGTGKEYAAKFIKKRRLsssrrgVSREEIER---EVNILREIQ---HPNIITLHDIFENKTDVVLI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGGDLMLHI-HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGY----VKIADFGLCKEgMGYG 775
Cdd:cd14195  87 LELVSGGELFDFLaEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVpnprIKLIDFGIAHK-IEAG 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 776 DRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSI--VN---DEvRYPRFLSAEAIG 850
Cdd:cd14195 166 NEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNIsaVNydfDE-EYFSNTSELAKD 244
                       250
                ....*....|....
gi 47132591 851 IMRRLLRRNPERRL 864
Cdd:cd14195 245 FIRRLLVKDPKKRM 258
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
624-863 5.06e-20

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 90.80  E-value: 5.06e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 624 LAVLGRGHFGKVLLSEFRPSGELFAIKALKKgDIVARDEVeslmceKRILAAVTSAGHPFLVNLFGCFQTPEHVCFVMEY 703
Cdd:cd14113  12 VAELGRGRFSVVKKCDQRGTKRAVATKFVNK-KLMKRDQV------THELGVLQSLQHPQLVGLLDTFETPTSYILVLEM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 704 SAGGDLMLHIHS-DVFSEPRAIFYSACVVLGLQFLHEHKIVY---RDLKLDNLLLDTEGYVKIADFGLCKEgMGYGDRTS 779
Cdd:cd14113  85 ADQGRLLDYVVRwGNLTEEKIRFYLREILEALQYLHNCRIAHldlKPENILVDQSLSKPTIKLADFGDAVQ-LNTTYYIH 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 780 TFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYP----RFLSAEAIGIMRRL 855
Cdd:cd14113 164 QLLGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDFSFPddyfKGVSQKAKDFVCFL 243

                ....*...
gi 47132591 856 LRRNPERR 863
Cdd:cd14113 244 LQMDPAKR 251
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
626-864 6.40e-20

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPK-activated protein kinases MK2, MK3, MK5 (also called PRAK for p38-regulated/activated protein kinase), and related proteins. These proteins contain a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. In addition, MK2 and MK3 contain an N-terminal proline-rich region that can bind to SH3 domains. MK2 and MK3 are bonafide substrates for the MAPK p38, while MK5 plays a functional role in the p38 MAPK pathway although their direct interaction has been difficult to detect. MK2 and MK3 are closely related and show, thus far, indistinguishable substrate specificity, while MK5 shows a distinct spectrum of substrates. MK2 and MK3 are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 90.43  E-value: 6.40e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGELFAIKALKKGDiVARDEVEslmcekriLAAVTSaGHPFLVNLFGCFQT--PEHVCF--VM 701
Cdd:cd14089   8 VLGLGINGKVLECFHKKTGEKFALKVLRDNP-KARREVE--------LHWRAS-GCPHIVRIIDVYENtyQGRKCLlvVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 702 EYSAGGDLMLHIHSDV---FSEPRA--IFYSACvvLGLQFLHEHKIVYRDLKLDN---LLLDTEGYVKIADFGLCKEGMG 773
Cdd:cd14089  78 ECMEGGELFSRIQERAdsaFTEREAaeIMRQIG--SAVAHLHSMNIAHRDLKPENllySSKGPNAILKLTDFGFAKETTT 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 774 yGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPF---------PGddeeeVFDSIVNDEVRYP--- 841
Cdd:cd14089 156 -KKSLQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFysnhglaisPG-----MKKRIRNGQYEFPnpe 229
                       250       260
                ....*....|....*....|....
gi 47132591 842 -RFLSAEAIGIMRRLLRRNPERRL 864
Cdd:cd14089 230 wSNVSEEAKDLIRGLLKTDPSERL 253
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
626-881 6.57e-20

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 1 subunit (PhKG1) is also referred to as the muscle gamma isoform. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 90.74  E-value: 6.57e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGELFAIKAL--KKGDIVARDEVESL----MCEKRILAAVTsaGHPFLVNLFGCFQTPEHVCF 699
Cdd:cd14182  10 ILGRGVSSVVRRCIHKPTRQEYAVKIIdiTGGGSFSPEEVQELreatLKEIDILRKVS--GHPNIIQLKDTYETNTFFFL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYSAGGDLMLHIHSDVF---SEPRAIFYSACVVLglQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEgMGYGD 776
Cdd:cd14182  88 VFDLMKKGELFDYLTEKVTlseKETRKIMRALLEVI--CALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQ-LDPGE 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 777 RTSTFCGTPEFLAPEVL------TDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRY--PRF--LSA 846
Cdd:cd14182 165 KLREVCGTPGYLAPEIIecsmddNHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGNYQFgsPEWddRSD 244
                       250       260       270
                ....*....|....*....|....*....|....*
gi 47132591 847 EAIGIMRRLLRRNPERRLgsserDAEDVKKQPFFR 881
Cdd:cd14182 245 TVKDLISRFLVVQPQKRY-----TAEEALAHPFFQ 274
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
619-863 1.09e-19

Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The PDGFR subfamily consists of PDGFR alpha, PDGFR beta, KIT, CSF-1R, the mammalian FLT3, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. PDGFR kinase domains are autoinhibited by their juxtamembrane regions containing tyr residues. The binding to their ligands leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR subfamily receptors are important in the development of a variety of cells. PDGFRs are expressed in a many cells including fibroblasts, neurons, endometrial cells, mammary epithelial cells, and vascular smooth muscle cells. PDGFR signaling is critical in normal embryonic development, angiogenesis, and wound healing. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. Mammalian FLT3 plays an important role in the survival, proliferation, and differentiation of stem cells. The PDGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 90.62  E-value: 1.09e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVL------LSEFRPSGELfAIKALKKgdIVARDEVESLMCEKRILAAVTSagHPFLVNLFGCFQ 692
Cdd:cd05055  35 NNLSFGKTLGAGAFGKVVeataygLSKSDAVMKV-AVKMLKP--TAHSSEREALMSELKIMSHLGN--HENIVNLLGACT 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 693 TPEHVCFVMEYSAGGDLM--LHIHSDVFSEPRAIF-YSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK 769
Cdd:cd05055 110 IGGPILVITEYCCYGDLLnfLRRKRESFLTLEDLLsFSYQVAKGMAFLASKNCIHRDLAARNVLLTHGKIVKICDFGLAR 189
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 770 EGM---GYGDRTSTFCGTpEFLAPEVLTDTSYTRAVDWWGLGVLLYEML-VGESPFPGDDEEEVFDSIVNDEVRY--PRF 843
Cdd:cd05055 190 DIMndsNYVVKGNARLPV-KWMAPESIFNCVYTFESDVWSYGILLWEIFsLGSNPYPGMPVDSKFYKLIKEGYRMaqPEH 268
                       250       260
                ....*....|....*....|
gi 47132591 844 LSAEAIGIMRRLLRRNPERR 863
Cdd:cd05055 269 APAEIYDIMKTCWDADPLKR 288
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
619-868 1.13e-19

Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Pek1/Skh1 from Schizosaccharomyces pombe and MKK2 from Saccharomyces cerevisiae, and related proteins. Both fission yeast Pek1 and baker's yeast MKK2 are components of the cell integrity MAPK pathway. In fission yeast, Pek1 phosphorylates and activates Pmk1/Spm1 and is regulated by the MAPKK kinase Mkh1. In baker's yeast, the pathway involves the MAPK Slt2, the MAPKKs MKK1 and MKK2, and the MAPKK kinase Bck1. The cell integrity MAPK cascade is activated by multiple stress conditions, and is essential in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 90.56  E-value: 1.13e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKalkkgdIVARDEveSLMCEKRI---LAAVTSAGHPFLVNLFGCFqTPE 695
Cdd:cd06621   1 DKIVELSSLGEGAGGSVTKCRLRNTKTIFALK------TITTDP--NPDVQKQIlreLEINKSCASPYIVKYYGAF-LDE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 696 HVCFV---MEYSAGGDLMlHIHSDVFSE-----PRAIFYSA-CVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFG 766
Cdd:cd06621  72 QDSSIgiaMEYCEGGSLD-SIYKKVKKKggrigEKVLGKIAeSVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFG 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 767 LCKEGMGYGDrtSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEE-----EVFDSIVN------ 835
Cdd:cd06621 151 VSGELVNSLA--GTFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFPPEGEPplgpiELLSYIVNmpnpel 228
                       250       260       270
                ....*....|....*....|....*....|....
gi 47132591 836 -DEVRYPRFLSAEAIGIMRRLLRRNPERRLGSSE 868
Cdd:cd06621 229 kDEPENGIKWSESFKDFIEKCLEKDGTRRPGPWQ 262
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
619-868 1.50e-19

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIA myosin is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. Mutations in human myosin IIIA are responsible for progressive nonsyndromic hearing loss. Human myosin IIIA possesses ATPase and kinase activities, and the ability to move actin filaments in a motility assay. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. Class III myosins may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. In photoreceptor cells, they may also function as cargo carriers during light-dependent translocation of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 90.07  E-value: 1.50e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKgdivARDEVESLMCEKRILAAVTSagHPFLVNLFGCF-----QT 693
Cdd:cd06638  18 DTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDP----IHDIDEEIEAEYNILKALSD--HPNVVKFYGMYykkdvKN 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 694 PEHVCFVMEYSAGG---DLMLHI--HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLC 768
Cdd:cd06638  92 GDQLWLVLELCNGGsvtDLVKGFlkRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGVS 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 769 KEGMGYGDRTSTFCGTPEFLAPEVLT-----DTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVND---EVRY 840
Cdd:cd06638 172 AQLTSTRLRRNTSVGTPFWMAPEVIAceqqlDSTYDARCDVWSLGITAIELGDGDPPLADLHPMRALFKIPRNpppTLHQ 251
                       250       260
                ....*....|....*....|....*...
gi 47132591 841 PRFLSAEAIGIMRRLLRRNPERRLGSSE 868
Cdd:cd06638 252 PELWSNEFNDFIRKCLTKDYEKRPTVSD 279
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
647-879 1.80e-19

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called Ribosomal protein S6 kinase alpha-1 or 90kDa ribosomal protein S6 kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK1 is also called S6K-alpha-1, RPS6KA1, p90RSK1 or MAPK-activated protein kinase 1a (MAPKAPK-1a). It is a component of the insulin transduction pathway, regulating the function of IRS1. It also interacts with PKA and promotes its inactivation. RSK1 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 90.09  E-value: 1.80e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 647 FAIKALKKGDIVARDEVESLMcekrilaavTSAGHPFLVNLFGCFQTPEHVCFVMEYSAGGDLMLHI-HSDVFSEPRAIF 725
Cdd:cd14175  29 YAVKVIDKSKRDPSEEIEILL---------RYGQHPNIITLKDVYDDGKHVYLVTELMRGGELLDKIlRQKFFSEREASS 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 726 YSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEG----YVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTDTSYTRA 801
Cdd:cd14175 100 VLHTICKTVEYLHSQGVVHRDLKPSNILYVDESgnpeSLRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKRQGYDEG 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 802 VDWWGLGVLLYEMLVGESPF---PGDDEEEVFDSIVNDEVRYP----RFLSAEAIGIMRRLLRRNPERRLgsserDAEDV 874
Cdd:cd14175 180 CDIWSLGILLYTMLAGYTPFangPSDTPEEILTRIGSGKFTLSggnwNTVSDAAKDLVSKMLHVDPHQRL-----TAKQV 254

                ....*
gi 47132591 875 KKQPF 879
Cdd:cd14175 255 LQHPW 259
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
619-880 1.83e-19

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Cdc7 kinase (or Hsk1 in fission yeast) is a critical regulator in the initiation of DNA replication. It forms a complex with a Dbf4-related regulatory subunit, a cyclin-like molecule that activates the kinase in late G1 phase, and is also referred to as Dbf4-dependent kinase (DDK). Its main targets are mini-chromosome maintenance (MCM) proteins. Cdc7 kinase may also have additional roles in meiosis, checkpoint responses, the maintenance and repair of chromosome structures, and cancer progression. The Cdc7 kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 88.82  E-value: 1.83e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSE-------FRPSGELFAIKALKKGDIVARDEVEsLMCEKRIlaavtsAGHPFLVNLFGCF 691
Cdd:cd14019   1 NKYRIIEKIGEGTFSSVYKAEdklhdlyDRNKGRLVALKHIYPTSSPSRILNE-LECLERL------GGSNNVSGLITAF 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 692 QTPEHVCFVMEYSAGGDLMLHIHSDVFSEPRAIFYsaCVVLGLQFLHEHKIVYRDLKLD--NLLLDTEGYVKIaDFGLCK 769
Cdd:cd14019  74 RNEDQVVAVLPYIEHDDFRDFYRKMSLTDIRIYLR--NLFKALKHVHSFGIIHRDVKPGnfLYNRETGKGVLV-DFGLAQ 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 770 EGMGYGDRTSTFCGTPEFLAPEVLTD-TSYTRAVDWWGLGVLLYEMLVGE-SPFPGDDEEEVFDSIVNdevrypRFLSAE 847
Cdd:cd14019 151 REEDRPEQRAPRAGTRGFRAPEVLFKcPHQTTAIDIWSAGVILLSILSGRfPFFFSSDDIDALAEIAT------IFGSDE 224
                       250       260       270
                ....*....|....*....|....*....|...
gi 47132591 848 AIGIMRRLLRRNPERRLgsserDAEDVKKQPFF 880
Cdd:cd14019 225 AYDLLDKLLELDPSKRI-----TAEEALKHPFF 252
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
619-820 1.87e-19

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST4 is sometimes referred to as MASK (MST3 and SOK1-related kinase). It plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. It influences cell growth and transformation by modulating the extracellular signal-regulated kinase (ERK) pathway. MST4 may also play a role in tumor formation and progression. It localizes in the Golgi apparatus by interacting with the Golgi matrix protein GM130 and may play a role in cell migration. The MST4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 89.73  E-value: 1.87e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDivARDEVESLMCEKRILAAVTSaghPFLVNLFGCFQTPEHVC 698
Cdd:cd06640   4 ELFTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEE--AEDEIEDIQQEITVLSQCDS---PYVTKYYGSYLKGTKLW 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGGDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRT 778
Cdd:cd06640  79 IIMEYLGGGSALDLLRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKR 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 47132591 779 STFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESP 820
Cdd:cd06640 159 NTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPP 200
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
626-868 1.98e-19

Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs) and include ASK1, ASK2, and MAPKKK15. ASK1 (also called MAPKKK5) functions in the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. It plays important roles in cytokine and stress responses, as well as in reactive oxygen species-mediated cellular responses. ASK1 is implicated in various diseases mediated by oxidative stress including inschemic heart disease, hypertension, vessel injury, brain ischemia, Fanconi anemia, asthma, and pulmonary edema, among others. ASK2 (also called MAPKKK6) functions only in a heteromeric complex with ASK1, and can activate ASK1 by direct phosphorylation. The function of MAPKKK15 is still unknown. The ASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 89.39  E-value: 1.98e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKV-----LLSEFRpsgelFAIKALKKGDIvarDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFV 700
Cdd:cd06624  15 VLGKGTFGVVyaardLSTQVR-----IAIKEIPERDS---REVQPLHEEIALHSRLS---HKNIVQYLGSVSEDGFFKIF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGGDLMLHIHSD----VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDT-EGYVKIADFGLCKEGMGYG 775
Cdd:cd06624  84 MEQVPGGSLSALLRSKwgplKDNENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTySGVVKISDFGTSKRLAGIN 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 776 DRTSTFCGTPEFLAPEVLTD--TSYTRAVDWWGLGVLLYEMLVGESPF--PGDDEEEVFD-SIVNDEVRYPRFLSAEAIG 850
Cdd:cd06624 164 PCTETFTGTLQYMAPEVIDKgqRGYGPPADIWSLGCTIIEMATGKPPFieLGEPQAAMFKvGMFKIHPEIPESLSEEAKS 243
                       250
                ....*....|....*...
gi 47132591 851 IMRRLLRRNPERRLGSSE 868
Cdd:cd06624 244 FILRCFEPDPDKRATASD 261
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
627-863 2.60e-19

Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SBK1, also called BSK146, is predominantly expressed in the brain. Its expression is increased in the developing brain during the late embryonic stage, coinciding with dramatic neuronal proliferation, migration, and maturation. SBK1 may play an important role in regulating brain development. The SBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 88.54  E-value: 2.60e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLmCEKRILAAvtsagHPFLVNLFG-CFQTPEHVCFVMEYSA 705
Cdd:cd13987   1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKLKDFLREY-NISLELSV-----HPHIIKTYDvAFETEDYYVFAQEYAP 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 706 GGDLMLHIHSDV-FSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGY--VKIADFGLCKEgmgYGDRTSTFC 782
Cdd:cd13987  75 YGDLFSIIPPQVgLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDCrrVKLCDFGLTRR---VGSTVKRVS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 783 GTPEFLAPEVL---------TDTSytraVDWWGLGVLLYEMLVGEspFPgddeeevFDSIVNDEVRYPRF---------- 843
Cdd:cd13987 152 GTIPYTAPEVCeakknegfvVDPS----IDVWAFGVLLFCCLTGN--FP-------WEKADSDDQFYEEFvrwqkrknta 218
                       250       260
                ....*....|....*....|....*..
gi 47132591 844 -------LSAEAIGIMRRLLRRNPERR 863
Cdd:cd13987 219 vpsqwrrFTPKALRMFKKLLAPEPERR 245
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
626-867 2.70e-19

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 89.71  E-value: 2.70e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGELFAIKALKKgdivaRDEVESlmcEKRILAAVTSAGHPFLVNLFGCFQTPEHVCFVMEYSA 705
Cdd:cd14179  14 PLGEGSFSICRKCLHKKTNQEYAVKIVSK-----RMEANT---QREIAALKLCEGHPNIVKLHEVYHDQLHTFLVMELLK 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 706 GGDLMLHIH-SDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEG---YVKIADFGLCKEGMGYGDRTSTF 781
Cdd:cd14179  86 GGELLERIKkKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESdnsEIKIIDFGFARLKPPDNQPLKTP 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 782 CGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDE-------EEVFDSIVNDEVRYP----RFLSAEAIG 850
Cdd:cd14179 166 CFTLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHDKsltctsaEEIMKKIKQGDFSFEgeawKNVSQEAKD 245
                       250
                ....*....|....*..
gi 47132591 851 IMRRLLRRNPERRLGSS 867
Cdd:cd14179 246 LIQGLLTVDPNKRIKMS 262
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
620-863 3.25e-19

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek4 is highly abundant in the testis. Its specific function is unknown. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. Nek4 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 88.26  E-value: 3.25e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKFLAVLGRGHFGKVLLSEFRPSGELFAIKA--LKKGDIVARDEVESlmcEKRILAAVTsagHPFLVNLFGCFQTPEHV 697
Cdd:cd08223   1 EYQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKlnLKNASKRERKAAEQ---EAKLLSKLK---HPNIVSYKESFEGEDGF 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 698 CF-VMEYSAGGDLMLHIHSD---VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMG 773
Cdd:cd08223  75 LYiVMGFCEGGDLYTRLKEQkgvLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLES 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 774 YGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEV-RYPRFLSAEAIGIM 852
Cdd:cd08223 155 SSDMATTLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEGKLpPMPKQYSPELGELI 234
                       250
                ....*....|.
gi 47132591 853 RRLLRRNPERR 863
Cdd:cd08223 235 KAMLHQDPEKR 245
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
619-879 3.39e-19

Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized proteins with similarity to MEKK3, MEKK2, and related proteins; they contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKKs), proteins that phosphorylate and activate MAPK kinases (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MEKK2 and MEKK3 activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 88.54  E-value: 3.39e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKAL--KKGDIVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEH 696
Cdd:cd06653   2 VNWRLGKLLGRGAFGEVYLCYDADTGRELAVKQVpfDPDSQETSKEVNALECEIQLLKNLR---HDRIVQYYGCLRDPEE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 697 --VCFVMEYSAGGDLMLHIHS-DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFG------- 766
Cdd:cd06653  79 kkLSIFVEYMPGGSVKDQLKAyGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGaskriqt 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 767 LCKEGMGYGDRTstfcGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPgddEEEVFDSIVN-----DEVRYP 841
Cdd:cd06653 159 ICMSGTGIKSVT----GTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPWA---EYEAMAAIFKiatqpTKPQLP 231
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 47132591 842 RFLSAEAIGIMRRLLRRNPERRLgsserdAEDVKKQPF 879
Cdd:cd06653 232 DGVSDACRDFLRQIFVEEKRRPT------AEFLLRHPF 263
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
622-869 3.54e-19

Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mos (or c-Mos) is a germ-cell specific kinase that plays roles in both the release of primary arrest and the induction of secondary arrest in oocytes. It is expressed towards the end of meiosis I and is quickly degraded upon fertilization. It is a component of the cytostatic factor (CSF), which is responsible for metaphase II arrest. In addition, Mos activates a phoshorylation cascade that leads to the activation of the p34 subunit of MPF (mitosis-promoting factor or maturation promoting factor), a cyclin-dependent kinase that is responsible for the release of primary arrest in meiosis I. The Mos subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 88.59  E-value: 3.54e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 622 KFLAVLGRGHFGKVLLSEFRpsGELFAIKALKK-GDIVARDEveSLMCEK-----------RILAAVTSAGhpflvnlFG 689
Cdd:cd13979   6 RLQEPLGSGGFGSVYKATYK--GETVAVKIVRRrRKNRASRQ--SFWAELnaarlrhenivRVLAAETGTD-------FA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 690 CFQTpehvcFVMEYSAGGDLMLHIH--SDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFG- 766
Cdd:cd13979  75 SLGL-----IIMEYCGNGTLQQLIYegSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGc 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 767 --LCKEGMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFdSIVNDEVR---YP 841
Cdd:cd13979 150 svKLGEGNEVGTPRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAGLRQHVLY-AVVAKDLRpdlSG 228
                       250       260       270
                ....*....|....*....|....*....|..
gi 47132591 842 RFLSAEaIGIMRRLLRR----NPERRLGSSER 869
Cdd:cd13979 229 LEDSEF-GQRLRSLISRcwsaQPAERPNADES 259
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
618-868 4.38e-19

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK2, also called DAPK-related protein 1 (DRP-1), is a Ca2+/calmodulin (CaM)-regulated protein containing an N-terminal kinase domain, a CaM autoinhibitory site and a dimerization module. It lacks the cytoskeletal binding regions of DAPK1 and the exogenous protein has been shown to be soluble and cytoplasmic. FLAG-tagged DAPK2, however, accumulated within membrane-enclosed autophagic vesicles. It is unclear where endogenous DAPK2 is localized. DAPK2 participates in TNF-alpha and FAS-receptor induced cell death and enhances neutrophilic maturation in myeloid leukemic cells. It contributes to the induction of anoikis and its down-regulation is implicated in the beta-catenin induced resistance of malignant epithelial cells to anoikis. The DAPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 88.47  E-value: 4.38e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 618 LEDFKFLA-VLGRGHFGKVLLSEFRPSGELFAIKALKKGDI------VARDEVESlmcEKRILAAVTsagHPFLVNLFGC 690
Cdd:cd14196   3 VEDFYDIGeELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrasrrgVSREEIER---EVSILRQVL---HPNIITLHDV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 691 FQTPEHVCFVMEYSAGGDLMLHI-HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEG----YVKIADF 765
Cdd:cd14196  77 YENRTDVVLILELVSGGELFDFLaQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDF 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 766 GLCKEgMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSI--VNDEVRYPRF 843
Cdd:cd14196 157 GLAHE-IEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANItaVSYDFDEEFF 235
                       250       260
                ....*....|....*....|....*..
gi 47132591 844 --LSAEAIGIMRRLLRRNPERRLGSSE 868
Cdd:cd14196 236 shTSELAKDFIRKLLVKETRKRLTIQE 262
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
619-864 4.57e-19

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 3 (MAPKAP3 or MK3) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK3 is a bonafide substrate for the MAPK p38. It is closely related to MK2 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK3 activity is only significant when MK2 is absent. The MK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 88.12  E-value: 4.57e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLA-VLGRGHFGKVLLSEFRPSGELFAIKALKKGDiVARDEVEslmCEKRilaavtSAGHPFLVNLFGCFQTPEH- 696
Cdd:cd14172   3 DDYKLSKqVLGLGVNGKVLECFHRRTGQKCALKLLYDSP-KARREVE---HHWR------ASGGPHIVHILDVYENMHHg 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 697 ---VCFVMEYSAGGDLMLHIHS---DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDN---LLLDTEGYVKIADFGL 767
Cdd:cd14172  73 krcLLIIMECMEGGELFSRIQErgdQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENllyTSKEKDAVLKLTDFGF 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 768 CKEgMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIvNDEVRYPRF---- 843
Cdd:cd14172 153 AKE-TTVQNALQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTGQAISPGM-KRRIRMGQYgfpn 230
                       250       260
                ....*....|....*....|....*.
gi 47132591 844 -----LSAEAIGIMRRLLRRNPERRL 864
Cdd:cd14172 231 pewaeVSEEAKQLIRHLLKTDPTERM 256
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
627-868 4.86e-19

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 89.16  E-value: 4.86e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKgdivaRDEVeslMCEKRILAAVTSAGHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd14180  14 LGEGSFSVCRKCRHRQSGQEYAVKIISR-----RMEA---NTQREVAALRLCQSHPNIVALHEVLHDQYHTYLVMELLRG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLMLHIHSD-VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEG---YVKIADFGLCKEGMGYGDRTSTFC 782
Cdd:cd14180  86 GELLDRIKKKaRFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESdgaVLKVIDFGFARLRPQGSRPLQTPC 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 783 GTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGdDEEEVFDSIVND---EVRYPRF---------LSAEAIG 850
Cdd:cd14180 166 FTLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQS-KRGKMFHNHAADimhKIKEGDFslegeawkgVSEEAKD 244
                       250
                ....*....|....*...
gi 47132591 851 IMRRLLRRNPERRLGSSE 868
Cdd:cd14180 245 LVRGLLTVDPAKRLKLSE 262
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
618-899 5.23e-19

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory. Increased expression of PAK6 is found in primary and metastatic prostate cancer. PAK6 may play a role in the regulation of motility. PAK6 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 88.50  E-value: 5.23e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 618 LEDFkflAVLGRGHFGKVLLSEFRPSGELFAIKALkkgDIVARDEVESLMCEKRILaavTSAGHPFLVNLFGCFQTPEHV 697
Cdd:cd06659  23 LENY---VKIGEGSTGVVCIAREKHSGRQVAVKMM---DLRKQQRRELLFNEVVIM---RDYQHPNVVEMYKSYLVGEEL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 698 CFVMEYSAGGDLmlhihSDVFSEPR---AIFYSAC--VVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGM 772
Cdd:cd06659  94 WVLMEYLQGGAL-----TDIVSQTRlneEQIATVCeaVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQIS 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 773 GYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVryPRFLSAEAIG-I 851
Cdd:cd06659 169 KDVPKRKSLVGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDSPP--PKLKNSHKASpV 246
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 47132591 852 MR----RLLRRNPERRlgsseRDAEDVKKQPFfrtlgweaLLARRLPPPFVP 899
Cdd:cd06659 247 LRdfleRMLVRDPQER-----ATAQELLDHPF--------LLQTGLPECLVP 285
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
614-825 6.99e-19

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK1 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K9. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Little is known about the specific function of MLK1. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. There could be redundancy in the function of MLKs. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 87.79  E-value: 6.99e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 614 SPLTLEDfkflaVLGRGHFGKVLLSEFrpSGELFAIKALKKG-DIVARDEVESLMCEKRILAAVTsagHPFLVNLFG-CF 691
Cdd:cd14145   6 SELVLEE-----IIGIGGFGKVYRAIW--IGDEVAVKAARHDpDEDISQTIENVRQEAKLFAMLK---HPNIIALRGvCL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 692 QTPeHVCFVMEYSAGGDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIV---YRDLKLD--------NLLLDTEGYV 760
Cdd:cd14145  76 KEP-NLCLVMEFARGGPLNRVLSGKRIPPDILVNWAVQIARGMNYLHCEAIVpviHRDLKSSnililekvENGDLSNKIL 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47132591 761 KIADFGLCKEGmgygDRTSTF--CGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDD 825
Cdd:cd14145 155 KITDFGLAREW----HRTTKMsaAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPFRGID 217
HR1 pfam02185
Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of ...
133-202 7.04e-19

Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of the N-terminal non-catalytic part of protein kinase PRK1(PKN). The first two of these repeats were later shown to bind the small G protein rho known to activate PKN in its GTP-bound form. Similar rho-binding domains also occur in a number of other protein kinases and in the rho-binding proteins rhophilin and rhotekin. Recently, the structure of the N-terminal HR1 repeat complexed with RhoA has been determined by X-ray crystallography. It forms an antiparallel coiled-coil fold termed an ACC finger.


Pssm-ID: 460478 [Multi-domain]  Cd Length: 67  Bit Score: 81.41  E-value: 7.04e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591   133 RVAGLEKQLAIELKVKQGAENMIQTYSNgsTKDRKLLLTAQQMLQDSKTKIDIIRMQLRRaLQAGQLENQ 202
Cdd:pfam02185   1 RLQELRKKIEVEKKIKEGAENMLRLLQA--TKDRKVLAEAESELRESNRKIQLLREQLRE-LQARHLPSD 67
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
647-864 7.45e-19

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called Ribosomal protein S6 kinase alpha-2 or 90kDa ribosomal protein S6 kinase 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK3 is also called S6K-alpha-2, RPS6KA2, p90RSK2 or MAPK-activated protein kinase 1c (MAPKAPK-1c). RSK3 binds muscle A-kinase anchoring protein (mAKAP)-b directly and regulates concentric cardiac myocyte growth. The RSK3 gene, RPS6KA2, is a putative tumor suppressor gene in sporadic epithelial ovarian cancer and variations to the gene may be associated with rectal cancer risk. RSK3 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 88.15  E-value: 7.45e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 647 FAIKALKKGDIVARDEVESLMcekrilaavTSAGHPFLVNLFGCFQTPEHVCFVMEYSAGGDLMLHI-HSDVFSEPRAIF 725
Cdd:cd14178  31 YAVKIIDKSKRDPSEEIEILL---------RYGQHPNIITLKDVYDDGKFVYLVMELMRGGELLDRIlRQKCFSEREASA 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 726 YSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEG----YVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTDTSYTRA 801
Cdd:cd14178 102 VLCTITKTVEYLHSQGVVHRDLKPSNILYMDESgnpeSIRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKRQGYDAA 181
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 802 VDWWGLGVLLYEMLVGESPF---PGDDEEEVFDSIVNDEVRYP----RFLSAEAIGIMRRLLRRNPERRL 864
Cdd:cd14178 182 CDIWSLGILLYTMLAGFTPFangPDDTPEEILARIGSGKYALSggnwDSISDAAKDIVSKMLHVDPHQRL 251
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
647-868 8.18e-19

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called 90kDa ribosomal protein S6 kinase 3 or Ribosomal protein S6 kinase alpha-3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK2 is also called p90RSK3, RPS6KA3, S6K-alpha-3, or MAPK-activated protein kinase 1b (MAPKAPK-1b). RSK2 is expressed highly in the regions of the brain with high synaptic activity. It plays a role in the maintenance and consolidation of excitatory synapses. It is a specific modulator of phospholipase D in calcium-regulated exocytosis. Mutations in the RSK2 gene, RPS6KA3, cause Coffin-Lowry syndrome (CLS), a rare syndromic form of X-linked mental retardation characterized by growth and psychomotor retardation and skeletal abnormalities. RSK2 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 88.92  E-value: 8.18e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 647 FAIKALKKGDIVARDEVESLMcekrilaavTSAGHPFLVNLFGCFQTPEHVCFVMEYSAGGDLMLHI-HSDVFSEPRAIF 725
Cdd:cd14176  47 FAVKIIDKSKRDPTEEIEILL---------RYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKIlRQKFFSEREASA 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 726 YSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEG----YVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTDTSYTRA 801
Cdd:cd14176 118 VLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLERQGYDAA 197
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47132591 802 VDWWGLGVLLYEMLVGESPF---PGDDEEEVFDSIVNDEVR----YPRFLSAEAIGIMRRLLRRNPERRLGSSE 868
Cdd:cd14176 198 CDIWSLGVLLYTMLTGYTPFangPDDTPEEILARIGSGKFSlsggYWNSVSDTAKDLVSKMLHVDPHQRLTAAL 271
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
619-820 8.45e-19

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. It may also regulate paxillin and consequently, cell migration. MST3 is present in human placenta, where it plays an essential role in the oxidative stress-induced apoptosis of trophoblasts in normal spontaneous delivery. Dysregulation of trophoblast apoptosis may result in pregnancy complications such as preeclampsia and intrauterine growth retardation. The MST3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 87.82  E-value: 8.45e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDivARDEVESLMCEKRILAAVTSaghPFLVNLFGCFQTPEHVC 698
Cdd:cd06641   4 ELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEE--AEDEIEDIQQEITVLSQCDS---PYVTKYYGSYLKDTKLW 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGGDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRT 778
Cdd:cd06641  79 IIMEYLGGGSALDLLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKR 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 47132591 779 STFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESP 820
Cdd:cd06641 159 N*FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPP 200
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
627-868 9.41e-19

Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK2 is localized in the sperm neck, equatorial segment, and mid-piece of the sperm tail. Both TSSK1 and TSSK2 phosphorylate their common substrate TSKS (testis-specific-kinase-substrate). TSSK1/TSSK2 double knock-out mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 87.14  E-value: 9.41e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKGDIvARDEVESLMC-EKRILAAVTsagHPFLVNLFGCFQTPE-HVCFVMEYS 704
Cdd:cd14165   9 LGEGSYAKVKSAYSERLKCNVAIKIIDKKKA-PDDFVEKFLPrELEILARLN---HKSIIKTYEIFETSDgKVYIVMELG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 705 AGGDLMLHI------HSDVfsePRAIFYSACvvLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEgMGYGDR- 777
Cdd:cd14165  85 VQGDLLEFIklrgalPEDV---ARKMFHQLS--SAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKR-CLRDENg 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 778 ----TSTFCGTPEFLAPEVLTDTSYT-RAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPR--FLSAEAIG 850
Cdd:cd14165 159 rivlSKTFCGSAAYAAPEVLQGIPYDpRIYDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQKEHRVRFPRskNLTSECKD 238
                       250
                ....*....|....*...
gi 47132591 851 IMRRLLRRNPERRLGSSE 868
Cdd:cd14165 239 LIYRLLQPDVSQRLCIDE 256
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
618-868 1.00e-18

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: General Control Non-derepressible-2 (GCN2) which is activated during amino acid or serum starvation; protein kinase regulated by RNA (PKR) which is activated by double stranded RNA; heme-regulated inhibitor kinase (HRI) which is activated under heme-deficient conditions; and PKR-like endoplasmic reticulum kinase (PERK) which is activated when misfolded proteins accumulate in the ER. The EIF2AK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 87.35  E-value: 1.00e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 618 LEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDivARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHV 697
Cdd:cd13996   5 LNDFEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIRLTE--KSSASEKVLREVKALAKLN---HPNIVRYYTAWVEEPPL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 698 CFVMEYSAGGDLMLHIHSDVFSEPR------AIFYSacVVLGLQFLHEHKIVYRDLKLDNL-LLDTEGYVKIADFGLCKE 770
Cdd:cd13996  80 YIQMELCEGGTLRDWIDRRNSSSKNdrklalELFKQ--ILKGVSYIHSKGIVHRDLKPSNIfLDNDDLQVKIGDFGLATS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 771 gMGYGDRT---------------STFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVgesPFPGDDE-----EEVF 830
Cdd:cd13996 158 -IGNQKRElnnlnnnnngntsnnSVGIGTPLYASPEQLDGENYNEKADIYSLGIILFEMLH---PFKTAMErstilTDLR 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 47132591 831 DSIVNDEV--RYPrflsAEAIgIMRRLLRRNPERRLGSSE 868
Cdd:cd13996 234 NGILPESFkaKHP----KEAD-LIQSLLSKNPEERPSAEQ 268
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
626-825 1.04e-18

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK4 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 87.02  E-value: 1.04e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRpsGELFAIKALKKG---DIVArdEVESLMCEKRILAAVTsagHPFLVNLFG-CFQTPeHVCFVM 701
Cdd:cd14146   1 IIGVGGFGKVYRATWK--GQEVAVKAARQDpdeDIKA--TAESVRQEAKLFSMLR---HPNIIKLEGvCLEEP-NLCLVM 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 702 EYSAGGDLMLHIH-SDVFSEPRA---------IFYSACVVLGLQFLHEHKIV---YRDLKLDNLLLDTE--------GYV 760
Cdd:cd14146  73 EFARGGTLNRALAaANAAPGPRRarripphilVNWAVQIARGMLYLHEEAVVpilHRDLKSSNILLLEKiehddicnKTL 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47132591 761 KIADFGLCKEGmgygDRTSTF--CGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDD 825
Cdd:cd14146 153 KITDFGLAREW----HRTTKMsaAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRGID 215
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
621-821 1.27e-18

Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). It is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may be involved in the regulation of cell migration and polarization. STK25 binds and phosphorylates CCM3 (cerebral cavernous malformation 3), also called PCD10 (programmed cell death 10), and may play a role in apoptosis. Human STK25 is a candidate gene responsible for pseudopseudohypoparathyroidism (PPHP), a disease that shares features with the Albright hereditary osteodystrophy (AHO) phenotype. The STK25 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 87.03  E-value: 1.27e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDivARDEVESLMCEKRILAAVTSaghPFLVNLFGCFQTPEHVCFV 700
Cdd:cd06642   6 FTKLERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEE--AEDEIEDIQQEITVLSQCDS---PYITRYYGSYLKGTKLWII 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGGDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTST 780
Cdd:cd06642  81 MEYLGGGSALDLLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNT 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 47132591 781 FCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPF 821
Cdd:cd06642 161 FVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPN 201
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
626-821 1.41e-18

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK2 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK2 also activates ERK1/2, c-Jun N-terminal kinase (JNK) and p38 through their respective MAPKKs MEK1/2, JNK-activating kinase 2 (JNKK2), and MKK3/6. MEKK2 plays roles in T cell receptor signaling, immune synapse formation, cytokine gene expression, as well as in EGF and FGF receptor signaling. The MEKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 86.64  E-value: 1.41e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGELFAIKALK--KGDIVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEH--VCFVM 701
Cdd:cd06652   9 LLGQGAFGRVYLCYDADTGRELAVKQVQfdPESPETSKEVNALECEIQLLKNLL---HERIVQYYGCLRDPQErtLSIFM 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 702 EYSAGGDLMLHIHS-DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFG-------LCKEGMG 773
Cdd:cd06652  86 EYMPGGSIKDQLKSyGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGaskrlqtICLSGTG 165
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 47132591 774 YGDRTstfcGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPF 821
Cdd:cd06652 166 MKSVT----GTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPW 209
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
619-863 1.45e-18

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The VEGFR subfamily consists of VEGFR1 (Flt1), VEGFR2 (Flk1), VEGFR3 (Flt4), and similar proteins. VEGFR subfamily members are receptor PTKss (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. There are five VEGF ligands in mammals, which bind, in an overlapping pattern to the three VEGFRs, which can form homo or heterodimers. VEGFRs regulate the cardiovascular system. They are critical for vascular development during embryogenesis and blood vessel formation in adults. They induce cellular functions common to other growth factor receptors such as cell migration, survival, and proliferation. The VEGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 87.55  E-value: 1.45e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVL-LSEF----RPSGELFAIKALKKGdivARD-EVESLMCEKRILAAVtsAGHPFLVNLFGCFQ 692
Cdd:cd05054   7 DRLKLGKPLGRGAFGKVIqASAFgidkSATCRTVAVKMLKEG---ATAsEHKALMTELKILIHI--GHHLNVVNLLGACT 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 693 TPEHVCFVM------------------EYSAGGDLMLHIH------SDVFSEPRA----IFYSACVVLGLQFLHEHKIVY 744
Cdd:cd05054  82 KPGGPLMVIvefckfgnlsnylrskreEFVPYRDKGARDVeeeeddDELYKEPLTledlICYSFQVARGMEFLASRKCIH 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 745 RDLKLDNLLLDTEGYVKIADFGLCKEgmGYGDR---TSTFCGTP-EFLAPEVLTDTSYTRAVDWWGLGVLLYEML-VGES 819
Cdd:cd05054 162 RDLAARNILLSENNVVKICDFGLARD--IYKDPdyvRKGDARLPlKWMAPESIFDKVYTTQSDVWSFGVLLWEIFsLGAS 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 47132591 820 PFPGDDEEEVFDSIVNDEVRY--PRFLSAEAIGIMRRLLRRNPERR 863
Cdd:cd05054 240 PYPGVQMDEEFCRRLKEGTRMraPEYTTPEIYQIMLDCWHGEPKER 285
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
621-815 1.90e-18

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 86.87  E-value: 1.90e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRP----SGELFAIKALKKGDIvarDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEH 696
Cdd:cd05081   6 LKYISQLGKGNFGSVELCRYDPlgdnTGALVAVKQLQHSGP---DQQRDFQREIQILKALH---SDFIVKYRGVSYGPGR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 697 VCF--VMEYSAGGDL--MLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK--- 769
Cdd:cd05081  80 RSLrlVMEYLPSGCLrdFLQRHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKllp 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 47132591 770 -EGMGYGDRTSTfcGTPEF-LAPEVLTDTSYTRAVDWWGLGVLLYEML 815
Cdd:cd05081 160 lDKDYYVVREPG--QSPIFwYAPESLSDNIFSRQSDVWSFGVVLYELF 205
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
619-821 2.93e-18

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIB myosin is expressed highly in retina. It is also present in the brain and testis. The human class IIIB myosin gene maps to a region that overlaps the locus for Bardet-Biedl syndrome, which is characterized by dysmorphic extremities, retinal dystrophy, obesity, male hypogenitalism, and renal abnormalities. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. They may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. They may also function as cargo carriers during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 86.20  E-value: 2.93e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALkkgDIVArDEVESLMCEKRILAAVTSagHPFLVNLFGCFQTPEHVC 698
Cdd:cd06639  22 DTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKIL---DPIS-DVDEEIEAEYNILRSLPN--HPNVVKFYGMFYKADQYV 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 -----FVMEYSAGGDLM-----LHIHSDVFSEP--RAIFYSAcvVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFG 766
Cdd:cd06639  96 ggqlwLVLELCNGGSVTelvkgLLKCGQRLDEAmiSYILYGA--LLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFG 173
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 767 LCKEGMGYGDRTSTFCGTPEFLAPEVLT-----DTSYTRAVDWWGLGVLLYEMLVGESPF 821
Cdd:cd06639 174 VSAQLTSARLRRNTSVGTPFWMAPEVIAceqqyDYSYDARCDVWSLGITAIELADGDPPL 233
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
617-880 2.96e-18

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK2 is ubiquitously expressed and is essential in autophagy induction. It displays partially redundant functions with ULK1 and is able to compensate for the loss of ULK1 in non-selective autophagy. It also displays neuron-specific functions and is important in axon development. The ULK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 85.83  E-value: 2.96e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 617 TLEDFKFLA--VLGRGHFGKVLLSEFRPSGEL-FAIKALKKGDIvARDEVeSLMCEKRILAAVTsagHPFLVNLFGCFQT 693
Cdd:cd14201   2 VVGDFEYSRkdLVGHGAFAVVFKGRHRKKTDWeVAIKSINKKNL-SKSQI-LLGKEIKILKELQ---HENIVALYDVQEM 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 694 PEHVCFVMEYSAGGDLMLHIHSD-VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGY---------VKIA 763
Cdd:cd14201  77 PNSVFLVMEYCNGGDLADYLQAKgTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASRkkssvsgirIKIA 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 764 DFGLCKEgMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEV---FDSIVNDEVRY 840
Cdd:cd14201 157 DFGFARY-LQSNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQDLrmfYEKNKNLQPSI 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 47132591 841 PRFLSAEAIGIMRRLLRRNPERRLgsserDAEDVKKQPFF 880
Cdd:cd14201 236 PRETSPYLADLLLGLLQRNQKDRM-----DFEAFFSHPFL 270
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
681-863 3.23e-18

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 85.83  E-value: 3.23e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 681 HPFLVNLFGCFQTPEH-VCFVMEYSAGGDLMLHI-HSDVFSEPRAIFYSACVVLGLQFLHEHK---IVY--RDLKLDNLL 753
Cdd:cd13990  63 HPRIVKLYDVFEIDTDsFCTVLEYCDGNDLDFYLkQHKSIPEREARSIIMQVVSALKYLNEIKppiIHYdlKPGNILLHS 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 754 LDTEGYVKIADFGLCK---------EGMgygDRTSTFCGTPEFLAPEVL----TDTSYTRAVDWWGLGVLLYEMLVGESP 820
Cdd:cd13990 143 GNVSGEIKITDFGLSKimddesynsDGM---ELTSQGAGTYWYLPPECFvvgkTPPKISSKVDVWSVGVIFYQMLYGRKP 219
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 47132591 821 FpGDD---EEEVF-DSIVN-DEVRYPR--FLSAEAIGIMRRLLRRNPERR 863
Cdd:cd13990 220 F-GHNqsqEAILEeNTILKaTEVEFPSkpVVSSEAKDFIRRCLTYRKEDR 268
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
627-884 4.65e-18

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 85.84  E-value: 4.65e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKalkKGDIVARDEVESLMCEKRILaavTSAGHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd06657  28 IGEGSTGIVCIATVKSSGKLVAVK---KMDLRKQQRRELLFNEVVIM---RDYQHENVVEMYNSYLVGDELWVVMEFLEG 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCGTPE 786
Cdd:cd06657 102 GALTDIVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPY 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 787 FLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVND---EVRYPRFLSAEAIGIMRRLLRRNPERR 863
Cdd:cd06657 182 WMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNlppKLKNLHKVSPSLKGFLDRLLVRDPAQR 261
                       250       260
                ....*....|....*....|.
gi 47132591 864 LGSSErdaedVKKQPFFRTLG 884
Cdd:cd06657 262 ATAAE-----LLKHPFLAKAG 277
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
619-829 5.09e-18

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 1; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. MEK1 also plays a role in cell cycle control. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 86.26  E-value: 5.09e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFA-------IKALKKGDIVardeveslmcekRILAAVTSAGHPFLVNLFGCF 691
Cdd:cd06650   5 DDFEKISELGAGNGGVVFKVSHKPSGLVMArklihleIKPAIRNQII------------RELQVLHECNSPYIVGFYGAF 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 692 QTPEHVCFVMEYSAGGDLMlHIHSDVFSEPRAIF--YSACVVLGLQFLHE-HKIVYRDLKLDNLLLDTEGYVKIADFGLc 768
Cdd:cd06650  73 YSDGEISICMEHMDGGSLD-QVLKKAGRIPEQILgkVSIAVIKGLTYLREkHKIMHRDVKPSNILVNSRGEIKLCDFGV- 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47132591 769 kEGMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEV 829
Cdd:cd06650 151 -SGQLIDSMANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIPPPDAKEL 210
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
621-821 5.13e-18

N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinase Kinase 4 and 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K4 is also called Nck Interacting kinase (NIK). It facilitates the activation of the MAPKs, extracellular signal-regulated kinase (ERK) 1, ERK2, and c-Jun N-terminal kinase (JNK), by phosphorylating and activating MEKK1. MAP4K4 plays a role in tumor necrosis factor (TNF) alpha-induced insulin resistance. MAP4K4 silencing in skeletal muscle cells from type II diabetic patients restores insulin-mediated glucose uptake. MAP4K4, through JNK, also plays a broad role in cell motility, which impacts inflammation, homeostasis, as well as the invasion and spread of cancer. MAP4K4 is found to be highly expressed in most tumor cell lines relative to normal tissue. MAP4K6 (also called MINK for Misshapen/NIKs-related kinase) is activated after Ras induction and mediates activation of p38 MAPK. MAP4K6 plays a role in cell cycle arrest, cytoskeleton organization, cell adhesion, and cell motility. The MAP4K4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 85.44  E-value: 5.13e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKkgdiVARDEVESLMCEKRILAAVTSagHPFLVNLFGCF--QTP---- 694
Cdd:cd06636  18 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMD----VTEDEEEEIKLEINMLKKYSH--HRNIATYYGAFikKSPpghd 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 695 EHVCFVMEYSAGG---DLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEG 771
Cdd:cd06636  92 DQLWLVMEFCGAGsvtDLVKNTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL 171
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 47132591 772 MGYGDRTSTFCGTPEFLAPEVLT-----DTSYTRAVDWWGLGVLLYEMLVGESPF 821
Cdd:cd06636 172 DRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPL 226
S_TK_X smart00133
Extension to Ser/Thr-type protein kinases;
885-945 5.48e-18

Extension to Ser/Thr-type protein kinases;


Pssm-ID: 214529  Cd Length: 64  Bit Score: 78.56  E-value: 5.48e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47132591    885 WEALLARRLPPPFVPTLSGRTDVSNFDEEFTGEAPTLSPPrDARPLTAAEQAAFLDFDFVA 945
Cdd:smart00133   5 WDKLENKEIEPPFVPKIKSPTDTSNFDPEFTEETPVLTPV-DSPLSGGIQQEPFRGFSYVF 64
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
619-864 6.38e-18

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 85.09  E-value: 6.38e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFR--PSGELF---AIKALKkGDIVARDEVESLMcEKRILAAVTSaghPFLVNLFGCFQT 693
Cdd:cd05032   6 EKITLIRELGQGSFGMVYEGLAKgvVKGEPEtrvAIKTVN-ENASMRERIEFLN-EASVMKEFNC---HHVVRLLGVVST 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 694 PEHVCFVMEYSAGGDLMLHI--------HSDVFSEP---RAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKI 762
Cdd:cd05032  81 GQPTLVVMELMAKGDLKSYLrsrrpeaeNNPGLGPPtlqKFIQMAAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVKI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 763 ADFGLCKEgMGYGD--RTSTFCGTP-EFLAPEVLTDTSYTRAVDWWGLGVLLYEML-VGESPFPGDDEEEVFDSIV-NDE 837
Cdd:cd05032 161 GDFGMTRD-IYETDyyRKGGKGLLPvRWMAPESLKDGVFTTKSDVWSFGVVLWEMAtLAEQPYQGLSNEEVLKFVIdGGH 239
                       250       260
                ....*....|....*....|....*..
gi 47132591 838 VRYPRFLSAEAIGIMRRLLRRNPERRL 864
Cdd:cd05032 240 LDLPENCPDKLLELMRMCWQYNPKMRP 266
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
626-821 7.16e-18

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK2 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K10. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK2 is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK2 also binds to normal huntingtin (Htt), which is important in neuronal transcription, development, and survival. MLK2 does not bind to the polyglutamine-expanded Htt, which is implicated in the pathogeneis of Huntington's disease, leading to neuronal toxicity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 84.65  E-value: 7.16e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRpsGELFAIKALKKG---DIVArdEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFVME 702
Cdd:cd14148   1 IIGVGGFGKVYKGLWR--GEEVAVKAARQDpdeDIAV--TAENVRQEARLFWMLQ---HPNIIALRGVCLNPPHLCLVME 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 703 YSAGGDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIV---YRDLKLD--------NLLLDTEGYVKIADFGLCKEG 771
Cdd:cd14148  74 YARGGALNRALAGKKVPPHVLVNWAVQIARGMNYLHNEAIVpiiHRDLKSSnililepiENDDLSGKTLKITDFGLAREW 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 47132591 772 mgygDRTSTF--CGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPF 821
Cdd:cd14148 154 ----HKTTKMsaAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPY 201
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
626-880 1.19e-17

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. It associates with three autophagy-related proteins (Atg13, FIP200 amd Atg101) to form the ULK1 complex. All fours proteins are essential for autophagosome formation. ULK1 is regulated by both mammalian target-of rapamycin complex 1 (mTORC1) and AMP-activated protein kinase (AMPK). mTORC1 negatively regulates the ULK1 complex in a nutrient-dependent manner while AMPK stimulates autophagy by inhibiting mTORC1. ULK1 also plays neuron-specific roles and is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, neurite extension, and axon branching. The ULK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 83.91  E-value: 1.19e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGEL-FAIKALKKGDIVARDEVesLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFVMEYS 704
Cdd:cd14202   9 LIGHGAFAVVFKGRHKEKHDLeVAVKCINKKNLAKSQTL--LGKEIKILKELK---HENIVALYDFQEIANSVYLVMEYC 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 705 AGGDLMLHIHS-DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEG---------YVKIADFGLCKEGMGy 774
Cdd:cd14202  84 NGGDLADYLHTmRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGgrksnpnniRIKIADFGFARYLQN- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 775 GDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEV---FDSIVNDEVRYPRFLSAEAIGI 851
Cdd:cd14202 163 NMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQDLrlfYEKNKSLSPNIPRETSSHLRQL 242
                       250       260
                ....*....|....*....|....*....
gi 47132591 852 MRRLLRRNPERRLgsserDAEDVKKQPFF 880
Cdd:cd14202 243 LLGLLQRNQKDRM-----DFDEFFHHPFL 266
HR1 pfam02185
Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of ...
220-279 1.22e-17

Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of the N-terminal non-catalytic part of protein kinase PRK1(PKN). The first two of these repeats were later shown to bind the small G protein rho known to activate PKN in its GTP-bound form. Similar rho-binding domains also occur in a number of other protein kinases and in the rho-binding proteins rhophilin and rhotekin. Recently, the structure of the N-terminal HR1 repeat complexed with RhoA has been determined by X-ray crystallography. It forms an antiparallel coiled-coil fold termed an ACC finger.


Pssm-ID: 460478 [Multi-domain]  Cd Length: 67  Bit Score: 77.95  E-value: 1.22e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591   220 RIEELRHHFRVEHAVAEGAKNVLRLLSAAKapDRKAVSEAQEKLTESNQKLGLLREALER 279
Cdd:pfam02185   1 RLQELRKKIEVEKKIKEGAENMLRLLQATK--DRKVLAEAESELRESNRKIQLLREQLRE 58
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
647-835 1.28e-17

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called Ribosomal protein S6 kinase alpha-6 or 90kDa ribosomal protein S6 kinase 6); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK4 is also called S6K-alpha-6, RPS6KA6, p90RSK6 or pp90RSK4. RSK4 is a substrate of ERK and is a modulator of p53-dependent proliferation arrest in human cells. Deletion of the RSK4 gene, RPS6KA6, frequently occurs in patients of X-linked deafness type 3, mental retardation and choroideremia. Studies of RSK4 in cancer cells and tissues suggest that it may be oncogenic or tumor suppressive depending on many factors. RSK4 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 84.68  E-value: 1.28e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 647 FAIKALKKGDIVARDEVESLMcekrilaavTSAGHPFLVNLFGCFQTPEHVCFVMEYSAGGDLMLHI-HSDVFSEPRAIF 725
Cdd:cd14177  32 FAVKIIDKSKRDPSEEIEILM---------RYGQHPNIITLKDVYDDGRYVYLVTELMKGGELLDRIlRQKFFSEREASA 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 726 YSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEG----YVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTDTSYTRA 801
Cdd:cd14177 103 VLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSanadSIRICDFGFAKQLRGENGLLLTPCYTANFVAPEVLMRQGYDAA 182
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 47132591 802 VDWWGLGVLLYEMLVGESPF---PGDDEEEVFDSIVN 835
Cdd:cd14177 183 CDIWSLGVLLYTMLAGYTPFangPNDTPEEILLRIGS 219
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
621-868 1.55e-17

Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 and CDK6 partner with D-type cyclins to regulate the early G1 phase of the cell cycle. They are the first kinases activated by mitogenic signals to release cells from the G0 arrested state. CDK4 and CDK6 are both expressed ubiquitously, associate with all three D cyclins (D1, D2 and D3), and phosphorylate the retinoblastoma (pRb) protein. They are also regulated by the INK4 family of inhibitors which associate with either the CDK alone or the CDK/cyclin complex. CDK4 and CDK6 show differences in subcellular localization, sensitivity to some inhibitors, timing in activation, tumor selectivity, and possibly substrate profiles. Although CDK4 and CDK6 seem to show some redundancy, they also have discrete, nonoverlapping functions. CDK6 plays an important role in cell differentiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4/6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 84.25  E-value: 1.55e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKkgdiVARDEV---ESLMCEKRILAAVTSAGHPFLVNLFgcfqtpeHV 697
Cdd:cd07838   1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKVR----VPLSEEgipLSTIREIALLKQLESFEHPNVVRLL-------DV 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 698 CFVMEYSAGGDLML---HIHSD-----------VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIA 763
Cdd:cd07838  70 CHGPRTDRELKLTLvfeHVDQDlatyldkcpkpGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 764 DFGLCKEgmgYGDRTS-TFC-GTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDE----EEVFDSI-VND 836
Cdd:cd07838 150 DFGLARI---YSFEMAlTSVvVTLWYRAPEVLLQSSYATPVDMWSVGCIFAELFNRRPLFRGSSEadqlGKIFDVIgLPS 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 47132591 837 EVRYPR--------F--------------LSAEAIGIMRRLLRRNPERRLGSSE 868
Cdd:cd07838 227 EEEWPRnsalprssFpsytprpfksfvpeIDEEGLDLLKKMLTFNPHKRISAFE 280
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
621-883 1.57e-17

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK7 plays essential roles in the cell cycle and in transcription. It associates with cyclin H and MAT1 and acts as a CDK-Activating Kinase (CAK) by phosphorylating and activating cell cycle CDKs (CDK1/2/4/6). In the brain, it activates CDK5. CDK7 is also a component of the general transcription factor TFIIH, which phosphorylates the C-terminal domain (CTD) of RNA polymerase II when it is bound with unphosphorylated DNA, as present in the pre-initiation complex. Following phosphorylation, the CTD dissociates from the DNA which allows transcription initiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 84.16  E-value: 1.57e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDI-VARDEVE-SLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVC 698
Cdd:cd07841   2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERkEAKDGINfTALREIKLLQELK---HPNIIGLLDVFGHKSNIN 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYsAGGDLMLHIH--SDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEgMGY-G 775
Cdd:cd07841  79 LVFEF-METDLEKVIKdkSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLARS-FGSpN 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 776 DRTSTFCGTPEFLAPEVLTD-TSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVN-----------DEVRYPRF 843
Cdd:cd07841 157 RKMTHQVVTRWYRAPELLFGaRHYGVGVDMWSVGCIFAELLLRVPFLPGDSDIDQLGKIFEalgtpteenwpGVTSLPDY 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 47132591 844 L-----------------SAEAIGIMRRLLRRNPERRLgsserDAEDVKKQPFFRTL 883
Cdd:cd07841 237 VefkpfpptplkqifpaaSDDALDLLQRLLTLNPNKRI-----TARQALEHPYFSND 288
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
620-883 1.60e-17

Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Tec-like subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases form the second largest subfamily of nonreceptor PTKs and are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. Tec kinases play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. Mutations in Btk cause the severe B-cell immunodeficiency, X-linked agammaglobulinaemia (XLA). The Tec-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 83.27  E-value: 1.60e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKFLAVLGRGHFGKVLLSEFRPSGELfAIKALKKGDIVARDEVEslmcEKRILaavTSAGHPFLVNLFGCFQTPEHVCF 699
Cdd:cd05059   5 ELTFLKELGSGQFGVVHLGKWRGKIDV-AIKMIKEGSMSEDDFIE----EAKVM---MKLSHPKLVQLYGVCTKQRPIFI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYSAGGDLMLHIHSDVFSEPRAIFYSAC--VVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMgyGDR 777
Cdd:cd05059  77 VTEYMANGCLLNYLRERRGKFQTEQLLEMCkdVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARYVL--DDE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 778 TSTFCGTP---EFLAPEVLTDTSYTRAVDWWGLGVLLYEMLV-GESPFPGDDEEEVFDSIVNDEVRY-PRFLSAEAIGIM 852
Cdd:cd05059 155 YTSSVGTKfpvKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSeGKMPYERFSNSEVVEHISQGYRLYrPHLAPTEVYTIM 234
                       250       260       270
                ....*....|....*....|....*....|.
gi 47132591 853 RRLLRRNPERRlgsserdaedvkkqPFFRTL 883
Cdd:cd05059 235 YSCWHEKPEER--------------PTFKIL 251
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
628-868 1.67e-17

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK4 is a MAPK kinase kinase that phosphorylates and activates the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. MEKK4 also plays roles in the re-polarization of the actin cytoskeleton in response to osmotic stress, in the proper closure of the neural tube, in cardiovascular development, and in immune responses. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270796 [Multi-domain]  Cd Length: 265  Bit Score: 83.51  E-value: 1.67e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 628 GRGHFGKVLLSEFRPSGELFAIK--ALKKGDivaRDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFVMEYSA 705
Cdd:cd06626   9 GEGTFGKVYTAVNLDTGELMAMKeiRFQDND---PKTIKEIADEMKVLEGLD---HPNLVRYYGVEVHREEVYIFMEYCQ 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 706 GGDL--MLHiHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK-----EGMGYGDRT 778
Cdd:cd06626  83 EGTLeeLLR-HGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVklknnTTTMAPGEV 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 779 STFCGTPEFLAPEVLTDTS---YTRAVDWWGLGVLLYEMLVGESPFPG-DDEEEVFDSIVNDEVryPRF-----LSAEAI 849
Cdd:cd06626 162 NSLVGTPAYMAPEVITGNKgegHGRAADIWSLGCVVLEMATGKRPWSElDNEWAIMYHVGMGHK--PPIpdslqLSPEGK 239
                       250
                ....*....|....*....
gi 47132591 850 GIMRRLLRRNPERRLGSSE 868
Cdd:cd06626 240 DFLSRCLESDPKKRPTASE 258
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
619-863 2.01e-17

Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 83.74  E-value: 2.01e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKkgdiVARDEVE--SLMCEKRILAAVTSaghPFLVNLFGCFQTPEH 696
Cdd:cd06622   1 DEIEVLDELGKGNYGSVYKVLHRPTGVTMAMKEIR----LELDESKfnQIIMELDILHKAVS---PYIVDFYGAFFIEGA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 697 VCFVMEYSAGGDL-MLH---IHSDVFSEPRAIFYSACVVLGLQFLHE-HKIVYRDLKLDNLLLDTEGYVKIADFGLckEG 771
Cdd:cd06622  74 VYMCMEYMDAGSLdKLYaggVATEGIPEDVLRRITYAVVKGLKFLKEeHNIIHRDVKPTNVLVNGNGQVKLCDFGV--SG 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 772 MGYGDRTSTFCGTPEFLAPE---VLTDT---SYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVF---DSIVN-DEVRYP 841
Cdd:cd06622 152 NLVASLAKTNIGCQSYMAPErikSGGPNqnpTYTVQSDVWSLGLSILEMALGRYPYPPETYANIFaqlSAIVDgDPPTLP 231
                       250       260
                ....*....|....*....|..
gi 47132591 842 RFLSAEAIGIMRRLLRRNPERR 863
Cdd:cd06622 232 SGYSDDAQDFVAKCLNKIPNRR 253
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
619-880 2.54e-17

Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RPK118 contains an N-terminal Phox homology (PX) domain, a Microtubule Interacting and Trafficking (MIT) domain, and a kinase domain containing a long uncharacterized insert. Also included in the family is human RPK60 (or ribosomal protein S6 kinase-like 1), which also contains MIT and kinase domains but lacks a PX domain. RPK118 binds sphingosine kinase, a key enzyme in the synthesis of sphingosine 1-phosphate (SPP), a lipid messenger involved in many cellular events. RPK118 may be involved in transmitting SPP-mediated signaling. RPK118 also binds the antioxidant peroxiredoxin-3. RPK118 may be involved in the transport of PRDX3 from the cytoplasm to its site of function in the mitochondria. The RPK118-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270728 [Multi-domain]  Cd Length: 265  Bit Score: 82.98  E-value: 2.54e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRghFGKVLLSEFRPSGELFAIKALKKGDIVARDEVeslmcekrilaAVTSAGHPFLVNLFGCFQTPEHVC 698
Cdd:cd05576   1 EELKAFRVLGV--IDKVLLVMDTRTQETFILKGLRKSSEYSRERK-----------TIIPRCVPNMVCLRKYIISEESVF 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGGDLMLHIHS--------------DVFSEPRAIFY---------SACVVLGLQFLHEHKIVYRDLKLDNLLLD 755
Cdd:cd05576  68 LVLQHAEGGKLWSYLSKflndkeihqlfadlDERLAAASRFYipeeciqrwAAEMVVALDALHREGIVCRDLNPNNILLN 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 756 TEGYVKIADFGLCKEGMGYGDRTST---FCgtpeflAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFpgddeeEVFDS 832
Cdd:cd05576 148 DRGHIQLTYFSRWSEVEDSCDSDAIenmYC------APEVGGISEETEACDWWSLGALLFELLTGKALV------ECHPA 215
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 47132591 833 IVN--DEVRYPRFLSAEAIGIMRRLLRRNPERRLGSSERDAEDVKKQPFF 880
Cdd:cd05576 216 GINthTTLNIPEWVSEEARSLLQQLLQFNPTERLGAGVAGVEDIKSHPFF 265
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
619-880 3.36e-17

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDKL1-5 and similar proteins. Some CDKLs, like CDKL1 and CDKL3, may be implicated in transformation and others, like CDKL3 and CDKL5, are associated with mental retardation when impaired. CDKL2 plays a role in learning and memory. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270827 [Multi-domain]  Cd Length: 288  Bit Score: 83.14  E-value: 3.36e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDivaRDEV--ESLMCEKRILAAVTsagHPFLVNLFGCFQTPEH 696
Cdd:cd07833   1 NKYEVLGVVGEGAYGVVLKCRNKATGEIVAIKKFKESE---DDEDvkKTALREVKVLRQLR---HENIVNLKEAFRRKGR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 697 VCFVMEYsaggdlmlhIHSDVFSE---------PRAI-FYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFG 766
Cdd:cd07833  75 LYLVFEY---------VERTLLELleaspgglpPDAVrSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFG 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 767 LCKEGMGYGDRTST-FCGTPEFLAPEVLT-DTSYTRAVDWWGLGVLLYEMLVGESPFPGDDE------------------ 826
Cdd:cd07833 146 FARALTARPASPLTdYVATRWYRAPELLVgDTNYGKPVDVWAIGCIMAELLDGEPLFPGDSDidqlyliqkclgplppsh 225
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47132591 827 EEVFDS--------------IVNDEVRYPRFLSAEAIGIMRRLLRRNPERRLgsserDAEDVKKQPFF 880
Cdd:cd07833 226 QELFSSnprfagvafpepsqPESLERRYPGKVSSPALDFLKACLRMDPKERL-----TCDELLQHPYF 288
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
616-863 4.43e-17

Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The FGFR subfamily consists of FGFR1, FGFR2, FGFR3, FGFR4, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, and to heparin/heparan sulfate (HS) results in the formation of a ternary complex, which leads to receptor dimerization and activation, and intracellular signaling. There are at least 23 FGFs and four types of FGFRs. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. FGF/FGFR signaling is important in the regulation of embryonic development, homeostasis, and regenerative processes. Depending on the cell type and stage, FGFR signaling produces diverse cellular responses including proliferation, growth arrest, differentiation, and apoptosis. Aberrant signaling leads to many human diseases such as skeletal, olfactory, and metabolic disorders, as well as cancer. The FGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 82.85  E-value: 4.43e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 616 LTLEDFKFLAVLGRGHFGKVLLSEF-----RPSGEL-FAIKALKkGDIVARDeVESLMCEKRILAAVtsAGHPFLVNLFG 689
Cdd:cd05053   9 LPRDRLTLGKPLGEGAFGQVVKAEAvgldnKPNEVVtVAVKMLK-DDATEKD-LSDLVSEMEMMKMI--GKHKNIINLLG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 690 CF--QTPEHVcfVMEYSAGGDL-----------------MLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLD 750
Cdd:cd05053  85 ACtqDGPLYV--VVEYASKGNLreflrarrppgeeaspdDPRVPEEQLTQKDLVSFAYQVARGMEYLASKKCIHRDLAAR 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 751 NLLLdTEGYV-KIADFGLCKeGMGYGD--RTSTFCGTP-EFLAPEVLTDTSYTRAVDWWGLGVLLYE-MLVGESPFPGDD 825
Cdd:cd05053 163 NVLV-TEDNVmKIADFGLAR-DIHHIDyyRKTTNGRLPvKWMAPEALFDRVYTHQSDVWSFGVLLWEiFTLGGSPYPGIP 240
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 47132591 826 EEEVFDSIVNDE-VRYPRFLSAEAIGIMRRLLRRNPERR 863
Cdd:cd05053 241 VEELFKLLKEGHrMEKPQNCTQELYMLMRDCWHEVPSQR 279
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
619-876 5.72e-17

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR1 (or Flt1) binds VEGFA, VEGFB, and placenta growth factor (PLGF). It regulates monocyte and macrophage migration, vascular permeability, haematopoiesis, and the recruitment of haematopietic progenitor cells from the bone marrow. VEGFR1 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 83.51  E-value: 5.72e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVL-LSEF----RPSGELFAIKALKKGdiVARDEVESLMCEKRILaavTSAGHPF-LVNLFG-CF 691
Cdd:cd14207   7 ERLKLGKSLGRGAFGKVVqASAFgikkSPTCRVVAVKMLKEG--ATASEYKALMTELKIL---IHIGHHLnVVNLLGaCT 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 692 QTPEHVCFVMEYSAGGDLMLHIHS--DVFS---------EPRA------------------------------------- 723
Cdd:cd14207  82 KSGGPLMVIVEYCKYGNLSNYLKSkrDFFVtnkdtslqeELIKekkeaeptggkkkrlesvtssesfassgfqedkslsd 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 724 ---------------------IFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGD--RTST 780
Cdd:cd14207 162 veeeeedsgdfykrpltmedlISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARDIYKNPDyvRKGD 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 781 FCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEML-VGESPFPGDDEEEVFDSIVNDEVRY--PRFLSAEAIGIMRRLLR 857
Cdd:cd14207 242 ARLPLKWMAPESIFDKIYSTKSDVWSYGVLLWEIFsLGASPYPGVQIDEDFCSKLKEGIRMraPEFATSEIYQIMLDCWQ 321
                       330
                ....*....|....*....
gi 47132591 858 RNPERRlgssERDAEDVKK 876
Cdd:cd14207 322 GDPNER----PRFSELVER 336
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
617-900 6.12e-17

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK10, also called PISSLRE, is essential for cell growth and proliferation, and acts through the G2/M phase of the cell cycle. CDK10 has also been identified as an important factor in endocrine therapy resistance in breast cancer. CDK10 silencing increases the transcription of c-RAF and the activation of the p42/p44 MAPK pathway, which leads to antiestrogen resistance. Patients who express low levels of CDK10 relapse early on tamoxifen. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK10 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 82.80  E-value: 6.12e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 617 TLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDivARD--EVESLMcEKRILAAVTsagHPFLVNLFGCF--Q 692
Cdd:cd07845   5 SVTEFEKLNRIGEGTYGIVYRARDTTSGEIVALKKVRMDN--ERDgiPISSLR-EITLLLNLR---HPNIVELKEVVvgK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 693 TPEHVCFVMEYSAGgDL--MLHIHSDVFSEPRAifysACVVL----GLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFG 766
Cdd:cd07845  79 HLDSIFLVMEYCEQ-DLasLLDNMPTPFSESQV----KCLMLqllrGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 767 LCKE-GMGYGDRTSTFCgTPEFLAPEVLT-DTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIV------NDEV 838
Cdd:cd07845 154 LARTyGLPAKPMTPKVV-TLWYRAPELLLgCTTYTTAIDMWAVGCILAELLAHKPLLPGKSEIEQLDLIIqllgtpNESI 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 839 -------------------------RYPrFLSAEAIGIMRRLLRRNPERRLgsserDAEDVKKQPFFRtlgwEALLArrL 893
Cdd:cd07845 233 wpgfsdlplvgkftlpkqpynnlkhKFP-WLSEAGLRLLNFLLMYDPKKRA-----TAEEALESSYFK----EKPLP--C 300

                ....*..
gi 47132591 894 PPPFVPT 900
Cdd:cd07845 301 EPEMMPT 307
HR1 cd00089
Protein kinase C-related kinase homology region 1 (HR1) domain that binds Rho family small ...
128-196 6.49e-17

Protein kinase C-related kinase homology region 1 (HR1) domain that binds Rho family small GTPases; The HR1 domain, also called the ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. It is found in Rho effector proteins including PKC-related kinases such as vertebrate PRK1 (or PKN) and yeast PKC1 protein kinases C, as well as in rhophilins and Rho-associated kinase (ROCK). Rho family members function as molecular switches, cycling between inactive and active forms, controlling a variety of cellular processes. HR1 domains may occur in repeat arrangements (PKN contains three HR1 domains), separated by a short linker region.


Pssm-ID: 212008 [Multi-domain]  Cd Length: 68  Bit Score: 75.83  E-value: 6.49e-17
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47132591 128 ATNLSRVAGLEKQLAIELKVKQGAENMIQTYSNGstKDRKLLLTAQQMLQDSKTKIDIIRMQLRRALQA 196
Cdd:cd00089   1 SKLQQRLEELRRKLEKELKIREGAENLLKLYSNP--KVKKDLAEVQLNLKESKEKIDLLKRQLERYNAL 67
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
621-864 6.55e-17

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 and three PIM2 isoforms as a result of alternative translation initiation sites, while there is only one PIM3 protein. Compound knockout mice deficient of all three PIM kinases that survive the perinatal period show a profound reduction in body size, indicating that PIMs are important for body growth. The PIM subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 81.51  E-value: 6.55e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLlSEFRPSGEL-FAIKALKKGDIVARDEV---ESLMCEKRILAAVTSAGHPFLVNLFGCFQTPEH 696
Cdd:cd14005   2 YEVGDLLGKGGFGTVY-SGVRIRDGLpVAVKFVPKSRVTEWAMIngpVPVPLEIALLLKASKPGVPGVIRLLDWYERPDG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 697 VCFVMEYSAGG-DLMLHI-HSDVFSE--PRAIFYSacVVLGLQFLHEHKIVYRDLKLDNLLLDTE-GYVKIADFG---LC 768
Cdd:cd14005  81 FLLIMERPEPCqDLFDFItERGALSEnlARIIFRQ--VVEAVRHCHQRGVLHRDIKDENLLINLRtGEVKLIDFGcgaLL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 769 KEGMgYgdrtSTFCGTPEFLAPEVLTDTSY-TRAVDWWGLGVLLYEMLVGESPFPGDDEeevfdsIVNDEVRYPRFLSAE 847
Cdd:cd14005 159 KDSV-Y----TDFDGTRVYSPPEWIRHGRYhGRPATVWSLGILLYDMLCGDIPFENDEQ------ILRGNVLFRPRLSKE 227
                       250
                ....*....|....*..
gi 47132591 848 AIGIMRRLLRRNPERRL 864
Cdd:cd14005 228 CCDLISRCLQFDPSKRP 244
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
620-814 6.93e-17

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek8 contains an N-terminal kinase catalytic domain and a C-terminal RCC1 (regulator of chromosome condensation) domain. A double point mutation in Nek8 causes cystic kidney disease in mice that genetically resembles human autosomal recessive polycystic kidney disease (ARPKD). Nek8 is also associated with a rare form of juvenile renal cystic disease, nephronophthisis type 9. It has been suggested that a defect in the ciliary localization of Nek8 contributes to the development of cysts manifested by these diseases. Nek8 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 81.32  E-value: 6.93e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKgDIVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCF 699
Cdd:cd08220   1 KYEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIPV-EQMTKEERQAALNEVKVLSMLH---HPNIIEYYESFLEDKALMI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYSAGGDLMLHIHS---DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDN-LLLDTEGYVKIADFGLCKEgMGYG 775
Cdd:cd08220  77 VMEYAPGGTLFEYIQQrkgSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNiLLNKKRTVVKIGDFGISKI-LSSK 155
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 47132591 776 DRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEM 814
Cdd:cd08220 156 SKAYTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYEL 194
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
621-815 7.31e-17

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 81.87  E-value: 7.31e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRP----SGELFAIKALKKGDivARDEVESLMCEKRILAAVTsagHPFLVNLFGCF--QTP 694
Cdd:cd05080   6 LKKIRDLGEGHFGKVSLYCYDPtndgTGEMVAVKALKADC--GPQHRSGWKQEIDILKTLY---HENIVKYKGCCseQGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 695 EHVCFVMEYSAGGDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK---EG 771
Cdd:cd05080  81 KSLQLIMEYVPLGSLRDYLPKHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAKavpEG 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 47132591 772 MGYGdRTSTFCGTPEF-LAPEVLTDTSYTRAVDWWGLGVLLYEML 815
Cdd:cd05080 161 HEYY-RVREDGDSPVFwYAPECLKEYKFYYASDVWSFGVTLYELL 204
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
621-880 1.19e-16

Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK9 and CDK12 from higher eukaryotes, yeast BUR1, C-type plant CDKs (CdkC), and similar proteins. CDK9, BUR1, and CdkC are functionally equivalent. They act as a kinase for the C-terminal domain of RNA polymerase II and participate in regulating mutliple steps of gene expression including transcription elongation and RNA processing. CDK9 and CdkC associate with T-type cyclins while BUR1 associates with the cyclin BUR2. CDK12 is a unique CDK that contains an arginine/serine-rich (RS) domain, which is predominantly found in splicing factors. CDK12 interacts with cyclins L1 and L2, and participates in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270832 [Multi-domain]  Cd Length: 291  Bit Score: 81.46  E-value: 1.19e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKgdivaRDEVESL----MCEKRILAAVtsaGHPFLVNLFGCFQTPEH 696
Cdd:cd07840   1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRM-----ENEKEGFpitaIREIKLLQKL---DHPNVVRLKEIVTSKGS 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 697 VCF------VMEYsAGGDLM-LHIHSDV-FSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLC 768
Cdd:cd07840  73 AKYkgsiymVFEY-MDHDLTgLLDNPEVkFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLA 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 769 kegmgygdRTSTFCGTPEFL---------APEVLT-DTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSI----- 833
Cdd:cd07840 152 --------RPYTKENNADYTnrvitlwyrPPELLLgATRYGPEVDMWSVGCILAELFTGKPIFQGKTELEQLEKIfelcg 223
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47132591 834 -VNDEV-----------------RYPR--------FLSAEAIGIMRRLLRRNPERRLgsserDAEDVKKQPFF 880
Cdd:cd07840 224 sPTEENwpgvsdlpwfenlkpkkPYKRrlrevfknVIDPSALDLLDKLLTLDPKKRI-----SADQALQHEYF 291
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
627-884 1.26e-16

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK5 is mainly expressed in the brain. It is not required for viability, but together with PAK6, it is required for normal levels of locomotion and activity, and for learning and memory. PAK5 cooperates with Inca (induced in neural crest by AP2) in the regulation of cell adhesion and cytoskeletal organization in the embryo and in neural crest cells during craniofacial development. PAK5 may also play a role in controlling the signaling of Raf-1, an effector of Ras, at the mitochondria. PAK5 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 81.62  E-value: 1.26e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKalkKGDIVARDEVESLMCEKRILaavTSAGHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd06658  30 IGEGSTGIVCIATEKHTGKQVAVK---KMDLRKQQRRELLFNEVVIM---RDYHHENVVDMYNSYLVGDELWVVMEFLEG 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCGTPE 786
Cdd:cd06658 104 GALTDIVTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKEVPKRKSLVGTPY 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 787 FLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVND---EVRYPRFLSAEAIGIMRRLLRRNPERR 863
Cdd:cd06658 184 WMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRDNlppRVKDSHKVSSVLRGFLDLMLVREPSQR 263
                       250       260
                ....*....|....*....|.
gi 47132591 864 lgsseRDAEDVKKQPFFRTLG 884
Cdd:cd06658 264 -----ATAQELLQHPFLKLAG 279
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
619-868 1.63e-16

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO3 is also known as JIK (c-Jun N-terminal kinase inhibitory kinase) or KFC (kinase from chicken). It specifically activates JNK, presumably by phosphorylating and activating MKK4/MKK7. In Saccharomyces cerevisiae, TAO3 is a component of the RAM (regulation of Ace2p activity and cellular morphogenesis) signaling pathway. TAO3 is upregulated in retinal ganglion cells after axotomy, and may play a role in apoptosis. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 81.62  E-value: 1.63e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVC 698
Cdd:cd06633  21 EIFVDLHEIGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNEKWQDIIKEVKFLQQLK---HPNTIEYKGCYLKDHTAW 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAG-GDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGlckeGMGYGDR 777
Cdd:cd06633  98 LVMEYCLGsASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFG----SASIASP 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 778 TSTFCGTPEFLAPEV---LTDTSYTRAVDWWGLGVLLYEMLVGESP-FPGDDEEEVFDSIVNDEvryPRFLSAEAIGIMR 853
Cdd:cd06633 174 ANSFVGTPYWMAPEVilaMDEGQYDGKVDIWSLGITCIELAERKPPlFNMNAMSALYHIAQNDS---PTLQSNEWTDSFR 250
                       250
                ....*....|....*....
gi 47132591 854 RL----LRRNPERRLGSSE 868
Cdd:cd06633 251 GFvdycLQKIPQERPSSAE 269
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
627-864 1.96e-16

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 5 (MAPKAP5 or MK5) is also called PRAK (p38-regulated/activated protein kinase). It contains a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 80.97  E-value: 1.96e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKAL---KKgdivARDEVE-SLMCekrilaavtsAGHPFLVNLFGCF----QTP---- 694
Cdd:cd14171  14 LGTGISGPVRVCVKKSTGERFALKILldrPK----ARTEVRlHMMC----------SGHPNIVQIYDVYansvQFPgess 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 695 --EHVCFVMEYSAGGDLMLHIHSDV-FSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLD---NLLLDTEGYVKIADFGLC 768
Cdd:cd14171  80 prARLLIVMELMEGGELFDRISQHRhFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPEnllLKDNSEDAPIKLCDFGFA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 769 KEGMGyGDRTSTFcgTPEFLAPEVL---------------TDTSYT--RAVDWWGLGVLLYEMLVGESPFPGDDEEEVFD 831
Cdd:cd14171 160 KVDQG-DLMTPQF--TPYYVAPQVLeaqrrhrkersgiptSPTPYTydKSCDMWSLGVIIYIMLCGYPPFYSEHPSRTIT 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 47132591 832 S-----IVNDEVRYP----RFLSAEAIGIMRRLLRRNPERRL 864
Cdd:cd14171 237 KdmkrkIMTGSYEFPeeewSQISEMAKDIVRKLLCVDPEERM 278
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
627-864 2.56e-16

Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The pseudokinase domain may function as a regulatory domain or a protein interaction domain. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 79.86  E-value: 2.56e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKaLKKGDivardevESLMCEKRILaavTSAGHPFLVNLFGCFQT-PEHVCFVMEYSA 705
Cdd:cd14109  12 EKRAAQGAPFHVTERSTGRNFLAQ-LRYGD-------PFLMREVDIH---NSLDHPNIVQMHDAYDDeKLAVTVIDNLAS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 706 GGDLM---LHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEgYVKIADFGLCKEgMGYGDRTSTFC 782
Cdd:cd14109  81 TIELVrdnLLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQDD-KLKLADFGQSRR-LLRGKLTTLIY 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 783 GTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIvnDEVRYP------RFLSAEAIGIMRRLL 856
Cdd:cd14109 159 GSPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDRETLTNV--RSGKWSfdssplGNISDDARDFIKKLL 236

                ....*...
gi 47132591 857 RRNPERRL 864
Cdd:cd14109 237 VYIPESRL 244
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
621-821 2.63e-16

Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TNIK is an effector of Rap2, a small GTP-binding protein from the Ras family. TNIK specifically activates the c-Jun N-terminal kinase (JNK) pathway and plays a role in regulating the actin cytoskeleton. The TNIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 80.53  E-value: 2.63e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKkgdiVARDEVESLMCEKRILAAVTSagHPFLVNLFGCF--QTP---- 694
Cdd:cd06637   8 FELVELVGNGTYGQVYKGRHVKTGQLAAIKVMD----VTGDEEEEIKQEINMLKKYSH--HRNIATYYGAFikKNPpgmd 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 695 EHVCFVMEYSAGG---DLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEG 771
Cdd:cd06637  82 DQLWLVMEFCGAGsvtDLIKNTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 47132591 772 MGYGDRTSTFCGTPEFLAPEVLT-----DTSYTRAVDWWGLGVLLYEMLVGESPF 821
Cdd:cd06637 162 DRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDFKSDLWSLGITAIEMAEGAPPL 216
Hr1 smart00742
Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical ...
219-279 2.96e-16

Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical domain found in vertebrate PRK1 and yeast PKC1 protein kinases C. The HR1 in rhophilin bind RhoGTP; those in PRK1 bind RhoA and RhoB. Also called RBD - Rho-binding domain


Pssm-ID: 128981  Cd Length: 57  Bit Score: 73.38  E-value: 2.96e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47132591    219 LRIEELRHHFRVEHAVAEGAKNVLRLLSAakapDRKAVSEAQEKLTESNQKLGLLREALER 279
Cdd:smart00742   1 LRLEDLRRKIEKELKVKEGAENMRKLTSN----DRKVLSEAQSMLRESNQKLDLLKEELEK 57
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
627-821 3.28e-16

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKalpha is involved in the non-canonical or alternative pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The non-canonical pathway functions in cells lacking NEMO (NF-kB Essential MOdulator) and IKKbeta. It is induced by a subset of TNFR family members including CD40, RANK, and B cell-activating factor receptor. IKKalpha processes the Inhibitor of NF-kB (IkB)-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus. This pathway is dependent on NIK (NF-kB Inducing Kinase) which phosphorylates and activates IKKalpha. The IKKalpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 80.35  E-value: 3.28e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKAlkkgdivARDEVESLMCEK--RILAAVTSAGHPflvNLFGCFQTPEHVCFV---- 700
Cdd:cd14039   1 LGTGGFGNVCLYQNQETGEKIAIKS-------CRLELSVKNKDRwcHEIQIMKKLNHP---NVVKACDVPEEMNFLvndv 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 ----MEYSAGGDL-----------------MLHIHSDVFSepraifysacvvlGLQFLHEHKIVYRDLKLDNLLLDTEG- 758
Cdd:cd14039  71 pllaMEYCSGGDLrkllnkpenccglkesqVLSLLSDIGS-------------GIQYLHENKIIHRDLKPENIVLQEINg 137
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47132591 759 --YVKIADFGLCKEgMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPF 821
Cdd:cd14039 138 kiVHKIIDLGYAKD-LDQGSLCTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPF 201
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
620-813 4.62e-16

Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 79.39  E-value: 4.62e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKFLAVLGRGHFGKVL-LSEFRPSGELFAIKALKKGDIVARDEvESLMCEKRILAAVTSAGHPFLVNLFGCFQTPEHVC 698
Cdd:cd14052   1 RFANVELIGSGEFSQVYkVSERVPTGKVYAVKKLKPNYAGAKDR-LRRLEEVSILRELTLDGHDNIVQLIDSWEYHGHLY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGGDLmlhihsDVF----------SEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGL- 767
Cdd:cd14052  80 IQTELCENGSL------DVFlselgllgrlDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMa 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 47132591 768 --CKEGMGY---GDRtstfcgtpEFLAPEVLTDTSYTRAVDWWGLGVLLYE 813
Cdd:cd14052 154 tvWPLIRGIereGDR--------EYIAPEILSEHMYDKPADIFSLGLILLE 196
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
616-863 5.31e-16

Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Byr1 from Schizosaccharomyces pombe, FUZ7 from Ustilago maydis, and related proteins. Byr1 phosphorylates its downstream target, the MAPK Spk1, and is regulated by the MAPKK kinase Byr2. The Spk1 cascade is pheromone-responsive and is essential for sporulation and sexual differentiation in fission yeast. FUZ7 phosphorylates and activates its target, the MAPK Crk1, which is required in mating and virulence in U. maydis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The Byr-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 79.41  E-value: 5.31e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 616 LTLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKkgdIVARDEVES-LMCEKRILAAVTSaghPFLVNLFGCFQT- 693
Cdd:cd06620   2 LKNQDLETLKDLGAGNGGSVSKVLHIPTGTIMAKKVIH---IDAKSSVRKqILRELQILHECHS---PYIVSFYGAFLNe 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 694 PEHVCFVMEYSAGGDL------MLHIHSDVFSEpraIFYSacVVLGLQFLH-EHKIVYRDLKLDNLLLDTEGYVKIADFG 766
Cdd:cd06620  76 NNNIIICMEYMDCGSLdkilkkKGPFPEEVLGK---IAVA--VLEGLTYLYnVHRIIHRDIKPSNILVNSKGQIKLCDFG 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 767 LCKEGMgyGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEE--------VFD---SIVN 835
Cdd:cd06620 151 VSGELI--NSIADTFVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAGSNDDDdgyngpmgILDllqRIVN 228
                       250       260       270
                ....*....|....*....|....*....|.
gi 47132591 836 DEV-RYP--RFLSAEAIGIMRRLLRRNPERR 863
Cdd:cd06620 229 EPPpRLPkdRIFPKDLRDFVDRCLLKDPRER 259
Hr1 smart00742
Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical ...
132-192 5.42e-16

Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical domain found in vertebrate PRK1 and yeast PKC1 protein kinases C. The HR1 in rhophilin bind RhoGTP; those in PRK1 bind RhoA and RhoB. Also called RBD - Rho-binding domain


Pssm-ID: 128981  Cd Length: 57  Bit Score: 72.99  E-value: 5.42e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47132591    132 SRVAGLEKQLAIELKVKQGAENMIQTYSNgstkDRKLLLTAQQMLQDSKTKIDIIRMQLRR 192
Cdd:smart00742   1 LRLEDLRRKIEKELKVKEGAENMRKLTSN----DRKVLSEAQSMLRESNQKLDLLKEELEK 57
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
619-863 5.47e-16

Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 78.71  E-value: 5.47e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKAL------KKGDIVARDEVESLMCEkRILAavtsaghpflvnLFGCFQ 692
Cdd:cd14111   3 KPYTFLDEKARGRFGVIRRCRENATGKNFPAKIVpyqaeeKQGVLQEYEILKSLHHE-RIMA------------LHEAYI 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 693 TPEHVCFVMEYSAGGDLmLHIHSDVF--SEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKE 770
Cdd:cd14111  70 TPRYLVLIAEFCSGKEL-LHSLIDRFrySEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQS 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 771 GMGYGDRT-STFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVN---DEVR-YPRfLS 845
Cdd:cd14111 149 FNPLSLRQlGRRTGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKILVakfDAFKlYPN-VS 227
                       250
                ....*....|....*...
gi 47132591 846 AEAIGIMRRLLRRNPERR 863
Cdd:cd14111 228 QSASLFLKKVLSSYPWSR 245
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
619-868 5.99e-16

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. The MK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 79.69  E-value: 5.99e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFL-AVLGRGHFGKVLLSEFRPSGELFAIKALKKGDiVARDEVEslmcekrILAAVTSAGHPF-LVNLF-GCFQTPE 695
Cdd:cd14170   1 DDYKVTsQVLGLGINGKVLQIFNKRTQEKFALKMLQDCP-KARREVE-------LHWRASQCPHIVrIVDVYeNLYAGRK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 696 HVCFVMEYSAGGDLMLHIHS---DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTE---GYVKIADFGLCK 769
Cdd:cd14170  73 CLLIVMECLDGGELFSRIQDrgdQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKrpnAILKLTDFGFAK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 770 EGMGYgDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPF---------PGDDEEevfdsIVNDEVRY 840
Cdd:cd14170 153 ETTSH-NSLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFysnhglaisPGMKTR-----IRMGQYEF 226
                       250       260       270
                ....*....|....*....|....*....|..
gi 47132591 841 PRF----LSAEAIGIMRRLLRRNPERRLGSSE 868
Cdd:cd14170 227 PNPewseVSEEVKMLIRNLLKTEPTQRMTITE 258
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
626-868 7.14e-16

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 79.30  E-value: 7.14e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARD----EVESL-MCEkrilaavtsaGHPFLVNLFGCFQTPEHVCFV 700
Cdd:cd14174   9 LLGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGHSRSrvfrEVETLyQCQ----------GNKNILELIEFFEDDTRFYLV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGGDLMLHIHS-DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTE---GYVKIADFGLcKEGMGYGD 776
Cdd:cd14174  79 FEKLRGGSILAHIQKrKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPdkvSPVKICDFDL-GSGVKLNS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 777 --------RTSTFCGTPEFLAPEVL---TD--TSYTRAVDWWGLGVLLYEMLVGESPFPGD-------DEEEV------- 829
Cdd:cd14174 158 actpittpELTTPCGSAEYMAPEVVevfTDeaTFYDKRCDLWSLGVILYIMLSGYPPFVGHcgtdcgwDRGEVcrvcqnk 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 47132591 830 -FDSIVNDEVRYP----RFLSAEAIGIMRRLLRRNPERRLGSSE 868
Cdd:cd14174 238 lFESIQEGKYEFPdkdwSHISSEAKDLISKLLVRDAKERLSAAQ 281
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
624-864 7.68e-16

Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle 1 (also called TTK); Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TTK/Mps1 is a spindle checkpoint kinase that was first discovered due to its necessity in centrosome duplication in budding yeast. It was later found to function in the spindle assembly checkpoint, which monitors the proper attachment of chromosomes to the mitotic spindle. In yeast, substrates of Mps1 include the spindle pole body components Spc98p, Spc110p, and Spc42p. The TTK/Mps1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 78.80  E-value: 7.68e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 624 LAVLGRGHFGKVLLSeFRPSGELFAikaLKKGDIVARDE--VESLMCEKRILAavTSAGHPFLVNLFG--CFQTPEHVCF 699
Cdd:cd14131   6 LKQLGKGGSSKVYKV-LNPKKKIYA---LKRVDLEGADEqtLQSYKNEIELLK--KLKGSDRIIQLYDyeVTDEDDYLYM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYsAGGDL--MLHIHSDVFSEPRAI-FYSACVVLGLQFLHEHKIVYRDLKLDNLLLdTEGYVKIADFGLCKeGMGyGD 776
Cdd:cd14131  80 VMEC-GEIDLatILKKKRPKPIDPNFIrYYWKQMLEAVHTIHEEGIVHSDLKPANFLL-VKGRLKLIDFGIAK-AIQ-ND 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 777 RTS----TFCGTPEFLAPEVLTDTSYT----------RAVDWWGLGVLLYEMLVGESPFPGDDEE-EVFDSIVND--EVR 839
Cdd:cd14131 156 TTSivrdSQVGTLNYMSPEAIKDTSASgegkpkskigRPSDVWSLGCILYQMVYGKTPFQHITNPiAKLQAIIDPnhEIE 235
                       250       260
                ....*....|....*....|....*
gi 47132591 840 YPRFLSAEAIGIMRRLLRRNPERRL 864
Cdd:cd14131 236 FPDIPNPDLIDVMKRCLQRDPKKRP 260
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
616-835 8.21e-16

Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of Csk, Chk, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Chk inhibit Src kinases using a noncatalytic mechanism by simply binding to them. As negative regulators of Src kinases, Csk and Chk play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. The Csk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 78.16  E-value: 8.21e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 616 LTLEDFKFLAVLGRGHFGKVLLSEFRpsGELFAIKALKKGDIVArdevESLMCEkrilAAV-TSAGHPFLVNLFGCFQTP 694
Cdd:cd05039   3 INKKDLKLGELIGKGEFGDVMLGDYR--GQKVAVKCLKDDSTAA----QAFLAE----ASVmTTLRHPNLVQLLGVVLEG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 695 EHVCFVMEYSAGGDLMLHIHS---DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEG 771
Cdd:cd05039  73 NGLYIVTEYMAKGSLVDYLRSrgrAVITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAKEA 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47132591 772 mGYGDRTSTFcgtP-EFLAPEVLTDTSYTRAVDWWGLGVLLYEML-VGESPFPGDDEEEVFDSIVN 835
Cdd:cd05039 153 -SSNQDGGKL---PiKWTAPEALREKKFSTKSDVWSFGILLWEIYsFGRVPYPRIPLKDVVPHVEK 214
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
620-863 9.26e-16

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. No function has yet been ascribed to Nek10. The gene encoding Nek10 is a putative causative gene for breast cancer; it is located within a breast cancer susceptibility loci on chromosome 3p24. Nek10 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 78.31  E-value: 9.26e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKFLAVLGRGHFGKVLLSEFRPSG-ELFAIKALKKGD-IVARDEVESLMCEKRILAAVT----SAGHPFLVNLFGCFQT 693
Cdd:cd08528   1 EYAVLELLGSGAFGCVYKVRKKSNGqTLLALKEINMTNpAFGRTEQERDKSVGDIISEVNiikeQLRHPNIVRYYKTFLE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 694 PEHVCFVMEYSAGGDLMLHIHS-----DVFSEPR--AIFYSacVVLGLQFLH-EHKIVYRDLKLDNLLLDTEGYVKIADF 765
Cdd:cd08528  81 NDRLYIVMELIEGAPLGEHFSSlkeknEHFTEDRiwNIFVQ--MVLALRYLHkEKQIVHRDLKPNNIMLGEDDKVTITDF 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 766 GLCKEGMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVN------DEVR 839
Cdd:cd08528 159 GLAKQKGPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVEaeyeplPEGM 238
                       250       260
                ....*....|....*....|....
gi 47132591 840 YprflSAEAIGIMRRLLRRNPERR 863
Cdd:cd08528 239 Y----SDDITFVIRSCLTPDPEAR 258
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
612-820 1.20e-15

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. MAP4K3 is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. mTOR regulates ribosome biogenesis and protein translation, and is frequently deregulated in cancer. MAP4Ks are involved in MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 78.16  E-value: 1.20e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 612 RKSPLtlEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALK--KGDIVARDEVESLMcekrilaaVTSAGHPFLVNLFG 689
Cdd:cd06645   6 RRNPQ--EDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKlePGEDFAVVQQEIIM--------MKDCKHSNIVAYFG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 690 CFQTPEHVCFVMEYSAGGDLMLHIH-SDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLC 768
Cdd:cd06645  76 SYLRRDKLWICMEFCGGGSLQDIYHvTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVS 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 47132591 769 KEGMGYGDRTSTFCGTPEFLAPEVLT---DTSYTRAVDWWGLGVLLYEMLVGESP 820
Cdd:cd06645 156 AQITATIAKRKSFIGTPYWMAPEVAAverKGGYNQLCDIWAVGITAIELAELQPP 210
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
626-863 1.31e-15

Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. RET is a receptor PTK (RTK) containing an extracellular region with four cadherin-like repeats, a calcium-binding site, and a cysteine-rich domain, a transmembrane segment, and an intracellular catalytic domain. It is part of a multisubunit complex that binds glial-derived neurotropic factor (GDNF) family ligands (GFLs) including GDNF, neurturin, artemin, and persephin. GFLs bind RET along with four GPI-anchored coreceptors, bringing two RET molecules together, leading to autophosphorylation, activation, and intracellular signaling. RET is essential for the development of the sympathetic, parasympathetic and enteric nervous systems, and the kidney. RET disruption by germline mutations causes diseases in humans including congenital aganglionosis of the gastrointestinal tract (Hirschsprung's disease) and three related inherited cancers: multiple endocrine neoplasia type 2A (MEN2A), MEN2B, and familial medullary thyroid carcinoma. The RET subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 78.47  E-value: 1.31e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLS-----EFRPSGELFAIKALKKGdiVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFV 700
Cdd:cd05045   7 TLGEGEFGKVVKAtafrlKGRAGYTTVAVKMLKEN--ASSSELRDLLSEFNLLKQVN---HPHVIKLYGACSQDGPLLLI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGGDLMLHIHSDVFSEP-------------------RA------IFYSACVVLGLQFLHEHKIVYRDLKLDNLLLD 755
Cdd:cd05045  82 VEYAKYGSLRSFLRESRKVGPsylgsdgnrnssyldnpdeRAltmgdlISFAWQISRGMQYLAEMKLVHRDLAARNVLVA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 756 TEGYVKIADFGLCK---EGMGYGDRTSTFCGTpEFLAPEVLTDTSYTRAVDWWGLGVLLYEML-VGESPFPGDDEEEVFD 831
Cdd:cd05045 162 EGRKMKISDFGLSRdvyEEDSYVKRSKGRIPV-KWMAIESLFDHIYTTQSDVWSFGVLLWEIVtLGGNPYPGIAPERLFN 240
                       250       260       270
                ....*....|....*....|....*....|...
gi 47132591 832 SI-VNDEVRYPRFLSAEAIGIMRRLLRRNPERR 863
Cdd:cd05045 241 LLkTGYRMERPENCSEEMYNLMLTCWKQEPDKR 273
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
626-879 1.33e-15

Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. YSK4 is a putative MAPKKK, whose mammalian gene has been isolated. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The YSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 77.86  E-value: 1.33e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKV---LLSEfrpsGELFAIK--ALKKGDIV-ARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCF 699
Cdd:cd06631   8 VLGKGAYGTVycgLTST----GQLIAVKqvELDTSDKEkAEKEYEKLQEEVDLLKTLK---HVNIVGYLGTCLEDNVVSI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYSAGGDLM-LHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFG----LCKEG--M 772
Cdd:cd06631  81 FMEFVPGGSIAsILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGcakrLCINLssG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 773 GYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRF---LSAEAI 849
Cdd:cd06631 161 SQSQLLKSMRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPWADMNPMAAIFAIGSGRKPVPRLpdkFSPEAR 240
                       250       260       270
                ....*....|....*....|....*....|
gi 47132591 850 GIMRRLLRRNPERRLgsserDAEDVKKQPF 879
Cdd:cd06631 241 DFVHACLTRDQDERP-----SAEQLLKHPF 265
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
619-829 1.60e-15

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 2; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK2 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 78.94  E-value: 1.60e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALK-KGDIVARDEVeslmceKRILAAVTSAGHPFLVNLFGCFQTPEHV 697
Cdd:cd06649   5 DDFERISELGAGNGGVVTKVQHKPSGLIMARKLIHlEIKPAIRNQI------IRELQVLHECNSPYIVGFYGAFYSDGEI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 698 CFVMEYSAGGDLmlhihSDVFSEPRAI------FYSACVVLGLQFLHE-HKIVYRDLKLDNLLLDTEGYVKIADFGLckE 770
Cdd:cd06649  79 SICMEHMDGGSL-----DQVLKEAKRIpeeilgKVSIAVLRGLAYLREkHQIMHRDVKPSNILVNSRGEIKLCDFGV--S 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 47132591 771 GMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEV 829
Cdd:cd06649 152 GQLIDSMANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYPIPPPDAKEL 210
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
621-815 2.01e-15

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak2 is widely expressed in many tissues and is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 77.75  E-value: 2.01e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRP----SGELFAIKALKkgdivaRDEVESLMCEKRILAAVTSAGHPFLVNLFG-CFQTPE 695
Cdd:cd14205   6 LKFLQQLGKGNFGSVEMCRYDPlqdnTGEVVAVKKLQ------HSTEEHLRDFEREIEILKSLQHDNIVKYKGvCYSAGR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 696 -HVCFVMEYSAGGDL--MLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK--- 769
Cdd:cd14205  80 rNLRLIMEYLPYGSLrdYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKvlp 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 47132591 770 -EGMGYGDRTSTfcGTPEF-LAPEVLTDTSYTRAVDWWGLGVLLYEML 815
Cdd:cd14205 160 qDKEYYKVKEPG--ESPIFwYAPESLTESKFSVASDVWSFGVVLYELF 205
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
619-868 2.33e-15

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Protein Kinase regulated by RNA; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKR (or EIF2AK2) contains an N-terminal double-stranded RNA (dsRNA) binding domain and a C-terminal catalytic kinase domain. It is activated by dsRNA, which is produced as a replication intermediate in virally infected cells. It plays a key role in mediating innate immune responses to viral infection. PKR is also directly activated by PACT (protein activator of PKR) and heparin, and is inhibited by viral proteins and RNAs. PKR also regulates transcription and signal transduction in diseased cells, playing roles in tumorigenesis and neurodegenerative diseases. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PKR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 77.15  E-value: 2.33e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLmcekrilaavTSAGHPFLVNLFGCFQTPEH-- 696
Cdd:cd14047   6 QDFKEIELIGSGGFGQVFKAKHRIDGKTYAIKRVKLNNEKAEREVKAL----------AKLDHPNIVRYNGCWDGFDYdp 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 697 -------------VCFV-MEYSAGGDLMLHIHSDVFS-----EPRAIFYSacVVLGLQFLHEHKIVYRDLKLDNLLLDTE 757
Cdd:cd14047  76 etsssnssrsktkCLFIqMEFCEKGTLESWIEKRNGEkldkvLALEIFEQ--ITKGVEYIHSKKLIHRDLKPSNIFLVDT 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 758 GYVKIADFGLCKEGMGYGDRTSTFcGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESpfPGDDEEEVFDSIVNDE 837
Cdd:cd14047 154 GKVKIGDFGLVTSLKNDGKRTKSK-GTLSYMSPEQISSQDYGKEVDIYALGLILFELLHVCD--SAFEKSKFWTDLRNGI 230
                       250       260       270
                ....*....|....*....|....*....|...
gi 47132591 838 VRyPRFLSAEAI--GIMRRLLRRNPERRLGSSE 868
Cdd:cd14047 231 LP-DIFDKRYKIekTIIKKMLSKKPEDRPNASE 262
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
616-822 2.98e-15

Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Csk is expressed in a wide variety of tissues. As a negative regulator of Src, Csk plays a role in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Csk is a cytoplasmic (or nonreceptor) PTK containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases, Csk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. In addition, Csk also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. The Csk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 76.56  E-value: 2.98e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 616 LTLEDFKFLAVLGRGHFGKVLLSEFRpsGELFAIKALKKgDIVArdevESLMCEKRILaavTSAGHPFLVNLFGCFQTPE 695
Cdd:cd05082   3 LNMKELKLLQTIGKGEFGDVMLGDYR--GNKVAVKCIKN-DATA----QAFLAEASVM---TQLRHSNLVQLLGVIVEEK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 696 HVCF-VMEYSAGGDLMLHIHS---DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEG 771
Cdd:cd05082  73 GGLYiVTEYMAKGSLVDYLRSrgrSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEA 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 47132591 772 MGYGDRTSTfcgTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEML-VGESPFP 822
Cdd:cd05082 153 SSTQDTGKL---PVKWTAPEALREKKFSTKSDVWSFGILLWEIYsFGRVPYP 201
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
619-868 3.48e-15

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 77.88  E-value: 3.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  619 EDFKFL-AVLGRGHFGKVLLSEFRPSGELFAIKALKKGDI---VARDEVESLMC-----EKRILAAVTSAGHPFLVNLFG 689
Cdd:PTZ00024   8 ERYIQKgAHLGEGTYGKVEKAYDTLTGKIVAIKKVKIIEIsndVTKDRQLVGMCgihftTLRELKIMNEIKHENIMGLVD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  690 CFQTPEHVCFVMEYSAGgDLMLHIHSDV-FSEPraifYSACVVL----GLQFLHEHKIVYRDLKLDNLLLDTEGYVKIAD 764
Cdd:PTZ00024  88 VYVEGDFINLVMDIMAS-DLKKVVDRKIrLTES----QVKCILLqilnGLNVLHKWYFMHRDLSPANIFINSKGICKIAD 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  765 FGLCKE-----GMGYGDRTSTFCG----TPE-----FLAPEVLT-DTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEV 829
Cdd:PTZ00024 163 FGLARRygyppYSDTLSKDETMQRreemTSKvvtlwYRAPELLMgAEKYHFAVDMWSVGCIFAELLTGKPLFPGENEIDQ 242
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47132591  830 FDSIVN-----DEVRYP-----------------------RFLSAEAIGIMRRLLRRNPERRLGSSE 868
Cdd:PTZ00024 243 LGRIFEllgtpNEDNWPqakklplyteftprkpkdlktifPNASDDAIDLLQSLLKLNPLERISAKE 309
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
621-880 3.51e-15

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Pho85 is a multifunctional CDK in yeast. It is regulated by 10 different cyclins (Pcls) and plays a role in G1 progression, cell polarity, phosphate and glycogen metabolism, gene expression, and in signaling changes in the environment. It is not essential for yeast viability and is the functional homolog of mammalian CDK5, which plays a role in central nervous system development. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The Pho85 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 77.14  E-value: 3.51e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALK----KGD-IVARDEVeSLMCEKRilaavtsagHPFLVNLFGCFQTPE 695
Cdd:cd07836   2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKEIHldaeEGTpSTAIREI-SLMKELK---------HENIVRLHDVIHTEN 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 696 HVCFVMEYsAGGDLMLHIhsDVFSEPRAI------FYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLck 769
Cdd:cd07836  72 KLMLVFEY-MDKDLKKYM--DTHGVRGALdpntvkSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGL-- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 770 eGMGYGDRTSTFCG---TPEFLAPEVLTDT-SYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVN-----DEVRY 840
Cdd:cd07836 147 -ARAFGIPVNTFSNevvTLWYRAPDVLLGSrTYSTSIDIWSVGCIMAEMITGRPLFPGTNNEDQLLKIFRimgtpTESTW 225
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47132591 841 PRF------------------------LSAEAIGIMRRLLRRNPERRLgsserDAEDVKKQPFF 880
Cdd:cd07836 226 PGIsqlpeykptfpryppqdlqqlfphADPLGIDLLHRLLQLNPELRI-----SAHDALQHPWF 284
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
632-868 4.44e-15

Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to Calcium/calmodulin-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized STKs with similarity to CaMKs, which are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. This uncharacterized subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 76.22  E-value: 4.44e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 632 FGKVLLSEFRPSGELFAIKALKKGDivARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFVMEYSAGGDLML 711
Cdd:cd14088  14 FCEIFRAKDKTTGKLYTCKKFLKRD--GRKVRKAAKNEINILKMVK---HPNILQLVDVFETRKEYFIFLELATGREVFD 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 712 HI-HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLL---LDTEGYVKIADFGLCKEGMGYgdrTSTFCGTPEF 787
Cdd:cd14088  89 WIlDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVyynRLKNSKIVISDFHLAKLENGL---IKEPCGTPEY 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 788 LAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEE--------VFDSIVNDEVRY--PRF--LSAEAIGIMRRL 855
Cdd:cd14088 166 LAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPFYDEAEEDdyenhdknLFRKILAGDYEFdsPYWddISQAAKDLVTRL 245
                       250
                ....*....|...
gi 47132591 856 LRRNPERRLGSSE 868
Cdd:cd14088 246 MEVEQDQRITAEE 258
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
623-880 4.51e-15

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek9, also called Nercc1, is primarily a cytoplasmic protein but can also localize in the nucleus. It is involved in modulating chromosome alignment and splitting during mitosis. It interacts with the gamma-tubulin ring complex and the Ran GTPase, and is implicated in microtubule organization. Nek9 associates with FACT (FAcilitates Chromatin Transcription) and modulates interphase progression. It also interacts with Nek6, and Nek7, during mitosis, resulting in their activation. Nek9 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 76.31  E-value: 4.51e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 623 FLAVLGRGHFGKVLLSEFRPSGELFAIK--ALKKgdiVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFV 700
Cdd:cd08221   4 PVRVLGRGAFGEAVLYRKTEDNSLVVWKevNLSR---LSEKERRDALNEIDILSLLN---HDNIITYYNHFLDGESLFIE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGGDL---MLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDR 777
Cdd:cd08221  78 MEYCNGGNLhdkIAQQKNQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLDSESSM 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 778 TSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIV--NDEVRYPRFlSAEAIGIMRRL 855
Cdd:cd08221 158 AESIVGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVqgEYEDIDEQY-SEEIIQLVHDC 236
                       250       260
                ....*....|....*....|....*
gi 47132591 856 LRRNPERRlgsseRDAEDVKKQPFF 880
Cdd:cd08221 237 LHQDPEDR-----PTAEELLERPLL 256
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
627-830 5.05e-15

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 76.98  E-value: 5.05e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEF------RPSGEL-FAIKALKkgDIVARDEVESLMCEKRILAAVtsAGHPFLVNLFGCFQTPEHVCF 699
Cdd:cd05101  32 LGEGCFGQVVMAEAvgidkdKPKEAVtVAVKMLK--DDATEKDLSDLVSEMEMMKMI--GKHKNIINLLGACTQDGPLYV 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYSAGGDLMLHIHSdvfSEPRAIFYS-----------------AC---VVLGLQFLHEHKIVYRDLKLDNLLLDTEGY 759
Cdd:cd05101 108 IVEYASKGNLREYLRA---RRPPGMEYSydinrvpeeqmtfkdlvSCtyqLARGMEYLASQKCIHRDLAARNVLVTENNV 184
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47132591 760 VKIADFGLCKE--GMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEML-VGESPFPGDDEEEVF 830
Cdd:cd05101 185 MKIADFGLARDinNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFtLGGSPYPGIPVEELF 258
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
627-863 5.40e-15

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 76.93  E-value: 5.40e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEF------RPSGEL-FAIKALKkgDIVARDEVESLMCEKRILAAVTSagHPFLVNLFG-CFQT-PEHV 697
Cdd:cd05099  20 LGEGCFGQVVRAEAygidksRPDQTVtVAVKMLK--DNATDKDLADLISEMELMKLIGK--HKNIINLLGvCTQEgPLYV 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 698 cfVMEYSAGGDL-----------------MLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYV 760
Cdd:cd05099  96 --IVEYAAKGNLreflrarrppgpdytfdITKVPEEQLSFKDLVSCAYQVARGMEYLESRRCIHRDLAARNVLVTEDNVM 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 761 KIADFGLCK--EGMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEML-VGESPFPGDDEEEVFdSIVNDE 837
Cdd:cd05099 174 KIADFGLARgvHDIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILMWEIFtLGGSPYPGIPVEELF-KLLREG 252
                       250       260
                ....*....|....*....|....*...
gi 47132591 838 VRY--PRFLSAEAIGIMRRLLRRNPERR 863
Cdd:cd05099 253 HRMdkPSNCTHELYMLMRECWHAVPTQR 280
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
621-868 6.29e-15

Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like protein kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity DYRKs and YAK1, as well as the S/T kinases (STKs), HIPKs. DYRKs and YAK1 autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. Proteins in this subfamily play important roles in cell proliferation, differentiation, survival, growth, and development. The DYRK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 75.77  E-value: 6.29e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVEslmcEKRILAAV---TSAGHPFLVNLFGCFQTPEHV 697
Cdd:cd14133   1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKIIKNNKDYLDQSLD----EIRLLELLnkkDKADKYHIVRLKDVFYFKNHL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 698 CFVME------YSAGGDLMLHihsdVFSEPRAIFYSACVVLGLQFLHEHKIV-------------YRDLKldnllldteg 758
Cdd:cd14133  77 CIVFEllsqnlYEFLKQNKFQ----YLSLPRIRKIAQQILEALVFLHSLGLIhcdlkpenillasYSRCQ---------- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 759 yVKIADFGLCKEgmgYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEV 838
Cdd:cd14133 143 -IKIIDFGSSCF---LTQRLYSYIQSRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIG 218
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 47132591 839 RYPRFLSAEA-------IGIMRRLLRRNPERRLGSSE 868
Cdd:cd14133 219 IPPAHMLDQGkaddelfVDFLKKLLEIDPKERPTASQ 255
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
627-821 7.13e-15

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKbeta is involved in the classical pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. It involves NEMO (NF-kB Essential MOdulator)- and IKKbeta-dependent phosphorylation and degradation of the Inhibitor of NF-kB (IkB), which liberates NF-kB dimers (typified by the p50-p65 heterodimer) from an inactive IkB/dimeric NF-kB complex, enabling them to migrate to the nucleus where they regulate gene transcription. The IKKbeta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 76.15  E-value: 7.13e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLmcEKRILAAVTsagHPflvNLFGCFQTPEHV--------- 697
Cdd:cd14038   2 LGTGGFGNVLRWINQETGEQVAIKQCRQELSPKNRERWCL--EIQIMKRLN---HP---NVVAARDVPEGLqklapndlp 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 698 CFVMEYSAGGDLMLHIhsDVFSEPRAIFYSACVVL------GLQFLHEHKIVYRDLKldnllldTEGYV----------K 761
Cdd:cd14038  74 LLAMEYCQGGDLRKYL--NQFENCCGLREGAILTLlsdissALRYLHENRIIHRDLK-------PENIVlqqgeqrlihK 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 762 IADFGLCKEgMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPF 821
Cdd:cd14038 145 IIDLGYAKE-LDQGSLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPF 203
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
613-821 7.28e-15

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK3 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. In addition, MEKK3 is involved in interleukin-1 receptor and Toll-like receptor 4 signaling. It is also a specific regulator of the proinflammatory cytokines IL-6 and GM-CSF in some immune cells. MEKK3 also regulates calcineurin, which plays a critical role in T cell activation, apoptosis, skeletal myocyte differentiation, and cardiac hypertrophy. The MEKK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 75.89  E-value: 7.28e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 613 KSPLTLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALK--KGDIVARDEVESLMCEKRILAAVTsagHPFLVNLFGC 690
Cdd:cd06651   1 KSPSAPINWRRGKLLGQGAFGRVYLCYDVDTGRELAAKQVQfdPESPETSKEVSALECEIQLLKNLQ---HERIVQYYGC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 691 FQ--TPEHVCFVMEYSAGGDLMLHIHS-DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGL 767
Cdd:cd06651  78 LRdrAEKTLTIFMEYMPGGSVKDQLKAyGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGA 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 47132591 768 CKEGM-----GYGDRTSTfcGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPF 821
Cdd:cd06651 158 SKRLQticmsGTGIRSVT--GTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW 214
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
626-868 7.83e-15

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 76.22  E-value: 7.83e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGELFAIKALKK--GDIVAR--DEVESL-MCEkrilaavtsaGHPFLVNLFGCFQTPEHVCFV 700
Cdd:cd14173   9 VLGEGAYARVQTCINLITNKEYAVKIIEKrpGHSRSRvfREVEMLyQCQ----------GHRNVLELIEFFEEEDKFYLV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGGDLMLHIHSDV-FSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGY---VKIADFGLcKEGMGYGD 776
Cdd:cd14173  79 FEKMRGGSILSHIHRRRhFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQvspVKICDFDL-GSGIKLNS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 777 RTS--------TFCGTPEFLAPEVLTDTS-----YTRAVDWWGLGVLLYEMLVGESPFPGD-------DEEE-------- 828
Cdd:cd14173 158 DCSpistpellTPCGSAEYMAPEVVEAFNeeasiYDKRCDLWSLGVILYIMLSGYPPFVGRcgsdcgwDRGEacpacqnm 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 47132591 829 VFDSIVNDEVRYPR----FLSAEAIGIMRRLLRRNPERRLGSSE 868
Cdd:cd14173 238 LFESIQEGKYEFPEkdwaHISCAAKDLISKLLVRDAKQRLSAAQ 281
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
619-863 8.80e-15

Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Itk, also known as Tsk or Emt, is a member of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Itk contains the Tec homology (TH) domain containing one proline-rich region and a zinc-binding region. Itk is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, Itk plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, Itk is crucial for the development of T-helper(Th)2 effector responses. The Itk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 75.37  E-value: 8.80e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELfAIKALKKGDIVARDEVEslmcEKRILAAVTsagHPFLVNLFG-CFQ-TPeh 696
Cdd:cd05112   4 SELTFVQEIGSGQFGLVHLGYWLNKDKV-AIKTIREGAMSEEDFIE----EAEVMMKLS---HPKLVQLYGvCLEqAP-- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 697 VCFVMEYSAGGDLMLHIHSDVFSEPRAIFYSAC--VVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKegMGY 774
Cdd:cd05112  74 ICLVFEFMEHGCLSDYLRTQRGLFSAETLLGMCldVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTR--FVL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 775 GDRTSTFCGTP---EFLAPEVLTDTSYTRAVDWWGLGVLLYEMLV-GESPFPGDDEEEVFDSIVNDEVRY-PRFLSAEAI 849
Cdd:cd05112 152 DDQYTSSTGTKfpvKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSeGKIPYENRSNSEVVEDINAGFRLYkPRLASTHVY 231
                       250
                ....*....|....
gi 47132591 850 GIMRRLLRRNPERR 863
Cdd:cd05112 232 EIMNHCWKERPEDR 245
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
619-822 9.63e-15

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 75.69  E-value: 9.63e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKgDIVARDEvESLMCEKRILAAVTSaghPFLVNLFGCFQTPEHVC 698
Cdd:cd06619   1 QDIQYQEILGHGNGGTVYKAYHLLTRRILAVKVIPL-DITVELQ-KQIMSELEILYKCDS---PYIIGFYGAFFVENRIS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGGDLmlhihsDVFSE-PRAIF--YSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMgyG 775
Cdd:cd06619  76 ICTEFMDGGSL------DVYRKiPEHVLgrIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLV--N 147
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 47132591 776 DRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFP 822
Cdd:cd06619 148 SIAKTYVGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFPYP 194
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
773-868 1.03e-14

Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB2 binds and negatively regulates the mitogen activated protein kinase (MAPK) kinases, MKK7 and MEK1, which are activators of the MAPKs, ERK and JNK. It controls the activation of inflammatory monocytes, which is essential in innate immune responses and the pathogenesis of inflammatory diseases such as atherosclerosis. TRB2 expression is down-regulated in human acute myeloid leukaemia (AML), which may lead to enhanced cell survival and pathogenesis of the disease. TRB2 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 74.69  E-value: 1.03e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 773 GYGDRTSTFCGTPEFLAPEVL-TDTSYT-RAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIG 850
Cdd:cd14022 138 GHDDSLSDKHGCPAYVSPEILnTSGSYSgKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKC 217
                        90
                ....*....|....*...
gi 47132591 851 IMRRLLRRNPERRLGSSE 868
Cdd:cd14022 218 LIRSILRREPSERLTSQE 235
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
626-872 1.04e-14

Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; Fer kinase; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fer kinase is a member of the Fes subfamily of proteins which are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. Fer kinase is expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells.


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 75.04  E-value: 1.04e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGELfAIKALKKgDIVARDEVEsLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFVMEYSA 705
Cdd:cd05085   3 LLGKGNFGEVYKGTLKDKTPV-AVKTCKE-DLPQELKIK-FLSEARILKQYD---HPNIVKLIGVCTQRQPIYIVMELVP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 706 GGDLM--LHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCG 783
Cdd:cd05085  77 GGDFLsfLRKKKDELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQEDDGVYSSSGLKQ 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 784 TP-EFLAPEVLTDTSYTRAVDWWGLGVLLYEML-VGESPFPGDDEEEVFDSIVND-EVRYPRFLSAEAIGIMRRLLRRNP 860
Cdd:cd05085 157 IPiKWTAPEALNYGRYSSESDVWSFGILLWETFsLGVCPYPGMTNQQAREQVEKGyRMSAPQRCPEDIYKIMQRCWDYNP 236
                       250
                ....*....|..
gi 47132591 861 ERRLGSSERDAE 872
Cdd:cd05085 237 ENRPKFSELQKE 248
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
611-814 1.07e-14

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). MAP4K5 also facilitates Wnt signaling in B cells, and may therefore be implicated in the control of cell fate, proliferation, and polarity. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 75.45  E-value: 1.07e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 611 LRKSPLtlEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALK--KGDIVARDEVESLMcekrilaaVTSAGHPFLVNLF 688
Cdd:cd06646   3 LRRNPQ--HDYELIQRVGSGTYGDVYKARNLHTGELAAVKIIKlePGDDFSLIQQEIFM--------VKECKHCNIVAYF 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 689 GCFQTPEHVCFVMEYSAGGDLMLHIH-SDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGL 767
Cdd:cd06646  73 GSYLSREKLWICMEYCGGGSLQDIYHvTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGV 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 47132591 768 CKEGMGYGDRTSTFCGTPEFLAPEVLT---DTSYTRAVDWWGLGVLLYEM 814
Cdd:cd06646 153 AAKITATIAKRKSFIGTPYWMAPEVAAvekNGGYNQLCDIWAVGITAIEL 202
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
620-824 1.12e-14

Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related kinase 6 and 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 and Nek7 are the shortest Neks, consisting only of the catalytic domain and a very short N-terminal extension. They show distinct expression patterns and both appear to be downstream substrates of Nek9. They are required for mitotic spindle formation and cytokinesis. They may also be regulators of the p70 ribosomal S6 kinase. Nek6/7 is part of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 75.00  E-value: 1.12e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIV---ARDEveslmCEKRIlAAVTSAGHPFLVNLFGCFQTPEH 696
Cdd:cd08224   1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQIFEMMdakARQD-----CLKEI-DLLQQLNHPNIIKYLASFIENNE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 697 VCFVMEYSAGGDLMLHI-----HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLckeG 771
Cdd:cd08224  75 LNIVLELADAGDLSRLIkhfkkQKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGL---G 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 47132591 772 MGYGDRTS---TFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGD 824
Cdd:cd08224 152 RFFSSKTTaahSLVGTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYGE 207
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
627-863 1.19e-14

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Many FGFR3 splice variants have been reported with the IIIb and IIIc isoforms being the predominant forms. FGFR3 IIIc is the isoform expressed in chondrocytes, the cells affected in dwarfism, while IIIb is expressed in epithelial cells. FGFR3 ligands include FGF1, FGF2, FGF4, FGF8, FGF9, and FGF23. It is a negative regulator of long bone growth. In the cochlear duct and in the lens, FGFR3 is involved in differentiation while it appears to have a role in cell proliferation in epithelial cells. Germline mutations in FGFR3 are associated with skeletal disorders including several forms of dwarfism. Some missense mutations are associated with multiple myeloma and carcinomas of the bladder and cervix. Overexpression of FGFR3 is found in thyroid carcinoma. FGFR3 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 76.21  E-value: 1.19e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEF------RPSGEL-FAIKALKkgDIVARDEVESLMCEKRILAAVtsAGHPFLVNLFG-CFQT-PEHV 697
Cdd:cd05100  20 LGEGCFGQVVMAEAigidkdKPNKPVtVAVKMLK--DDATDKDLSDLVSEMEMMKMI--GKHKNIINLLGaCTQDgPLYV 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 698 cfVMEYSAGGDLMLHIHSdvfSEPRAIFYS--AC------------------VVLGLQFLHEHKIVYRDLKLDNLLLDTE 757
Cdd:cd05100  96 --LVEYASKGNLREYLRA---RRPPGMDYSfdTCklpeeqltfkdlvscayqVARGMEYLASQKCIHRDLAARNVLVTED 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 758 GYVKIADFGLCKE--GMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEML-VGESPFPGDDEEEVFDSIV 834
Cdd:cd05100 171 NVMKIADFGLARDvhNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFtLGGSPYPGIPVEELFKLLK 250
                       250       260       270
                ....*....|....*....|....*....|
gi 47132591 835 N-DEVRYPRFLSAEAIGIMRRLLRRNPERR 863
Cdd:cd05100 251 EgHRMDKPANCTHELYMIMRECWHAVPSQR 280
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
621-842 1.22e-14

Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. Gain of function alterations, through their overexpression, deletions, or point mutations in their kinase domains, have been implicated in various cancers. These receptors are targets of many small molecule inhibitors and monoclonal antibodies used in cancer therapy. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 75.14  E-value: 1.22e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGEL----FAIKALKkgDIVARDEVESLMCEKRILAAVtsaGHPFLVNLFGCFQTPEH 696
Cdd:cd05057   9 LEKGKVLGSGAFGTVYKGVWIPEGEKvkipVAIKVLR--EETGPKANEEILDEAYVMASV---DHPHLVRLLGICLSSQV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 697 vCFVMEYSAGGDLMLHI--HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEgMGY 774
Cdd:cd05057  84 -QLITQLMPLGCLLDYVrnHRDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGLAKL-LDV 161
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47132591 775 GDRTSTFCG--TP-EFLAPEVLTDTSYTRAVDWWGLGVLLYEMLV-GESPFPGDDEEEVFDSIVNDEvRYPR 842
Cdd:cd05057 162 DEKEYHAEGgkVPiKWMALESIQYRIYTHKSDVWSYGVTVWELMTfGAKPYEGIPAVEIPDLLEKGE-RLPQ 232
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
619-863 1.29e-14

Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (Srm) and Breast tumor kinase (Brk); PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Srm and Brk (also called protein tyrosine kinase 6) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Brk has been found to be overexpressed in a majority of breast tumors. Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Srm and Brk however, lack the N-terminal myristylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The Srm/Brk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 74.78  E-value: 1.29e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELfAIKALKKGDIVARDEVESlmcEKRILAAVTsagHPFLVNLFGCFQTPEHVC 698
Cdd:cd05148   6 EEFTLERKLGSGYFGEVWEGLWKNRVRV-AIKILKSDDLLKQQDFQK---EVQALKRLR---HKHLISLFAVCSVGEPVY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGGDLMLHIHS---DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDtEGYV-KIADFGLC---KEG 771
Cdd:cd05148  79 IITELMEKGSLLAFLRSpegQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVG-EDLVcKVADFGLArliKED 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 772 MGYGDRTStfcgTP-EFLAPEVLTDTSYTRAVDWWGLGVLLYEMLV-GESPFPGDDEEEVFDSIVNDeVRYPRFLS--AE 847
Cdd:cd05148 158 VYLSSDKK----IPyKWTAPEAASHGTFSTKSDVWSFGILLYEMFTyGQVPYPGMNNHEVYDQITAG-YRMPCPAKcpQE 232
                       250
                ....*....|....*.
gi 47132591 848 AIGIMRRLLRRNPERR 863
Cdd:cd05148 233 IYKIMLECWAAEPEDR 248
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
627-821 1.42e-14

Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TNNI3K, also called cardiac ankyrin repeat kinase (CARK), is a cardiac-specific troponin I-interacting kinase that promotes cardiac myogenesis, improves cardiac performance, and protects the myocardium from ischemic injury. It contains N-terminal ankyrin repeats, a catalytic kinase domain, and a C-terminal serine-rich domain. TNNI3K exerts a disease-accelerating effect on cardiac dysfunction and reduced survival in mouse models of cardiomyopathy. The TNNI3K subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 74.49  E-value: 1.42e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRpsGELFAIKALKKGDIVARDEVESLMCEKRILAAVTsagHPFLVNLFG-CFQTPEHVCFVMEYSA 705
Cdd:cd14064   1 IGSGSFGKVYKGRCR--NKIVAIKRYRANTYCSKSDVDMFCREVSILCRLN---HPCVIQFVGaCLDDPSQFAIVTQYVS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 706 GGDL--MLHIHSDVFSEPRAIFYSACVVLGLQFLHE--HKIVYRDLKLDNLLLDTEGYVKIADFG----LCKEgmgYGDR 777
Cdd:cd14064  76 GGSLfsLLHEQKRVIDLQSKLIIAVDVAKGMEYLHNltQPIIHRDLNSHNILLYEDGHAVVADFGesrfLQSL---DEDN 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 47132591 778 TSTFCGTPEFLAPEVLTD-TSYTRAVDWWGLGVLLYEMLVGESPF 821
Cdd:cd14064 153 MTKQPGNLRWMAPEVFTQcTRYSIKADVFSYALCLWELLTGEIPF 197
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
627-830 1.59e-14

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Alternative splicing of FGFR1 transcripts produces a variety of isoforms, which are differentially expressed in cells. FGFR1 binds the ligands, FGF1 and FGF2, with high affinity and has also been reported to bind FGF4, FGF6, and FGF9. FGFR1 signaling is critical in the control of cell migration during embryo development. It promotes cell proliferation in fibroblasts. Nuclear FGFR1 plays a role in the regulation of transcription. Mutations, insertions or deletions of FGFR1 have been identified in patients with Kallman's syndrome (KS), an inherited disorder characterized by hypogonadotropic hypogonadism and loss of olfaction. Aberrant FGFR1 expression has been found in some human cancers including 8P11 myeloproliferative syndrome (EMS), breast cancer, and pancreatic adenocarcinoma. FGFR1 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 75.43  E-value: 1.59e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEF------RPSG-ELFAIKALKKgDIVARDeVESLMCEKRILAAVtsAGHPFLVNLFG-CFQT-PEHV 697
Cdd:cd05098  21 LGEGCFGQVVLAEAigldkdKPNRvTKVAVKMLKS-DATEKD-LSDLISEMEMMKMI--GKHKNIINLLGaCTQDgPLYV 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 698 cfVMEYSAGGDLMLHIHSdvfSEPRAIFYS-----------------AC---VVLGLQFLHEHKIVYRDLKLDNLLLDTE 757
Cdd:cd05098  97 --IVEYASKGNLREYLQA---RRPPGMEYCynpshnpeeqlsskdlvSCayqVARGMEYLASKKCIHRDLAARNVLVTED 171
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47132591 758 GYVKIADFGLCKE--GMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEML-VGESPFPGDDEEEVF 830
Cdd:cd05098 172 NVMKIADFGLARDihHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFtLGGSPYPGVPVEELF 247
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
620-863 2.69e-14

Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular carcinoma and Resting lymphocyte kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tec and Rlk (also named Txk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. Instead of PH, Rlk contains an N-terminal cysteine-rich region. In addition to PH, Tec also contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells. Tec is more widely-expressed than other Tec-like subfamily kinases. It is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Rlk is expressed in T-cells and mast cell lines. Tec and Rlk are both key components of T-cell receptor (TCR) signaling. They are important in TCR-stimulated proliferation, IL-2 production and phopholipase C-gamma1 activation. The Tec/Rlk subfamily is part of a larger superfamily, that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 74.13  E-value: 2.69e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKFLAVLGRGHFGKVLLSEFRPSGELfAIKALKKGDIVARDEVEslmcEKRILAAVTsagHPFLVNLFGCFQTPEHVCF 699
Cdd:cd05114   5 ELTFMKELGSGLFGVVRLGKWRAQYKV-AIKAIREGAMSEEDFIE----EAKVMMKLT---HPKLVQLYGVCTQQKPIYI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYSAGGDLMLHIHSDVFSEPRAIFYSAC--VVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMgyGDR 777
Cdd:cd05114  77 VTEFMENGCLLNYLRQRRGKLSRDMLLSMCqdVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRYVL--DDQ 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 778 TSTFCGTP---EFLAPEVLTDTSYTRAVDWWGLGVLLYEMLV-GESPFPGDDEEEVFDSIVNDEVRY-PRFLSAEAIGIM 852
Cdd:cd05114 155 YTSSSGAKfpvKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTeGKMPFESKSNYEVVEMVSRGHRLYrPKLASKSVYEVM 234
                       250
                ....*....|.
gi 47132591 853 RRLLRRNPERR 863
Cdd:cd05114 235 YSCWHEKPEGR 245
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
621-868 2.76e-14

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 75.09  E-value: 2.76e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFV 700
Cdd:cd06635  27 FSDLREIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQRIK---HPNSIEYKGCYLREHTAWLV 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGG-DLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGlckeGMGYGDRTS 779
Cdd:cd06635 104 MEYCLGSaSDLLEVHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFG----SASIASPAN 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 780 TFCGTPEFLAPEV---LTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVryPRFLSAEAIGIMRRL- 855
Cdd:cd06635 180 SFVGTPYWMAPEVilaMDEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNES--PTLQSNEWSDYFRNFv 257
                       250
                ....*....|....*.
gi 47132591 856 ---LRRNPERRLGSSE 868
Cdd:cd06635 258 dscLQKIPQDRPTSEE 273
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
619-863 2.77e-14

Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; Tie1; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie1 is a receptor tyr kinase (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. No specific ligand has been identified for Tie1, although the angiopoietin, Ang-1, binds to Tie1 through integrins at high concentrations. In vivo studies of Tie1 show that it is critical in vascular development.


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 74.65  E-value: 2.77e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELF--AIKALKkgDIVARDEVESLMCEKRILAAVtsAGHPFLVNLFGCFQTPEH 696
Cdd:cd05089   2 EDIKFEDVIGEGNFGQVIKAMIKKDGLKMnaAIKMLK--EFASENDHRDFAGELEVLCKL--GHHPNIINLLGACENRGY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 697 VCFVMEYSAGGDLM-----------------LHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGY 759
Cdd:cd05089  78 LYIAIEYAPYGNLLdflrksrvletdpafakEHGTASTLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLV 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 760 VKIADFGLCKEGMGYGDRTSTFCGTpEFLAPEVLTDTSYTRAVDWWGLGVLLYEML-VGESPFPGDDEEEVFDSIVND-E 837
Cdd:cd05089 158 SKIADFGLSRGEEVYVKKTMGRLPV-RWMAIESLNYSVYTTKSDVWSFGVLLWEIVsLGGTPYCGMTCAELYEKLPQGyR 236
                       250       260
                ....*....|....*....|....*.
gi 47132591 838 VRYPRFLSAEAIGIMRRLLRRNPERR 863
Cdd:cd05089 237 MEKPRNCDDEVYELMRQCWRDRPYER 262
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
612-863 2.90e-14

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 7; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK7 is a dual-specificity PK that phosphorylates and activates its downstream target, c-Jun N-terminal kinase (JNK), on specific threonine and tyrosine residues. Although MKK7 is capable of dual phosphorylation, it prefers to phosphorylate the threonine residue of JNK. Thus, optimal activation of JNK requires both MKK4 and MKK7. MKK7 is primarily activated by cytokines. MKK7 is essential for liver formation during embryogenesis. It plays roles in G2/M cell cycle arrest and cell growth. In addition, it is involved in the control of programmed cell death, which is crucial in oncogenesis, cancer chemoresistance, and antagonism to TNFalpha-induced killing, through its inhibition by Gadd45beta and the subsequent suppression of the JNK cascade. The MKK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 74.33  E-value: 2.90e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 612 RKSPLTLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDivARDEveslmcEKRILA--AVTSAGH--PFLVNL 687
Cdd:cd06618   8 KKYKADLNDLENLGEIGSGTCGQVYKMRHKKTGHVMAVKQMRRSG--NKEE------NKRILMdlDVVLKSHdcPYIVKC 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 688 FGCFQTPEHVCFVME-YSAGGDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHE-HKIVYRDLKLDNLLLDTEGYVKIADF 765
Cdd:cd06618  80 YGYFITDSDVFICMElMSTCLDKLLKRIQGPIPEDILGKMTVSIVKALHYLKEkHGVIHRDVKPSNILLDESGNVKLCDF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 766 GLCKEGMGYGDRTSTfCGTPEFLAPEVL---TDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEE-EVFDSIVNDEVryP 841
Cdd:cd06618 160 GISGRLVDSKAKTRS-AGCAAYMAPERIdppDNPKYDIRADVWSLGISLVELATGQFPYRNCKTEfEVLTKILNEEP--P 236
                       250       260
                ....*....|....*....|....*..
gi 47132591 842 RFLSAEAIGIM-----RRLLRRNPERR 863
Cdd:cd06618 237 SLPPNEGFSPDfcsfvDLCLTKDHRYR 263
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
617-824 3.38e-14

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek7 is required for mitotic spindle formation and cytokinesis. It is enriched in the centrosome and is critical for microtubule nucleation. Nek7 is activated by Nek9 during mitosis, and may regulate the p70 ribosomal S6 kinase. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 74.30  E-value: 3.38e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 617 TLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEH 696
Cdd:cd08229  22 TLANFRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLN---HPNVIKYYASFIEDNE 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 697 VCFVMEYSAGGDLMLHI-----HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLckeG 771
Cdd:cd08229  99 LNIVLELADAGDLSRMIkhfkkQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGL---G 175
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 47132591 772 MGYGDRTS---TFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGD 824
Cdd:cd08229 176 RFFSSKTTaahSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGD 231
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
619-863 4.38e-14

Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow kinase on the X chromosome; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Btk and Bmx (also named Etk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Btk contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor, leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. Bmx is primarily expressed in bone marrow and the arterial endothelium, and plays an important role in ischemia-induced angiogenesis. It facilitates arterial growth, capillary formation, vessel maturation, and bone marrow-derived endothelial progenitor cell mobilization. The Btk/Bmx subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 73.38  E-value: 4.38e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELfAIKALKKGDIVARDEVEslmcEKRILAAVTsagHPFLVNLFGCFQTPEHVC 698
Cdd:cd05113   4 KDLTFLKELGTGQFGVVKYGKWRGQYDV-AIKMIKEGSMSEDEFIE----EAKVMMNLS---HEKLVQLYGVCTKQRPIF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGGDLMLHIHSDVFSEPRAIFYSAC--VVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMgyGD 776
Cdd:cd05113  76 IITEYMANGCLLNYLREMRKRFQTQQLLEMCkdVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVL--DD 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 777 RTSTFCGTP---EFLAPEVLTDTSYTRAVDWWGLGVLLYEML-VGESPFPGDDEEEVFDSIVNDEVRY-PRFLSAEAIGI 851
Cdd:cd05113 154 EYTSSVGSKfpvRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYsLGKMPYERFTNSETVEHVSQGLRLYrPHLASEKVYTI 233
                       250
                ....*....|..
gi 47132591 852 MRRLLRRNPERR 863
Cdd:cd05113 234 MYSCWHEKADER 245
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
618-824 4.54e-14

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 is required for the transition from metaphase to anaphase. It also plays important roles in mitotic spindle formation and cytokinesis. Activated by Nek9 during mitosis, Nek6 phosphorylates Eg5, a kinesin that is important for spindle bipolarity. Nek6 localizes to spindle microtubules during metaphase and anaphase, and to the midbody during cytokinesis. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 73.52  E-value: 4.54e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 618 LEDFKFLAVLGRGHFGKVllseFRPSGELFAIK-ALKKGDIVARDEVESLM-CEKRIlAAVTSAGHPFLVNLFGCFQTPE 695
Cdd:cd08228   1 LANFQIEKKIGRGQFSEV----YRATCLLDRKPvALKKVQIFEMMDAKARQdCVKEI-DLLKQLNHPNVIKYLDSFIEDN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 696 HVCFVMEYSAGGDL---MLHIHSDVFSEPRAIFYSACVVL--GLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLcke 770
Cdd:cd08228  76 ELNIVLELADAGDLsqmIKYFKKQKRLIPERTVWKYFVQLcsAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGL--- 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 47132591 771 GMGYGDRTS---TFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGD 824
Cdd:cd08228 153 GRFFSSKTTaahSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGD 209
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
626-863 4.86e-14

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR3 (or Flt4) preferentially binds the ligands VEGFC and VEGFD. VEGFR3 is essential for lymphatic endothelial cell (EC) development and function. It has been shown to regulate adaptive immunity during corneal transplantation. VEGFR3 is upregulated on blood vascular ECs in pathological conditions such as vascular tumors and the periphery of solid tumors. It plays a role in cancer progression and lymph node metastasis. Missense mutations in the VEGFR3 gene are associated with primary human lymphedema. VEGFR3 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 74.63  E-value: 4.86e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVL-LSEF----RPSGELFAIKALKKGDIVArdEVESLMCEKRILAAVtsAGHPFLVNLFG-CFQTPEHVCF 699
Cdd:cd05102  14 VLGHGAFGKVVeASAFgidkSSSCETVAVKMLKEGATAS--EHKALMSELKILIHI--GNHLNVVNLLGaCTKPNGPLMV 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYSAGGDL--MLHIHSDVFS-----EPRA------------------------------------------------- 723
Cdd:cd05102  90 IVEFCKYGNLsnFLRAKREGFSpyrerSPRTrsqvrsmveavradrrsrqgsdrvasftestsstnqprqevddlwqspl 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 724 -----IFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEgmGYGDRTSTFCGTP----EFLAPEVLT 794
Cdd:cd05102 170 tmedlICYSFQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARD--IYKDPDYVRKGSArlplKWMAPESIF 247
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47132591 795 DTSYTRAVDWWGLGVLLYEML-VGESPFPGDDEEEVFDSIVND--EVRYPRFLSAEAIGIMRRLLRRNPERR 863
Cdd:cd05102 248 DKVYTTQSDVWSFGVLLWEIFsLGASPYPGVQINEEFCQRLKDgtRMRAPEYATPEIYRIMLSCWHGDPKER 319
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
626-863 5.37e-14

Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes cyclin G-Associated Kinase (GAK), Drosophila melanogaster Numb-Associated Kinase (NAK)-like proteins, and similar protein kinases. GAK plays regulatory roles in clathrin-mediated membrane trafficking, the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses. NAK plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. The GAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 73.14  E-value: 5.37e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGELFAIKALKKGDIvarDEVESLMCEKRILAAVtsAGHPFLVNLFGC--FQTP--EHVCFVM 701
Cdd:cd13985   7 QLGEGGFSYVYLAHDVNTGRRYALKRMYFNDE---EQLRVAIKEIEIMKRL--CGHPNIVQYYDSaiLSSEgrKEVLLLM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 702 EYSAGG--DLMLHIHSDVFSEPRA--IFYSACVvlGLQFLHEHK--IVYRDLKLDNLLLDTEGYVKIADFG--------- 766
Cdd:cd13985  82 EYCPGSlvDILEKSPPSPLSEEEVlrIFYQICQ--AVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFGsattehypl 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 767 LCKEGMGYGDRTSTFCGTPEFLAPEVLTDTSY---TRAVDWWGLGVLLYEMLVGESPFpgDDEEEVFDSIVN----DEVR 839
Cdd:cd13985 160 ERAEEVNIIEEEIQKNTTPMYRAPEMIDLYSKkpiGEKADIWALGCLLYKLCFFKLPF--DESSKLAIVAGKysipEQPR 237
                       250       260
                ....*....|....*....|....
gi 47132591 840 YPRFLSAeaigIMRRLLRRNPERR 863
Cdd:cd13985 238 YSPELHD----LIRHMLTPDPAER 257
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
628-863 6.61e-14

Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals.The MLTK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 72.30  E-value: 6.61e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 628 GRGHFGKVLLSEFRPSGELFAIKALKKgdIVARDEVESLMCEKRIlaavtsaghpflVNLFGCFQTPEHVCFVMEYSAGG 707
Cdd:cd14060   2 GGGSFGSVYRAIWVSQDKEVAVKKLLK--IEKEAEILSVLSHRNI------------IQFYGAILEAPNYGIVTEYASYG 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 708 DLMLHIHSDVFSE---PRAIFYSACVVLGLQFLHEH---KIVYRDLKLDNLLLDTEGYVKIADFGLCKEgmgYGDRTS-T 780
Cdd:cd14060  68 SLFDYLNSNESEEmdmDQIMTWATDIAKGMHYLHMEapvKVIHRDLKSRNVVIAADGVLKICDFGASRF---HSHTTHmS 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 781 FCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIV--NDEVRYPRFLSAEAIGIMRRLLRR 858
Cdd:cd14060 145 LVGTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKGLEGLQVAWLVVekNERPTIPSSCPRSFAELMRRCWEA 224

                ....*
gi 47132591 859 NPERR 863
Cdd:cd14060 225 DVKER 229
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
617-868 6.98e-14

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 72.64  E-value: 6.98e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 617 TLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKkgdiVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEH 696
Cdd:cd14110   1 TEKTYAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIP----YKPEDKQLVLREYQVLRRLS---HPRIAQLHSAYLSPRH 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 697 VCFVMEYSAGGDLMLHI-HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFG----LCKEG 771
Cdd:cd14110  74 LVLIEELCSGPELLYNLaERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGnaqpFNQGK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 772 MGYGDRTSTFCgtpEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRF---LSAEA 848
Cdd:cd14110 154 VLMTDKKGDYV---ETMAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSSDLNWERDRNIRKGKVQLSRCyagLSGGA 230
                       250       260
                ....*....|....*....|
gi 47132591 849 IGIMRRLLRRNPERRLGSSE 868
Cdd:cd14110 231 VNFLKSTLCAKPWGRPTASE 250
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
627-873 8.45e-14

Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 72.69  E-value: 8.45e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRpSGELFAIKALKKGDiVARDEVESLMcEKRILAAVTsagHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd14066   1 IGSGGFGTVYKGVLE-NGTVVAVKRLNEMN-CAASKKEFLT-ELEMLGRLR---HPNLVRLLGYCLESDEKLLVYEYMPN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLMLHIHSDVFSEP-------RAIFYSACvvlGLQFLHE---HKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGD 776
Cdd:cd14066  75 GSLEDRLHCHKGSPPlpwpqrlKIAKGIAR---GLEYLHEecpPPIIHGDIKSSNILLDEDFEPKLTDFGLARLIPPSES 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 777 --RTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVnDEVRyprflsAEAIGIMRR 854
Cdd:cd14066 152 vsKTSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDENRENASRKDLV-EWVE------SKGKEELED 224
                       250
                ....*....|....*....
gi 47132591 855 LLRRNPERRLGSSERDAED 873
Cdd:cd14066 225 ILDKRLVDDDGVEEEEVEA 243
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
621-821 8.68e-14

Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNKs comprise a subfamily of STKs with an unusual placement of a catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. They are also involved in cell signaling, survival, proliferation, and organ development. WNKs are activated by hyperosmotic or low-chloride hypotonic stress and they function upstream of SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. There are four vertebrate WNKs which show varying expression patterns. WNK1 and WNK2 are widely expressed while WNK3 and WNK4 show a more restricted expression pattern. Because mutations in human WNK1 and WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension (due to increased sodium reabsorption) and hyperkalemia (due to impaired renal potassium secretion), there are more studies conducted on these two proteins, compared to WNK2 and WNK3. The WNK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 72.26  E-value: 8.68e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDiVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVC-- 698
Cdd:cd13983   3 LKFNEVLGRGSFKTVYRAFDTEEGIEVAWNEIKLRK-LPKAERQRFKQEIEILKSLK---HPNIIKFYDSWESKSKKEvi 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGGDLMLHIHSDVFSEPRAIfYSAC--VVLGLQFLHEHK--IVYRDLK-LDNLLLDTEGYVKIADFGLCKEgMG 773
Cdd:cd13983  79 FITELMTSGTLKQYLKRFKRLKLKVI-KSWCrqILEGLNYLHTRDppIIHRDLKcDNIFINGNTGEVKIGDLGLATL-LR 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 47132591 774 YGDRTSTFcGTPEFLAPEVLtDTSYTRAVDWWGLGVLLYEMLVGESPF 821
Cdd:cd13983 157 QSFAKSVI-GTPEFMAPEMY-EEHYDEKVDIYAFGMCLLEMATGEYPY 202
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
619-863 9.49e-14

Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lck and Blk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lck is expressed in T-cells and natural killer cells. It plays a critical role in T-cell maturation, activation, and T-cell receptor (TCR) signaling. Lck phosphorylates ITAM (immunoreceptor tyr activation motif) sequences on several subunits of TCRs, leading to the activation of different second messenger cascades. Phosphorylated ITAMs serve as binding sites for other signaling factor such as Syk and ZAP-70, leading to their activation and propagation of downstream events. In addition, Lck regulates drug-induced apoptosis by interfering with the mitochondrial death pathway. The apototic role of Lck is independent of its primary function in T-cell signaling. Blk is expressed specifically in B-cells. It is involved in pre-BCR (B-cell receptor) signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lck/Blk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 72.23  E-value: 9.49e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELfAIKALKKGDIvardEVESLMCEKRILAAVTsagHPFLVNLFGCFqTPEHVC 698
Cdd:cd05067   7 ETLKLVERLGAGQFGEVWMGYYNGHTKV-AIKSLKQGSM----SPDAFLAEANLMKQLQ---HQRLVRLYAVV-TQEPIY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGGDLMLHIHSDV---FSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK--EGMG 773
Cdd:cd05067  78 IITEYMENGSLVDFLKTPSgikLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARliEDNE 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 774 YGDRTSTfcGTP-EFLAPEVLTDTSYTRAVDWWGLGVLLYEMLV-GESPFPGDDEEEVfdsIVNDEVRY----PRFLSAE 847
Cdd:cd05067 158 YTAREGA--KFPiKWTAPEAINYGTFTIKSDVWSFGILLTEIVThGRIPYPGMTNPEV---IQNLERGYrmprPDNCPEE 232
                       250
                ....*....|....*.
gi 47132591 848 AIGIMRRLLRRNPERR 863
Cdd:cd05067 233 LYQLMRLCWKERPEDR 248
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
627-863 9.66e-14

Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes (or Fps) is a cytoplasmic (or nonreceptor) PTK containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated PTK activity. Fes kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells. It plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. A recent study implicates Fes kinase as a tumor suppressor in colorectal cancer. The Fes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 72.27  E-value: 9.66e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKkgDIVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd05084   4 IGRGNFGEVFSGRLRADNTPVAVKSCR--ETLPPDLKAKFLQEARILKQYS---HPNIVRLIGVCTQKQPIYIVMELVQG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLMLHIHSD--VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGM-GYGDRTSTFCG 783
Cdd:cd05084  79 GDFLTFLRTEgpRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSREEEdGVYAATGGMKQ 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 784 TP-EFLAPEVLTDTSYTRAVDWWGLGVLLYEML-VGESPFPGDDEEEVFDSIvNDEVRY--PRFLSAEAIGIMRRLLRRN 859
Cdd:cd05084 159 IPvKWTAPEALNYGRYSSESDVWSFGILLWETFsLGAVPYANLSNQQTREAV-EQGVRLpcPENCPDEVYRLMEQCWEYD 237

                ....
gi 47132591 860 PERR 863
Cdd:cd05084 238 PRKR 241
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
619-863 1.39e-13

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 71.98  E-value: 1.39e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELfAIKALKKGDIvardEVESLMCEKRILAAVTsagHPFLVNLFGCFqTPEHVC 698
Cdd:cd05073  11 ESLKLEKKLGAGQFGEVWMATYNKHTKV-AVKTMKPGSM----SVEAFLAEANVMKTLQ---HDKLVKLHAVV-TKEPIY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGGDLMLHIHSDVFSE---PRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK--EGMG 773
Cdd:cd05073  82 IITEFMAKGSLLDFLKSDEGSKqplPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARviEDNE 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 774 YGDRTSTfcGTP-EFLAPEVLTDTSYTRAVDWWGLGVLLYEMLV-GESPFPGDDEEEVFDSIVNDeVRYPRFLSA--EAI 849
Cdd:cd05073 162 YTAREGA--KFPiKWTAPEAINFGSFTIKSDVWSFGILLMEIVTyGRIPYPGMSNPEVIRALERG-YRMPRPENCpeELY 238
                       250
                ....*....|....
gi 47132591 850 GIMRRLLRRNPERR 863
Cdd:cd05073 239 NIMMRCWKNRPEER 252
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
627-821 1.62e-13

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The IKK complex functions as a master regulator of Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. It is composed of two kinases, IKKalpha and IKKbeta, and the regulatory subunit IKKgamma or NEMO (NF-kB Essential MOdulator). IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. There are two IKK pathways that regulate NF-kB signaling, called the classical (involving IKKbeta and NEMO) and non-canonical (involving IKKalpha) pathways. The classical pathway regulates the majority of genes activated by NF-kB. The IKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 72.10  E-value: 1.62e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKA----LKKGDI-VARDEVE-SLMCEKR---ILAAVTSAGHPFLvnlfgcfQTPEHV 697
Cdd:cd13989   1 LGSGGFGYVTLWKHQDTGEYVAIKKcrqeLSPSDKnRERWCLEvQIMKKLNhpnVVSARDVPPELEK-------LSPNDL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 698 CFV-MEYSAGGDLmlhihSDVFSEPRaifySAC-------------VVLGLQFLHEHKIVYRDLKLDNLLLDTEG---YV 760
Cdd:cd13989  74 PLLaMEYCSGGDL-----RKVLNQPE----NCCglkesevrtllsdISSAISYLHENRIIHRDLKPENIVLQQGGgrvIY 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47132591 761 KIADFGLCKEgMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPF 821
Cdd:cd13989 145 KLIDLGYAKE-LDQGSLCTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPF 204
Hr1 smart00742
Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical ...
52-99 1.97e-13

Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical domain found in vertebrate PRK1 and yeast PKC1 protein kinases C. The HR1 in rhophilin bind RhoGTP; those in PRK1 bind RhoA and RhoB. Also called RBD - Rho-binding domain


Pssm-ID: 128981  Cd Length: 57  Bit Score: 65.67  E-value: 1.97e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 47132591     52 IRKELKLKEGAENLRRATTDLGRSLGPVELLLRGSSRRLDLLHQQLQE 99
Cdd:smart00742  10 IEKELKVKEGAENMRKLTSNDRKVLSEAQSMLRESNQKLDLLKEELEK 57
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
627-863 2.09e-13

Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; Fes subfamily; catalytic (c) domain. Fes subfamily members include Fes (or Fps), Fer, and similar proteins. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes subfamily proteins are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated tyr kinase activity. Fes and Fer kinases play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Fes and Fer show redundancy in their biological functions.


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 70.94  E-value: 2.09e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKGDivARDEVESLMCEKRILAAVTsagHPFLVNLFG-CFQTpEHVCFVMEYSA 705
Cdd:cd05041   3 IGRGNFGDVYRGVLKPDNTEVAVKTCRETL--PPDLKRKFLQEARILKQYD---HPNIVKLIGvCVQK-QPIMIVMELVP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 706 GGDLMLHIHSDVFSEPRAIFYSACV--VLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTfcG 783
Cdd:cd05041  77 GGSLLTFLRKKGARLTVKQLLQMCLdaAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSREEEDGEYTVSD--G 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 784 TPE----FLAPEVLTDTSYTRAVDWWGLGVLLYEML-VGESPFPGDDEEEVFDSIvndEVRY----PRFLSAEAIGIMRR 854
Cdd:cd05041 155 LKQipikWTAPEALNYGRYTSESDVWSFGILLWEIFsLGATPYPGMSNQQTREQI---ESGYrmpaPELCPEAVYRLMLQ 231

                ....*....
gi 47132591 855 LLRRNPERR 863
Cdd:cd05041 232 CWAYDPENR 240
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
773-868 2.36e-13

Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB1 interacts directly with the mitogen activated protein kinase (MAPK) kinase MKK4, an activator of JNK. It regulates vascular smooth muscle cell proliferation and chemotaxis through the JNK signaling pathway. It is found to be down-regulated in human acute myeloid leukaemia (AML) and may play a role in the pathogenesis of the disease. It has also been identified as a potential biomarker for antibody-mediated allograft failure. TRB1 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB1 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 70.85  E-value: 2.36e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 773 GYGDRTSTFCGTPEFLAPEVLTDT-SYT-RAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIG 850
Cdd:cd14023 138 GEDDALSDKHGCPAYVSPEILNTTgTYSgKSADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPDHVSPKARC 217
                        90
                ....*....|....*...
gi 47132591 851 IMRRLLRRNPERRLGSSE 868
Cdd:cd14023 218 LIRSLLRREPSERLTAPE 235
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
621-821 2.63e-13

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human TAO2 is also known as prostate-derived Ste20-like kinase (PSK) and was identified in a screen for overexpressed RNAs in prostate cancer. TAO2 possesses mitogen-activated protein kinase (MAPK) kinase kinase activity and activates both p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating their respective MAP/ERK kinases, MEK3/MEK6 and MKK4/MKK7. It contains a long C-terminal extension with autoinhibitory segments, and is activated by the release of this inhibition and the phosphorylation of its activation loop serine. TAO2 functions as a regulator of actin cytoskeletal and microtubule organization. In addition, it regulates the transforming growth factor-activated kinase 1 (TAK1), which is a MAPKKK that plays an essential role in the signaling pathways of tumor necrosis factor, interleukin 1, and Toll-like receptor. The TAO2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 71.98  E-value: 2.63e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFV 700
Cdd:cd06634  17 FSDLREIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQKLR---HPNTIEYRGCYLREHTAWLV 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAG-GDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGlckeGMGYGDRTS 779
Cdd:cd06634  94 MEYCLGsASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFG----SASIMAPAN 169
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 47132591 780 TFCGTPEFLAPEV---LTDTSYTRAVDWWGLGVLLYEMLVGESPF 821
Cdd:cd06634 170 SFVGTPYWMAPEVilaMDEGQYDGKVDVWSLGITCIELAERKPPL 214
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
621-814 2.67e-13

Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 70.94  E-value: 2.67e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFqTPEHVCF- 699
Cdd:cd06607   3 FEDLREIGHGSFGAVYYARNKRTSEVVAIKKMSYSGKQSTEKWQDIIKEVKFLRQLR---HPNTIEYKGCY-LREHTAWl 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYSAG--GDlMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGlckeGMGYGDR 777
Cdd:cd06607  79 VMEYCLGsaSD-IVEVHKKPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFG----SASLVCP 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 47132591 778 TSTFCGTPEFLAPEV---LTDTSYTRAVDWWGLGVLLYEM 814
Cdd:cd06607 154 ANSFVGTPYWMAPEVilaMDEGQYDGKVDVWSLGITCIEL 193
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
624-841 2.92e-13

Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also called protein tyrosine kinase 7 (PTK7), is an orphan receptor PTK (RTK) containing an extracellular region with seven immunoglobulin domains, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Studies in mice reveal that CCK4 is essential for neural development. Mouse embryos containing a truncated CCK4 die perinatally and display craniorachischisis, a severe form of neural tube defect. The mechanism of action of the CCK4 pseudokinase is still unknown. Other pseudokinases such as HER3 rely on the activity of partner RTKs. The CCK4 subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 71.34  E-value: 2.92e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 624 LAVLGRGHFGKVLLSEFRPSGE-----LFAIKALKKgdivaRDEVESLMCEKRILAAVTSAGHPFLVNLFGCFQTPEHVC 698
Cdd:cd05046  10 ITTLGRGEFGEVFLAKAKGIEEeggetLVLVKALQK-----TKDENLQSEFRRELDMFRKLSHKNVVRLLGLCREAEPHY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGGDL--MLHIHS--DVFSEPRAIFYSACVVL------GLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLC 768
Cdd:cd05046  85 MILEYTDLGDLkqFLRATKskDEKLKPPPLSTKQKVALctqialGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLSLS 164
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47132591 769 KEgmGYGDRTSTFCGT--P-EFLAPEVLTDTSYTRAVDWWGLGVLLYEMLV-GESPFPGDDEEEVFDSIVNDEVRYP 841
Cdd:cd05046 165 KD--VYNSEYYKLRNAliPlRWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTqGELPFYGLSDEEVLNRLQAGKLELP 239
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
627-815 3.36e-13

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. Vertebrate have two members, LIMK1 and LIMK2. The LIMK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 71.00  E-value: 3.36e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKGDivarDEVESLMCEKriLAAVTSAGHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd14154   1 LGKGFFGQAIKVTHRETGEVMVMKELIRFD----EEAQRNFLKE--VKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDL--MLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK-----------EGMG 773
Cdd:cd14154  75 GTLkdVLKDMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLARliveerlpsgnMSPS 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 47132591 774 YGDRTS---------TFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEML 815
Cdd:cd14154 155 ETLRHLkspdrkkryTVVGNPYWMAPEMLNGRSYDEKVDIFSFGIVLCEII 205
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
617-880 3.63e-13

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), Bypass UAS Requirement 1, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BUR1, also called SGV1, is a yeast CDK that is functionally equivalent to mammalian CDK9. It associates with the cyclin BUR2. BUR genes were orginally identified in a genetic screen as factors involved in general transcription. The BUR1/BUR2 complex phosphorylates the C-terminal domain of RNA polymerase II. In addition, this complex regulates histone modification by phosporylating Rad6 and mediating the association of the Paf1 complex with chromatin. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The BUR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 71.58  E-value: 3.63e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 617 TLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAikaLKKgdIVARDEVESL----MCEKRILAAVTsagHPFLVNLFGCF- 691
Cdd:cd07866   6 KLRDYEILGKLGEGTFGEVYKARQIKTGRVVA---LKK--ILMHNEKDGFpitaLREIKILKKLK---HPNVVPLIDMAv 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 692 -----QTPEHVCF--VMEYSAGgDL--MLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKI 762
Cdd:cd07866  78 erpdkSKRKRGSVymVTPYMDH-DLsgLLENPSVKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKI 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 763 ADFGLC----------KEGMGYGDRTSTFC-GTPEFLAPE-VLTDTSYTRAVDWWGLGVLLYEMLVGESPFPG----DDE 826
Cdd:cd07866 157 ADFGLArpydgpppnpKGGGGGGTRKYTNLvVTRWYRPPElLLGERRYTTAVDIWGIGCVFAEMFTRRPILQGksdiDQL 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 827 EEVFDSI-------------------VNDEVRYPRFLS-------AEAIGIMRRLLRRNPERRLgsserDAEDVKKQPFF 880
Cdd:cd07866 237 HLIFKLCgtpteetwpgwrslpgcegVHSFTNYPRTLEerfgklgPEGLDLLSKLLSLDPYKRL-----TASDALEHPYF 311
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
627-823 4.90e-13

Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Syk-like subfamily is composed of Syk, ZAP-70, Shark, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. They are involved in the signaling downstream of activated receptors (including B-cell, T-cell, and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. Syk is important in B-cell receptor signaling, while Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor signaling. Syk also plays a central role in Fc receptor-mediated phagocytosis in the adaptive immune system. Shark is exclusively expressed in ectodermally derived epithelia, and is localized preferentially to the apical surface of the epithelial cells, it may play a role in a signaling pathway for epithelial cell polarity. The Syk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 70.07  E-value: 4.90e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFR-PSGELF--AIKALKKGDIVArDEVEsLMCEKRILAAVTsagHPFLVNLFGCFQTPEhVCFVMEY 703
Cdd:cd05060   3 LGHGNFGSVRKGVYLmKSGKEVevAVKTLKQEHEKA-GKKE-FLREASVMAQLD---HPCIVRLIGVCKGEP-LMLVMEL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 704 SAGGDLMLHIHSD-VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKeGMGYGD---RTS 779
Cdd:cd05060  77 APLGPLLKYLKKRrEIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSR-ALGAGSdyyRAT 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 47132591 780 TFCGTP-EFLAPEVLTDTSYTRAVDWWGLGVLLYEML-VGESPFPG 823
Cdd:cd05060 156 TAGRWPlKWYAPECINYGKFSSKSDVWSYGVTLWEAFsYGAKPYGE 201
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
618-884 5.28e-13

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-1 is expressed ubiquitously and is localized in the cytoplasm. Its kinase activity is cell cycle dependent and peaks at the S and G2 phases. PCTAIRE-1 is highly expressed in the brain and may play a role in regulating neurite outgrowth. It can also associate with Trap (Tudor repeat associator with PCTAIRE-2), a physiological partner of PCTAIRE-2; with p11, a small dimeric protein with similarity to S100; and with 14-3-3 proteins, mediators of phosphorylation-dependent interactions in many different proteins. PCTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 70.80  E-value: 5.28e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 618 LEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKkgdivaRDEVESLMCEK-RILAAVTSAGHPFLVNLFGCFQTPEH 696
Cdd:cd07873   1 LETYIKLDKLGEGTYATVYKGRSKLTDNLVALKEIR------LEHEEGAPCTAiREVSLLKDLKHANIVTLHDIIHTEKS 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 697 VCFVMEYsAGGDLMLHIHS--DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEG--- 771
Cdd:cd07873  75 LTLVFEY-LDKDLKQYLDDcgNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKsip 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 772 -MGYGDRTSTFCGTPeflaPEVLT-DTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIV--------------- 834
Cdd:cd07873 154 tKTYSNEVVTLWYRP----PDILLgSTDYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEQLHFIFrilgtpteetwpgil 229
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47132591 835 -NDEVR---YPRF-----------LSAEAIGIMRRLLRRNPERRLGsserdAEDVKKQPFFRTLG 884
Cdd:cd07873 230 sNEEFKsynYPKYradalhnhaprLDSDGADLLSKLLQFEGRKRIS-----AEEAMKHPYFHSLG 289
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
619-880 5.77e-13

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL1, also called p42 KKIALRE, is a glial protein that is upregulated in gliosis. It is present in neuroblastoma and A431 human carcinoma cells, and may be implicated in neoplastic transformation. The function of CDKL4 is unknown. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 70.48  E-value: 5.77e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIK---------ALKKgdiVARDEVESLMCEKrilaavtsagHPFLVNLFG 689
Cdd:cd07847   1 EKYEKLSKIGEGSYGVVFKCRNRETGQIVAIKkfveseddpVIKK---IALREIRMLKQLK----------HPNLVNLIE 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 690 CFQTPEHVCFVMEY---SAGGDLMLHIHSDVFSEPRAIFYSacVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFG 766
Cdd:cd07847  68 VFRRKRKLHLVFEYcdhTVLNELEKNPRGVPEHLIKKIIWQ--TLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFG 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 767 LCKEGMGYGDRTSTFCGTPEFLAPEVLT-DTSYTRAVDWWGLGVLLYEMLVGESPFPGDDE------------------E 827
Cdd:cd07847 146 FARILTGPGDDYTDYVATRWYRAPELLVgDTQYGPPVDVWAIGCVFAELLTGQPLWPGKSDvdqlylirktlgdliprhQ 225
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47132591 828 EVF--------------DSIVNDEVRYPRfLSAEAIGIMRRLLRRNPERRLGSSErdaedVKKQPFF 880
Cdd:cd07847 226 QIFstnqffkglsipepETREPLESKFPN-ISSPALSFLKGCLQMDPTERLSCEE-----LLEHPYF 286
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
626-868 7.25e-13

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 69.60  E-value: 7.25e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRpsGELFAIKALKKGdivardevESLMCEKRILAAVTSAGHPFLVNLFGCFQTPEhvCFVMEYSA 705
Cdd:cd14068   1 LLGDGGFGSVYRAVYR--GEDVAVKIFNKH--------TSFRLLRQELVVLSHLHHPSLVALLAAGTAPR--MLVMELAP 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 706 GGDLMLHIHSDVFSEPRAIFYSAC--VVLGLQFLHEHKIVYRDLKLDNLLLDT-----EGYVKIADFGLCKEGMGYGDRT 778
Cdd:cd14068  69 KGSLDALLQQDNASLTRTLQHRIAlhVADGLRYLHSAMIIYRDLKPHNVLLFTlypncAIIAKIADYGIAQYCCRMGIKT 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 779 StfCGTPEFLAPEVLT-DTSYTRAVDWWGLGVLLYEMLVGES------PFPGDDEEEVFDSIVNDEVR-YPRFLSAEAIG 850
Cdd:cd14068 149 S--EGTPGFRAPEVARgNVIYNQQADVYSFGLLLYDILTCGEriveglKFPNEFDELAIQGKLPDPVKeYGCAPWPGVEA 226
                       250
                ....*....|....*...
gi 47132591 851 IMRRLLRRNPERRLGSSE 868
Cdd:cd14068 227 LIKDCLKENPQCRPTSAQ 244
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
642-868 7.41e-13

Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Tribbles Homolog (TRB) proteins interact with many proteins involved in signaling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, differentiation, and gene expression. TRB proteins bind to the middle kinase in mitogen activated protein kinase (MAPK) signaling cascades, MAPK kinases. They regulate the activity of MAPK kinases, and thus, affect MAPK signaling. In Drosophila, Tribbles regulates String, the ortholog of mammalian Cdc25, during morphogenesis. String is implicated in the progression of mitosis during embryonic development. Vertebrates contain three TRB proteins encoded by three separate genes: Tribbles-1 (TRB1 or TRIB1), Tribbles-2 (TRB2 or TRIB2), and Tribbles-3 (TRB3 or TRIB3). The TRB subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 69.38  E-value: 7.41e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 642 PSGELFAIKALKKGDivardeveslmCEKRILAAVTSAGHPFLVNLFGCFqTPEHVCFVMEYSAGGDLmlhiHSDVFS-- 719
Cdd:cd13976  16 HTGEELVCKVVPVPE-----------CHAVLRAYFRLPSHPNISGVHEVI-AGETKAYVFFERDHGDL----HSYVRSrk 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 720 -----EPRAIFYSACVVLglQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLckEGM----GYGDRTSTFCGTPEFLAP 790
Cdd:cd13976  80 rlrepEAARLFRQIASAV--AHCHRNGIVLRDLKLRKFVFADEERTKLRLESL--EDAvileGEDDSLSDKHGCPAYVSP 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 791 EVL-TDTSYT-RAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNPERRLGSSE 868
Cdd:cd13976 156 EILnSGATYSgKAADVWSLGVILYTMLVGRYPFHDSEPASLFAKIRRGQFAIPETLSPRARCLIRSLLRREPSERLTAED 235
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
626-863 7.62e-13

Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie proteins, consisting of Tie1 and Tie2, are receptor PTKs (RTKs) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2, while no specific ligand has been identified for Tie1. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. In vivo studies of Tie1 show that it is critical in vascular development. The Tie subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 69.68  E-value: 7.62e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGELF--AIKALKkgDIVARDEVESLMCEKRILAAVtsAGHPFLVNLFGCFQTPEHVCFVMEY 703
Cdd:cd05047   2 VIGEGNFGQVLKARIKKDGLRMdaAIKRMK--EYASKDDHRDFAGELEVLCKL--GHHPNIINLLGACEHRGYLYLAIEY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 704 SAGGDLM-----------------LHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFG 766
Cdd:cd05047  78 APHGNLLdflrksrvletdpafaiANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 767 LCKEGMGYGDRTSTFCGTpEFLAPEVLTDTSYTRAVDWWGLGVLLYEML-VGESPFPGDDEEEVFDSIVND-EVRYPRFL 844
Cdd:cd05047 158 LSRGQEVYVKKTMGRLPV-RWMAIESLNYSVYTTNSDVWSYGVLLWEIVsLGGTPYCGMTCAELYEKLPQGyRLEKPLNC 236
                       250
                ....*....|....*....
gi 47132591 845 SAEAIGIMRRLLRRNPERR 863
Cdd:cd05047 237 DDEVYDLMRQCWREKPYER 255
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
618-868 7.97e-13

Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GCN2 (or EIF2AK4) is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. Its kinase domain is activated via conformational changes as a result of the binding of uncharged tRNA to the HisRS-like domain. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 69.71  E-value: 7.97e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 618 LEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKkgdIVARDEVESlmcekRILAAVT---SAGHPFLVNLFGCFqTP 694
Cdd:cd14046   5 LTDFEELQVLGKGAFGQVVKVRNKLDGRYYAIKKIK---LRSESKNNS-----RILREVMllsRLNHQHVVRYYQAW-IE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 695 EHVCFV-MEYSAGGDLMLHIHSDVFSEPRAIF-YSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGM 772
Cdd:cd14046  76 RANLYIqMEYCEKSTLRDLIDSGLFQDTDRLWrLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLATSNK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 773 ------------------GYGDRTSTFCGTPEFLAPEVLTDT--SYTRAVDWWGLGVLLYEMLVgesPF-PGDDEEEVFD 831
Cdd:cd14046 156 lnvelatqdinkstsaalGSSGDLTGNVGTALYVAPEVQSGTksTYNEKVDMYSLGIIFFEMCY---PFsTGMERVQILT 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 47132591 832 SIVNDEVRYP----RFLSAEAIGIMRRLLRRNPERRLGSSE 868
Cdd:cd14046 233 ALRSVSIEFPpdfdDNKHSKQAKLIRWLLNHDPAKRPSAQE 273
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
621-880 9.59e-13

Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MOK, also called Renal tumor antigen 1 (RAGE-1), is widely expressed and is enriched in testis, kidney, lung, and brain. It is expressed in approximately 50% of renal cell carcinomas (RCC) and is a potential target for immunotherapy. MOK is stabilized by its association with the HSP90 molecular chaperone. It is induced by the transcription factor Cdx2 and may be involved in regulating intestinal epithelial development and differentiation. The MOK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 69.61  E-value: 9.59e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKgDIVARDEVESLmceKRILAAVTSAGHPFLVNLFGCF--QTPEHVC 698
Cdd:cd07831   1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKCMKK-HFKSLEQVNNL---REIQALRRLSPHPNILRLIEVLfdRKTGRLA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEysaggdLM-------LHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEgYVKIADFGLCKeg 771
Cdd:cd07831  77 LVFE------LMdmnlyelIKGRKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDD-ILKLADFGSCR-- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 772 mgygdrtSTFCGTP--EFL------APE-VLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVN------- 835
Cdd:cd07831 148 -------GIYSKPPytEYIstrwyrAPEcLLTDGYYGPKMDIWAVGCVFFEILSLFPLFPGTNELDQIAKIHDvlgtpda 220
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47132591 836 --DEVRYPRF--------------------LSAEAIGIMRRLLRRNPERRLGSSErdaedVKKQPFF 880
Cdd:cd07831 221 evLKKFRKSRhmnynfpskkgtglrkllpnASAEGLDLLKKLLAYDPDERITAKQ-----ALRHPYF 282
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
627-863 9.99e-13

Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, and Yes. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, and Lyn show a limited expression pattern. The Src-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 68.85  E-value: 9.99e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELfAIKALKKGDIvardEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd05034   3 LGAGQFGEVWMGVWNGTTKV-AVKTLKPGTM----SPEAFLQEAQIMKKLR---HDKLVQLYAVCSDEEPIYIVTELMSK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLMLHIHSD---VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK--EGMGYGDRTST- 780
Cdd:cd05034  75 GSLLDYLRTGegrALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLARliEDDEYTAREGAk 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 781 FcgtP-EFLAPEVLTDTSYTRAVDWWGLGVLLYEMLV-GESPFPGDDEEEVFDSIvndEVRY----PRFLSAEAIGIMRR 854
Cdd:cd05034 155 F---PiKWTAPEAALYGRFTIKSDVWSFGILLYEIVTyGRVPYPGMTNREVLEQV---ERGYrmpkPPGCPDELYDIMLQ 228

                ....*....
gi 47132591 855 LLRRNPERR 863
Cdd:cd05034 229 CWKKEPEER 237
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
621-834 1.12e-12

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase; Protein Kinases (PKs), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK) subfamily, catalytic (c) domain. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. The DYRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein S/T PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. Vertebrates contain multiple DYRKs (DYRK1-4) and mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A is involved in neuronal differentiation and is implicated in the pathogenesis of DS (Down syndrome). DYRK1B plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRK2 promotes apoptosis in response to DNA damage by phosphorylating the tumor suppressor p53, while DYRK3 promotes cell survival by phosphorylating SIRT1 and promoting p53 deacetylation. DYRK4 is a testis-specific kinase that may function during spermiogenesis.


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 69.88  E-value: 1.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALkkgdivaRDEVESLM---CEKRILAAVTSAG---HPFLVNLFGCFQTP 694
Cdd:cd14210  15 YEVLSVLGKGSFGQVVKCLDHKTGQLVAIKII-------RNKKRFHQqalVEVKILKHLNDNDpddKHNIVRYKDSFIFR 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 695 EHVCFVMEYsAGGDLMLHIHSDVF-----SEPRAIFYSACVvlGLQFLHEHKIVY----------RDLKLDNllldtegy 759
Cdd:cd14210  88 GHLCIVFEL-LSINLYELLKSNNFqglslSLIRKFAKQILQ--ALQFLHKLNIIHcdlkpenillKQPSKSS-------- 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47132591 760 VKIADFGL-CKEG-MGYGDRTSTFcgtpeFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIV 834
Cdd:cd14210 157 IKVIDFGSsCFEGeKVYTYIQSRF-----YRAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFPGENEEEQLACIM 228
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
627-862 1.22e-12

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated Kinase-1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAK1 is also known as mitogen-activated protein kinase kinase kinase 7 (MAPKKK7 or MAP3K7), TAK, or MEKK7. As a MAPKKK, it is an important mediator of cellular responses to extracellular signals. It regulates both the c-Jun N-terminal kinase and p38 MAPK cascades by activating the MAPK kinases, MKK4 and MKK3/6. In addition, TAK1 plays diverse roles in immunity and development, in different biological contexts, through many signaling pathways including TGFbeta/BMP, Wnt/Fz, and NF-kB. It is also implicated in the activation of the tumor suppressor kinase, LKB1. The TAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 69.00  E-value: 1.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRpsGELFAIKAlkkgdIVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd14058   1 VGRGSFGVVCKARWR--NQIVAVKI-----IESESEKKAFEVEVRQLSRVD---HPNIIKLYGACSNQKPVCLVMEYAEG 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLMLHIHSDvfsEPRAIFYSACVV-------LGLQFLHEHK---IVYRDLKLDNLLLDTEGYV-KIADFGLCKEGMGYg 775
Cdd:cd14058  71 GSLYNVLHGK---EPKPIYTAAHAMswalqcaKGVAYLHSMKpkaLIHRDLKPPNLLLTNGGTVlKICDFGTACDISTH- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 776 drTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFpgddeeevfdsivnDEVRYPRFLSAEAIGIMRR- 854
Cdd:cd14058 147 --MTNNKGSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPF--------------DHIGGPAFRIMWAVHNGERp 210

                ....*....
gi 47132591 855 -LLRRNPER 862
Cdd:cd14058 211 pLIKNCPKP 219
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
616-833 1.29e-12

Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Chk is also referred to as megakaryocyte-associated tyrosine kinase (Matk). Chk inhibits Src kinases using a noncatalytic mechanism by simply binding to them. As a negative regulator of Src kinases, Chk may play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Chk is expressed in brain and hematopoietic cells. Like Csk, it is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases that are anchored to the plasma membrane, Chk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Studies in mice reveal that Chk is not functionally redundant with Csk and that it plays an important role as a regulator of immune responses. Chk also plays a role in neural differentiation in a manner independent of Src by enhancing Mapk activation via Ras-mediated signaling. The Chk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 68.75  E-value: 1.29e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 616 LTLEDFKFLAVLGRGHFGKVLLSEFrpSGELFAIKALKkGDIVARDEVESLmcekrilAAVTSAGHPFLVNLFGCFqTPE 695
Cdd:cd05083   3 LNLQKLTLGEIIGEGEFGAVLQGEY--MGQKVAVKNIK-CDVTAQAFLEET-------AVMTKLQHKNLVRLLGVI-LHN 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 696 HVCFVMEYSAGGDLMLHIHS---DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGM 772
Cdd:cd05083  72 GLYIVMELMSKGNLVNFLRSrgrALVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAKVGS 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47132591 773 GYGDRTSTfcgTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEML-VGESPFPGDDEEEVFDSI 833
Cdd:cd05083 152 MGVDNSRL---PVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFsYGRAPYPKMSVKEVKEAV 210
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
627-863 1.32e-12

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Kalirin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kalirin, also called Duo or Duet, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. As a GEF, it activates Rac1, RhoA, and RhoG. It is highly expressed in neurons and is required for spine formation. The kalirin gene produces at least 10 isoforms from alternative promoter use and splicing. Of the major isoforms (Kalirin-7, -9, and -12), only kalirin-12 contains the C-terminal kinase domain. Kalirin-12 is highly expressed during embryonic development and it plays an important role in axon outgrowth. The Kalirin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 68.83  E-value: 1.32e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKgdivARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd14115   1 IGRGRFSIVKKCLHKATRKDVAVKFVSK----KMKKKEQAAHEAALLQHLQ---HPQYITLHDTYESPTSYILVLELMDD 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLMLH-IHSDVFSEPRAIFYSACVVLGLQFLHEHKIVY---RDLKLDNLLLDTEGYVKIADFGLCKEGMGYgDRTSTFC 782
Cdd:cd14115  74 GRLLDYlMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHldiKPENLLIDLRIPVPRVKLIDLEDAVQISGH-RHVHHLL 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 783 GTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPR--F--LSAEAIGIMRRLLRR 858
Cdd:cd14115 153 GNPEFAAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPDeyFgdVSQAARDFINVILQE 232

                ....*
gi 47132591 859 NPERR 863
Cdd:cd14115 233 DPRRR 237
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
627-831 1.43e-12

Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Axl is widely expressed in a variety of organs and cells including epithelial, mesenchymal, hematopoietic, as well as non-transformed cells. It is important in many cellular functions such as survival, anti-apoptosis, proliferation, migration, and adhesion. Axl was originally isolated from patients with chronic myelogenous leukemia and a chronic myeloproliferative disorder. It is overexpressed in many human cancers including colon, squamous cell, thyroid, breast, and lung carcinomas. Axl is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to its ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Axl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 69.27  E-value: 1.43e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELF--AIKALKKGdIVARDEVESLMCEKrilAAVTSAGHPFLVNLFG-CFQTPEHVCF---- 699
Cdd:cd05075   8 LGEGEFGSVMEGQLNQDDSVLkvAVKTMKIA-ICTRSEMEDFLSEA---VCMKEFDHPNVMRLIGvCLQNTESEGYpspv 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 -VMEYSAGGDLMLHI-HSDVFSEP------RAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEg 771
Cdd:cd05075  84 vILPFMKHGDLHSFLlYSRLGDCPvylptqMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADFGLSKK- 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47132591 772 MGYGD--RTSTFCGTP-EFLAPEVLTDTSYTRAVDWWGLGVLLYEMLV-GESPFPGDDEEEVFD 831
Cdd:cd05075 163 IYNGDyyRQGRISKMPvKWIAIESLADRVYTTKSDVWSFGVTMWEIATrGQTPYPGVENSEIYD 226
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
627-815 1.47e-12

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 69.19  E-value: 1.47e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRP----SGELFAIKALKKGDivARDEVESLMCEKRILAAVTsagHPFLVNLFG-CFQTPEH-VCFV 700
Cdd:cd05079  12 LGEGHFGKVELCRYDPegdnTGEQVAVKSLKPES--GGNHIADLKKEIEILRNLY---HENIVKYKGiCTEDGGNgIKLI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGGDLMLHIHSDV--FSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK---EGMGY- 774
Cdd:cd05079  87 MEFLPSGSLKEYLPRNKnkINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKaieTDKEYy 166
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 47132591 775 ---GDRTStfcgtPEF-LAPEVLTDTSYTRAVDWWGLGVLLYEML 815
Cdd:cd05079 167 tvkDDLDS-----PVFwYAPECLIQSKFYIASDVWSFGVTLYELL 206
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
621-826 1.48e-12

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. CDK2, together with CDK4, also regulates embryonic cell proliferation. Despite these important roles, mice deleted for the cdk2 gene are viable and normal except for being sterile. This may be due to compensation provided by CDK1 (also called Cdc2), which can also bind cyclin E and drive the G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 69.07  E-value: 1.48e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAikaLKKgdIVARDEVESLMCEK-RILAAVTSAGHPFLVNLFGCFQTPEHVCF 699
Cdd:cd07860   2 FQKVEKIGEGTYGVVYKARNKLTGEVVA---LKK--IRLDTETEGVPSTAiREISLLKELNHPNIVKLLDVIHTENKLYL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYsAGGDLMLHIHSDVFSE-PRAIFYSACVVL--GLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKeGMGYGD 776
Cdd:cd07860  77 VFEF-LHQDLKKFMDASALTGiPLPLIKSYLFQLlqGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLAR-AFGVPV 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 47132591 777 RTSTF-CGTPEFLAPEVLTDTS-YTRAVDWWGLGVLLYEMLVGESPFPGDDE 826
Cdd:cd07860 155 RTYTHeVVTLWYRAPEILLGCKyYSTAVDIWSLGCIFAEMVTRRALFPGDSE 206
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
621-883 1.54e-12

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Typical MAPK pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPK kinase (MAP2K or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAP3K or MKKK). Each cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. There are three typical MAPK subfamilies: Extracellular signal-Regulated Kinase (ERK), c-Jun N-terminal Kinase (JNK), and p38. Some MAPKs are atypical in that they are not regulated by MAP2Ks. These include MAPK4, MAPK6, NLK, and ERK7. The MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 69.86  E-value: 1.54e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKgdiVARDEVESlmceKRILAAVT---SAGHPFLVNLFGCFQTPEHV 697
Cdd:cd07834   2 YELLKPIGSGAYGVVCSAYDKRTGRKVAIKKISN---VFDDLIDA----KRILREIKilrHLKHENIIGLLDILRPPSPE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 698 CF-----VMEysaggdLM---LH--IHSDVFSEPRAIFYSACVVL-GLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFG 766
Cdd:cd07834  75 EFndvyiVTE------LMetdLHkvIKSPQPLTDDHIQYFLYQILrGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFG 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 767 LCKEGMGYGDrtstfcgtPEFL----------APEV-LTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDD---------- 825
Cdd:cd07834 149 LARGVDPDED--------KGFLteyvvtrwyrAPELlLSSKKYTKAIDIWSVGCIFAELLTRKPLFPGRDyidqlnlive 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 826 -----EEEVFDSIVNDEVRypRFL------------------SAEAIGIMRRLLRRNPERRLgsserDAEDVKKQPFFRT 882
Cdd:cd07834 221 vlgtpSEEDLKFISSEKAR--NYLkslpkkpkkplsevfpgaSPEAIDLLEKMLVFNPKKRI-----TADEALAHPYLAQ 293

                .
gi 47132591 883 L 883
Cdd:cd07834 294 L 294
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
627-864 1.58e-12

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkA is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkA to its ligand, nerve growth factor (NGF), results in receptor oligomerization and activation of the catalytic domain. TrkA is expressed mainly in neural-crest-derived sensory and sympathetic neurons of the peripheral nervous system, and in basal forebrain cholinergic neurons of the central nervous system. It is critical for neuronal growth, differentiation and survival. Alternative TrkA splicing has been implicated as a pivotal regulator of neuroblastoma (NB) behavior. Normal TrkA expression is associated with better NB prognosis, while the hypoxia-regulated TrkAIII splice variant promotes NB pathogenesis and progression. Aberrant TrkA expression has also been demonstrated in non-neural tumors including prostate, breast, lung, and pancreatic cancers. The TrkA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 69.22  E-value: 1.58e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFR---PSGE--LFAIKALKKGDIVARDEVESlmcEKRILaavTSAGHPFLVNLFGCFQTPEHVCFVM 701
Cdd:cd05092  13 LGEGAFGKVFLAECHnllPEQDkmLVAVKALKEATESARQDFQR---EAELL---TVLQHQHIVRFYGVCTEGEPLIMVF 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 702 EYSAGGDL--MLHIH---SDVFSE-----------PRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADF 765
Cdd:cd05092  87 EYMRHGDLnrFLRSHgpdAKILDGgegqapgqltlGQMLQIASQIASGMVYLASLHFVHRDLATRNCLVGQGLVVKIGDF 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 766 GLCKE--GMGY---GDRTStfcgTP-EFLAPEVLTDTSYTRAVDWWGLGVLLYEMLV-GESPFPGDDEEEVFDSIVND-E 837
Cdd:cd05092 167 GMSRDiySTDYyrvGGRTM----LPiRWMPPESILYRKFTTESDIWSFGVVLWEIFTyGKQPWYQLSNTEAIECITQGrE 242
                       250       260
                ....*....|....*....|....*..
gi 47132591 838 VRYPRFLSAEAIGIMRRLLRRNPERRL 864
Cdd:cd05092 243 LERPRTCPPEVYAIMQGCWQREPQQRH 269
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
619-880 1.70e-12

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L1, also called PITSLRE, exists in different isoforms which are named using the alias CDK11(p). The CDC2L1 gene produces two protein products, CDK11(p110) and CDK11(p58). CDC2L1 is also represented by the caspase-processed CDK11(p46). CDK11(p110), the major isoform, associates with cyclin L and is expressed throughout the cell cycle. It is involved in RNA processing and the regulation of transcription. CDK11(p58) associates with cyclin D3 and is expressed during the G2/M phase of the cell cycle. It plays roles in spindle morphogenesis, centrosome maturation, sister chromatid cohesion, and the completion of mitosis. CDK11(p46) is formed from the larger isoforms by caspases during TNFalpha- and Fas-induced apoptosis. It functions as a downstream effector kinase in apoptotic signaling pathways and interacts with eukaryotic initiation factor 3f (eIF3f), p21-activated kinase (PAK1), and Ran-binding protein (RanBPM). CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 69.18  E-value: 1.70e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALK---KGD---IVARDEVESLMcekrilaavtSAGHPFLVNL----F 688
Cdd:cd07843   5 DEYEKLNRIEEGTYGVVYRARDKKTGEIVALKKLKmekEKEgfpITSLREINILL----------KLQHPNIVTVkevvV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 689 GcfQTPEHVCFVMEYSAGG--DLMlhihsDVFSEPRAIFYSACVVL----GLQFLHEHKIVYRDLKLDNLLLDTEGYVKI 762
Cdd:cd07843  75 G--SNLDKIYMVMEYVEHDlkSLM-----ETMKQPFLQSEVKCLMLqllsGVAHLHDNWILHRDLKTSNLLLNNRGILKI 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 763 ADFGLCKEgmgYGDRTSTFcgTPE-----FLAPEVLTDTS-YTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVN- 835
Cdd:cd07843 148 CDFGLARE---YGSPLKPY--TQLvvtlwYRAPELLLGAKeYSTAIDMWSVGCIFAELLTKKPLFPGKSEIDQLNKIFKl 222
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47132591 836 ----DEVRYPRF---------------------------LSAEAIGIMRRLLRRNPERRLgsserDAEDVKKQPFF 880
Cdd:cd07843 223 lgtpTEKIWPGFselpgakkktftkypynqlrkkfpalsLSDNGFDLLNRLLTYDPAKRI-----SAEDALKHPYF 293
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
627-880 1.79e-12

Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 68.39  E-value: 1.79e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKAlkkgdIVARDEVESlmCEKRILAAVTSAGHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd14108  10 IGRGAFSYLRRVKEKSSDLSFAAKF-----IPVRAKKKT--SARRELALLAELDHKSIVRFHDAFEKRRVVIIVTELCHE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 gDLMLHIH---SDVFSEPRAIFYSacVVLGLQFLHEHKIVYRDLKLDNLLLDTEG--YVKIADFGLCKEgMGYGDRTSTF 781
Cdd:cd14108  83 -ELLERITkrpTVCESEVRSYMRQ--LLEGIEYLHQNDVLHLDLKPENLLMADQKtdQVRICDFGNAQE-LTPNEPQYCK 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 782 CGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYP----RFLSAEAIGIMRRLLR 857
Cdd:cd14108 159 YGTPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNIRNYNVAFEesmfKDLCREAKGFIIKVLV 238
                       250       260
                ....*....|....*....|...
gi 47132591 858 RNPERrlgsseRDAEDVKKQPFF 880
Cdd:cd14108 239 SDRLR------PDAEETLEHPWF 255
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
616-863 1.89e-12

Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie2 is a receptor PTK (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie2 is expressed mainly in endothelial cells and hematopoietic stem cells. It is also found in a subset of tumor-associated monocytes and eosinophils. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. Tie2 signaling plays key regulatory roles in vascular integrity and quiescence, and in inflammation. The Tie2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 69.26  E-value: 1.89e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 616 LTLEDFKFLAVLGRGHFGKVLLSEFRPSGELF--AIKALKkgDIVARDEVESLMCEKRILAAVtsAGHPFLVNLFGCFQT 693
Cdd:cd05088   4 LEWNDIKFQDVIGEGNFGQVLKARIKKDGLRMdaAIKRMK--EYASKDDHRDFAGELEVLCKL--GHHPNIINLLGACEH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 694 PEHVCFVMEYSAGGDLM-----------------LHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDT 756
Cdd:cd05088  80 RGYLYLAIEYAPHGNLLdflrksrvletdpafaiANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 757 EGYVKIADFGLCKEGMGYGDRTSTFCGTpEFLAPEVLTDTSYTRAVDWWGLGVLLYEML-VGESPFPGDDEEEVFDSI-V 834
Cdd:cd05088 160 NYVAKIADFGLSRGQEVYVKKTMGRLPV-RWMAIESLNYSVYTTNSDVWSYGVLLWEIVsLGGTPYCGMTCAELYEKLpQ 238
                       250       260
                ....*....|....*....|....*....
gi 47132591 835 NDEVRYPRFLSAEAIGIMRRLLRRNPERR 863
Cdd:cd05088 239 GYRLEKPLNCDDEVYDLMRQCWREKPYER 267
HR1 cd00089
Protein kinase C-related kinase homology region 1 (HR1) domain that binds Rho family small ...
52-104 1.93e-12

Protein kinase C-related kinase homology region 1 (HR1) domain that binds Rho family small GTPases; The HR1 domain, also called the ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. It is found in Rho effector proteins including PKC-related kinases such as vertebrate PRK1 (or PKN) and yeast PKC1 protein kinases C, as well as in rhophilins and Rho-associated kinase (ROCK). Rho family members function as molecular switches, cycling between inactive and active forms, controlling a variety of cellular processes. HR1 domains may occur in repeat arrangements (PKN contains three HR1 domains), separated by a short linker region.


Pssm-ID: 212008 [Multi-domain]  Cd Length: 68  Bit Score: 63.11  E-value: 1.93e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 47132591  52 IRKELKLKEGAENLRRATTDLG--RSLGPVELLLRGSSRRLDLLHQQLQELHAHV 104
Cdd:cd00089  14 LEKELKIREGAENLLKLYSNPKvkKDLAEVQLNLKESKEKIDLLKRQLERYNALV 68
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
616-863 2.08e-12

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 68.88  E-value: 2.08e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 616 LTLEDFKFLAVLGRGHFGKVLLSEFRPSG----ELFAIKALKkgDIVARDEVESLMCEKRILAAVTsagHPFLVNLFGCF 691
Cdd:cd05090   2 LPLSAVRFMEELGECAFGKIYKGHLYLPGmdhaQLVAIKTLK--DYNNPQQWNEFQQEASLMTELH---HPNIVCLLGVV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 692 QTPEHVCFVMEYSAGGDL-----MLHIHSDV--FSEPRAIFYSAC-----------VVLGLQFLHEHKIVYRDLKLDNLL 753
Cdd:cd05090  77 TQEQPVCMLFEFMNQGDLhefliMRSPHSDVgcSSDEDGTVKSSLdhgdflhiaiqIAAGMEYLSSHFFVHKDLAARNIL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 754 LDTEGYVKIADFGLCKEGMGygdrTSTFCGTPE------FLAPEVLTDTSYTRAVDWWGLGVLLYEML-VGESPFPGDDE 826
Cdd:cd05090 157 VGEQLHVKISDLGLSREIYS----SDYYRVQNKsllpirWMPPEAIMYGKFSSDSDIWSFGVVLWEIFsFGLQPYYGFSN 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 47132591 827 EEVFDSIVNDEVR------YPRFLsaeaiGIMRRLLRRNPERR 863
Cdd:cd05090 233 QEVIEMVRKRQLLpcsedcPPRMY-----SLMTECWQEIPSRR 270
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
626-863 2.45e-12

Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. Vertebrates contain two members, LRRK1 and LRRK2, which show complementary expression in the brain. Mutations in LRRK2 are linked to both familial and sporadic forms of Parkinson's disease. The normal roles of LRRKs are not clearly defined. They may be involved in mitogen-activated protein kinase (MAPK) pathways, protein translation control, programmed cell death pathways, and cytoskeletal dynamics. The LRRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 68.41  E-value: 2.45e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRpsGELFAIKALKKGDIVARDEVESLM--------------CEKRILAAVTSA-GHPFLVNLFGC 690
Cdd:cd14000   1 LLGDGGFGSVYRASYK--GEPVAVKIFNKHTSSNFANVPADTmlrhlratdamknfRLLRQELTVLSHlHHPSIVYLLGI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 691 FQTPehVCFVMEYSAGGDL---MLHIHSDVFSEPRAIFYSAC--VVLGLQFLHEHKIVYRDLKLD-----NLLLDTEGYV 760
Cdd:cd14000  79 GIHP--LMLVLELAPLGSLdhlLQQDSRSFASLGRTLQQRIAlqVADGLRYLHSAMIIYRDLKSHnvlvwTLYPNSAIII 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 761 KIADFGLCKEGMGYGDRTSTfcGTPEFLAPEVLT-DTSYTRAVDWWGLGVLLYEMLVGESPFPG--------DDEEEVFD 831
Cdd:cd14000 157 KIADYGISRQCCRMGAKGSE--GTPGFRAPEIARgNVIYNEKVDVFSFGMLLYEILSGGAPMVGhlkfpnefDIHGGLRP 234
                       250       260       270
                ....*....|....*....|....*....|..
gi 47132591 832 SIVNDEVRYPRFLSAeaigIMRRLLRRNPERR 863
Cdd:cd14000 235 PLKQYECAPWPEVEV----LMKKCWKENPQQR 262
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
695-868 2.79e-12

Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB3 binds and regulates ATF4, p65/RelA, and PKB (or Akt). It negatively regulates ATF4-mediated gene expression including that of CHOP (C/EBP homologous protein) and HO-1, which are both involved in modulating apoptosis. It also inhibits insulin-mediated phosphorylation of PKB and is a possible determinant of insulin resistance and related disorders. In osteoarthritic chondrocytes where it inhibits insulin-like growth factor 1-mediated cell survival, TRB3 is overexpressed, resulting in increased cell death. TRB3 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB3 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 67.60  E-value: 2.79e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 695 EHVCFVMEYSAG------------GDLMLHIHS-DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVK 761
Cdd:cd14024  45 EGVCSVLEVVIGqdrayaffsrhyGDMHSHVRRrRRLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELRTK 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 762 IADFGL--CKEGMGYGDRTSTFCGTPEFLAPEVLTD-TSYT-RAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDE 837
Cdd:cd14024 125 LVLVNLedSCPLNGDDDSLTDKHGCPAYVGPEILSSrRSYSgKAADVWSLGVCLYTMLLGRYPFQDTEPAALFAKIRRGA 204
                       170       180       190
                ....*....|....*....|....*....|.
gi 47132591 838 VRYPRFLSAEAIGIMRRLLRRNPERRLGSSE 868
Cdd:cd14024 205 FSLPAWLSPGARCLVSCMLRRSPAERLKASE 235
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
627-863 2.91e-12

Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes Ack1, thirty-eight-negative kinase 1 (Tnk1), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal catalytic domain, an SH3 domain, a Cdc42-binding CRIB domain, and a proline-rich region. They are mainly expressed in brain and skeletal tissues and are involved in the regulation of cell adhesion and growth, receptor degradation, and axonal guidance. Ack1 is also associated with androgen-independent prostate cancer progression. Tnk1 regulates TNFalpha signaling and may play an important role in cell death. The Ack-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 67.75  E-value: 2.91e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFR-PSGELF--AIKALKKGDIVARDEVESLMCEkriLAAVTSAGHPFLVNLFGCFQTPEhVCFVMEY 703
Cdd:cd05040   3 LGDGSFGVVRRGEWTtPSGKVIqvAVKCLKSDVLSQPNAMDDFLKE---VNAMHSLDHPNLIRLYGVVLSSP-LMMVTEL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 704 SAGGDLM--LHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKeGMGYGDR--TS 779
Cdd:cd05040  79 APLGSLLdrLRKDQGHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLMR-ALPQNEDhyVM 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 780 TF--------CgtpeflAPEVLTDTSYTRAVDWWGLGVLLYEMLV-GESPFPGDDEEEVFDSIVNDEVRYPR--FLSAEA 848
Cdd:cd05040 158 QEhrkvpfawC------APESLKTRKFSHASDVWMFGVTLWEMFTyGEEPWLGLNGSQILEKIDKEGERLERpdDCPQDI 231
                       250
                ....*....|....*
gi 47132591 849 IGIMRRLLRRNPERR 863
Cdd:cd05040 232 YNVMLQCWAHKPADR 246
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
618-884 2.97e-12

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 68.87  E-value: 2.97e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 618 LEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKkgdivaRDEVESLMCEK-RILAAVTSAGHPFLVNLFGCFQTPEH 696
Cdd:cd07872   5 METYIKLEKLGEGTYATVFKGRSKLTENLVALKEIR------LEHEEGAPCTAiREVSLLKDLKHANIVTLHDIVHTDKS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 697 VCFVMEYsAGGDLMLHIHS--DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGY 774
Cdd:cd07872  79 LTLVFEY-LDKDLKQYMDDcgNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSVP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 775 GDRTSTFCGTPEFLAPEVLTDTS-YTRAVDWWGLGVLLYEMLVGESPFPG---DDE------------EEVFDSI-VNDE 837
Cdd:cd07872 158 TKTYSNEVVTLWYRPPDVLLGSSeYSTQIDMWGVGCIFFEMASGRPLFPGstvEDElhlifrllgtptEETWPGIsSNDE 237
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47132591 838 VR---YPRF-----------LSAEAIGIMRRLLRRNPERRLgsserDAEDVKKQPFFRTLG 884
Cdd:cd07872 238 FKnynFPKYkpqplinhaprLDTEGIELLTKFLQYESKKRI-----SAEEAMKHAYFRSLG 293
Pkinase_C pfam00433
Protein kinase C terminal domain;
901-943 4.20e-12

Protein kinase C terminal domain;


Pssm-ID: 459809 [Multi-domain]  Cd Length: 42  Bit Score: 61.45  E-value: 4.20e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 47132591   901 LSGRTDVSNFDEEFTGEAPTLSPPrDARPLTAAEQAAFLDFDF 943
Cdd:pfam00433   1 VKSETDTSNFDPEFTEEPPVLTPP-DSSILSSNDQEEFRGFSY 42
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
626-863 4.62e-12

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are three PIM2 isoforms resulting from alternative translation initiation sites. PIM2 is highly expressed in leukemia and lymphomas and has been shown to promote the survival and proliferation of tumor cells. The PIM2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 67.18  E-value: 4.62e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGELFAIKalkkgdIVARDEVE-------SLMC--EKRILAAVTS-AGHPFLVNLFGCFQTPE 695
Cdd:cd14101   7 LLGKGGFGTVYAGHRISDGLQVAIK------QISRNRVQqwsklpgVNPVpnEVALLQSVGGgPGHRGVIRLLDWFEIPE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 696 HVCFVMEYSA-GGDLMlhihsDVFSEPRAIFYSAC------VVLGLQFLHEHKIVYRDLKLDNLLLDTE-GYVKIADFG- 766
Cdd:cd14101  81 GFLLVLERPQhCQDLF-----DYITERGALDESLArrffkqVVEAVQHCHSKGVVHRDIKDENILVDLRtGDIKLIDFGs 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 767 --LCKEGMgYGDrtstFCGTPEFLAPE-VLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEeevfdsIVNDEVRYPRF 843
Cdd:cd14101 156 gaTLKDSM-YTD----FDGTRVYSPPEwILYHQYHALPATVWSLGILLYDMVCGDIPFERDTD------ILKAKPSFNKR 224
                       250       260
                ....*....|....*....|
gi 47132591 844 LSAEAIGIMRRLLRRNPERR 863
Cdd:cd14101 225 VSNDCRSLIRSCLAYNPSDR 244
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
619-897 6.56e-12

Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ERK5 (also called Big MAPK1 (BMK1) or MAPK7) has a unique C-terminal extension, making it approximately twice as big as other MAPKs. This extension contains transcriptional activation capability which is inhibited by the N-terminal half. ERK5 is activated in response to growth factors and stress by a cascade that leads to its phosphorylation by the MAP2K MEK5, which in turn is regulated by the MAP3Ks MEKK2 and MEKK3. Activated ERK5 phosphorylates its targets including myocyte enhancer factor 2 (MEF2), Sap1a, c-Myc, and RSK. It plays a role in EGF-induced cell proliferation during the G1/S phase transition. Studies on knockout mice revealed that ERK5 is essential for cardiovascular development and plays an important role in angiogenesis. It is also critical for neural differentiation and survival. The ERK5 pathway has been implicated in the pathogenesis of many diseases including cancer, cardiac hypertrophy, and atherosclerosis. MAPKs are important mediators of cellular responses to extracellular signals. The ERK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 67.78  E-value: 6.56e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKgdivARDEVESLMCEKRILAAVTSAGHPFLVNLFGCFQTPE--- 695
Cdd:cd07855   5 DRYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIPN----AFDVVTTAKRTLRELKILRHFKHDNIIAIRDILRPKVpya 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 696 ---HVCFVMeysaggDLM---LH--IHSDV-FSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFG 766
Cdd:cd07855  81 dfkDVYVVL------DLMesdLHhiIHSDQpLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 767 LCKEGMGYGDRTSTF----CGTPEFLAPEV-LTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDD---------------E 826
Cdd:cd07855 155 MARGLCTSPEEHKYFmteyVATRWYRAPELmLSLPEYTQAIDMWSVGCIFAEMLGRRQLFPGKNyvhqlqliltvlgtpS 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 827 EEVFDSIVNDEVR-----------------YPRfLSAEAIGIMRRLLRRNPERRLgsserDAEDVKKQPFFRTLgWEALL 889
Cdd:cd07855 235 QAVINAIGADRVRryiqnlpnkqpvpwetlYPK-ADQQALDLLSQMLRFDPSERI-----TVAEALQHPFLAKY-HDPDD 307

                ....*...
gi 47132591 890 ARRLPPPF 897
Cdd:cd07855 308 EPDCAPPF 315
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
627-849 7.45e-12

Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The STK_BAK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 66.75  E-value: 7.45e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFrPSGELFAIKALKKGDIVARDEVESlmcekRILAAVTSAGHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd14664   1 IGRGGAGTVYKGVM-PNGTLVAVKRLKGEGTQGGDHGFQ-----AEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLMLHIHSDVFSEP--------RAIFYSAcvvLGLQFLHEH---KIVYRDLKLDNLLLDTEGYVKIADFGLCKEgMGYG 775
Cdd:cd14664  75 GSLGELLHSRPESQPpldwetrqRIALGSA---RGLAYLHHDcspLIIHRDVKSNNILLDEEFEAHVADFGLAKL-MDDK 150
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47132591 776 DR--TSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFpgdDEEEVFDSivNDEVRYPRFLSAEAI 849
Cdd:cd14664 151 DShvMSSVAGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRPF---DEAFLDDG--VDIVDWVRGLLEEKK 221
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
626-863 7.81e-12

Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyro3 (or Sky) is predominantly expressed in the central nervous system and the brain, and functions as a neurotrophic factor. It is also expressed in osteoclasts and has a role in bone resorption. Tyro3 is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Tyro3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 66.86  E-value: 7.81e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKV---LLSEFRPSGELFAIKALKkGDIVARDEVESLMCEKrilAAVTSAGHPFLVNLFGC---------FQT 693
Cdd:cd05074  16 MLGKGEFGSVreaQLKSEDGSFQKVAVKMLK-ADIFSSSDIEEFLREA---ACMKEFDHPNVIKLIGVslrsrakgrLPI 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 694 PEHVCFVMEYsagGDL-----MLHIHSDVFSEPRAIF--YSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFG 766
Cdd:cd05074  92 PMVILPFMKH---GDLhtfllMSRIGEEPFTLPLQTLvrFMIDIASGMEYLSSKNFIHRDLAARNCMLNENMTVCVADFG 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 767 LCKEgMGYGDRTSTFCGTP---EFLAPEVLTDTSYTRAVDWWGLGVLLYE-MLVGESPFPGDDEEEVFDSIVNDE-VRYP 841
Cdd:cd05074 169 LSKK-IYSGDYYRQGCASKlpvKWLALESLADNVYTTHSDVWAFGVTMWEiMTRGQTPYAGVENSEIYNYLIKGNrLKQP 247
                       250       260
                ....*....|....*....|..
gi 47132591 842 RFLSAEAIGIMRRLLRRNPERR 863
Cdd:cd05074 248 PDCLEDVYELMCQCWSPEPKCR 269
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
621-868 7.92e-12

Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They function in the regulation of the cell cycle, cell development, cell differentiation, senescence, tumorigenesis, apoptosis, pain development and pain progression, and immune responses. p38 kinases are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. p38 substrates include other protein kinases and factors that regulate transcription, nuclear export, mRNA stability and translation. p38 kinases are drug targets for the inflammatory diseases psoriasis, rheumatoid arthritis, and chronic pulmonary disease. Vertebrates contain four isoforms of p38, named alpha, beta, gamma, and delta, which show varying substrate specificity and expression patterns. p38alpha and p38beta are ubiquitously expressed, p38gamma is predominantly found in skeletal muscle, and p38delta is found in the heart, lung, testis, pancreas, and small intestine. The p38 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 67.70  E-value: 7.92e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALkkgdivaRDEVESLMCEKRI---LAAVTSAGHPFLVNLFGCFQTPEH- 696
Cdd:cd07851  17 YQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKL-------SRPFQSAIHAKRTyreLRLLKHMKHENVIGLLDVFTPASSl 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 697 -----VCFVMEYsAGGDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLC--- 768
Cdd:cd07851  90 edfqdVYLVTHL-MGADLNNIVKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLArht 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 769 -KEGMGYgdrtstfCGTPEFLAPEV-LTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDD---------------EEEVFD 831
Cdd:cd07851 169 dDEMTGY-------VATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLTGKTLFPGSDhidqlkrimnlvgtpDEELLK 241
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 47132591 832 SIVNDEVR-----YPRF-----------LSAEAIGIMRRLLRRNPERRLGSSE 868
Cdd:cd07851 242 KISSESARnyiqsLPQMpkkdfkevfsgANPLAIDLLEKMLVLDPDKRITAAE 294
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
616-838 8.59e-12

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror2 plays important roles in skeletal and heart formation. Ror2-deficient mice show widespread bone abnormalities, ventricular defects in the heart, and respiratory dysfunction. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Ror2 is also implicated in neural development. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 66.97  E-value: 8.59e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 616 LTLEDFKFLAVLGRGHFGKVLlsefrpSGELF-----------AIKALK-KGDIVARDEVE-SLMCEKRIlaavtsaGHP 682
Cdd:cd05091   3 INLSAVRFMEELGEDRFGKVY------KGHLFgtapgeqtqavAIKTLKdKAEGPLREEFRhEAMLRSRL-------QHP 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 683 FLVNLFGCFQTPEHVCFVMEYSAGGDL-----MLHIHSDVFS-----------EPRAIFY-SACVVLGLQFLHEHKIVYR 745
Cdd:cd05091  70 NIVCLLGVVTKEQPMSMIFSYCSHGDLheflvMRSPHSDVGStdddktvkstlEPADFLHiVTQIAAGMEYLSSHHVVHK 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 746 DLKLDNLLLDTEGYVKIADFGLCKEgMGYGDRTSTFCGTP---EFLAPEVLTDTSYTRAVDWWGLGVLLYEML-VGESPF 821
Cdd:cd05091 150 DLATRNVLVFDKLNVKISDLGLFRE-VYAADYYKLMGNSLlpiRWMSPEAIMYGKFSIDSDIWSYGVVLWEVFsYGLQPY 228
                       250
                ....*....|....*..
gi 47132591 822 PGDDEEEVFDSIVNDEV 838
Cdd:cd05091 229 CGYSNQDVIEMIRNRQV 245
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
618-828 1.00e-11

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-3 shows a restricted pattern of expression and is present in brain, kidney, and intestine. It is elevated in Alzheimer's disease (AD) and has been shown to associate with paired helical filaments (PHFs) and stimulate Tau phosphorylation. As AD progresses, phosphorylated Tau aggregates and forms PHFs, which leads to the formation of neurofibrillary tangles. In human glioma cells, PCTAIRE-3 induces cell cycle arrest and cell death. PCTAIRE-3 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 66.96  E-value: 1.00e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 618 LEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKkgdivaRDEVESLMCEK-RILAAVTSAGHPFLVNLFGCFQTPEH 696
Cdd:cd07871   4 LETYVKLDKLGEGTYATVFKGRSKLTENLVALKEIR------LEHEEGAPCTAiREVSLLKNLKHANIVTLHDIIHTERC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 697 VCFVMEYsAGGDLMLHIHS--DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEG--- 771
Cdd:cd07871  78 LTLVFEY-LDSDLKQYLDNcgNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLARAKsvp 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 47132591 772 -MGYGDRTSTFCGTPeflaPEVLT-DTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEE 828
Cdd:cd07871 157 tKTYSNEVVTLWYRP----PDVLLgSTEYSTPIDMWGVGCILYEMATGRPMFPGSTVKE 211
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
616-833 1.02e-11

Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Ror subfamily consists of Ror1, Ror2, and similar proteins. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. Ror kinases are expressed in many tissues during development. They play important roles in bone and heart formation. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Drosophila Ror is expressed only in the developing nervous system during neurite outgrowth and neuronal differentiation, suggesting a role for Drosophila Ror in neural development. More recently, mouse Ror1 and Ror2 have also been found to play an important role in regulating neurite growth in central neurons. Ror1 and Ror2 are believed to have some overlapping and redundant functions. The Ror subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 66.63  E-value: 1.02e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 616 LTLEDFKFLAVLGRGHFGKVLLSE-FRPSGE----LFAIKALKKGDIVA-----RDEVEsLMCEKRilaavtsagHPFLV 685
Cdd:cd05048   2 IPLSAVRFLEELGEGAFGKVYKGElLGPSSEesaiSVAIKTLKENASPKtqqdfRREAE-LMSDLQ---------HPNIV 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 686 NLFGCFQTPEHVCFVMEYSAGGDL-----MLHIHSDV-FSEPRAIFYSAC-----------VVLGLQFLHEHKIVYRDLK 748
Cdd:cd05048  72 CLLGVCTKEQPQCMLFEYMAHGDLheflvRHSPHSDVgVSSDDDGTASSLdqsdflhiaiqIAAGMEYLSSHHYVHRDLA 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 749 LDNLLLDTEGYVKIADFGLCKEGMGyGD--RTSTFCGTP-EFLAPEVLTDTSYTRAVDWWGLGVLLYEML-VGESPFPGD 824
Cdd:cd05048 152 ARNCLVGDGLTVKISDFGLSRDIYS-SDyyRVQSKSLLPvRWMPPEAILYGKFTTESDVWSFGVVLWEIFsYGLQPYYGY 230

                ....*....
gi 47132591 825 DEEEVFDSI 833
Cdd:cd05048 231 SNQEVIEMI 239
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
593-864 1.15e-11

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 67.54  E-value: 1.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  593 PELPSETQETPGPALCSPLRKSPLTLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDivaRDEVESLMCekRI 672
Cdd:PLN00034  48 PPPSSSSSSSSSSSASGSAPSAAKSLSELERVNRIGSGAGGTVYKVIHRPTGRLYALKVIYGNH---EDTVRRQIC--RE 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  673 LAAVTSAGHPFLVNLFGCFQTPEHVCFVMEYSAGGDLMLHihsDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNL 752
Cdd:PLN00034 123 IEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSLEGT---HIADEQFLADVARQILSGIAYLHRRHIVHRDIKPSNL 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  753 LLDTEGYVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPE-VLTDTSYTR----AVDWWGLGVLLYEMLVGESPFP----G 823
Cdd:PLN00034 200 LINSAKNVKIADFGVSRILAQTMDPCNSSVGTIAYMSPErINTDLNHGAydgyAGDIWSLGVSILEFYLGRFPFGvgrqG 279
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 47132591  824 DDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNPERRL 864
Cdd:PLN00034 280 DWASLMCAICMSQPPEAPATASREFRHFISCCLQREPAKRW 320
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
627-815 1.22e-11

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK2 activation is induced by transforming growth factor-beta l (TGFb-l) and shares the same subcellular location as the cofilin family member twinfilin, which may be its biological substrate. LIMK2 plays a role in spermatogenesis, and may contribute to tumor progression and metastasis formation in some cancer cells. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 66.12  E-value: 1.22e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKGDivaRDEVESLMCEKRILaavTSAGHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd14222   1 LGKGFFGQAIKVTHKATGKVMVMKELIRCD---EETQKTFLTEVKVM---RSLDHPNVLKFIGVLYKDKRLNLLTEFIEG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLMLHIHS-DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLC----------------- 768
Cdd:cd14222  75 GTLKDFLRAdDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSrliveekkkpppdkptt 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 47132591 769 -KEGMGYGDRTS--TFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEML 815
Cdd:cd14222 155 kKRTLRKNDRKKryTVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCEII 204
HR1 pfam02185
Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of ...
52-108 1.35e-11

Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of the N-terminal non-catalytic part of protein kinase PRK1(PKN). The first two of these repeats were later shown to bind the small G protein rho known to activate PKN in its GTP-bound form. Similar rho-binding domains also occur in a number of other protein kinases and in the rho-binding proteins rhophilin and rhotekin. Recently, the structure of the N-terminal HR1 repeat complexed with RhoA has been determined by X-ray crystallography. It forms an antiparallel coiled-coil fold termed an ACC finger.


Pssm-ID: 460478 [Multi-domain]  Cd Length: 67  Bit Score: 60.61  E-value: 1.35e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591    52 IRKELKLKEGAENLRR---ATTDLgRSLGPVELLLRGSSRRLDLLHQQLQELHAHVVLPD 108
Cdd:pfam02185   9 IEVEKKIKEGAENMLRllqATKDR-KVLAEAESELRESNRKIQLLREQLRELQARHLPSD 67
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
627-865 1.56e-11

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 65.75  E-value: 1.56e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVL--LSEFRPSGELFAIKALKK--GDIVARDEvesLMCEKRILAAVTSaghPFLVNLFGCFQTpEHVCFVME 702
Cdd:cd05116   3 LGSGNFGTVKkgYYQMKKVVKTVAVKILKNeaNDPALKDE---LLREANVMQQLDN---PYIVRMIGICEA-ESWMLVME 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 703 YSAGGDLMLHIHSDV-FSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK---EGMGYGDRT 778
Cdd:cd05116  76 MAELGPLNKFLQKNRhVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKalrADENYYKAQ 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 779 STFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEML-VGESPFPGDDEEEVFDSIVNDE-VRYPRFLSAEAIGIMRRLL 856
Cdd:cd05116 156 THGKWPVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFsYGQKPYKGMKGNEVTQMIEKGErMECPAGCPPEMYDLMKLCW 235

                ....*....
gi 47132591 857 RRNPERRLG 865
Cdd:cd05116 236 TYDVDERPG 244
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
619-833 1.80e-11

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK6 is regulated by D-type cyclins and INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein, implicating it to function in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the cytoplasm. It is also present in the ruffling edge of spreading fibroblasts and may play a role in cell spreading. It binds to the p21 inhibitor without any effect on its own activity and it is overexpressed in squamous cell carcinomas and neuroblastomas. CDK6 has also been shown to inhibit cell differentiation in many cell types. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 66.21  E-value: 1.80e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAikALKKGDIVARDEVESL--MCEKRILAAVTSAGHPFLVNLFgcfqtpeH 696
Cdd:cd07862   1 QQYECVAEIGEGAYGKVFKARDLKNGGRFV--ALKRVRVQTGEEGMPLstIREVAVLRHLETFEHPNVVRLF-------D 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 697 VCFVMEYSAGGDLML---HIHSDVFS------EP-------RAIFYSacVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYV 760
Cdd:cd07862  72 VCTVSRTDRETKLTLvfeHVDQDLTTyldkvpEPgvptetiKDMMFQ--LLRGLDFLHSHRVVHRDLKPQNILVTSSGQI 149
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47132591 761 KIADFGLCKEgMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEE----VFDSI 833
Cdd:cd07862 150 KLADFGLARI-YSFQMALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRGSSDVDqlgkILDVI 225
HR1 cd00089
Protein kinase C-related kinase homology region 1 (HR1) domain that binds Rho family small ...
218-284 1.88e-11

Protein kinase C-related kinase homology region 1 (HR1) domain that binds Rho family small GTPases; The HR1 domain, also called the ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. It is found in Rho effector proteins including PKC-related kinases such as vertebrate PRK1 (or PKN) and yeast PKC1 protein kinases C, as well as in rhophilins and Rho-associated kinase (ROCK). Rho family members function as molecular switches, cycling between inactive and active forms, controlling a variety of cellular processes. HR1 domains may occur in repeat arrangements (PKN contains three HR1 domains), separated by a short linker region.


Pssm-ID: 212008 [Multi-domain]  Cd Length: 68  Bit Score: 60.42  E-value: 1.88e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47132591 218 ELRIEELRHHFRVEHAVAEGAKNVLRLLSaaKAPDRKAVSEAQEKLTESNQKLGLLREALERRLGEL 284
Cdd:cd00089   4 QQRLEELRRKLEKELKIREGAENLLKLYS--NPKVKKDLAEVQLNLKESKEKIDLLKRQLERYNALV 68
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
620-831 2.18e-11

Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER3 contains an impaired tyr kinase domain, which lacks crucial residues for catalytic activity against exogenous substrates but is still able to bind ATP and autophosphorylate. HER3 binds the neuregulin ligands, NRG1 and NRG2, and it relies on its heterodimerization partners for activity following ligand binding. The HER2-HER3 heterodimer constitutes a high affinity co-receptor capable of potent mitogenic signaling. HER3 participates in a signaling pathway involved in the proliferation, survival, adhesion, and motility of tumor cells. The HER3 subfamily is part of a larger superfamily that includes other pseudokinases and the the catalytic domains of active kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 65.75  E-value: 2.18e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKgDIVARDEVESLMCEKRILAAVTSAGHPFLVNLFGCFQTPEhVCF 699
Cdd:cd05111   8 ELRKLKVLGSGVFGTVHKGIWIPEGDSIKIPVAIK-VIQDRSGRQSFQAVTDHMLAIGSLDHAYIVRLLGICPGAS-LQL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYSAGGDLMLHI--HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKegMGYGDR 777
Cdd:cd05111  86 VTQLLPLGSLLDHVrqHRGSLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQVQVADFGVAD--LLYPDD 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 47132591 778 TSTF---CGTP-EFLAPEVLTDTSYTRAVDWWGLGVLLYEMLV-GESPFPGDDEEEVFD 831
Cdd:cd05111 164 KKYFyseAKTPiKWMALESIHFGKYTHQSDVWSYGVTVWEMMTfGAEPYAGMRLAEVPD 222
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
638-868 2.29e-11

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 65.07  E-value: 2.29e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 638 SEFRPSGELFAIKALKKGDIVARDEVESLMCEKrilaavtsagHPFLVNLFgCFQTPE-------HVCFVMEYSAGGDL- 709
Cdd:cd14012  24 GKFLTSQEYFKTSNGKKQIQLLEKELESLKKLR----------HPNLVSYL-AFSIERrgrsdgwKVYLLTEYAPGGSLs 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 710 -MLHIHSDVFSEpRAIFYSACVVLGLQFLHEHKIVYRDLKLDN---LLLDTEGYVKIADFGLCKEGMGYGDRTSTFCGTP 785
Cdd:cd14012  93 eLLDSVGSVPLD-TARRWTLQLLEALEYLHRNGVVHKSLHAGNvllDRDAGTGIVKLTDYSLGKTLLDMCSRGSLDEFKQ 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 786 EF-LAPEV-LTDTSYTRAVDWWGLGVLLYEMLVGESPFpgddeeEVFDSIvnDEVRYPRFLSAEAIGIMRRLLRRNPERR 863
Cdd:cd14012 172 TYwLPPELaQGSKSPTRKTDVWDLGLLFLQMLFGLDVL------EKYTSP--NPVLVSLDLSASLQDFLSKCLSLDPKKR 243

                ....*
gi 47132591 864 LGSSE 868
Cdd:cd14012 244 PTALE 248
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
619-879 2.40e-11

Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the mitogen-activated protein kinases (MAPKs) ERK1, ERK2, baker's yeast Fus3, and similar proteins. MAPK pathways are important mediators of cellular responses to extracellular signals. ERK1/2 activation is preferentially by mitogenic factors, differentiation stimuli, and cytokines, through a kinase cascade involving the MAPK kinases MEK1/2 and a MAPK kinase kinase from the Raf family. ERK1/2 have numerous substrates, many of which are nuclear and participate in transcriptional regulation of many cellular processes. They regulate cell growth, cell proliferation, and cell cycle progression from G1 to S phase. Although the distinct roles of ERK1 and ERK2 have not been fully determined, it is known that ERK2 can maintain most functions in the absence of ERK1, and that the deletion of ERK2 is embryonically lethal. The MAPK, Fus3, regulates yeast mating processes including mating-specific gene expression, G1 arrest, mating projection, and cell fusion. This ERK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 66.17  E-value: 2.40e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDivardevESLMC-----EKRILaavTSAGHPFLVNLFGcFQT 693
Cdd:cd07849   5 PRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKISPFE-------HQTYClrtlrEIKIL---LRFKHENIIGILD-IQR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 694 PEHVCFVMEYSAGGDLM---LH--IHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLC 768
Cdd:cd07849  74 PPTFESFKDVYIVQELMetdLYklIKTQHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 769 KEGMGYGDRTST---FCGTPEFLAPEV-LTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDD---------------EEEV 829
Cdd:cd07849 154 RIADPEHDHTGFlteYVATRWYRAPEImLNSKGYTKAIDIWSVGCILAEMLSNRPLFPGKDylhqlnlilgilgtpSQED 233
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47132591 830 FDSIVNDEVR-----------------YPRfLSAEAIGIMRRLLRRNPERRLgsserDAEDVKKQPF 879
Cdd:cd07849 234 LNCIISLKARnyikslpfkpkvpwnklFPN-ADPKALDLLDKMLTFNPHKRI-----TVEEALAHPY 294
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
621-826 2.46e-11

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mutations in the gene encoding CDKL5, previously called STK9, are associated with early onset epilepsy and severe mental retardation [X-linked infantile spasm syndrome (ISSX) or West syndrome]. In addition, CDKL5 mutations also sometimes cause a phenotype similar to Rett syndrome (RTT), a progressive neurodevelopmental disorder. These pathogenic mutations are located in the N-terminal portion of the protein within the kinase domain. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 65.40  E-value: 2.46e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKkgDIVARDEV-ESLMCEKRILAAVTSAGhpfLVNLFGCFQTPEHVCF 699
Cdd:cd07848   3 FEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFK--DSEENEEVkETTLRELKMLRTLKQEN---IVELKEAFRRRGKLYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYSAGGDL-MLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKE-GMGYGDR 777
Cdd:cd07848  78 VFEYVEKNMLeLLEEMPNGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNlSEGSNAN 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 47132591 778 TSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDE 826
Cdd:cd07848 158 YTEYVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGESE 206
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
626-841 2.61e-11

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 65.38  E-value: 2.61e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGE---LFAIKALKKGdiVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFVME 702
Cdd:cd05063  12 VIGAGEFGEVFRGILKMPGRkevAVAIKTLKPG--YTEKQRQDFLSEASIMGQFS---HHNIIRLEGVVTKFKPAMIITE 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 703 YSAGG--DLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK--EGMGYGDRT 778
Cdd:cd05063  87 YMENGalDKYLRDHDGEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRvlEDDPEGTYT 166
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47132591 779 STFCGTP-EFLAPEVLTDTSYTRAVDWWGLGVLLYE-MLVGESPFPGDDEEEVFDSIvNDEVRYP 841
Cdd:cd05063 167 TSGGKIPiRWTAPEAIAYRKFTSASDVWSFGIVMWEvMSFGERPYWDMSNHEVMKAI-NDGFRLP 230
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
627-815 2.66e-11

Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. Members of this subfamily include LIMK, Testicular or testis-specific protein kinase (TESK), and similar proteins. LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 64.82  E-value: 2.66e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKGDivardEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd14065   1 LGKGFFGEVYKVTHRETGKVMVMKELKRFD-----EQRSFLKEVKLMRRLS---HPNILRFIGVCVKDNKLNFITEYVNG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDL--MLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDN---LLLDTEGYVKIADFGLCKEGMGY----GDR 777
Cdd:cd14065  73 GTLeeLLKSMDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNclvREANRGRNAVVADFGLAREMPDEktkkPDR 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 47132591 778 TS--TFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEML 815
Cdd:cd14065 153 KKrlTVVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEII 192
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
619-863 3.50e-11

Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte Tyrosine Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyr residues in protein substrates. ALK and LTK are orphan receptor PTKs (RTKs) whose ligands are not yet well-defined. ALK appears to play an important role in mammalian neural development as well as visceral muscle differentiation in Drosophila. ALK is aberrantly expressed as fusion proteins, due to chromosomal translocations, in about 60% of anaplastic large cell lymphomas (ALCLs). ALK fusion proteins are also found in rare cases of diffuse large B cell lymphomas (DLBCLs). LTK is mainly expressed in B lymphocytes and neuronal tissues. It is important in cell proliferation and survival. Transgenic mice expressing TLK display retarded growth and high mortality rate. In addition, a polymorphism in mouse and human LTK is implicated in the pathogenesis of systemic lupus erythematosus. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. They are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The ALK/LTK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 65.10  E-value: 3.50e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKV----LLSEFRPSGEL-FAIKALKKgDIVARDEVESLMcEKRILAAVTsagHPFLVNLFG-CFQ 692
Cdd:cd05036   6 KNLTLIRALGQGAFGEVyegtVSGMPGDPSPLqVAVKTLPE-LCSEQDEMDFLM-EALIMSKFN---HPNIVRCIGvCFQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 693 TPEHVcFVMEYSAGGDL--MLHIHSDVFSEPRAIFYSAC------VVLGLQFLHEHKIVYRDLKLDNLLLDTEG---YVK 761
Cdd:cd05036  81 RLPRF-ILLELMAGGDLksFLRENRPRPEQPSSLTMLDLlqlaqdVAKGCRYLEENHFIHRDIAARNCLLTCKGpgrVAK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 762 IADFGLCKE--GMGY---GDRTSTfcgtP-EFLAPEVLTDTSYTRAVDWWGLGVLLYE-MLVGESPFPGDDEEEVFDSIV 834
Cdd:cd05036 160 IGDFGMARDiyRADYyrkGGKAML----PvKWMPPEAFLDGIFTSKTDVWSFGVLLWEiFSLGYMPYPGKSNQEVMEFVT 235
                       250       260       270
                ....*....|....*....|....*....|
gi 47132591 835 NDE-VRYPRFLSAEAIGIMRRLLRRNPERR 863
Cdd:cd05036 236 SGGrMDPPKNCPGPVYRIMTQCWQHIPEDR 265
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
697-880 3.61e-11

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 65.57  E-value: 3.61e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 697 VCFVMEYsAGGDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYV-KIADFGLCK------ 769
Cdd:cd07854  91 VYIVQEY-METDLANVLEQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTEDLVlKIGDFGLARivdphy 169
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 770 EGMGYGDRTSTfcgTPEFLAPE-VLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEE----VFDSI-VNDE------ 837
Cdd:cd07854 170 SHKGYLSEGLV---TKWYRSPRlLLSPNNYTKAIDMWAAGCIFAEMLTGKPLFAGAHELEqmqlILESVpVVREedrnel 246
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47132591 838 -------VR----YPRF--------LSAEAIGIMRRLLRRNPERRLgsserDAEDVKKQPFF 880
Cdd:cd07854 247 lnvipsfVRndggEPRRplrdllpgVNPEALDFLEQILTFNPMDRL-----TAEEALMHPYM 303
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
627-864 3.73e-11

Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily contains c-ros, Sevenless, and similar proteins. The proto-oncogene c-ros encodes an orphan receptor PTK (RTK) with an unknown ligand. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. C-ros is expressed in embryonic cells of the kidney, intestine and lung, but disappears soon after birth. It persists only in the adult epididymis. Male mice bearing inactive mutations of c-ros lack the initial segment of the epididymis and are infertile. The Drosophila protein, Sevenless, is required for the specification of the R7 photoreceptor cell during eye development. The c-ros subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 64.75  E-value: 3.73e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKV-------LLSEfrPSGEL-FAIKALKKGdivARD-EVESLMCEkrilAAVTSA-GHPFLVNLFG-CFQTpE 695
Cdd:cd05044   3 LGSGAFGEVfegtakdILGD--GSGETkVAVKTLRKG---ATDqEKAEFLKE----AHLMSNfKHPNILKLLGvCLDN-D 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 696 HVCFVMEYSAGGDLMLHIHSDVFSEPRAI------FYSAC--VVLGLQFLHEHKIVYRDLKLDNLLLDTEGY----VKIA 763
Cdd:cd05044  73 PQYIILELMEGGDLLSYLRAARPTAFTPPlltlkdLLSICvdVAKGCVYLEDMHFVHRDLAARNCLVSSKDYrervVKIG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 764 DFGLC----------KEGMGYgdrtstfcgTP-EFLAPEVLTDTSYTRAVDWWGLGVLLYEML-VGESPFPGDDEEEVFd 831
Cdd:cd05044 153 DFGLArdiykndyyrKEGEGL---------LPvRWMAPESLVDGVFTTQSDVWAFGVLMWEILtLGQQPYPARNNLEVL- 222
                       250       260       270
                ....*....|....*....|....*....|....*
gi 47132591 832 SIVNDEVRY--PRFLSAEAIGIMRRLLRRNPERRL 864
Cdd:cd05044 223 HFVRAGGRLdqPDNCPDDLYELMLRCWSTDPEERP 257
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
671-880 3.79e-11

Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. Its mRNA levels is low at birth, increases at puberty, and remains high throughout adulthood. The TSSK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 64.63  E-value: 3.79e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 671 RILAAVTSAGHPFLVNLFGCFQTPE-HVCFVMEYSAGGDLMLHI-HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLK 748
Cdd:cd14163  49 RELQIVERLDHKNIIHVYEMLESADgKIYLVMELAEDGDVFDCVlHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLK 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 749 LDNLLLdtEGY-VKIADFGLCKE-GMGYGDRTSTFCGTPEFLAPEVLTDTSY-TRAVDWWGLGVLLYEMLVGESPFpgdD 825
Cdd:cd14163 129 CENALL--QGFtLKLTDFGFAKQlPKGGRELSQTFCGSTAYAAPEVLQGVPHdSRKGDIWSMGVVLYVMLCAQLPF---D 203
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 47132591 826 EEEVFDSIVNDE--VRYPRFL--SAEAIGIMRRLLRrnPERRLGSSerdAEDVKKQPFF 880
Cdd:cd14163 204 DTDIPKMLCQQQkgVSLPGHLgvSRTCQDLLKRLLE--PDMVLRPS---IEEVSWHPWL 257
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
627-868 4.26e-11

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR2 (or Flk1) binds the ligands VEGFA, VEGFC, VEGFD and VEGFE. VEGFR2 signaling is implicated in all aspects of normal and pathological vascular endothelial cell biology. It induces a variety of cellular effects including migration, survival, and proliferation. It is critical in regulating embryonic vascular development and angiogenesis. VEGFR2 is the major signal transducer in pathological angiogenesis including cancer and diabetic retinopathy, and is a target for inhibition in cancer therapy. The carboxyl terminus of VEGFR2 plays an important role in its autophosphorylation and activation. VEGFR2 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 65.39  E-value: 4.26e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEF-----RPSGELFAIKALKKGdiVARDEVESLMCEKRILAAVtsaGHPF-LVNLFG-CFQTPEHVCF 699
Cdd:cd05103  15 LGRGAFGQVIEADAfgidkTATCRTVAVKMLKEG--ATHSEHRALMSELKILIHI---GHHLnVVNLLGaCTKPGGPLMV 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYSAGGDLMLHIHS-----------------------DV---------------------FSEPRA------------ 723
Cdd:cd05103  90 IVEFCKFGNLSAYLRSkrsefvpyktkgarfrqgkdyvgDIsvdlkrrldsitssqssassgFVEEKSlsdveeeeagqe 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 724 ------------IFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEgmGYGDRTSTFCGTP----EF 787
Cdd:cd05103 170 dlykdfltledlICYSFQVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARD--IYKDPDYVRKGDArlplKW 247
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 788 LAPEVLTDTSYTRAVDWWGLGVLLYEML-VGESPFPGDDEEEVFDSIVND--EVRYPRFLSAEAIGIMRRLLRRNPERRL 864
Cdd:cd05103 248 MAPETIFDRVYTIQSDVWSFGVLLWEIFsLGASPYPGVKIDEEFCRRLKEgtRMRAPDYTTPEMYQTMLDCWHGEPSQRP 327

                ....
gi 47132591 865 GSSE 868
Cdd:cd05103 328 TFSE 331
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
621-863 4.92e-11

Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 64.62  E-value: 4.92e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKAL----KKGDIVARDEVEslMCEKrilaavtsAGHPFLVNLFG-CFQTPE 695
Cdd:cd13986   2 YRIQRLLGEGGFSFVYLVEDLSTGRLYALKKIlchsKEDVKEAMREIE--NYRL--------FNHPNILRLLDsQIVKEA 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 696 H----VCFVMEYSAGGDLMLHI-----HSDVFSEPR--AIFYSACvvLGLQFLHEHKIV---YRDLKLDNLLLDTEGYVK 761
Cdd:cd13986  72 GgkkeVYLLLPYYKRGSLQDEIerrlvKGTFFPEDRilHIFLGIC--RGLKAMHEPELVpyaHRDIKPGNVLLSEDDEPI 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 762 IADFGLC----------KEGMGYGDRTSTFCgTPEFLAPE---VLTDTSYTRAVDWWGLGVLLYEMLVGESPFpgDDEEE 828
Cdd:cd13986 150 LMDLGSMnparieiegrREALALQDWAAEHC-TMPYRAPElfdVKSHCTIDEKTDIWSLGCTLYALMYGESPF--ERIFQ 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 47132591 829 VFDS----IVNDEVRYPR--FLSAEAIGIMRRLLRRNPERR 863
Cdd:cd13986 227 KGDSlalaVLSGNYSFPDnsRYSEELHQLVKSMLVVNPAER 267
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
626-863 4.94e-11

Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Mer (or Mertk) is named after its original reported expression pattern (monocytes, epithelial, and reproductive tissues). It is required for the ingestion of apoptotic cells by phagocytes such as macrophages, retinal pigment epithelial cells, and dendritic cells. Mer is also important in maintaining immune homeostasis. Mer is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Mer subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 64.57  E-value: 4.94e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFR-PSG--ELFAIKALKKGDIVARdEVESLMCEKrilAAVTSAGHPFLVNLFG-CFQ-TPEHV--- 697
Cdd:cd14204  14 VLGEGEFGSVMEGELQqPDGtnHKVAVKTMKLDNFSQR-EIEEFLSEA---ACMKDFNHPNVIRLLGvCLEvGSQRIpkp 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 698 CFVMEYSAGGDLMLHI-HSDVFSEPRAI------FYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKE 770
Cdd:cd14204  90 MVILPFMKYGDLHSFLlRSRLGSGPQHVplqtllKFMIDIALGMEYLSSRNFLHRDLAARNCMLRDDMTVCVADFGLSKK 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 771 gMGYGD--RTSTFCGTP-EFLAPEVLTDTSYTRAVDWWGLGVLLYEMLV-GESPFPGDDEEEVFDSI-VNDEVRYPRFLS 845
Cdd:cd14204 170 -IYSGDyyRQGRIAKMPvKWIAVESLADRVYTVKSDVWAFGVTMWEIATrGMTPYPGVQNHEIYDYLlHGHRLKQPEDCL 248
                       250
                ....*....|....*...
gi 47132591 846 AEAIGIMRRLLRRNPERR 863
Cdd:cd14204 249 DELYDIMYSCWRSDPTDR 266
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
621-863 6.78e-11

Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The TAM subfamily consists of Tyro3 (or Sky), Axl, Mer (or Mertk), and similar proteins. TAM subfamily members are receptor tyr kinases (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. TAM proteins are implicated in a variety of cellular effects including survival, proliferation, migration, and phagocytosis. They are also associated with several types of cancer as well as inflammatory, autoimmune, vascular, and kidney diseases. The TAM subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 64.09  E-value: 6.78e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALK--KGDIVARDEVESLMCEKrilAAVTSAGHPFLVNLFG-CFQTPEHV 697
Cdd:cd05035   1 LKLGKILGEGEFGSVMEAQLKQDDGSQLKVAVKtmKVDIHTYSEIEEFLSEA---ACMKDFDHPNVMRLIGvCFTASDLN 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 698 CF-----VMEYSAGGDLmlhiHSDVFSEPRA-----------IFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVK 761
Cdd:cd05035  78 KPpspmvILPFMKHGDL----HSYLLYSRLGglpeklplqtlLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVC 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 762 IADFGLCKEgMGYGD--RTSTFCGTP-EFLAPEVLTDTSYTRAVDWWGLGVLLYEMLV-GESPFPGDDEEEVFDSIVN-D 836
Cdd:cd05035 154 VADFGLSRK-IYSGDyyRQGRISKMPvKWIALESLADNVYTSKSDVWSFGVTMWEIATrGQTPYPGVENHEIYDYLRNgN 232
                       250       260
                ....*....|....*....|....*..
gi 47132591 837 EVRYPRFLSAEAIGIMRRLLRRNPERR 863
Cdd:cd05035 233 RLKQPEDCLDEVYFLMYFCWTVDPKDR 259
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
730-880 8.04e-11

Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is an ER-localized type I transmembrane protein with kinase and endoribonuclease domains in the cytoplasmic side. It acts as an ER stress sensor and is the oldest and most conserved component of the unfolded protein response (UPR) in eukaryotes. The UPR is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. During ER stress, IRE1 dimerizes and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and XBP1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). The Ire1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 63.83  E-value: 8.04e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 730 VVLGLQFLHEHKIVYRDLK-----LDNLLLDTEGYVKIADFGLCKE---GMGYGDRTSTFCGTPEFLAPEVLTDTSY--- 798
Cdd:cd13982 108 IASGLAHLHSLNIVHRDLKpqnilISTPNAHGNVRAMISDFGLCKKldvGRSSFSRRSGVAGTSGWIAPEMLSGSTKrrq 187
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 799 TRAVDWWGLGVLLYEMLV-GESPFPGDDEEEVfdSIVNDEVRYPRFLSA-----EAIGIMRRLLRRNPERRlgsseRDAE 872
Cdd:cd13982 188 TRAVDIFSLGCVFYYVLSgGSHPFGDKLEREA--NILKGKYSLDKLLSLgehgpEAQDLIERMIDFDPEKR-----PSAE 260

                ....*...
gi 47132591 873 DVKKQPFF 880
Cdd:cd13982 261 EVLNHPFF 268
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
620-863 8.45e-11

Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER1, ErbB1) is a receptor PTK (RTK) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands for EGFR include EGF, heparin binding EGF-like growth factor (HBEGF), epiregulin, amphiregulin, TGFalpha, and betacellulin. Upon ligand binding, EGFR can form homo- or heterodimers with other EGFR subfamily members. The EGFR signaling pathway is one of the most important pathways regulating cell proliferation, differentiation, survival, and growth. Overexpression and mutation in the kinase domain of EGFR have been implicated in the development and progression of a variety of cancers. A number of monoclonal antibodies and small molecule inhibitors have been developed that target EGFR, including the antibodies Cetuximab and Panitumumab, which are used in combination with other therapies for the treatment of colorectal cancer and non-small cell lung carcinoma (NSCLC). The small molecule inhibitors Gefitinib (Iressa) and Erlotinib (Tarceva), already used for NSCLC, are undergoing clinical trials for other types of cancer including gastrointestinal, breast, head and neck, and bladder. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 64.27  E-value: 8.45e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKFLAVLGRGHFGKVLLSEFRPSGELF----AIKALKkgdivardEVESLMCEKRILA---AVTSAGHPFLVNLFG-CF 691
Cdd:cd05108   8 EFKKIKVLGSGAFGTVYKGLWIPEGEKVkipvAIKELR--------EATSPKANKEILDeayVMASVDNPHVCRLLGiCL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 692 -QTPEHVCFVMEYsagGDLMLHI--HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLC 768
Cdd:cd05108  80 tSTVQLITQLMPF---GCLLDYVreHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLA 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 769 KEgMGYGDRTSTFCG--TP-EFLAPEVLTDTSYTRAVDWWGLGVLLYE-MLVGESPFPGDDEEEVFDSIVNDE-VRYPRF 843
Cdd:cd05108 157 KL-LGAEEKEYHAEGgkVPiKWMALESILHRIYTHQSDVWSYGVTVWElMTFGSKPYDGIPASEISSILEKGErLPQPPI 235
                       250       260
                ....*....|....*....|
gi 47132591 844 LSAEAIGIMRRLLRRNPERR 863
Cdd:cd05108 236 CTIDVYMIMVKCWMIDADSR 255
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
627-815 9.68e-11

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK1 activation is induced by bone morphogenic protein, vascular endothelial growth factor, and thrombin. It plays roles in microtubule disassembly and cell cycle progression, and is critical in the regulation of neurite outgrowth. LIMK1 knockout mice show abnormalities in dendritic spine morphology and synaptic function. LIMK1 is one of the genes deleted in patients with Williams Syndrome, which is characterized by distinct craniofacial features, cardiovascular problems, as well as behavioral and neurological abnormalities. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 63.44  E-value: 9.68e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKGDivaRDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd14221   1 LGKGCFGQAIKVTHRETGEVMVMKELIRFD---EETQRTFLKEVKVMRCLE---HPNVLKFIGVLYKDKRLNFITEYIKG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLMLHIHSDVFSEP--RAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK------------EGM 772
Cdd:cd14221  75 GTLRGIIKSMDSHYPwsQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLARlmvdektqpeglRSL 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 47132591 773 GYGDRTS--TFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEML 815
Cdd:cd14221 155 KKPDRKKryTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEII 199
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
622-885 1.06e-10

Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Frk and Srk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Frk, also known as Rak, is specifically expressed in liver, lung, kidney, intestine, mammary glands, and the islets of Langerhans. Rodent homologs were previously referred to as GTK (gastrointestinal tyr kinase), BSK (beta-cell Src-like kinase), or IYK (intestinal tyr kinase). Studies in mice reveal that Frk is not essential for viability. It plays a role in the signaling that leads to cytokine-induced beta-cell death in Type I diabetes. It also regulates beta-cell number during embryogenesis and early in life. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Frk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 63.19  E-value: 1.06e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 622 KFLAVLGRGHFGKV---LLSEFRPsgelFAIKALKKGDIVARDevesLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVC 698
Cdd:cd05068  11 KLLRKLGSGQFGEVwegLWNNTTP----VAVKTLKPGTMDPED----FLREAQIMKKLR---HPKLIQLYAVCTLEEPIY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGGDLMLHIHSD--VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMG--- 773
Cdd:cd05068  80 IITELMKHGSLLEYLQGKgrSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGLARVIKVede 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 774 YGDRTST-FcgtP-EFLAPEVLTDTSYTRAVDWWGLGVLLYEMLV-GESPFPGDDEEEVFDSiVNDEVRYPRFLS--AEA 848
Cdd:cd05068 160 YEAREGAkF---PiKWTAPEAANYNRFSIKSDVWSFGILLTEIVTyGRIPYPGMTNAEVLQQ-VERGYRMPCPPNcpPQL 235
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 47132591 849 IGIMRRLLRRNPERRlgsserdaedvkkqPFFRTLGW 885
Cdd:cd05068 236 YDIMLECWKADPMER--------------PTFETLQW 258
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
621-840 1.30e-10

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 63.89  E-value: 1.30e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEveslMCEKRILAAVTS--AGHPFLVNLFGCFQTPEHVC 698
Cdd:cd14229   2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILKNHPSYARQG----QIEVGILARLSNenADEFNFVRAYECFQHRNHTC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGgDLMLHIHSDVFSeP------RAIFYSACVVL----GLQFLHEHkivYRDLKLDNLLLDTEGY-VKIADFGl 767
Cdd:cd14229  78 LVFEMLEQ-NLYDFLKQNKFS-PlplkviRPILQQVATALkklkSLGLIHAD---LKPENIMLVDPVRQPYrVKVIDFG- 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47132591 768 ckeGMGYGDRT--STFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEeevfdsivNDEVRY 840
Cdd:cd14229 152 ---SASHVSKTvcSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGALE--------YDQIRY 215
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
620-827 1.40e-10

Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 63.14  E-value: 1.40e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKFLAVLGRGHFGKVLLSefRPSGELfAIKALKkgdiVARDEVESLMCEKRILAAVTSAGHPFLVNLFGCFQTPEHVCF 699
Cdd:cd14063   1 ELEIKEVIGKGRFGRVHRG--RWHGDV-AIKLLN----IDYLNEEQLEAFKEEVAAYKNTRHDNLVLFMGACMDPPHLAI 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYSAGGDLMLHIHS--DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTeGYVKIADFGLCK-EGMGYGD 776
Cdd:cd14063  74 VTSLCKGRTLYSLIHErkEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLEN-GRVVITDFGLFSlSGLLQPG 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47132591 777 RTSTFCGTPE----FLAPEVLTDTS----------YTRAVDWWGLGVLLYEMLVGESPFPGDDEE 827
Cdd:cd14063 153 RREDTLVIPNgwlcYLAPEIIRALSpdldfeeslpFTKASDVYAFGTVWYELLAGRWPFKEQPAE 217
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
615-880 1.60e-10

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A splice variant of TLK1, called TLK1B, is expressed in the presence of double strand breaks (DSBs). It lacks the N-terminal part of TLK1, but is expected to phosphorylate the same substrates. TLK1/1B interacts with Rad9, which is critical in DNA damage-activated checkpoint response, and plays a role in the repair of linearized DNA with incompatible ends. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. The TLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 63.15  E-value: 1.60e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 615 PLTLEDFKFLAVLGRGHFGKVLlSEFRPSGELFAIKALKKGDIVARDE----VESLMC-EKRILAAVTsagHPFLVNLFG 689
Cdd:cd14040   2 PTLNERYLLLHLLGRGGFSEVY-KAFDLYEQRYAAVKIHQLNKSWRDEkkenYHKHACrEYRIHKELD---HPRIVKLYD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 690 CFQ-TPEHVCFVMEYSAGGDLMLHI-HSDVFSEPRAIFYSACVVLGLQFLHEHK--IVY---RDLKLDNLLLDTEGYVKI 762
Cdd:cd14040  78 YFSlDTDTFCTVLEYCEGNDLDFYLkQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHydlKPGNILLVDGTACGEIKI 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 763 ADFGLCK--EGMGYG----DRTSTFCGTPEFLAPEVLT----DTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVF-- 830
Cdd:cd14040 158 TDFGLSKimDDDSYGvdgmDLTSQGAGTYWYLPPECFVvgkePPKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDIlq 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 47132591 831 -DSIVN-DEVRYP--RFLSAEAIGIMRRLLRRNPERRLgsserDAEDVKKQPFF 880
Cdd:cd14040 238 eNTILKaTEVQFPvkPVVSNEAKAFIRRCLAYRKEDRF-----DVHQLASDPYL 286
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
627-821 2.13e-10

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 63.28  E-value: 2.13e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVEslmceKRILAAVTSAGHPFLVNLFGCF--QTPEHVCFVMEYS 704
Cdd:cd13988   1 LGQGATANVFRGRHKKTGDLYAVKVFNNLSFMRPLDVQ-----MREFEVLKKLNHKNIVKLFAIEeeLTTRHKVLVMELC 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 705 AGGDL--MLHIHSDVFSEPRAIFYSAC--VVLGLQFLHEHKIVYRDLK----LDNLLLDTEGYVKIADFGLCKEgMGYGD 776
Cdd:cd13988  76 PCGSLytVLEEPSNAYGLPESEFLIVLrdVVAGMNHLRENGIVHRDIKpgniMRVIGEDGQSVYKLTDFGAARE-LEDDE 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 47132591 777 RTSTFCGTPEFLAPE-----VL---TDTSYTRAVDWWGLGVLLYEMLVGESPF 821
Cdd:cd13988 155 QFVSLYGTEEYLHPDmyeraVLrkdHQKKYGATVDLWSIGVTFYHAATGSLPF 207
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
627-821 2.70e-10

Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Zap-70 is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) signaling. Zap-70 binds the phosphorylated ITAM (immunoreceptor tyr activation motif) sequences of the activated TCR zeta-chain through its SH2 domains, leading to its phosphorylation and activation. It then phosphorylates target proteins, which propagate the signals to downstream pathways. Zap-70 is hardly detected in normal peripheral B-cells, but is present in some B-cell malignancies. It is used as a diagnostic marker for chronic lymphocytic leukemia (CLL) as it is associated with the more aggressive subtype of the disease. The Zap-70 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 62.27  E-value: 2.70e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELF--AIKALKKGDIVA-RDEvesLMCEKRILAAVTSaghPFLVNLFGCFQTpEHVCFVMEY 703
Cdd:cd05115  12 LGSGNFGCVKKGVYKMRKKQIdvAIKVLKQGNEKAvRDE---MMREAQIMHQLDN---PYIVRMIGVCEA-EALMLVMEM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 704 SAGGDL--MLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKeGMGYGD---RT 778
Cdd:cd05115  85 ASGGPLnkFLSGKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSK-ALGADDsyyKA 163
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 47132591 779 STFCGTP-EFLAPEVLTDTSYTRAVDWWGLGVLLYEML-VGESPF 821
Cdd:cd05115 164 RSAGKWPlKWYAPECINFRKFSSRSDVWSYGVTMWEAFsYGQKPY 208
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
713-868 2.76e-10

Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SHIK, also referred to as STK40 or LYK4, is a cytoplasmic and nuclear protein that is involved in the negative regulation of NF-kappaB- and p53-mediated transcription. It was identified as a protein related to SINK, a p65-interacting protein that inhibits p65 phosphorylation by the catalytic subunit of PKA, thereby inhibiting transcriptional competence of NF-kappaB. The SHIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 62.42  E-value: 2.76e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 713 IHSDVFSEPRA--IFYSacVVLGLQFLHEHKIVYRDLKLDNLLLDTEGY-VKIADFGLCKEGMGYGDRTSTFCGTPEFLA 789
Cdd:cd13974 124 IREKRLSEREAlvIFYD--VVRVVEALHKKNIVHRDLKLGNMVLNKRTRkITITNFCLGKHLVSEDDLLKDQRGSPAYIS 201
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 790 PEVLTDTSYT-RAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPR--FLSAEAIGIMRRLLRRNPERRLGS 866
Cdd:cd13974 202 PDVLSGKPYLgKPSDMWALGVVLFTMLYGQFPFYDSIPQELFRKIKAAEYTIPEdgRVSENTVCLIRKLLVLNPQKRLTA 281

                ..
gi 47132591 867 SE 868
Cdd:cd13974 282 SE 283
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
619-868 2.88e-10

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 61.78  E-value: 2.88e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVL--LSEFRPSGELFAIKALKKGDivARDEVESLMCEKRILAavtsagHPFLVNLFGCFQTPEH 696
Cdd:cd14112   3 GRFSFGSEIFRGRFSVIVkaVDSTTETDAHCAVKIFEVSD--EASEAVREFESLRTLQ------HENVQRLIAAFKPSNF 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 697 VCFVMEYSAGGDLMLHIHSDVFSEPRAIFYSACVVLGLQFLH----------EHKIVYRDLKLDNllldtegyVKIADFG 766
Cdd:cd14112  75 AYLVMEKLQEDVFTRFSSNDYYSEEQVATTVRQILDALHYLHfkgiahldvqPDNIMFQSVRSWQ--------VKLVDFG 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 767 LCKEGMGYGDRTStfCGTPEFLAPEVL-TDTSYTRAVDWWGLGVLLYEMLVGESPFPG--DDEEEVFDSIVNDEVRY--- 840
Cdd:cd14112 147 RAQKVSKLGKVPV--DGDTDWASPEFHnPETPITVQSDIWGLGVLTFCLLSGFHPFTSeyDDEEETKENVIFVKCRPnli 224
                       250       260
                ....*....|....*....|....*...
gi 47132591 841 PRFLSAEAIGIMRRLLRRNPERRLGSSE 868
Cdd:cd14112 225 FVEATQEALRFATWALKKSPTRRMRTDE 252
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
730-863 3.31e-10

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR alpha is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR alpha forms homodimers or heterodimers with PDGFR beta, depending on the nature of the PDGF ligand. PDGF-AA, PDGF-AB, and PDGF-CC induce PDGFR alpha homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR alpha signaling is important in the formation of lung alveoli, intestinal villi, mesenchymal dermis, and hair follicles, as well as in the development of oligodendrocytes, retinal astrocytes, neural crest cells, and testicular cells. Aberrant PDGFR alpha expression is associated with some human cancers. Mutations in PDGFR alpha have been found within a subset of gastrointestinal stromal tumors (GISTs). An active fusion protein FIP1L1-PDGFR alpha, derived from interstitial deletion, is associated with idiopathic hypereosinophilic syndrome and chronic eosinophilic leukemia. The PDGFR alpha subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 63.12  E-value: 3.31e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 730 VVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGM---GYGDRTSTFCGTpEFLAPEVLTDTSYTRAVDWWG 806
Cdd:cd05105 246 VARGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGLARDIMhdsNYVSKGSTFLPV-KWMAPESIFDNLYTTLSDVWS 324
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 807 LGVLLYEML-VGESPFPGDDEEEVFDSIVNDEVRY--PRFLSAEAIGIMRRLLRRNPERR 863
Cdd:cd05105 325 YGILLWEIFsLGGTPYPGMIVDSTFYNKIKSGYRMakPDHATQEVYDIMVKCWNSEPEKR 384
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
618-815 4.72e-10

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3 or PKR-like Endoplasmic Reticulum Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PERK (or EIF2AK3) is a type-I ER transmembrane protein containing a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PERK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 61.43  E-value: 4.72e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 618 LEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGD-IVARDEVeslMCEKRILAAVTsagHPFLVNLFGCF--QTP 694
Cdd:cd14048   5 LTDFEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRIRLPNnELAREKV---LREVRALAKLD---HPGIVRYFNAWleRPP 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 695 E---------HVCFVMEYSAGGDLMLHIHSDVFSEPRAIFYsaC------VVLGLQFLHEHKIVYRDLKLDNLLLDTEGY 759
Cdd:cd14048  79 EgwqekmdevYLYIQMQLCRKENLKDWMNRRCTMESRELFV--ClnifkqIASAVEYLHSKGLIHRDLKPSNVFFSLDDV 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47132591 760 VKIADFGLCKEgMGYGDRTSTF-------------CGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEML 815
Cdd:cd14048 157 VKVGDFGLVTA-MDQGEPEQTVltpmpayakhtgqVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELI 224
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
619-883 4.80e-10

Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 62.28  E-value: 4.80e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKK---GDIVARDEVESLmcekRILAAVTsagHPFLVNLFGCFqTPE 695
Cdd:cd07880  15 DRYRDLKQVGSGAYGTVCSALDRRTGAKVAIKKLYRpfqSELFAKRAYREL----RLLKHMK---HENVIGLLDVF-TPD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 696 HVC-------FVMEYsAGGDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLC 768
Cdd:cd07880  87 LSLdrfhdfyLVMPF-MGTDLGKLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLA 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 769 KEGmgyGDRTSTFCGTPEFLAPEVLTD-TSYTRAVDWWGLGVLLYEMLVGESPFPGDDE---------------EEVFDS 832
Cdd:cd07880 166 RQT---DSEMTGYVVTRWYRAPEVILNwMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHldqlmeimkvtgtpsKEFVQK 242
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47132591 833 IVNDEVR-----YPRF-----------LSAEAIGIMRRLLRRNPERRLGSSERDAedvkkQPFFRTL 883
Cdd:cd07880 243 LQSEDAKnyvkkLPRFrkkdfrsllpnANPLAVNVLEKMLVLDAESRITAAEALA-----HPYFEEF 304
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
633-862 6.35e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 62.32  E-value: 6.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  633 GKVLLSEFRPSGELFAIKALKKGD----IVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFVM-EYSAgg 707
Cdd:PHA03212  93 GFSILETFTPGAEGFAFACIDNKTcehvVIKAGQRGGTATEAHILRAIN---HPSIIQLKGTFTYNKFTCLILpRYKT-- 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  708 DLMLHIHS-------DVFSEPRAifysacVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFG-LCKEGMGYGDRTS 779
Cdd:PHA03212 168 DLYCYLAAkrniaicDILAIERS------VLRAIQYLHENRIIHRDIKAENIFINHPGDVCLGDFGaACFPVDINANKYY 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  780 TFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGE-SPFPGD------DEEEVFDSIVNDEVRYPRFLSAEAIGIM 852
Cdd:PHA03212 242 GWAGTIATNAPELLARDPYGPAVDIWSAGIVLFEMATCHdSLFEKDgldgdcDSDRQIKLIIRRSGTHPNEFPIDAQANL 321
                        250
                 ....*....|
gi 47132591  853 RRLLRRNPER 862
Cdd:PHA03212 322 DEIYIGLAKK 331
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
620-842 7.38e-10

Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER4 (ErbB4) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands that bind HER4 fall into two groups, the neuregulins (or heregulins) and some EGFR (HER1) ligands including betacellulin, HBEGF, and epiregulin. All four neuregulins (NRG1-4) interact with HER4. Upon ligand binding, HER4 forms homo- or heterodimers with other HER proteins. HER4 is essential in embryonic development. It is implicated in mammary gland, cardiac, and neural development. As a postsynaptic receptor of NRG1, HER4 plays an important role in synaptic plasticity and maturation. The impairment of NRG1/HER4 signaling may contribute to schizophrenia. The HER4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 61.24  E-value: 7.38e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKFLAVLGRGHFGKVLLSEFRPSGELF----AIKALKKgDIVARDEVEsLMCEKRILAavtSAGHPFLVNLFGCFQTPE 695
Cdd:cd05110   8 ELKRVKVLGSGAFGTVYKGIWVPEGETVkipvAIKILNE-TTGPKANVE-FMDEALIMA---SMDHPHLVRLLGVCLSPT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 696 hVCFVMEYSAGGDLM--LHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMG 773
Cdd:cd05110  83 -IQLVTQLMPHGCLLdyVHEHKDNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLARLLEG 161
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47132591 774 YGDRTSTFCGTP--EFLAPEVLTDTSYTRAVDWWGLGVLLYEMLV-GESPFPGDDEEEVFDSIVNDEvRYPR 842
Cdd:cd05110 162 DEKEYNADGGKMpiKWMALECIHYRKFTHQSDVWSYGVTIWELMTfGGKPYDGIPTREIPDLLEKGE-RLPQ 232
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
621-880 8.64e-10

Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK, CDK2, and CDK3. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression while the CDK1/cyclin B complex is critical for G2 to M phase transition. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. Studies in knockout mice revealed that CDK1 can compensate for the loss of the cdk2 gene as it can also bind cyclin E and drive G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 60.77  E-value: 8.64e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGElfaIKALKKgdIVARDEVE----------SLMCEKRilaavtsagHPFLVNLFGC 690
Cdd:cd07835   1 YQKLEKIGEGTYGVVYKARDKLTGE---IVALKK--IRLETEDEgvpstaireiSLLKELN---------HPNIVRLLDV 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 691 FQTPEHVCFVMEYSaggDLMLHIHSD---VFSEPRAIF--YSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADF 765
Cdd:cd07835  67 VHSENKLYLVFEFL---DLDLKKYMDsspLTGLDPPLIksYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADF 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 766 GLCKeGMGYGDRTSTF-CGTPEFLAPEVLT-DTSYTRAVDWWGLGVLLYEMLVGESPFPGDDE-EEVF----------DS 832
Cdd:cd07835 144 GLAR-AFGVPVRTYTHeVVTLWYRAPEILLgSKHYSTPVDIWSVGCIFAEMVTRRPLFPGDSEiDQLFrifrtlgtpdED 222
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47132591 833 IVNDEVRYPRF------------------LSAEAIGIMRRLLRRNPERRLgsserDAEDVKKQPFF 880
Cdd:cd07835 223 VWPGVTSLPDYkptfpkwarqdlskvvpsLDEDGLDLLSQMLVYDPAKRI-----SAKAALQHPYF 283
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
627-868 9.37e-10

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkC is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkC to its ligand, neurotrophin 3 (NT3), results in receptor oligomerization and activation of the catalytic domain. TrkC is broadly expressed in the nervous system and in some non-neural tissues including the developing heart. NT3/TrkC signaling plays an important role in the innervation of the cardiac conducting system and the development of smooth muscle cells. Mice deficient with NT3 and TrkC have multiple heart defects. NT3/TrkC signaling is also critical for the development and maintenance of enteric neurons that are important for the control of gut peristalsis. The TrkC subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 60.79  E-value: 9.37e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSE---FRPSGE--LFAIKALKKGDIVARDEVEslmcekRILAAVTSAGHPFLVNLFGCFQTPEHVCFVM 701
Cdd:cd05094  13 LGEGAFGKVFLAEcynLSPTKDkmLVAVKTLKDPTLAARKDFQ------REAELLTNLQHDHIVKFYGVCGDGDPLIMVF 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 702 EYSAGGDL--MLHIHSD-----VFSEPRA----------IFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIAD 764
Cdd:cd05094  87 EYMKHGDLnkFLRAHGPdamilVDGQPRQakgelglsqmLHIATQIASGMVYLASQHFVHRDLATRNCLVGANLLVKIGD 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 765 FGLCKEGMGYG-DRTSTFCGTP-EFLAPEVLTDTSYTRAVDWWGLGVLLYEMLV-GESPFPGDDEEEVFDSIVNDEV-RY 840
Cdd:cd05094 167 FGMSRDVYSTDyYRVGGHTMLPiRWMPPESIMYRKFTTESDVWSFGVILWEIFTyGKQPWFQLSNTEVIECITQGRVlER 246
                       250       260
                ....*....|....*....|....*...
gi 47132591 841 PRFLSAEAIGIMRRLLRRNPERRLGSSE 868
Cdd:cd05094 247 PRVCPKEVYDIMLGCWQREPQQRLNIKE 274
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
730-881 1.33e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 61.05  E-value: 1.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  730 VVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK----EGMGYGdrtstFCGTPEFLAPEVLTDTSYTRAVDWW 805
Cdd:PHA03209 166 ILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLGAAQfpvvAPAFLG-----LAGTVETNAPEVLARDKYNSKADIW 240
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47132591  806 GLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSaeAIGIMRRLLRRNPERRLGSSERDAEDVKKQPFFR 881
Cdd:PHA03209 241 SAGIVLFEMLAYPSTIFEDPPSTPEEYVKSCHSHLLKIIS--TLKVHPEEFPRDPGSRLVRGFIEYASLERQPYTR 314
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
619-825 1.43e-09

Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase (also called MAPK14); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38alpha/MAPK14 is expressed in most tissues and is the major isoform involved in the immune and inflammatory response. It is the central p38 MAPK involved in myogenesis. It plays a role in regulating cell cycle check-point transition and promoting cell differentiation. p38alpha also regulates cell proliferation and death through crosstalk with the JNK pathway. Its substrates include MAPK activated protein kinase 2 (MK2), MK5, and the transcription factors ATF2 and Mitf. p38 kinases MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 60.82  E-value: 1.43e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKgdivardEVESLMCEKRI---LAAVTSAGHPFLVNLFGCFqTPE 695
Cdd:cd07877  17 ERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSR-------PFQSIIHAKRTyreLRLLKHMKHENVIGLLDVF-TPA 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 696 HV------CFVMEYSAGGDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK 769
Cdd:cd07877  89 RSleefndVYLVTHLMGADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLAR 168
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 47132591 770 EGmgyGDRTSTFCGTPEFLAPEVLTD-TSYTRAVDWWGLGVLLYEMLVGESPFPGDD 825
Cdd:cd07877 169 HT---DDEMTGYVATRWYRAPEIMLNwMHYNQTVDIWSVGCIMAELLTGRTLFPGTD 222
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
734-880 1.99e-09

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and similar MAPKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human MAPK15 is also called Extracellular signal Regulated Kinase 8 (ERK8) while the rat protein is called ERK7. ERK7 and ERK8 display both similar and different biochemical properties. They autophosphorylate and activate themselves and do not require upstream activating kinases. ERK7 is constitutively active and is not affected by extracellular stimuli whereas ERK8 shows low basal activity and is activated by DNA-damaging agents. ERK7 and ERK8 also have different substrate profiles. Genome analysis shows that they are orthologs with similar gene structures. ERK7 and ERK 8 may be involved in the signaling of some nuclear receptor transcription factors. ERK7 regulates hormone-dependent degradation of estrogen receptor alpha while ERK8 down-regulates the transcriptional co-activation androgen and glucocorticoid receptors. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK15 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 60.26  E-value: 1.99e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 734 LQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK-----EGMGYGDRTSTFCGTPEFLAPEVL-TDTSYTRAVDWWGL 807
Cdd:cd07852 120 LKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLARslsqlEEDDENPVLTDYVATRWYRAPEILlGSTRYTKGVDMWSV 199
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 808 GVLLYEMLVGESPFPG--------------------DDE-------EEVFDSIVNDEVRYPRFL----SAEAIGIMRRLL 856
Cdd:cd07852 200 GCILGEMLLGKPLFPGtstlnqlekiievigrpsaeDIEsiqspfaATMLESLPPSRPKSLDELfpkaSPDALDLLKKLL 279
                       170       180
                ....*....|....*....|....
gi 47132591 857 RRNPERRLgsserDAEDVKKQPFF 880
Cdd:cd07852 280 VFNPNKRL-----TAEEALRHPYV 298
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
619-830 2.38e-09

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 59.71  E-value: 2.38e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKkgdivARDEVESLMCEKRILAAVTSAGHPFLVNLFGCFQTPEHVC 698
Cdd:cd07869   5 DSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIR-----LQEEEGTPFTAIREASLLKGLKHANIVLLHDIIHTKETLT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYsAGGDLMLHI--HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGD 776
Cdd:cd07869  80 LVFEY-VHTDLCQYMdkHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARAKSVPSH 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 777 RTSTFCGTPEFLAPEVLT-DTSYTRAVDWWGLGVLLYEMLVGESPFPG-----DDEEEVF 830
Cdd:cd07869 159 TYSNEVVTLWYRPPDVLLgSTEYSTCLDMWGVGCIFVEMIQGVAAFPGmkdiqDQLERIF 218
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
627-880 2.41e-09

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK5 is unusual in that it is regulated by non-cyclin proteins, p35 and p39. It is highly expressed in the nervous system and is critical in normal neural development and function. It plays a role in neuronal migration and differentiation, and is also important in synaptic plasticity and learning. CDK5 also participates in protecting against cell death and promoting angiogenesis. Impaired CDK5 activity is implicated in Alzheimer's disease, amyotrophic lateral sclerosis, Parkinson's disease, Huntington's disease and acute neuronal injury. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 59.37  E-value: 2.41e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGElfaIKALKKGDIVARDE-VESLMCekRILAAVTSAGHPFLVNLFGCFQTPEHVCFVMEY-- 703
Cdd:cd07839   8 IGEGTYGTVFKAKNRETHE---IVALKRVRLDDDDEgVPSSAL--REICLLKELKHKNIVRLYDVLHSDKKLTLVFEYcd 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 704 --------SAGGDLMLHI-HSDVFSEPRaifysacvvlGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKegmGY 774
Cdd:cd07839  83 qdlkkyfdSCNGDIDPEIvKSFMFQLLK----------GLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLAR---AF 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 775 GDRTSTFCG---TPEFLAPEVLTD-TSYTRAVDWWGLGVLLYEMLVGESP-FPGDDEEEVFDSI---------------- 833
Cdd:cd07839 150 GIPVRCYSAevvTLWYRPPDVLFGaKLYSTSIDMWSAGCIFAELANAGRPlFPGNDVDDQLKRIfrllgtpteeswpgvs 229
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 834 -VNDEVRYPRF------------LSAEAIGIMRRLLRRNPERRLgsserDAEDVKKQPFF 880
Cdd:cd07839 230 kLPDYKPYPMYpattslvnvvpkLNSTGRDLLQNLLVCNPVQRI-----SAEEALQHPYF 284
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
625-863 2.49e-09

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3). PIM3 can inhibit apoptosis and promote cell survival and protein translation, therefore, it can enhance the proliferation of normal and cancer cells. Mice deficient with PIM3 show minimal effects, suggesting that PIM3 msy not be essential. Since its expression is enhanced in several cancers, it may make a good molecular target for cancer drugs. The PIM3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 59.20  E-value: 2.49e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 625 AVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRI-LAAVTSAGHPFLVNLFGCFQTPEHVCFVMEY 703
Cdd:cd14102   6 SVLGSGGFGTVYAGSRIADGLPVAVKHVVKERVTEWGTLNGVMVPLEIvLLKKVGSGFRGVIKLLDWYERPDGFLIVMER 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 704 -SAGGDLMLHI-HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTE-GYVKIADFGlckEGMGYGDRTST 780
Cdd:cd14102  86 pEPVKDLFDFItEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDLRtGELKLIDFG---SGALLKDTVYT 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 781 -FCGTPEFLAPEVLTDTSY-TRAVDWWGLGVLLYEMLVGESPFPGDDEeevfdsIVNDEVRYPRFLSAEAIGIMRRLLRR 858
Cdd:cd14102 163 dFDGTRVYSPPEWIRYHRYhGRSATVWSLGVLLYDMVCGDIPFEQDEE------ILRGRLYFRRRVSPECQQLIKWCLSL 236

                ....*
gi 47132591 859 NPERR 863
Cdd:cd14102 237 RPSDR 241
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
621-863 2.54e-09

Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 58.86  E-value: 2.54e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKgdiVARDEVESlmceKRILAAVTS----AGHPFLVNLFGCFQTPEH 696
Cdd:cd14050   3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKRSRS---RFRGEKDR----KRKLEEVERheklGEHPNCVRFIKAWEEKGI 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 697 VCFVMEYSAGG-DLMLHIHSDVfSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEgMGYG 775
Cdd:cd14050  76 LYIQTELCDTSlQQYCEETHSL-PESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLVVE-LDKE 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 776 DRTSTFCGTPEFLAPEVLtDTSYTRAVDWWGLGVLLYEMLVG-ESPFPGDDEEEVFDSIVNDEVRYPrfLSAEAIGIMRR 854
Cdd:cd14050 154 DIHDAQEGDPRYMAPELL-QGSFTKAADIFSLGITILELACNlELPSGGDGWHQLRQGYLPEEFTAG--LSPELRSIIKL 230

                ....*....
gi 47132591 855 LLRRNPERR 863
Cdd:cd14050 231 MMDPDPERR 239
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
730-881 3.18e-09

Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 59.26  E-value: 3.18e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 730 VVLGLQFLHEH-KIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCG-----------TPEFLAPEVLTDTS 797
Cdd:cd14011 123 ISEALSFLHNDvKLVHGNICPESVVINSNGEWKLAGFDFCISSEQATDQFPYFREydpnlpplaqpNLNYLAPEYILSKT 202
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 798 YTRAVDWWGLGVLLYEMLV-GESPFPGDDEEEVFDSIVNdEVRYPRFLSAEAIG-----IMRRLLRRNPERRLgsserDA 871
Cdd:cd14011 203 CDPASDMFSLGVLIYAIYNkGKPLFDCVNNLLSYKKNSN-QLRQLSLSLLEKVPeelrdHVKTLLNVTPEVRP-----DA 276
                       170
                ....*....|
gi 47132591 872 EDVKKQPFFR 881
Cdd:cd14011 277 EQLSKIPFFD 286
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
627-868 3.20e-09

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 59.28  E-value: 3.20e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSE---FRPSGE--LFAIKALKKGDIVARDEVEslmcekRILAAVTSAGHPFLVNLFGCFQTPEHVCFVM 701
Cdd:cd05093  13 LGEGAFGKVFLAEcynLCPEQDkiLVAVKTLKDASDNARKDFH------REAELLTNLQHEHIVKFYGVCVEGDPLIMVF 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 702 EYSAGGDL--MLHIHSD------------VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGL 767
Cdd:cd05093  87 EYMKHGDLnkFLRAHGPdavlmaegnrpaELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGM 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 768 CKEGMGYG-DRTSTFCGTP-EFLAPEVLTDTSYTRAVDWWGLGVLLYEMLV-GESPFPGDDEEEVFDSIVNDEV-RYPRF 843
Cdd:cd05093 167 SRDVYSTDyYRVGGHTMLPiRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGRVlQRPRT 246
                       250       260
                ....*....|....*....|....*
gi 47132591 844 LSAEAIGIMRRLLRRNPERRLGSSE 868
Cdd:cd05093 247 CPKEVYDLMLGCWQREPHMRLNIKE 271
HR1_PKN_3 cd11625
Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
133-195 3.69e-09

Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N; PKN, also called Protein-kinase C-related kinase (PRK), is a serine/threonine protein kinase that can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytoskeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. In some vertebrates, there are three PKN isoforms from different genes (designated PKN1, PKN2, and PKN3), which show different enzymatic properties, tissue distribution, and varied functions. PKN proteins contain three HR1 domains, a C2 domain, and a kinase domain. This model characterizes the third HR1 domain of PKN. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family.


Pssm-ID: 212015  Cd Length: 74  Bit Score: 53.83  E-value: 3.69e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47132591 133 RVAGLEKQLAIELKVKQGAENMIQTYSNGSTKDRKLLLTAQQMLQDSKTKIDIIRMQLRRALQ 195
Cdd:cd11625  10 RIEELRHHLRVETAVVEGAKNVIKLLQNAKKDDKKALQEAQKSLSESSQKLDLLRLSLERRLA 72
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
622-841 4.23e-09

Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 58.54  E-value: 4.23e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 622 KFLAVLGRGHFGKVLLSEFRPSGE---LFAIKALKKGdIVARDEVESLMcEKRILAAVTsagHPFLVNLFGCFQTPEHVC 698
Cdd:cd05033   7 TIEKVIGGGEFGEVCSGSLKLPGKkeiDVAIKTLKSG-YSDKQRLDFLT-EASIMGQFD---HPNVIRLEGVVTKSRPVM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGGDL--MLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEgMGYGD 776
Cdd:cd05033  82 IVTEYMENGSLdkFLRENDGKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLSRR-LEDSE 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47132591 777 RTSTFCG--TP-EFLAPEVLTDTSYTRAVDWWGLGVLLYE-MLVGESPFPGDDEEEVFDSiVNDEVRYP 841
Cdd:cd05033 161 ATYTTKGgkIPiRWTAPEAIAYRKFTSASDVWSFGIVMWEvMSYGERPYWDMSNQDVIKA-VEDGYRLP 228
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
627-863 4.68e-09

Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Musk is a receptor PTK (RTK) containing an extracellular region with four immunoglobulin-like domains and a cysteine-rich cluster, a transmembrane segment, and an intracellular catalytic domain. Musk is expressed and concentrated in the postsynaptic membrane in skeletal muscle. It is essential for the establishment of the neuromuscular junction (NMJ), a peripheral synapse that conveys signals from motor neurons to muscle cells. Agrin, a large proteoglycan released from motor neurons, stimulates Musk autophosphorylation and activation, leading to the clustering of acetylcholine receptors (AChRs). To date, there is no evidence to suggest that agrin binds directly to Musk. Mutations in AChR, Musk and other partners are responsible for diseases of the NMJ, such as the autoimmune syndrome myasthenia gravis. The Musk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 58.69  E-value: 4.68e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVL------LSEFRPSgELFAIKALKKGdivARDEVEslMCEKRILAAVTSAGHPFLVNLFGCFQTPEHVCFV 700
Cdd:cd05050  13 IGQGAFGRVFqarapgLLPYEPF-TMVAVKMLKEE---ASADMQ--ADFQREAALMAEFDHPNIVKLLGVCAVGKPMCLL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGGDL---MLH-----IHSDVFSEPRAIFY---------------SACVVLGLQFLHEHKIVYRDLKLDNLLLDTE 757
Cdd:cd05050  87 FEYMAYGDLnefLRHrspraQCSLSHSTSSARKCglnplplscteqlciAKQVAAGMAYLSERKFVHRDLATRNCLVGEN 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 758 GYVKIADFGLCKEGMgygdrTSTFCGTPE-------FLAPEVLTDTSYTRAVDWWGLGVLLYEML-VGESPFPGDDEEEV 829
Cdd:cd05050 167 MVVKIADFGLSRNIY-----SADYYKASEndaipirWMPPESIFYNRYTTESDVWAYGVVLWEIFsYGMQPYYGMAHEEV 241
                       250       260       270
                ....*....|....*....|....*....|....*
gi 47132591 830 FDSIVNDEV-RYPRFLSAEAIGIMRRLLRRNPERR 863
Cdd:cd05050 242 IYYVRDGNVlSCPDNCPLELYNLMRLCWSKLPSDR 276
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
626-822 5.16e-09

Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Met and Ron are receptor PTKs (RTKs) composed of an alpha-beta heterodimer. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. Met binds to the ligand, hepatocyte growth factor/scatter factor (HGF/SF), and is also called the HGF receptor. HGF/Met signaling plays a role in growth, transformation, cell motility, invasion, metastasis, angiogenesis, wound healing, and tissue regeneration. Aberrant expression of Met through mutations or gene amplification is associated with many human cancers including hereditary papillary renal and gastric carcinomas. The ligand for Ron is macrophage stimulating protein (MSP). Ron signaling is important in regulating cell motility, adhesion, proliferation, and apoptosis. Aberrant Ron expression is implicated in tumorigenesis and metastasis. The Met/Ron subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 58.25  E-value: 5.16e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGEL---FAIKALKKgdIVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPE---HVcf 699
Cdd:cd05058   2 VIGKGHFGCVYHGTLIDSDGQkihCAVKSLNR--ITDIEEVEQFLKEGIIMKDFS---HPNVLSLLGICLPSEgspLV-- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYSAGGDLMLHIHSDVfSEPRA---IFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMG--- 773
Cdd:cd05058  75 VLPYMKHGDLRNFIRSET-HNPTVkdlIGFGLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLARDIYDkey 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 47132591 774 YGDRTSTFCGTP-EFLAPEVLTDTSYTRAVDWWGLGVLLYEMLV-GESPFP 822
Cdd:cd05058 154 YSVHNHTGAKLPvKWMALESLQTQKFTTKSDVWSFGVLLWELMTrGAPPYP 204
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
624-821 5.19e-09

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP2, also called RICK or CARDIAK, harbors a C-terminal Caspase Activation and Recruitment domain (CARD) belonging to the Death domain (DD) superfamily. It functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR) family, Nod1 and Nod2, which recognizes bacterial peptidoglycans released upon infection. RIP2 may also be involved in regulating wound healing and keratinocyte proliferation. RIP kinases serve as essential sensors of cellular stress. The RIP2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 58.39  E-value: 5.19e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 624 LAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAavtSAGHPFLVNLFGCFQTPEHVCFVMEY 703
Cdd:cd14026   2 LRYLSRGAFGTVSRARHADWRVTVAIKCLKLDSPVGDSERNCLLKEAEILH---KARFSYILPILGICNEPEFLGIVTEY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 704 SAGGDL--MLH---IHSDVFSEPR-AIFYSacVVLGLQFLHEHK--IVYRDLKLDNLLLDTEGYVKIADFGLCKEGM--- 772
Cdd:cd14026  79 MTNGSLneLLHekdIYPDVAWPLRlRILYE--IALGVNYLHNMSppLLHHDLKTQNILLDGEFHVKIADFGLSKWRQlsi 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 47132591 773 --GYGDRTSTFCGTPEFLAPEVLTDTSYTRAV---DWWGLGVLLYEMLVGESPF 821
Cdd:cd14026 157 sqSRSSKSAPEGGTIIYMPPEEYEPSQKRRASvkhDIYSYAIIMWEVLSRKIPF 210
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
622-863 7.14e-09

Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. CSF-1R, also called c-Fms, is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of CSF-1R to its ligand, CSF-1, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. It leads to increases in gene transcription and protein translation, and induces cytoskeletal remodeling. CSF-1R signaling leads to a variety of cellular responses including survival, proliferation, and differentiation of target cells. It plays an important role in innate immunity, tissue development and function, and the pathogenesis of some diseases including atherosclerosis and cancer. CSF-1R signaling is also implicated in mammary gland development during pregnancy and lactation. Aberrant CSF-1/CSF-1R expression correlates with tumor cell invasiveness, poor clinical prognosis, and bone metastasis in breast cancer. Although the structure of the human CSF-1R catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. The CSF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133237 [Multi-domain]  Cd Length: 374  Bit Score: 58.70  E-value: 7.14e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 622 KFLAVLGRGHFGKVLLSEFRPSGE-----LFAIKALKKGdiVARDEVESLMCEKRILAAVtsAGHPFLVNLFGCFQTPEH 696
Cdd:cd05106  41 QFGKTLGAGAFGKVVEATAFGLGKednvlRVAVKMLKAS--AHTDEREALMSELKILSHL--GQHKNIVNLLGACTHGGP 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 697 VCFVMEYSAGGDLM-----------------------------LHIH--------------SDVFSEPRAI--------- 724
Cdd:cd05106 117 VLVITEYCCYGDLLnflrkkaetflnfvmalpeisetssdyknITLEkkyirsdsgfssqgSDTYVEMRPVsssssqssd 196
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 725 -------------------FYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMgyGDRTSTFCGTP 785
Cdd:cd05106 197 skdeedtedswpldlddllRFSSQVAQGMDFLASKNCIHRDVAARNVLLTDGRVAKICDFGLARDIM--NDSNYVVKGNA 274
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 786 ----EFLAPEVLTDTSYTRAVDWWGLGVLLYEML-VGESPFPGDDEEEVFDSIVND--EVRYPRFLSAEAIGIMRRLLRR 858
Cdd:cd05106 275 rlpvKWMAPESIFDCVYTVQSDVWSYGILLWEIFsLGKSPYPGILVNSKFYKMVKRgyQMSRPDFAPPEIYSIMKMCWNL 354

                ....*
gi 47132591 859 NPERR 863
Cdd:cd05106 355 EPTER 359
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
624-823 8.08e-09

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-2 is also referred to as ALS2CR7 (amyotrophic lateral sclerosis 2 (juvenile) chromosome region candidate 7). It may be associated with amyotrophic lateral sclerosis 2 (ALS2), an autosomal recessive form of juvenile ALS. The function of PFTAIRE-2 is not yet known. It shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 58.05  E-value: 8.08e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 624 LAVLGRGHFGKVLLSEFRPSGELFAIKalkkgdivardeVESLMCEKRI-LAAVTSAG------HPFLVNLFGCFQTPEH 696
Cdd:cd07870   5 LEKLGEGSYATVYKGISRINGQLVALK------------VISMKTEEGVpFTAIREASllkglkHANIVLLHDIIHTKET 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 697 VCFVMEYsaggdlmlhIHSDV---FSEPRAIFYSACVVL-------GLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFG 766
Cdd:cd07870  73 LTFVFEY---------MHTDLaqyMIQHPGGLHPYNVRLfmfqllrGLAYIHGQHILHRDLKPQNLLISYLGELKLADFG 143
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 47132591 767 LCKEGMGYGDRTSTFCGTPEFLAPEVLT-DTSYTRAVDWWGLGVLLYEMLVGESPFPG 823
Cdd:cd07870 144 LARAKSIPSQTYSSEVVTLWYRPPDVLLgATDYSSALDIWGAGCIFIEMLQGQPAFPG 201
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
726-863 9.79e-09

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR beta is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR beta forms homodimers or heterodimers with PDGFR alpha, depending on the nature of the PDGF ligand. PDGF-BB and PDGF-DD induce PDGFR beta homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR beta signaling leads to a variety of cellular effects including the stimulation of cell growth and chemotaxis, as well as the inhibition of apoptosis and GAP junctional communication. It is critical in normal angiogenesis as it is involved in the recruitment of pericytes and smooth muscle cells essential for vessel stability. Aberrant PDGFR beta expression is associated with some human cancers. The continuously-active fusion proteins of PDGFR beta with COL1A1 and TEL are associated with dermatofibrosarcoma protuberans (DFSP) and a subset of chronic myelomonocytic leukemia (CMML), respectively. The PDGFR beta subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 58.48  E-value: 9.79e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 726 YSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGM---GYGDRTSTFCGTpEFLAPEVLTDTSYTRAV 802
Cdd:cd05107 244 FSYQVANGMEFLASKNCVHRDLAARNVLICEGKLVKICDFGLARDIMrdsNYISKGSTFLPL-KWMAPESIFNNLYTTLS 322
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47132591 803 DWWGLGVLLYEML-VGESPFPGDDEEEVFDSIVNDEVRY--PRFLSAEAIGIMRRLLRRNPERR 863
Cdd:cd05107 323 DVWSFGILLWEIFtLGGTPYPELPMNEQFYNAIKRGYRMakPAHASDEIYEIMQKCWEEKFEIR 386
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
626-883 9.93e-09

The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GSK3 is a mutifunctional kinase involved in many cellular processes including cell division, proliferation, differentiation, adhesion, and apoptosis. In plants, GSK3 plays a role in the response to osmotic stress. In Caenorhabditis elegans, it plays a role in regulating normal oocyte-to-embryo transition and response to oxidative stress. In Chlamydomonas reinhardtii, GSK3 regulates flagellar length and assembly. In mammals, there are two isoforms, GSK3alpha and GSK3beta, which show both distinct and redundant functions. The two isoforms differ mainly in their N-termini. They are both involved in axon formation and in Wnt signaling.They play distinct roles in cardiogenesis, with GSKalpha being essential in cardiomyocyte survival, and GSKbeta regulating heart positioning and left-right symmetry. GSK3beta was first identified as a regulator of glycogen synthesis, but has since been determined to play other roles. It regulates the degradation of beta-catenin and IkB. Beta-catenin is the main effector of Wnt, which is involved in normal haematopoiesis and stem cell function. IkB is a central inhibitor of NF-kB, which is critical in maintaining leukemic cell growth. GSK3beta is enriched in the brain and is involved in regulating neuronal signaling pathways. It is implicated in the pathogenesis of many diseases including Type II diabetes, obesity, mood disorders, Alzheimer's disease, osteoporosis, and some types of cancer, among others. The GSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 57.51  E-value: 9.93e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGELFAIK-ALKKGDIVARdEVESLmcekRILaavtsaGHPFLVNLFGCFQT----PEHVC-- 698
Cdd:cd14137  11 VIGSGSFGVVYQAKLLETGEVVAIKkVLQDKRYKNR-ELQIM----RRL------KHPNIVKLKYFFYSsgekKDEVYln 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEY--SAGGDLMLHiHSDVFSEPRAIF---YSACVVLGLQFLHEHKIVYR----------DLKldnllldteGYVKIA 763
Cdd:cd14137  80 LVMEYmpETLYRVIRH-YSKNKQTIPIIYvklYSYQLFRGLAYLHSLGICHRdikpqnllvdPET---------GVLKLC 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 764 DFGLCKEgMGYGDRTSTFCGTPEFLAPEVLTD-TSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVN------- 835
Cdd:cd14137 150 DFGSAKR-LVPGEPNVSYICSRYYRAPELIFGaTDYTTAIDIWSAGCVLAELLLGQPLFPGESSVDQLVEIIKvlgtptr 228
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 836 DEVRY----------------------PRFLSAEAIGIMRRLLRRNPERRLgsserDAEDVKKQPFFRTL 883
Cdd:cd14137 229 EQIKAmnpnytefkfpqikphpwekvfPKRTPPDAIDLLSKILVYNPSKRL-----TALEALAHPFFDEL 293
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
621-840 9.98e-09

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors including homeodomain proteins (Nkx and HOX families), Smad1-4, Pax6, c-Myb, AML1, the histone acetyltransferase p300, and the tumor repressor p53, among others. It regulates gene transcription during development and in DNA damage response (DDR), and mediates cell processes such as apoptosis, survival, differentiation, and proliferation. HIPK2 mediates apoptosis by phosphorylating and activating p53 during DDR, resulting in the activation of apoptotic genes. In the absence of p53, HIPK2 targets the anti-apoptotic corepressor C-terminal binding protein (CtBP), leading to CtBP's degradation and the promotion of apoptosis. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 58.18  E-value: 9.98e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEveslMCEKRILAAVT--SAGHPFLVNLFGCFQTPEHVC 698
Cdd:cd14227  17 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQG----QIEVSILARLSteSADDYNFVRAYECFQHKNHTC 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGgDLMLHIHSDVFSePRAIFY-------SACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGY-VKIADFGlcKE 770
Cdd:cd14227  93 LVFEMLEQ-NLYDFLKQNKFS-PLPLKYirpilqqVATALMKLKSLGLIHADLKPENIMLVDPSRQPYrVKVIDFG--SA 168
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 771 GMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEevfdsivnDEVRY 840
Cdd:cd14227 169 SHVSKAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEY--------DQIRY 230
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
617-880 1.04e-08

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 57.76  E-value: 1.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 617 TLED-FKFLAVLGRGHFGKVLlSEFRPSGELFAIKALKKGDIVARDE----VESLMC-EKRILAAVTsagHPFLVNLFGC 690
Cdd:cd14041   3 TLNDrYLLLHLLGRGGFSEVY-KAFDLTEQRYVAVKIHQLNKNWRDEkkenYHKHACrEYRIHKELD---HPRIVKLYDY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 691 FQ-TPEHVCFVMEYSAGGDLMLHI-HSDVFSEPRAIFYSACVVLGLQFLHEHK--IVY---RDLKLDNLLLDTEGYVKIA 763
Cdd:cd14041  79 FSlDTDSFCTVLEYCEGNDLDFYLkQHKLMSEKEARSIIMQIVNALKYLNEIKppIIHydlKPGNILLVNGTACGEIKIT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 764 DFGLCK--EGMGYG-----DRTSTFCGTPEFLAPEVLT----DTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVF-- 830
Cdd:cd14041 159 DFGLSKimDDDSYNsvdgmELTSQGAGTYWYLPPECFVvgkePPKISNKVDVWSVGVIFYQCLYGRKPFGHNQSQQDIlq 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 47132591 831 -DSIVN-DEVRYP--RFLSAEAIGIMRRLLRRNPERRLgsserDAEDVKKQPFF 880
Cdd:cd14041 239 eNTILKaTEVQFPpkPVVTPEAKAFIRRCLAYRKEDRI-----DVQQLACDPYL 287
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
627-863 1.15e-08

Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes a subset of Src-like PTKs including Src, Fyn, Yrk, and Yes, which are all widely expressed. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. They are also implicated in acute inflammatory responses and osteoclast function. The Src/Fyn-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 56.85  E-value: 1.15e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELfAIKALKKGDIVArdevESLMCEKRILAAVTsagHPFLVNLFGCFqTPEHVCFVMEYSAG 706
Cdd:cd14203   3 LGQGCFGEVWMGTWNGTTKV-AIKTLKPGTMSP----EAFLEEAQIMKKLR---HDKLVQLYAVV-SEEPIYIVTEFMSK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLMLHIHSD---VFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEgmgYGDRTSTFCG 783
Cdd:cd14203  74 GSLLDFLKDGegkYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARL---IEDNEYTARQ 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 784 TPEF----LAPEVLTDTSYTRAVDWWGLGVLLYEMLV-GESPFPGDDEEEVFDSIvndEVRY----PRFLSAEAIGIMRR 854
Cdd:cd14203 151 GAKFpikwTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQV---ERGYrmpcPPGCPESLHELMCQ 227

                ....*....
gi 47132591 855 LLRRNPERR 863
Cdd:cd14203 228 CWRKDPEER 236
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
629-868 1.16e-08

Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K8 is also called Tumor progression locus 2 (Tpl2) or Cancer Osaka thyroid (Cot), and was first identified as a proto-oncogene in T-cell lymphoma induced by MoMuL virus and in breast carcinoma induced by MMTV. Activated MAP3K8 induces various MAPK pathways including Extracellular Regulated Kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38. It plays a pivotal role in innate immunity, linking Toll-like receptors to the production of TNF and the activation of ERK in macrophages. It is also required in interleukin-1beta production and is critical in host defense against Gram-positive bacteria. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K8 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 56.94  E-value: 1.16e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 629 RGHFGKVLLSEFRPSGELFAIKALKKGDIVARDeVESLMCEKrilaavtsagHPFLVNLFGCFQTPEHVCFVMEYSAGGD 708
Cdd:cd13995  14 RGAFGKVYLAQDTKTKKRMACKLIPVEQFKPSD-VEIQACFR----------HENIAELYGALLWEETVHLFMEAGEGGS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 709 LMLHIHS-DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVkIADFGLC---KEGMGYgdrTSTFCGT 784
Cdd:cd13995  83 VLEKLEScGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAV-LVDFGLSvqmTEDVYV---PKDLRGT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 785 PEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDS---IVNDEVRYPRFLSAEAIGIMRRL----LR 857
Cdd:cd13995 159 EIYMSPEVILCRGHNTKADIYSLGATIIHMQTGSPPWVRRYPRSAYPSylyIIHKQAPPLEDIAQDCSPAMRELleaaLE 238
                       250
                ....*....|.
gi 47132591 858 RNPERRLGSSE 868
Cdd:cd13995 239 RNPNHRSSAAE 249
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
700-863 1.19e-08

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 58.65  E-value: 1.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  700 VMEYSAGGDLMLHIHSD-VFSEPRAIFYSACVVLGLQFLHEHKIVYRdlkldnllldTEGYVKIADFGLCK----EGMGY 774
Cdd:NF033483  85 VMEYVDGRTLKDYIREHgPLSPEEAVEIMIQILSALEHAHRNGIVHRdikpqnilitKDGRVKVTDFGIARalssTTMTQ 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  775 gdrTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDeeEVfdSI----VNDEVRYPRFL------ 844
Cdd:NF033483 165 ---TNSVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFDGDS--PV--SVaykhVQEDPPPPSELnpgipq 237
                        170
                 ....*....|....*....
gi 47132591  845 SAEAIgIMrRLLRRNPERR 863
Cdd:NF033483 238 SLDAV-VL-KATAKDPDDR 254
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
733-842 1.23e-08

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 partners with all three D-type cyclins (D1, D2, and D3) and is also regulated by INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein and plays a role in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the nucleus. CDK4 also shows kinase activity towards Smad3, a signal transducer of TGF-beta signaling which modulates transcription and plays a role in cell proliferation and apoptosis. CDK4 is inhibited by the p21 inhibitor and is specifically mutated in human melanoma. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 57.28  E-value: 1.23e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 733 GLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEgMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLY 812
Cdd:cd07863 120 GLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLARI-YSCQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFA 198
                        90       100       110
                ....*....|....*....|....*....|....*
gi 47132591 813 EMLVGESPFPGDDEEE----VFDSI-VNDEVRYPR 842
Cdd:cd07863 199 EMFRRKPLFCGNSEADqlgkIFDLIgLPPEDDWPR 233
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
621-826 1.37e-08

Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and -Regulated Kinases 2 and 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of DYRK2 and DYRK3, and similar proteins. Drosophila DYRK2 interacts and phosphorylates the chromatin remodelling factor, SNR1 (Snf5-related 1), and also interacts with the essential chromatin component, trithorax. It may play a role in chromatin remodelling. Vertebrate DYRK2 phosphorylates and regulates the tumor suppressor p53 to induce apoptosis in response to DNA damage. It can also phosphorylate the transcription factor, nuclear factor of activated T cells (NFAT). DYRK2 is overexpressed in lung adenocarcinoma and esophageal carcinomas, and is a predictor for favorable prognosis in lung adenocarcinoma. DYRK3, also called regulatory erythroid kinase (REDK), is highly expressed in erythroid cells and the testis, and is also present in adult kidney and liver. It promotes cell survival by phosphorylating and activating SIRT1, an NAD(+)-dependent protein deacetylase, which promotes p53 deacetylation, resulting in the inhibition of apoptosis. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other S/T kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 57.83  E-value: 1.37e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVEslmcEKRILAAVT---SAGHPFLVNLFGCFQTPEHV 697
Cdd:cd14224  67 YEVLKVIGKGSFGQVVKAYDHKTHQHVALKMVRNEKRFHRQAAE----EIRILEHLKkqdKDNTMNVIHMLESFTFRNHI 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 698 CFVMEYsaggdLMLHIHSDV-------FSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGY--VKIADFGL- 767
Cdd:cd14224 143 CMTFEL-----LSMNLYELIkknkfqgFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRsgIKVIDFGSs 217
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 47132591 768 CKEGmgygDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDE 826
Cdd:cd14224 218 CYEH----QRIYTYIQSRFYRAPEVILGARYGMPIDMWSFGCILAELLTGYPLFPGEDE 272
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
618-864 1.66e-08

Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Trk subfamily consists of TrkA, TrkB, TrkC, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, the nerve growth factor (NGF) family of neutrotrophins, leads to Trk receptor oligomerization and activation of the catalytic domain. Trk receptors are mainly expressed in the peripheral and central nervous systems. They play important roles in cell fate determination, neuronal survival and differentiation, as well as in the regulation of synaptic plasticity. Altered expression of Trk receptors is associated with many human diseases. The Trk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 56.71  E-value: 1.66e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 618 LEDFKFLAVLGRGHFGKVLLSEFR---PSGE--LFAIKALKKG-DIVARDEVESlmcEKRILAAVTsagHPFLVNLFGCF 691
Cdd:cd05049   4 RDTIVLKRELGEGAFGKVFLGECYnlePEQDkmLVAVKTLKDAsSPDARKDFER---EAELLTNLQ---HENIVKFYGVC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 692 QTPEHVCFVMEYSAGGDL--MLHIHSD----VFSEPRAIF---------YSACVVLGLQFLHEHKIVYRDLKLDNLLLDT 756
Cdd:cd05049  78 TEGDPLLMVFEYMEHGDLnkFLRSHGPdaafLASEDSAPGeltlsqllhIAVQIASGMVYLASQHFVHRDLATRNCLVGT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 757 EGYVKIADFGLCKEgmGYGDRTSTFCGTP----EFLAPEVLTDTSYTRAVDWWGLGVLLYEMLV-GESPFPGDDEEEVFD 831
Cdd:cd05049 158 NLVVKIGDFGMSRD--IYSTDYYRVGGHTmlpiRWMPPESILYRKFTTESDVWSFGVVLWEIFTyGKQPWFQLSNTEVIE 235
                       250       260       270
                ....*....|....*....|....*....|....
gi 47132591 832 SIVNDEV-RYPRFLSAEAIGIMRRLLRRNPERRL 864
Cdd:cd05049 236 CITQGRLlQRPRTCPSEVYAVMLGCWKREPQQRL 269
HR1_Ste20-like cd11627
Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of ...
128-195 1.68e-08

Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Schizosaccharomyces pombe Ste20-like proteins; This group is composed of predominantly uncharacterized fungal proteins, which contain two known domains: HR1 at the N-terminal region and REM (Ras exchanger motif) at the C-terminal region. One member protein from Schizosaccharomyces pombe is named Ste16 while its gene is called ste20 (a target of rapamycin complex 2 subunit). It is a subunit in the protein kinase TOR complexes in fission yeast. The REM domain is usually found in nucleotide exchange factors for Ras-like small GTPases. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family.


Pssm-ID: 212017 [Multi-domain]  Cd Length: 71  Bit Score: 51.99  E-value: 1.68e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47132591 128 ATNLSRVAGLEKQLAIELKVKQGAENMIQTYSNGSTKDRKLL-LTAQQMLQDSKTKIDIIRMQLRRALQ 195
Cdd:cd11627   1 LVSEQRLEELRGKLEIETKIKDGAENLLQVLDSKNAKEKKDQrARVESELNSSNRKIAQLTSQLEEEIQ 69
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
620-868 2.03e-08

Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1a subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 56.57  E-value: 2.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLmceKRILAAVTSAGHPFLVNLFGCFQTPEHVCF 699
Cdd:cd14138   6 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNAL---REVYAHAVLGQHSHVVRYYSAWAEDDHMLI 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYSAGGDLMLHIHSD-----VFSEPRAIFYSACVVLGLQFLHEHKIVYR---------DLKLDNLLLDTEGY------ 759
Cdd:cd14138  83 QNEYCNGGSLADAISENyrimsYFTEPELKDLLLQVARGLKYIHSMSLVHMdikpsnifiSRTSIPNAASEEGDedewas 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 760 ----VKIADfglckegMGYGDRTSTFC---GTPEFLAPEVLT-DTSYTRAVDWWGLGVLLYEMlVGESPFP--GDDEEEV 829
Cdd:cd14138 163 nkviFKIGD-------LGHVTRVSSPQveeGDSRFLANEVLQeNYTHLPKADIFALALTVVCA-AGAEPLPtnGDQWHEI 234
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 47132591 830 FDSIVNdevRYPRFLSAEAIGIMRRLLRRNPERRLGSSE 868
Cdd:cd14138 235 RQGKLP---RIPQVLSQEFLDLLKVMIHPDPERRPSAVA 270
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
627-831 2.16e-08

Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). The TEL gene is a frequent fusion partner of other tyr kinase oncogenes, including Tel/Abl, Tel/PDGFRbeta, and Tel/Jak2, found in patients with leukemia and myeloproliferative disorders. The Abl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 56.28  E-value: 2.16e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKGDIvardEVESLMCEKRILAAVTsagHPFLVNLFG-CFQTPEHVcFVMEYSA 705
Cdd:cd05052  14 LGGGQYGEVYEGVWKKYNLTVAVKTLKEDTM----EVEEFLKEAAVMKEIK---HPNLVQLLGvCTREPPFY-IITEFMP 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 706 GGDLMLHIHSDVFSE--PRAIFYSAC-VVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKegMGYGDRTSTFC 782
Cdd:cd05052  86 YGNLLDYLRECNREElnAVVLLYMATqIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSR--LMTGDTYTAHA 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 47132591 783 GTP---EFLAPEVLTDTSYTRAVDWWGLGVLLYEMLV-GESPFPGDDEEEVFD 831
Cdd:cd05052 164 GAKfpiKWTAPESLAYNKFSIKSDVWAFGVLLWEIATyGMSPYPGIDLSQVYE 216
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
622-836 2.34e-08

Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EphB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphB receptors play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphBs are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion. The EphB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 56.42  E-value: 2.34e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 622 KFLAVLGRGHFGKVLLSEFRPSG--ELF-AIKALKKGdiVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVC 698
Cdd:cd05065   7 KIEEVIGAGEFGEVCRGRLKLPGkrEIFvAIKTLKSG--YTEKQRRDFLSEASIMGQFD---HPNIIHLEGVVTKSRPVM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGG--DLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK---EGMG 773
Cdd:cd05065  82 IITEFMENGalDSFLRQNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRfleDDTS 161
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47132591 774 YGDRTSTFCGT-P-EFLAPEVLTDTSYTRAVDWWGLGVLLYE-MLVGESPFPGDDEEEVFDSIVND 836
Cdd:cd05065 162 DPTYTSSLGGKiPiRWTAPEAIAYRKFTSASDVWSYGIVMWEvMSYGERPYWDMSNQDVINAIEQD 227
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
619-833 2.39e-08

Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fyn and Yrk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Fyn/Yrk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase.


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 56.23  E-value: 2.39e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELfAIKALKKGDIVArdevESLMCEKRILAAVTsagHPFLVNLFGCFqTPEHVC 698
Cdd:cd05070   9 ESLQLIKRLGNGQFGEVWMGTWNGNTKV-AIKTLKPGTMSP----ESFLEEAQIMKKLK---HDKLVQLYAVV-SEEPIY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGGDLMLHI---HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK--EGMG 773
Cdd:cd05070  80 IVTEYMSKGSLLDFLkdgEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARliEDNE 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47132591 774 YGDRTSTFCGTpEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLV-GESPFPGDDEEEVFDSI 833
Cdd:cd05070 160 YTARQGAKFPI-KWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQV 219
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
623-842 2.41e-08

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk1 (or simply Aatyk) is also called lemur tyrosine kinase 1 (Lmtk1). It is a cytoplasmic (or nonreceptor) kinase containing a long C-terminal region. The expression of Aatyk1 is upregulated during growth arrest and apoptosis in myeloid cells. Aatyk1 has been implicated in neural differentiation, and is a regulator of the Na-K-2Cl cotransporter, a membrane protein involved in cell proliferation and survival, epithelial transport, and blood pressure control. The Aatyk1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 56.15  E-value: 2.41e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 623 FLAVLGRGHFGKVLLSEFRP--SGELFAIKALKKGDIVaRDEVESLMcEKRILAAVTSagHPFLVNLFGCFQTPEHVcFV 700
Cdd:cd05087   1 YLKEIGHGWFGKVFLGEVNSglSSTQVVVKELKASASV-QDQMQFLE-EAQPYRALQH--TNLLQCLAQCAEVTPYL-LV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGGDLMLHIHS-----DVFSEPRAIFYSAC-VVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGL--CKEGM 772
Cdd:cd05087  76 MEFCPLGDLKGYLRScraaeSMAPDPLTLQRMACeVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGLshCKYKE 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47132591 773 GYGDRTSTFCGTPEFLAPEVLTD-------TSYTRAVDWWGLGVLLYEML-VGESPFPGDDEEEVFDSIVND-EVRYPR 842
Cdd:cd05087 156 DYFVTADQLWVPLRWIAPELVDEvhgnllvVDQTKQSNVWSLGVTIWELFeLGNQPYRHYSDRQVLTYTVREqQLKLPK 234
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
620-898 2.69e-08

Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER2 (ErbB2, HER2/neu) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER2 does not bind to any known EGFR subfamily ligands, but contributes to the kinase activity of all possible heterodimers. It acts as the preferred partner of other ligand-bound EGFR proteins and functions as a signal amplifier, with the HER2-HER3 heterodimer being the most potent pair in mitogenic signaling. HER2 plays an important role in cell development, proliferation, survival and motility. Overexpression of HER2 results in its activation and downstream signaling, even in the absence of ligand. HER2 overexpression, mainly due to gene amplification, has been shown in a variety of human cancers. Its role in breast cancer is especially well-documented. HER2 is up-regulated in about 25% of breast tumors and is associated with increases in tumor aggressiveness, recurrence and mortality. HER2 is a target for monoclonal antibodies and small molecule inhibitors, which are being developed as treatments for cancer. The first humanized antibody approved for clinical use is Trastuzumab (Herceptin), which is being used in combination with other therapies to improve the survival rates of patients with HER2-overexpressing breast cancer. The HER2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 56.19  E-value: 2.69e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 620 DFKFLAVLGRGHFGKVLLSEFRPSGE----LFAIKALKKGdiVARDEVESLMCEKRILAAVtsaGHPFLVNLFG-CF-QT 693
Cdd:cd05109   8 ELKKVKVLGSGAFGTVYKGIWIPDGEnvkiPVAIKVLREN--TSPKANKEILDEAYVMAGV---GSPYVCRLLGiCLtST 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 694 PEHVCFVMEYsagGDLMLHIHSDVFSEPRAIFYSACVVL--GLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLC--- 768
Cdd:cd05109  83 VQLVTQLMPY---GCLLDYVRENKDRIGSQDLLNWCVQIakGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLArll 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 769 ----KEGMGYGDRTSTfcgtpEFLAPEVLTDTSYTRAVDWWGLGVLLYE-MLVGESPFPGDDEEEVFDSIVNDE-VRYPR 842
Cdd:cd05109 160 dideTEYHADGGKVPI-----KWMALESILHRRFTHQSDVWSYGVTVWElMTFGAKPYDGIPAREIPDLLEKGErLPQPP 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 47132591 843 FLSAEAIGIMRRLLRRNPERRlgsserdaedvkkqPFFRTLGWEALLARRLPPPFV 898
Cdd:cd05109 235 ICTIDVYMIMVKCWMIDSECR--------------PRFRELVDEFSRMARDPSRFV 276
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
619-841 2.78e-08

Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) PTK that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy. The FAK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 56.28  E-value: 2.78e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEF-RPSGELF--AIKALKKGDivARDEVESLMCEKRILAAVTsagHPFLVNLFG-CFQTP 694
Cdd:cd05056   6 EDITLGRCIGEGQFGDVYQGVYmSPENEKIavAVKTCKNCT--SPSVREKFLQEAYIMRQFD---HPHIVKLIGvITENP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 695 ehVCFVMEYSAGGDL--MLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKegm 772
Cdd:cd05056  81 --VWIVMELAPLGELrsYLQVNKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSR--- 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47132591 773 gYGDRTSTFCGT----P-EFLAPEVLTDTSYTRAVDWWGLGVLLYEMLV-GESPFPGDDEEEVFDSIVNDEvRYP 841
Cdd:cd05056 156 -YMEDESYYKASkgklPiKWMAPESINFRRFTSASDVWMFGVCMWEILMlGVKPFQGVKNNDVIGRIENGE-RLP 228
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
706-825 2.83e-08

Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase (also called MAPK11); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38beta/MAPK11 is widely expressed in tissues and shows more similarity with p38alpha than with the other isoforms. Both are sensitive to pyridinylimidazoles and share some common substrates such as MAPK activated protein kinase 2 (MK2) and the transcription factors ATF2, c-Fos and, ELK-1. p38beta is involved in regulating the activation of the cyclooxygenase-2 promoter and the expression of TGFbeta-induced alpha-smooth muscle cell actin. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 56.60  E-value: 2.83e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 706 GGDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGmgyGDRTSTFCGTP 785
Cdd:cd07878 103 GADLNNIVKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLARQA---DDEMTGYVATR 179
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 47132591 786 EFLAPEVLTD-TSYTRAVDWWGLGVLLYEMLVGESPFPGDD 825
Cdd:cd07878 180 WYRAPEIMLNwMHYNQTVDIWSVGCIMAELLKGKALFPGND 220
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
621-883 3.32e-08

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 56.97  E-value: 3.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALkkgdivardeVESLMCEKRILAAVTSAGHP---FLVNLF--GCFQTPE 695
Cdd:PTZ00036  68 YKLGNIIGNGSFGVVYEAICIDTSEKVAIKKV----------LQDPQYKNRELLIMKNLNHIniiFLKDYYytECFKKNE 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  696 HVCF---VMEY--SAGGDLMLHIHSDVFSEPRAI--FYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGY-VKIADFGL 767
Cdd:PTZ00036 138 KNIFlnvVMEFipQTVHKYMKHYARNNHALPLFLvkLYSYQLCRALAYIHSKFICHRDLKPQNLLIDPNTHtLKLCDFGS 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  768 CKEGMGyGDRTSTFCGTPEFLAPEV-LTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDD----------------EEEV- 829
Cdd:PTZ00036 218 AKNLLA-GQRSVSYICSRFYRAPELmLGATNYTTHIDLWSLGCIIAEMILGYPIFSGQSsvdqlvriiqvlgtptEDQLk 296
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47132591  830 ----------FDSIVNDEVR--YPRFLSAEAIGIMRRLLRRNPERRLGSSERDAEdvkkqPFFRTL 883
Cdd:PTZ00036 297 emnpnyadikFPDVKPKDLKkvFPKGTPDDAINFISQFLKYEPLKRLNPIEALAD-----PFFDDL 357
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
627-873 4.22e-08

Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases Sty1 and Hog1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs Sty1 from Schizosaccharomyces pombe, Hog1 from Saccharomyces cerevisiae, and similar proteins. Sty1 and Hog1 are stress-activated MAPKs that partipate in transcriptional regulation in response to stress. Sty1 is activated in response to oxidative stress, osmotic stress, and UV radiation. It is regulated by the MAP2K Wis1, which is activated by the MAP3Ks Wis4 and Win1, which receive signals of the stress condition from membrane-spanning histidine kinases Mak1-3. Activated Sty1 stabilizes the Atf1 transcription factor and induces transcription of Atf1-dependent genes of the core environmetal stress response. Hog1 is the key element in the high osmolarity glycerol (HOG) pathway and is activated upon hyperosmotic stress. Activated Hog1 accumulates in the nucleus and regulates stress-induced transcription. The HOG pathway is mediated by two transmembrane osmosensors, Sln1 and Sho1. MAPKs are important mediators of cellular responses to extracellular signals. The Sty1/Hog1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 56.04  E-value: 4.22e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKK---GDIVARDEVESLMCEKRILaavtsagHPFLVNLFGCFQTP-EHVCFVME 702
Cdd:cd07856  18 VGMGAFGLVCSARDQLTGQNVAVKKIMKpfsTPVLAKRTYRELKLLKHLR-------HENIISLSDIFISPlEDIYFVTE 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 703 YsAGGDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK----EGMGYgdrt 778
Cdd:cd07856  91 L-LGTDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLARiqdpQMTGY---- 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 779 stfCGTPEFLAPEV-LTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDE---------------EEVFDSIVNDEV---- 838
Cdd:cd07856 166 ---VSTRYYRAPEImLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDHvnqfsiitellgtppDDVINTICSENTlrfv 242
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 47132591 839 -------RYP---RFLSAE--AIGIMRRLLRRNPERRLGSSERDAED 873
Cdd:cd07856 243 qslpkreRVPfseKFKNADpdAIDLLEKMLVFDPKKRISAAEALAHP 289
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
627-821 4.39e-08

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK4 plays a critical role in NFkB activation by its interaction with MyD88, which acts as a scaffold that enables IRAK4 to phosphorylate and activate IRAK1 and/or IRAK2. It also plays an important role in type I IFN production induced by TLR7/8/9. The IRAK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 55.58  E-value: 4.39e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFrpSGELFAIKALKK-GDIVARDEVESLMCEKRILAavtSAGHPFLVNLFGCFQTPEHVCFVMEYSA 705
Cdd:cd14158  23 LGEGGFGVVFKGYI--NDKNVAVKKLAAmVDISTEDLTKQFEQEIQVMA---KCQHENLVELLGYSCDGPQLCLVYTYMP 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 706 GGDLM--LHIHSDVfsePRAIFYSACVVL-----GLQFLHEHKIVYRdLKLDNLLLDTEGYV-KIADFGLCKEGMGYGD- 776
Cdd:cd14158  98 NGSLLdrLACLNDT---PPLSWHMRCKIAqgtanGINYLHENNHIHR-DIKSANILLDETFVpKISDFGLARASEKFSQt 173
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 47132591 777 -RTSTFCGTPEFLAPEVLTDtSYTRAVDWWGLGVLLYEMLVGESPF 821
Cdd:cd14158 174 iMTERIVGTTAYMAPEALRG-EITPKSDIFSFGVVLLEIITGLPPV 218
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
624-821 4.94e-08

Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A-Raf cooperates with C-Raf in regulating ERK transient phosphorylation that is associated with cyclin D expression and cell cycle progression. Mice deficient in A-Raf are born alive but show neurological and intestinal defects. A-Raf demonstrates low kinase activity to MEK, compared with B- and C-Raf, and may also have alternative functions other than in the ERK signaling cascade. It regulates the M2 type pyruvate kinase, a key glycolytic enzyme. It also plays a role in endocytic membrane trafficking. A-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The A-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 55.41  E-value: 4.94e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 624 LAVLGRGHFGKVLLSEFRpsGELfAIKALKkgdiVARDEVESLMCEKRILAAVTSAGHpflVN--LFGCFQTPEHVCFVM 701
Cdd:cd14150   5 LKRIGTGSFGTVFRGKWH--GDV-AVKILK----VTEPTPEQLQAFKNEMQVLRKTRH---VNilLFMGFMTRPNFAIIT 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 702 EYSAGGDLMLHIH--SDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLC--KEGMGYGDR 777
Cdd:cd14150  75 QWCEGSSLYRHLHvtETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLAtvKTRWSGSQQ 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 47132591 778 TSTFCGTPEFLAPEV--LTDTS-YTRAVDWWGLGVLLYEMLVGESPF 821
Cdd:cd14150 155 VEQPSGSILWMAPEVirMQDTNpYSFQSDVYAYGVVLYELMSGTLPY 201
HR1_PKN3_3 cd11637
Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
123-196 5.68e-08

Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N3; PKN3, also called PKNbeta, is a serine/threonine protein kinase that is activated by the Rho family of small GTPases, preferentially by RhoC. Both PKN1 and RhoC show limited and barely detectable expression in normal tissues, but are both upregulated in cancer cells, particularly in late-stage malignancies. PKN3 has been implicated to play a role in the metastatic growth and invasiveness of cancer cells, downstream of the oncogenic phosphoinositide 3-kinase signaling network. PKN3 shares a common domain architecture with other PKNs, containing three HR1 domains, a C2 domain, and a kinase domain. In addition, PKN3 contains two proline-rich regions between its C2 and kinase domains, and has been shown to associate with SH3 domain containing proteins like GRAFs, GAP for RhoA, and Cdc42Hs. This model characterizes the third HR1 domain of PKN3. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; PKN3 binds Rho family GTPases, preferentially RhoC.


Pssm-ID: 212027  Cd Length: 74  Bit Score: 50.63  E-value: 5.68e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47132591 123 GPTCSATNLsRVAGLEKQLAIELKVKQGAENMIQTYSNGSTKDRKLLLTAQQMLQDSKTKIDIIRMQLRRALQA 196
Cdd:cd11637   1 GRPMSAPEL-RVEELRHHLRIEAAVAEGAKNVVKLLGGRRFQDRKILAEAQARLQESSQKIDLLRLSLERCLAA 73
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
621-840 5.86e-08

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK1 has been implicated in regulating eye size, lens formation, and retinal morphogenesis during late embryogenesis. It also contributes to the regulation of haematopoiesis and leukaemogenesis by phosphorylating and repressing the transcription factor c-Myb, which is crucial in T- and B-cell development. In glucose-deprived conditions, HIPK1 phosphorylates Daxx, leading to its relocalization from the nucleus to the cytoplasm, where it binds and stabilizes ASK1 (apoptosis signal-regulating kinase 1), a mitogen-activated protein kinase (MAPK) kinase kinase that activates the JNK and p38 MAPK pathways. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 55.87  E-value: 5.86e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEveslMCEKRILAAVTS--AGHPFLVNLFGCFQTPEHVC 698
Cdd:cd14228  17 YEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQG----QIEVSILSRLSSenADEYNFVRSYECFQHKNHTC 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGgDLMLHIHSDVFSePRAIFY-------SACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGY-VKIADFGlcKE 770
Cdd:cd14228  93 LVFEMLEQ-NLYDFLKQNKFS-PLPLKYirpilqqVATALMKLKSLGLIHADLKPENIMLVDPVRQPYrVKVIDFG--SA 168
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 771 GMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEevfdsivnDEVRY 840
Cdd:cd14228 169 SHVSKAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEY--------DQIRY 230
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
624-880 6.45e-08

Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase (also called MAPK13); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38delta/MAPK13 is found in skeletal muscle, heart, lung, testis, pancreas, and small intestine. It regulates microtubule function by phosphorylating Tau. It activates the c-jun promoter and plays a role in G2 cell cycle arrest. It also controls the degration of c-Myb, which is associated with myeloid leukemia and poor prognosis in colorectal cancer. p38delta is the main isoform involved in regulating the differentiation and apoptosis of keratinocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 55.68  E-value: 6.45e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 624 LAVLGRGHFGKVLLSEFRPSGELFAIKALKK---GDIVARDEVESLMCEK--------RILAAVTSA--GHPFlvnlfgc 690
Cdd:cd07879  20 LKQVGSGAYGSVCSAIDKRTGEKVAIKKLSRpfqSEIFAKRAYRELTLLKhmqhenviGLLDVFTSAvsGDEF------- 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 691 fqtpEHVCFVMEYSAGgDLMlHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKe 770
Cdd:cd07879  93 ----QDFYLVMPYMQT-DLQ-KIMGHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLAR- 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 771 gmgYGDRTST-FCGTPEFLAPEVLTD-TSYTRAVDWWGLGVLLYEMLVGESPF------------------PGDDEEEVF 830
Cdd:cd07879 166 ---HADAEMTgYVVTRWYRAPEVILNwMHYNQTVDIWSVGCIMAEMLTGKTLFkgkdyldqltqilkvtgvPGPEFVQKL 242
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47132591 831 DSI-----VNDEVRYPR--------FLSAEAIGIMRRLLRRNPERRLGSSE----------RDAEDVKKQPFF 880
Cdd:cd07879 243 EDKaaksyIKSLPKYPRkdfstlfpKASPQAVDLLEKMLELDVDKRLTATEalehpyfdsfRDADEETEQQPY 315
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
618-821 6.99e-08

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 56.67  E-value: 6.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591   618 LEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARdEVESLMCEKRILAAVTsagHPFLVNLFGCF--QTPE 695
Cdd:PTZ00266   12 LNEYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISYRGLKER-EKSQLVIEVNVMRELK---HKNIVRYIDRFlnKANQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591   696 HVCFVMEYSAGGDLMLHIHS--DVFSEpraIFYSACVVLGLQFLHE-------------HKIVYRDLKLDNLLLDT---- 756
Cdd:PTZ00266   88 KLYILMEFCDAGDLSRNIQKcyKMFGK---IEEHAIVDITRQLLHAlaychnlkdgpngERVLHRDLKPQNIFLSTgirh 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591   757 -------------EGYVKIADFGLCKEgMGYGDRTSTFCGTPEFLAPEVL--TDTSYTRAVDWWGLGVLLYEMLVGESPF 821
Cdd:PTZ00266  165 igkitaqannlngRPIAKIGDFGLSKN-IGIESMAHSCVGTPYYWSPELLlhETKSYDDKSDMWALGCIIYELCSGKTPF 243
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
617-833 8.72e-08

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 54.68  E-value: 8.72e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 617 TLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKgdIVarDEVEslmcEKRIL----AAVTSAGHPFLVNLFGCFQ 692
Cdd:cd06616   4 TAEDLKDLGEIGRGAFGTVNKMLHKPSGTIMAVKRIRS--TV--DEKE----QKRLLmdldVVMRSSDCPYIVKFYGALF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 693 TpEHVCFV-MEysaggdLMlHIHSDVFSE----------PRAIF--YSACVVLGLQFL-HEHKIVYRDLKLDNLLLDTEG 758
Cdd:cd06616  76 R-EGDCWIcME------LM-DISLDKFYKyvyevldsviPEEILgkIAVATVKALNYLkEELKIIHRDVKPSNILLDRNG 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 759 YVKIADFGLCkegmgyGDRTSTFCGTPE-----FLAPEVLtDTSYTRA-----VDWWGLGVLLYEMLVGESPFPGDDeeE 828
Cdd:cd06616 148 NIKLCDFGIS------GQLVDSIAKTRDagcrpYMAPERI-DPSASRDgydvrSDVWSLGITLYEVATGKFPYPKWN--S 218

                ....*
gi 47132591 829 VFDSI 833
Cdd:cd06616 219 VFDQL 223
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
681-822 8.81e-08

Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Dusty protein kinase is also called Receptor-interacting protein kinase 5 (RIPK5 or RIP5) or RIP-homologous kinase. It is widely distributed in the central nervous system, and may be involved in inducing both caspase-dependent and caspase-independent cell death. The Dusty subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 54.42  E-value: 8.81e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 681 HPFLVNLFGCfqtpehvcfVMEYSAGGD-------LMLHIHSDVFSEPRA-------IFYSACVVLGLQFLHEHKIVYRD 746
Cdd:cd13975  57 HERIVSLHGS---------VIDYSYGGGssiavllIMERLHRDLYTGIKAglsleerLQIALDVVEGIRFLHSQGLVHRD 127
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47132591 747 LKLDNLLLDTEGYVKIADFGLCK-EGMGYGdrtsTFCGTPEFLAPEVLTDtSYTRAVDWWGLGVLLYEMLVGESPFP 822
Cdd:cd13975 128 IKLKNVLLDKKNRAKITDLGFCKpEAMMSG----SIVGTPIHMAPELFSG-KYDNSVDVYAFGILFWYLCAGHVKLP 199
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
626-833 9.22e-08

Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). EphRs contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 54.49  E-value: 9.22e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGE---LFAIKALKKG--DIVARDevesLMCEKRILAAVTsagHPFLVNLFGCFQTPEHVCFV 700
Cdd:cd05066  11 VIGAGEFGEVCSGRLKLPGKreiPVAIKTLKAGytEKQRRD----FLSEASIMGQFD---HPNIIHLEGVVTRSKPVMIV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGG--DLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK--EGMGYGD 776
Cdd:cd05066  84 TEYMENGslDAFLRKHDGQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRvlEDDPEAA 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 47132591 777 RTSTFCGTP-EFLAPEVLTDTSYTRAVDWWGLGVLLYE-MLVGESPFPGDDEEEVFDSI 833
Cdd:cd05066 164 YTTRGGKIPiRWTAPEAIAYRKFTSASDVWSYGIVMWEvMSYGERPYWEMSNQDVIKAI 222
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
627-823 9.89e-08

Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Raf kinases act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain, and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. The Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 54.32  E-value: 9.89e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVllseFRpsGELFAIKALKKGDIVARDEvESLMCEKRILAAVTSAGHPFLVNLFGCFQTPEhVCFVMEYSAG 706
Cdd:cd14062   1 IGSGSFGTV----YK--GRWHGDVAVKKLNVTDPTP-SQLQAFKNEVAVLRKTRHVNILLFMGYMTKPQ-LAIVTQWCEG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLMLHIH-SDVFSEPRAIFYSA-CVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLC--KEGMGYGDRTSTFC 782
Cdd:cd14062  73 SSLYKHLHvLETKFEMLQLIDIArQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLAtvKTRWSGSQQFEQPT 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 47132591 783 GTPEFLAPEVL---TDTSYTRAVDWWGLGVLLYEMLVGESPFPG 823
Cdd:cd14062 153 GSILWMAPEVIrmqDENPYSFQSDVYAFGIVLYELLTGQLPYSH 196
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
694-815 1.05e-07

Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 54.87  E-value: 1.05e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 694 PEHVC---FVMEYSAGGDLMLHIHSDvfSEPRAIFYSACVVLG--LQFLHEHKIVYRDLKLDN---LLLDTEGYVKIADF 765
Cdd:cd13977 104 PRSACylwFVMEFCDGGDMNEYLLSR--RPDRQTNTSFMLQLSsaLAFLHRNQIVHRDLKPDNiliSHKRGEPILKVADF 181
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47132591 766 GLCKEGMGYGDRT-----------STFCGTPEFLAPEVLtDTSYTRAVDWWGLGVLLYEML 815
Cdd:cd13977 182 GLSKVCSGSGLNPeepanvnkhflSSACGSDFYMAPEVW-EGHYTAKADIFALGIIIWAMV 241
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
619-863 1.38e-07

Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. InsR is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the insulin ligand to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR signaling plays an important role in many cellular processes including glucose homeostasis, glycogen synthesis, lipid and protein metabolism, ion and amino acid transport, cell cycle and proliferation, cell differentiation, gene transcription, and nitric oxide synthesis. Insulin resistance, caused by abnormalities in InsR signaling, has been described in diabetes, hypertension, cardiovascular disease, metabolic syndrome, heart failure, and female infertility. The InsR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 54.20  E-value: 1.38e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRP--SGELFAIKALKKGDIVA--RDEVESLMcEKRILAAVtSAGHpfLVNLFGCFQTP 694
Cdd:cd05061   6 EKITLLRELGQGSFGMVYEGNARDiiKGEAETRVAVKTVNESAslRERIEFLN-EASVMKGF-TCHH--VVRLLGVVSKG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 695 EHVCFVMEYSAGGDLMLHIHS---DVFSEP--------RAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIA 763
Cdd:cd05061  82 QPTLVVMELMAHGDLKSYLRSlrpEAENNPgrppptlqEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 764 DFGLCKE--GMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEM-LVGESPFPGDDEEEVFDSIVN-DEVR 839
Cdd:cd05061 162 DFGMTRDiyETDYYRKGGKGLLPVRWMAPESLKDGVFTTSSDMWSFGVVLWEItSLAEQPYQGLSNEQVLKFVMDgGYLD 241
                       250       260
                ....*....|....*....|....
gi 47132591 840 YPRFLSAEAIGIMRRLLRRNPERR 863
Cdd:cd05061 242 QPDNCPERVTDLMRMCWQFNPKMR 265
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
639-863 1.45e-07

Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 53.93  E-value: 1.45e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 639 EFRPSGELFAIKALKKGDIVARDEVESL--MCEKRilaavtsagHPFLVNLFG-CFQTPEhVCFVMEYSAGGDLMLHIHS 715
Cdd:cd13992  20 VGVYGGRTVAIKHITFSRTEKRTILQELnqLKELV---------HDNLNKFIGiCINPPN-IAVVTEYCTRGSLQDVLLN 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 716 DVFSEPRaIFYSACV---VLGLQFLHEHKIVYRDLKLDNLLLDTEGYV-KIADFGL--------CKEGMGYGDRTSTFCG 783
Cdd:cd13992  90 REIKMDW-MFKSSFIkdiVKGMNYLHSSSIGYHGRLKSSNCLVDSRWVvKLTDFGLrnlleeqtNHQLDEDAQHKKLLWT 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 784 TPEFLApEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRF--------LSAEAIGIMRRL 855
Cdd:cd13992 169 APELLR-GSLLEVRGTQKGDVYSFAIILYEILFRSDPFALEREVAIVEKVISGGNKPFRPelavlldeFPPRLVLLVKQC 247

                ....*...
gi 47132591 856 LRRNPERR 863
Cdd:cd13992 248 WAENPEKR 255
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
619-863 1.48e-07

Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK, containing an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region with a conserved tyr. It is activated by autophosphorylation at the tyr kinase domain, and is negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). c-Src is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. The Src subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 53.92  E-value: 1.48e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELfAIKALKKGDIVArdevESLMCEKRILAAVTsagHPFLVNLFGCFqTPEHVC 698
Cdd:cd05071   9 ESLRLEVKLGQGCFGEVWMGTWNGTTRV-AIKTLKPGTMSP----EAFLQEAQVMKKLR---HEKLVQLYAVV-SEEPIY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGGDLMLHI---HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK--EGMG 773
Cdd:cd05071  80 IVTEYMSKGSLLDFLkgeMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARliEDNE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 774 YGDRTSTFCGTpEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLV-GESPFPGDDEEEVFDSIVND-EVRYPRFLSAEAIGI 851
Cdd:cd05071 160 YTARQGAKFPI-KWTAPEAALYGRFTIKSDVWSFGILLTELTTkGRVPYPGMVNREVLDQVERGyRMPCPPECPESLHDL 238
                       250
                ....*....|..
gi 47132591 852 MRRLLRRNPERR 863
Cdd:cd05071 239 MCQCWRKEPEER 250
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
621-825 1.84e-07

Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs MPK1 from Saccharomyces cerevisiae, Pmk1 from Schizosaccharomyces pombe, and similar proteins. MPK1 (also called Slt2) and Pmk1 (also called Spm1) are stress-activated MAPKs that regulate the cell wall integrity pathway, and are therefore important in the maintainance of cell shape, cell wall construction, morphogenesis, and ion homeostasis. MPK1 is activated in response to cell wall stress including heat stimulation, osmotic shock, UV irradiation, and any agents that interfere with cell wall biogenesis such as chitin antagonists, caffeine, or zymolase. MPK1 is regulated by the MAP2Ks Mkk1/2, which are regulated by the MAP3K Bck1. Pmk1 is also activated by multiple stresses including elevated temperatures, hyper- or hypotonic stress, glucose deprivation, exposure to cell-wall damaging compounds, and oxidative stress. It is regulated by the MAP2K Pek1, which is regulated by the MAP3K Mkh1. MAPKs are important mediators of cellular responses to extracellular signals. The MPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 54.33  E-value: 1.84e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIkALKKgdiVARDEVESLMCeKRILAAVT----SAGHPFLVNLFG------- 689
Cdd:cd07857   2 YELIKELGQGAYGIVCSARNAETSEEETV-AIKK---ITNVFSKKILA-KRALRELKllrhFRGHKNITCLYDmdivfpg 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 690 ------CFQTPehvcfvMEYsaggDLMLHIHSDV-FSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKI 762
Cdd:cd07857  77 nfnelyLYEEL------MEA----DLHQIIRSGQpLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKI 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47132591 763 ADFGL---CKEGMGYGDRTST-FCGTPEFLAPEV-LTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDD 825
Cdd:cd07857 147 CDFGLargFSENPGENAGFMTeYVATRWYRAPEImLSFQSYTKAIDVWSVGCILAELLGRKPVFKGKD 214
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
627-842 2.43e-07

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Aatyk subfamily is also referred to as the lemur tyrosine kinase (Lmtk) subfamily. It consists of Aatyk1 (Lmtk1), Aatyk2 (Lmtk2, Brek), Aatyk3 (Lmtk3), and similar proteins. Aatyk proteins are mostly receptor PTKs (RTKs) containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk1 does not contain a transmembrane segment and is a cytoplasmic (or nonreceptor) kinase. Aatyk proteins are classified as PTKs based on overall sequence similarity and the phylogenetic tree. However, analysis of catalytic residues suggests that Aatyk proteins may be multispecific kinases, functioning also as serine/threonine kinases. They are involved in neural differentiation, nerve growth factor (NGF) signaling, apoptosis, and spermatogenesis. The Aatyk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270638 [Multi-domain]  Cd Length: 269  Bit Score: 53.36  E-value: 2.43e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLsefrpsGELFAikalkkGDIVARDEVESLMCEKRILAAVT--SAGHPFLV----NLFGCF-QTPEHVCF 699
Cdd:cd05042   3 IGNGWFGKVLL------GEIYS------GTSVAQVVVKELKASANPKEQDTflKEGQPYRIlqhpNILQCLgQCVEAIPY 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 --VMEYSAGGDLMLHIHSDVFSE-----PRAIFYSAC-VVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLckeg 771
Cdd:cd05042  71 llVMEFCDLGDLKAYLRSEREHErgdsdTRTLQRMACeVAAGLAHLHKLNFVHSDLALRNCLLTSDLTVKIGDYGL---- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 772 mGYGDRTSTFCGTPE-------FLAPEVLTD-------TSYTRAVDWWGLGVLLYEML-VGESPFPGDDEEEVFDSIVND 836
Cdd:cd05042 147 -AHSRYKEDYIETDDklwfplrWTAPELVTEfhdrllvVDQTKYSNIWSLGVTLWELFeNGAQPYSNLSDLDVLAQVVRE 225

                ....*..
gi 47132591 837 E-VRYPR 842
Cdd:cd05042 226 QdTKLPK 232
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
621-883 2.51e-07

Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 53.63  E-value: 2.51e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALkkgdivaRDEVESLMCEKRILAAVT---SAGHPFLVNLFGCFQTPE-- 695
Cdd:cd07859   2 YKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKI-------NDVFEHVSDATRILREIKllrLLRHPDIVEIKHIMLPPSrr 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 696 -----HVCF-VMEysagGDLMLHIHS-DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLC 768
Cdd:cd07859  75 efkdiYVVFeLME----SDLHQVIKAnDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 769 KegMGYGDRTST-----FCGTPEFLAPEVLTD--TSYTRAVDWWGLGVLLYEMLVGESPFPGDD---------------E 826
Cdd:cd07859 151 R--VAFNDTPTAifwtdYVATRWYRAPELCGSffSKYTPAIDIWSIGCIFAEVLTGKPLFPGKNvvhqldlitdllgtpS 228
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47132591 827 EEVFDSIVNDEVRypRFLSA------------------EAIGIMRRLLRRNPERRlgsseRDAEDVKKQPFFRTL 883
Cdd:cd07859 229 PETISRVRNEKAR--RYLSSmrkkqpvpfsqkfpnadpLALRLLERLLAFDPKDR-----PTAEEALADPYFKGL 296
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
733-883 2.61e-07

Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TEY subtype of plant MAPKs and is further subdivided into three groups (A, B, and C). Group A is represented by AtMPK3, AtMPK6, Nicotiana tabacum BTF4 (NtNTF4), among others. They are mostly involved in environmental and hormonal responses. AtMPK3 and AtMPK6 are also key regulators for stomatal development and patterning. Group B is represented by AtMPK4, AtMPK13, and NtNTF6, among others. They may be involved in both cell division and environmental stress response. AtMPK4 also participates in regulating innate immunity. Group C is represented by AtMPK1, AtMPK2, NtNTF3, Oryza sativa MAPK4 (OsMAPK4), among others. They may also be involved in stress responses. AtMPK1 and AtMPK2 are activated following mechanical injury and in the presence of stress chemicals such as jasmonic acid, hydrogen peroxide and abscisic acid. OsMAPK4 is also called OsMSRMK3 for Multiple Stress-Responsive MAPK3. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20. The TEY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 53.53  E-value: 2.61e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 733 GLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTDTS-YTRAVDWWGLGVLL 811
Cdd:cd07858 120 GLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLARTTSEKGDFMTEYVVTRWYRAPELLLNCSeYTTAIDVWSVGCIF 199
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 812 YEMLVGESPFPGDD---------------EEEVFDSIVNDEVR-----------------YPRfLSAEAIGIMRRLLRRN 859
Cdd:cd07858 200 AELLGRKPLFPGKDyvhqlklitellgspSEEDLGFIRNEKARryirslpytprqsfarlFPH-ANPLAIDLLEKMLVFD 278
                       170       180
                ....*....|....*....|....
gi 47132591 860 PERRLgsserDAEDVKKQPFFRTL 883
Cdd:cd07858 279 PSKRI-----TVEEALAHPYLASL 297
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
661-821 2.95e-07

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 52.70  E-value: 2.95e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 661 DEVESLMCEKrilaavtsagHPFLVNLFGCFQTP--EHVCFVM--EYSAGGDLMLHIHSDVFSEPRAI-FYSACVVLGLQ 735
Cdd:cd14033  49 EEVEMLKGLQ----------HPNIVRFYDSWKSTvrGHKCIILvtELMTSGTLKTYLKRFREMKLKLLqRWSRQILKGLH 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 736 FLHEH--KIVYRDLK-LDNLLLDTEGYVKIADFGLCKegMGYGDRTSTFCGTPEFLAPEvLTDTSYTRAVDWWGLGVLLY 812
Cdd:cd14033 119 FLHSRcpPILHRDLKcDNIFITGPTGSVKIGDLGLAT--LKRASFAKSVIGTPEFMAPE-MYEEKYDEAVDVYAFGMCIL 195

                ....*....
gi 47132591 813 EMLVGESPF 821
Cdd:cd14033 196 EMATSEYPY 204
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
627-868 3.28e-07

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of NF-kB proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 52.90  E-value: 3.28e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKkgdiVARDEVESLMCekriLAAVTSaghPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd13991  14 IGRGSFGEVHRMEDKQTGFQCAVKKVR----LEVFRAEELMA----CAGLTS---PRVVPLYGAVREGPWVNIFMDLKEG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDL-MLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEG-YVKIADFGL--CKEGMGYGDRTST-- 780
Cdd:cd13991  83 GSLgQLIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGsDAFLCDFGHaeCLDPDGLGKSLFTgd 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 781 -FCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVND-----EVryP---RFLSAEAIgi 851
Cdd:cd13991 163 yIPGTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPWTQYYSGPLCLKIANEppplrEI--PpscAPLTAQAI-- 238
                       250
                ....*....|....*..
gi 47132591 852 mRRLLRRNPERRLGSSE 868
Cdd:cd13991 239 -QAGLRKEPVHRASAAE 254
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
619-880 4.24e-07

Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CdkB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 52.92  E-value: 4.24e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAikaLKKGDIVARDE-VESLMCEKRILAAVTSAGhPFLVNLFGCFQTPEH- 696
Cdd:cd07837   1 DAYEKLEKIGEGTYGKVYKARDKNTGKLVA---LKKTRLEMEEEgVPSTALREVSLLQMLSQS-IYIVRLLDVEHVEENg 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 697 ---VCFVMEYsAGGDLMLHIHSDVFSEPRAI--------FYSACvvLGLQFLHEHKIVYRDLKLDNLLLDTE-GYVKIAD 764
Cdd:cd07837  77 kplLYLVFEY-LDTDLKKFIDSYGRGPHNPLpaktiqsfMYQLC--KGVAHCHSHGVMHRDLKPQNLLVDKQkGLLKIAD 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 765 FGLckeGMGYGDRTSTFCG---TPEFLAPEVLT-DTSYTRAVDWWGLGVLLYEMLVGESPFPGDDE-------------- 826
Cdd:cd07837 154 LGL---GRAFTIPIKSYTHeivTLWYRAPEVLLgSTHYSTPVDMWSVGCIFAEMSRKQPLFPGDSElqqllhifrllgtp 230
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47132591 827 -EEVFDSIVN--DEVRYPRF-----------LSAEAIGIMRRLLRRNPERRLgsserDAEDVKKQPFF 880
Cdd:cd07837 231 nEEVWPGVSKlrDWHEYPQWkpqdlsravpdLEPEGVDLLTKMLAYDPAKRI-----SAKAALQHPYF 293
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
619-863 4.64e-07

Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Yes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 52.38  E-value: 4.64e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELfAIKALKKGDIVArdevESLMCEKRILAAVTsagHPFLVNLFGCFqTPEHVC 698
Cdd:cd05069  12 ESLRLDVKLGQGCFGEVWMGTWNGTTKV-AIKTLKPGTMMP----EAFLQEAQIMKKLR---HDKLVPLYAVV-SEEPIY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVMEYSAGGDLMlhihsDVFSE--------PRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK- 769
Cdd:cd05069  83 IVTEFMGKGSLL-----DFLKEgdgkylklPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARl 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 770 -EGMGYGDRTSTFCGTpEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLV-GESPFPGDDEEEVFDSIVND-EVRYPRFLSA 846
Cdd:cd05069 158 iEDNEYTARQGAKFPI-KWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMVNREVLEQVERGyRMPCPQGCPE 236
                       250
                ....*....|....*..
gi 47132591 847 EAIGIMRRLLRRNPERR 863
Cdd:cd05069 237 SLHELMKLCWKKDPDER 253
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
621-822 6.35e-07

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 52.57  E-value: 6.35e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKalkkgdiVARDE---VESLMCEKRILAAVTSA---GHPFLVNLFGCFQTP 694
Cdd:cd14134  14 YKILRLLGEGTFGKVLECWDRKRKRYVAVK-------IIRNVekyREAAKIEIDVLETLAEKdpnGKSHCVQLRDWFDYR 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 695 EHVCFVME------YsaggDLMLHIHSDVF--SEPRAIFYSACVvlGLQFLHEHKIV---------------------YR 745
Cdd:cd14134  87 GHMCIVFEllgpslY----DFLKKNNYGPFplEHVQHIAKQLLE--AVAFLHDLKLThtdlkpenillvdsdyvkvynPK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 746 DLKLDNLLLDTEgyVKIADFGLCkegmgygdrT------STFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGES 819
Cdd:cd14134 161 KKRQIRVPKSTD--IKLIDFGSA---------TfddeyhSSIVSTRHYRAPEVILGLGWSYPCDVWSIGCILVELYTGEL 229

                ...
gi 47132591 820 PFP 822
Cdd:cd14134 230 LFQ 232
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
626-863 7.18e-07

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 isoforms resulting from alternative translation initiation sites. PIM1 is the founding member of the PIM subfamily. It is involved in regulating cell growth, differentiation, and apoptosis. It promotes cancer development when overexpressed by inhibiting apoptosis, promoting cell proliferation, and promoting genomic instability. The PIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 51.51  E-value: 7.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVES---LMCEKRILAAVTSaGHPFLVNLFGCFQTPEHVCFVME 702
Cdd:cd14100   7 LLGSGGFGSVYSGIRVADGAPVAIKHVEKDRVSEWGELPNgtrVPMEIVLLKKVGS-GFRGVIRLLDWFERPDSFVLVLE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 703 Y-SAGGDLMLHI-HSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLL-LDTEGYVKIADFG---LCKEGMgYGD 776
Cdd:cd14100  86 RpEPVQDLFDFItERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILiDLNTGELKLIDFGsgaLLKDTV-YTD 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 777 rtstFCGTPEFLAPEVLTDTSY-TRAVDWWGLGVLLYEMLVGESPFPGDDEeevfdsIVNDEVRYPRFLSAEAIGIMRRL 855
Cdd:cd14100 165 ----FDGTRVYSPPEWIRFHRYhGRSAAVWSLGILLYDMVCGDIPFEHDEE------IIRGQVFFRQRVSSECQHLIKWC 234

                ....*...
gi 47132591 856 LRRNPERR 863
Cdd:cd14100 235 LALRPSDR 242
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
619-863 8.23e-07

Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The DDR subfamily consists of homologs of mammalian DDR1, DDR2, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 51.95  E-value: 8.23e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSE----------------FRPSGELFAIKALKKGdivARDEV-ESLMCEKRILAAVTsagH 681
Cdd:cd05051   5 EKLEFVEKLGEGQFGEVHLCEanglsdltsddfigndNKDEPVLVAVKMLRPD---ASKNArEDFLKEVKIMSQLK---D 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 682 PFLVNLFGCFQTPEHVCFVMEYSAGGDL--MLHIHSDVFSEPRA-----------IFYSACVVLGLQFLHEHKIVYRDLK 748
Cdd:cd05051  79 PNIVRLLGVCTRDEPLCMIVEYMENGDLnqFLQKHEAETQGASAtnsktlsygtlLYMATQIASGMKYLESLNFVHRDLA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 749 LDNLLLDTEGYVKIADFGLckegmgygDRtSTFCGT----------P-EFLAPEVLTDTSYTRAVDWWGLGVLLYE--ML 815
Cdd:cd05051 159 TRNCLVGPNYTIKIADFGM--------SR-NLYSGDyyriegravlPiRWMAWESILLGKFTTKSDVWAFGVTLWEilTL 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 47132591 816 VGESPFPGDDEEEVFDSIVNDEVRY--------PRFLSAEAIGIMRRLLRRNPERR 863
Cdd:cd05051 230 CKEQPYEHLTDEQVIENAGEFFRDDgmevylsrPPNCPKEIYELMLECWRRDEEDR 285
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
627-832 8.53e-07

Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR-like proteins are members of the DDR subfamily, which are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 51.90  E-value: 8.53e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLL--------------SEFRPSGELFAIKALKKGdiVARDEVESLMCEKRILAAVTsagHPFLVNLFGCFQ 692
Cdd:cd05097  13 LGEGQFGEVHLceaeglaeflgegaPEFDGQPVLVAVKMLRAD--VTKTARNDFLKEIKIMSRLK---NPNIIRLLGVCV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 693 TPEHVCFVMEYSAGGDL-----------MLHIHSDVFSEPRA--IFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGY 759
Cdd:cd05097  88 SDDPLCMITEYMENGDLnqflsqreiesTFTHANNIPSVSIAnlLYMAVQIASGMKYLASLNFVHRDLATRNCLVGNHYT 167
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47132591 760 VKIADFGLCKEgMGYGD--RTSTFCGTP-EFLAPEVLTDTSYTRAVDWWGLGVLLYEM--LVGESPFPGDDEEEVFDS 832
Cdd:cd05097 168 IKIADFGMSRN-LYSGDyyRIQGRAVLPiRWMAWESILLGKFTTASDVWAFGVTLWEMftLCKEQPYSLLSDEQVIEN 244
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
627-830 9.84e-07

Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. C-Raf, also known as Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around midgestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. C-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The C-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 51.57  E-value: 9.84e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRpsGELfAIKALKkgdiVARDEVESLMCEKRILAAVTSAGHPFLVnLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd14149  20 IGSGSFGTVYKGKWH--GDV-AVKILK----VVDPTPEQFQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEG 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLMLHIH--SDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLC--KEGMGYGDRTSTFC 782
Cdd:cd14149  92 SSLYKHLHvqETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvKSRWSGSQQVEQPT 171
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 47132591 783 GTPEFLAPEVL---TDTSYTRAVDWWGLGVLLYEMLVGESPFP--GDDEEEVF 830
Cdd:cd14149 172 GSILWMAPEVIrmqDNNPFSFQSDVYSYGIVLYELMTGELPYShiNNRDQIIF 224
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
730-834 1.06e-06

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 may play roles in the pathogenesis of these diseases. Initially, it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 51.97  E-value: 1.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 730 VVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGmgygdrTSTFCGTPE-----FLAPEVLTDTSYTRAVDW 804
Cdd:cd07875 135 MLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTA------GTSFMMTPYvvtryYRAPEVILGMGYKENVDI 208
                        90       100       110
                ....*....|....*....|....*....|
gi 47132591 805 WGLGVLLYEMLVGESPFPGDDEEEVFDSIV 834
Cdd:cd07875 209 WSVGCIMGEMIKGGVLFPGTDHIDQWNKVI 238
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
681-825 1.18e-06

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. They are also essential regulators of physiological and pathological processes and are involved in the pathogenesis of several diseases such as diabetes, atherosclerosis, stroke, Parkinson's and Alzheimer's. Vetebrates harbor three different JNK genes (Jnk1, Jnk2, and Jnk3) that are alternatively spliced to produce at least 10 isoforms. JNKs are specifically activated by the MAPK kinases MKK4 and MKK7, which are in turn activated by upstream MAPK kinase kinases as a result of different stimuli including stresses such as ultraviolet (UV) irradiation, hyperosmolarity, heat shock, or cytokines. JNKs activate a large number of different substrates based on specific stimulus, cell type, and cellular condition, and may be implicated in seemingly contradictory functions. The JNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 51.65  E-value: 1.18e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 681 HPFLVNLFGCFqTPE-------HVCFVMEysaggdLMLH-----IHSDVFSEpRAIFYSACVVLGLQFLHEHKIVYRDLK 748
Cdd:cd07850  58 HKNIIGLLNVF-TPQksleefqDVYLVME------LMDAnlcqvIQMDLDHE-RMSYLLYQMLCGIKHLHSAGIIHRDLK 129
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47132591 749 LDNLLLDTEGYVKIADFGLCKEGmGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDD 825
Cdd:cd07850 130 PSNIVVKSDCTLKILDFGLARTA-GTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIRGTVLFPGTD 205
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
619-828 1.23e-06

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK2 plays a role in hepatic insulin signaling and glucose metabolism. It is induced by the insulin/Akt pathway as part of the hepatic refeeding reponse, and it directly phosphorylates the SR domain of PGC-1alpha, which results in decreased gluconeogenic gene expression and glucose output. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 51.56  E-value: 1.23e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVL-LSEFRPSGELFAIKALK---KGDIVARDEVESLmceKRILAAVTSAGHpFLVNLFGCFQTP 694
Cdd:cd14215  12 ERYEIVSTLGEGTFGRVVqCIDHRRGGARVALKIIKnveKYKEAARLEINVL---EKINEKDPENKN-LCVQMFDWFDYH 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 695 EHVCFVMEYSAGGDLMLHIHSDVFSEP----RAIFYSACvvLGLQFLHEHKIVYRDLKLDNLLLDTEGY----------- 759
Cdd:cd14215  88 GHMCISFELLGLSTFDFLKENNYLPYPihqvRHMAFQVC--QAVKFLHDNKLTHTDLKPENILFVNSDYeltynlekkrd 165
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47132591 760 --------VKIADFGlckEGMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEE 828
Cdd:cd14215 166 ersvkstaIRVVDFG---SATFDHEHHSTIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNRE 239
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
627-824 1.44e-06

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 50.98  E-value: 1.44e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSgeLFAIKALKKG-----DIVA---RDEVESLMCEKrilaavtsagHPFLVNLFG-CFQTPEHv 697
Cdd:cd14159   1 IGEGGFGCVYQAVMRNT--EYAVKRLKEDseldwSVVKnsfLTEVEKLSRFR----------HPNIVDLAGySAQQGNY- 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 698 CFVMEYSAGGDLMLHIHSDVFSEPRAIFYSACVVLG----LQFLHEHK--IVYRDLKLDNLLLDTEGYVKIADFGL---C 768
Cdd:cd14159  68 CLIYVYLPNGSLEDRLHCQVSCPCLSWSQRLHVLLGtaraIQYLHSDSpsLIHGDVKSSNILLDAALNPKLGDFGLarfS 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47132591 769 KEGMGYGD-----RTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGD 824
Cdd:cd14159 148 RRPKQPGMsstlaRTQTVRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLTGRRAMEVD 208
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
621-827 1.70e-06

Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK8, CDC2L6, and similar proteins. CDK8 functions as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II-dependent transcription. CDC2L6 also associates with Mediator in complexes lacking CDK8. In VP16-dependent transcriptional activation, CDK8 and CDC2L6 exerts opposing effects by positive and negative regulation, respectively, in similar conditions. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 51.13  E-value: 1.70e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLL--SEFRPSGELFAIKALKkGDIVARDEVESLMCekRILAAVTSAGHPFLVNLFGCFQTPEHVC 698
Cdd:cd07842   2 YEIEGCIGRGTYGRVYKakRKNGKDGKEYAIKKFK-GDKEQYTGISQSAC--REIALLRELKHENVVSLVEVFLEHADKS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 699 FVM--EYsAGGDLmLHI-----HSDVFSEPRAIFYSACVVL--GLQFLHEHKIVYR----DLKLDNLLLDTEGYVKIADF 765
Cdd:cd07842  79 VYLlfDY-AEHDL-WQIikfhrQAKRVSIPPSMVKSLLWQIlnGIHYLHSNWVLHRdlkpANILVMGEGPERGVVKIGDL 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47132591 766 GLCK------EGMGYGDRTSTfcgTPEFLAPEVLTDTS-YTRAVDWWGLGVLLYEMLVGESPFPGDDEE 827
Cdd:cd07842 157 GLARlfnaplKPLADLDPVVV---TIWYRAPELLLGARhYTKAIDIWAIGCIFAELLTLEPIFKGREAK 222
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
681-864 2.17e-06

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK3 shows a restricted expression pattern; it is found at high levels in the pituary glands and is also expressed in the kidney and brain. It has been shown to regulate many ion transporters including members of the SLC12A family of cation-chloride cotransporters such as NCC and NKCC2, the renal potassium channel ROMK, and the epithelial calcium channels TRPV5 and TRPV6. WNK3 appears to sense low-chloride hypotonic stress and under these conditions, it activates SPAK, which directly interacts and phosphorylates cation-chloride cotransporters. WNK3 has also been shown to promote cell survival, possibly through interaction with procaspase-3 and HSP70. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 50.49  E-value: 2.17e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 681 HPFLVNLFGCFQT----PEHVCFVMEYSAGGDLMLHIHSDVFSEPRaIFYSAC--VVLGLQFLHEHK--IVYRDLK-LDN 751
Cdd:cd14031  68 HPNIVRFYDSWESvlkgKKCIVLVTELMTSGTLKTYLKRFKVMKPK-VLRSWCrqILKGLQFLHTRTppIIHRDLKcDNI 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 752 LLLDTEGYVKIADFGLCKegMGYGDRTSTFCGTPEFLAPEvLTDTSYTRAVDWWGLGVLLYEMLVGESPFPG-DDEEEVF 830
Cdd:cd14031 147 FITGPTGSVKIGDLGLAT--LMRTSFAKSVIGTPEFMAPE-MYEEHYDESVDVYAFGMCMLEMATSEYPYSEcQNAAQIY 223
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 47132591 831 DSIVN--DEVRYPRFLSAEAIGIMRRLLRRNPERRL 864
Cdd:cd14031 224 RKVTSgiKPASFNKVTDPEVKEIIEGCIRQNKSERL 259
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
687-821 2.23e-06

Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. B-Raf activates ERK with the strongest magnitude, compared with other Raf kinases. Mice embryos deficient in B-Raf die around midgestation due to vascular hemorrhage caused by apoptotic endothelial cells. Mutations in B-Raf have been implicated in initiating tumorigenesis and tumor progression, and are found in malignant cutaneous melanoma, papillary thyroid cancer, as well as in ovarian and colorectal carcinomas. Most oncogenic B-Raf mutations are located at the activation loop of the kinase and surrounding regions; the V600E mutation accounts for around 90% of oncogenic mutations. The V600E mutant constitutively activates MEK, resulting in sustained activation of ERK. B-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The B-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 50.44  E-value: 2.23e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 687 LFGCFQTPEHVCFVMEYSAGGDLMLHIHS--DVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIAD 764
Cdd:cd14151  68 LFMGYSTKPQLAIVTQWCEGSSLYHHLHIieTKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGD 147
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47132591 765 FGLC--KEGMGYGDRTSTFCGTPEFLAPEV--LTDTS-YTRAVDWWGLGVLLYEMLVGESPF 821
Cdd:cd14151 148 FGLAtvKSRWSGSHQFEQLSGSILWMAPEVirMQDKNpYSFQSDVYAFGIVLYELMTGQLPY 209
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
619-821 2.49e-06

Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase Kinases 3 and 6; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK3 and MKK6 are dual-specificity PKs that phosphorylate and activate their downstream target, p38 MAPK, on specific threonine and tyrosine residues. MKK3/6 play roles in the regulation of cell cycle progression, cytokine- and stress-induced apoptosis, oncogenic transformation, and adult tissue regeneration. In addition, MKK6 plays a critical role in osteoclast survival in inflammatory disease while MKK3 is associated with tumor invasion, progression, and poor patient survival in glioma. The MKK3/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 50.12  E-value: 2.49e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 619 EDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALkkgdivaRDEVESlMCEKRIL----AAVTSAGHPFLVNLFGCFQTP 694
Cdd:cd06617   1 DDLEVIEELGRGAYGVVDKMRHVPTGTIMAVKRI-------RATVNS-QEQKRLLmdldISMRSVDCPYTVTFYGALFRE 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 695 EHVCFVME---------YSAGGDLMLHIHSDVFSEpraIFYSacVVLGLQFLHEH-KIVYRDLKLDNLLLDTEGYVKIAD 764
Cdd:cd06617  73 GDVWICMEvmdtsldkfYKKVYDKGLTIPEDILGK---IAVS--IVKALEYLHSKlSVIHRDVKPSNVLINRNGQVKLCD 147
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47132591 765 FGL---------------CKEGMGygdrtstfcgtPEFLAPEvLTDTSYTRAVDWWGLGVLLYEMLVGESPF 821
Cdd:cd06617 148 FGIsgylvdsvaktidagCKPYMA-----------PERINPE-LNQKGYDVKSDVWSLGITMIELATGRFPY 207
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
623-832 2.85e-06

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR1 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR1 results in a slow but sustained receptor activation. DDR1 binds to all collagens tested to date (types I-IV). It is widely expressed in many tissues. It is abundant in the brain and is also found in keratinocytes, colonic mucosa epithelium, lung epithelium, thyroid follicles, and the islets of Langerhans. During embryonic development, it is found in the developing neuroectoderm. DDR1 is a key regulator of cell morphogenesis, differentiation and proliferation. It is important in the development of the mammary gland, the vasculator and the kidney. DDR1 is also found in human leukocytes, where it facilitates cell adhesion, migration, maturation, and cytokine production. The DDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 50.32  E-value: 2.85e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 623 FLAVLGRGHFGKVLLSEFRPSGELFAIK---ALKKGD--IVA---------RDEVESLMCEKRILAAVTSaghPFLVNLF 688
Cdd:cd05096   9 FKEKLGEGQFGEVHLCEVVNPQDLPTLQfpfNVRKGRplLVAvkilrpdanKNARNDFLKEVKILSRLKD---PNIIRLL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 689 GCFQTPEHVCFVMEYSAGGDLMLHIHSDVFSEPR--------------AIFYSACVVL------GLQFLHEHKIVYRDLK 748
Cdd:cd05096  86 GVCVDEDPLCMITEYMENGDLNQFLSSHHLDDKEengndavppahclpAISYSSLLHValqiasGMKYLSSLNFVHRDLA 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 749 LDNLLLDTEGYVKIADFGLCKEgMGYGD--RTSTFCGTP-EFLAPEVLTDTSYTRAVDWWGLGVLLYEMLV--GESPFPG 823
Cdd:cd05096 166 TRNCLVGENLTIKIADFGMSRN-LYAGDyyRIQGRAVLPiRWMAWECILMGKFTTASDVWAFGVTLWEILMlcKEQPYGE 244

                ....*....
gi 47132591 824 DDEEEVFDS 832
Cdd:cd05096 245 LTDEQVIEN 253
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
671-834 3.23e-06

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 50.41  E-value: 3.23e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 671 RILAAVTSAGHPFLVNLFGCFqTPEH-------VCFVMEYsAGGDLMLHIHSDVFSEpRAIFYSACVVLGLQFLHEHKIV 743
Cdd:cd07876  69 RELVLLKCVNHKNIISLLNVF-TPQKsleefqdVYLVMEL-MDANLCQVIHMELDHE-RMSYLLYQMLCGIKHLHSAGII 145
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 744 YRDLKLDNLLLDTEGYVKIADFGLCKEGmgygdrTSTFCGTP-----EFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGE 818
Cdd:cd07876 146 HRDLKPSNIVVKSDCTLKILDFGLARTA------CTNFMMTPyvvtrYYRAPEVILGMGYKENVDIWSVGCIMGELVKGS 219
                       170
                ....*....|....*.
gi 47132591 819 SPFPGDDEEEVFDSIV 834
Cdd:cd07876 220 VIFQGTDHIDQWNKVI 235
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
733-828 3.84e-06

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 49.69  E-value: 3.84e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 733 GLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKE----GMGYGDRTSTFCGTPeflaPEVLT-DTSYTRAVDWWGL 807
Cdd:cd07844 110 GLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLARAksvpSKTYSNEVVTLWYRP----PDVLLgSTEYSTSLDMWGV 185
                        90       100
                ....*....|....*....|...
gi 47132591 808 GVLLYEMLVGESPFPG--DDEEE 828
Cdd:cd07844 186 GCIFYEMATGRPLFPGstDVEDQ 208
HR1_PKN3_2 cd11632
Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
220-274 4.33e-06

Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N3; PKN3, also called PKNbeta, is a serine/threonine protein kinase that is activated by the Rho family of small GTPases, preferentially by RhoC. Both PKN1 and RhoC show limited and barely detectable expression in normal tissues, but are both upregulated in cancer cells, particularly in late-stage malignancies. PKN3 has been implicated to play a role in the metastatic growth and invasiveness of cancer cells, downstream of the oncogenic phosphoinositide 3-kinase signaling network. PKN3 shares a common domain architecture with other PKNs, containing three HR1 domains, a C2 domain, and a kinase domain. In addition, PKN3 contains two proline-rich regions between its C2 and kinase domains, and has been shown to associate with SH3 domain containing proteins like GRAFs, GAP for RhoA, and Cdc42Hs. This model characterizes the second HR1 domain of PKN3. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; PKN3 binds Rho family GTPases, preferentially RhoC.


Pssm-ID: 212022  Cd Length: 74  Bit Score: 45.30  E-value: 4.33e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 47132591 220 RIEELRHHFRVEHAVAEGAKNVLRLLSAAKAPDRKAVSEAQEKLTESNQKLGLLR 274
Cdd:cd11632  10 RLEALKRQLHVELKVKQGAENMIQTYSSGTSKERKLLATAQQMLQDSRTKIELLR 64
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
627-825 4.41e-06

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 49.88  E-value: 4.41e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGELFAIKALKKGDI---VARDEVESLMCEKriLAAVTSAGHPFLVNLFGCF--QTPE--HVCF 699
Cdd:cd14136  18 LGWGHFSTVWLCWDLQNKRFVALKVVKSAQHyteAALDEIKLLKCVR--EADPKDPGREHVVQLLDDFkhTGPNgtHVCM 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 700 VMEYsaGGDLMLH--IHSDVFSEPRAIFYSAC--VVLGLQFLHEH-KIVYrdlkldnllldT------------EGYVKI 762
Cdd:cd14136  96 VFEV--LGPNLLKliKRYNYRGIPLPLVKKIArqVLQGLDYLHTKcGIIH-----------TdikpenvllcisKIEVKI 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47132591 763 ADFG-LCkegmgYGDR--TSTFcGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGE---SPFPGDD 825
Cdd:cd14136 163 ADLGnAC-----WTDKhfTEDI-QTRQYRSPEVILGAGYGTPADIWSTACMAFELATGDylfDPHSGED 225
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
621-840 4.62e-06

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). They show speckled localization in the nucleus, apart from the nucleoles. They play roles in the regulation of many nuclear pathways including gene transcription, cell survival, proliferation, differentiation, development, and DNA damage response. Vertebrates contain three HIPKs (HIPK1-3) and mammals harbor an additional family member HIPK4, which does not contain a homeobox-interacting domain and is localized in the cytoplasm. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors and it regulates gene transcription during development and in DNA damage response. The HIPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 49.75  E-value: 4.62e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARD---EVESLMCekriLAAVTSAGHPFlVNLFGCFQTPEHV 697
Cdd:cd14211   1 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQgqiEVSILSR----LSQENADEFNF-VRAYECFQHKNHT 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 698 CFVMEYSAgGDLMLHIHSDVFS-----EPRAIFYSACVVL----GLQFLHEH------------KIVYRdlkldnllldt 756
Cdd:cd14211  76 CLVFEMLE-QNLYDFLKQNKFSplplkYIRPILQQVLTALlklkSLGLIHADlkpenimlvdpvRQPYR----------- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 757 egyVKIADFG--------LCkegmgygdrtSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEe 828
Cdd:cd14211 144 ---VKVIDFGsashvskaVC----------STYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGSSEY- 209
                       250
                ....*....|..
gi 47132591 829 vfdsivnDEVRY 840
Cdd:cd14211 210 -------DQIRY 214
pknD PRK13184
serine/threonine-protein kinase PknD;
618-866 4.69e-06

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 50.54  E-value: 4.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  618 LEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKgdivarDEVESLMCEKRIL--AAVTS-AGHPFLVNLFGCFQTP 694
Cdd:PRK13184   1 MQRYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIRE------DLSENPLLKKRFLreAKIAAdLIHPGIVPVYSICSDG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  695 EHVCFVMEYSAGGDLMLHIHS----DVFSEPRA----------IFYSACVvlGLQFLHEHKIVYRDLKLDNLLLDTEGYV 760
Cdd:PRK13184  75 DPVYYTMPYIEGYTLKSLLKSvwqkESLSKELAektsvgaflsIFHKICA--TIEYVHSKGVLHRDLKPDNILLGLFGEV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  761 KIADFG--LCKEG-------MGYGDRTSTF---------CGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFp 822
Cdd:PRK13184 153 VILDWGaaIFKKLeeedlldIDVDERNICYssmtipgkiVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPY- 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 47132591  823 gddEEEVFDSIVNDEV-----------RYPRFLSAeaigIMRRLLRRNPERRLGS 866
Cdd:PRK13184 232 ---RRKKGRKISYRDVilspievapyrEIPPFLSQ----IAMKALAVDPAERYSS 279
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
730-834 6.85e-06

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK3 is expressed primarily in the brain, and to a lesser extent in the heart and testis. Mice deficient in JNK3 are protected against kainic acid-induced seizures, stroke, sciatic axotomy neural death, and neuronal death due to NGF deprivation, oxidative stress, or exposure to beta-amyloid peptide. This suggests that JNK3 may play roles in the pathogenesis of these diseases. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 49.32  E-value: 6.85e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 730 VVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGmGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGV 809
Cdd:cd07874 128 MLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTA-GTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGC 206
                        90       100
                ....*....|....*....|....*
gi 47132591 810 LLYEMLVGESPFPGDDEEEVFDSIV 834
Cdd:cd07874 207 IMGEMVRHKILFPGRDYIDQWNKVI 231
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
618-830 7.21e-06

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 49.05  E-value: 7.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  618 LEDFKFLAVLGRGHFGKVLLSEFRPSGElfaIKALKKGDIVARDE-VESLMCekRILAAVTSAGHPFLVNLFGCFQTPEH 696
Cdd:PLN00009   1 MDQYEKVEKIGEGTYGVVYKARDRVTNE---TIALKKIRLEQEDEgVPSTAI--REISLLKEMQHGNIVRLQDVVHSEKR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591  697 VCFVMEYSaggDLMLHIHSDVFSE----PRAI-FYSACVVLGLQFLHEHKIVYRDLKLDNLL-LDTEGYVKIADFGLCKe 770
Cdd:PLN00009  76 LYLVFEYL---DLDLKKHMDSSPDfaknPRLIkTYLYQILRGIAYCHSHRVLHRDLKPQNLLiDRRTNALKLADFGLAR- 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47132591  771 GMGYGDRTSTF-CGTPEFLAPEVLTDT-SYTRAVDWWGLGVLLYEMLVGESPFPGDDE-EEVF 830
Cdd:PLN00009 152 AFGIPVRTFTHeVVTLWYRAPEILLGSrHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEiDELF 214
C2_PKC_epsilon cd04014
C2 domain in Protein Kinase C (PKC) epsilon; A single C2 domain is found in PKC epsilon. The ...
401-474 9.98e-06

C2 domain in Protein Kinase C (PKC) epsilon; A single C2 domain is found in PKC epsilon. The PKC family of serine/threonine kinases regulates apoptosis, proliferation, migration, motility, chemo-resistance, and differentiation. There are 3 groups: group 1 (alpha, betaI, beta II, gamma) which require phospholipids and calcium, group 2 (delta, epsilon, theta, eta) which do not require calcium for activation, and group 3 (xi, iota/lambda) which are atypical and can be activated in the absence of diacylglycerol and calcium. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-II topology.


Pssm-ID: 175981 [Multi-domain]  Cd Length: 132  Bit Score: 46.11  E-value: 9.98e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 401 LKLDNTVVGQTSWKP--CGPnAWDQSFTLELERARELELAVFWRDQRGL------CALKFlklEDFLDNERH--EVQLDM 470
Cdd:cd04014  41 IDVDDTHIGKTSTKPktNSP-VWNEEFTTEVHNGRNLELTVFHDAAIGPddfvanCTISF---EDLIQRGSGsfDLWVDL 116

                ....
gi 47132591 471 EPQG 474
Cdd:cd04014 117 EPQG 120
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
726-863 1.17e-05

Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. Kit signaling is involved in major cellular functions including cell survival, proliferation, differentiation, adhesion, and chemotaxis. Mutations in Kit, which result in constitutive ligand-independent activation, are found in human cancers such as gastrointestinal stromal tumor (GIST) and testicular germ cell tumor (TGCT). The aberrant expression of Kit and/or SCF is associated with other tumor types such as systemic mastocytosis and cancers of the breast, neurons, lung, prostate, colon, and rectum. Although the structure of the human Kit catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. Kit is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of Kit to its ligand, the stem-cell factor (SCF), leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. The Kit subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270682 [Multi-domain]  Cd Length: 375  Bit Score: 48.75  E-value: 1.17e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 726 YSACVVLGLQFLHEHKIVYRDLKLDNLLLdTEGYV-KIADFGLCKEGMgyGDRTSTFCGTP----EFLAPEVLTDTSYTR 800
Cdd:cd05104 219 FSYQVAKGMEFLASKNCIHRDLAARNILL-THGRItKICDFGLARDIR--NDSNYVVKGNArlpvKWMAPESIFECVYTF 295
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47132591 801 AVDWWGLGVLLYEML-VGESPFPGDDEEEVFDSIVNDEVRY--PRFLSAEAIGIMRRLLRRNPERR 863
Cdd:cd05104 296 ESDVWSYGILLWEIFsLGSSPYPGMPVDSKFYKMIKEGYRMdsPEFAPSEMYDIMRSCWDADPLKR 361
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
618-879 1.24e-05

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK12 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 48.26  E-value: 1.24e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 618 LEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKAL-----KKG-DIVARDEVE--------SLMCEKRILAAVTSA---- 679
Cdd:cd07864   6 VDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVrldneKEGfPITAIREIKilrqlnhrSVVNLKEIVTDKQDAldfk 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 680 ---GHPFLVnlfgcFQTPEHvcfvmeysaggDLMLHIHSDV--FSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLL 754
Cdd:cd07864  86 kdkGAFYLV-----FEYMDH-----------DLMGLLESGLvhFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILL 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 755 DTEGYVKIADFGLCK-----EGMGYGDRTSTFCGTPeflaPEVLT-DTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEE 828
Cdd:cd07864 150 NNKGQIKLADFGLARlynseESRPYTNKVITLWYRP----PELLLgEERYGPAIDVWSCGCILGELFTKKPIFQANQELA 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 829 VFDSIVN-----------DEVRYPRF-------------------LSAEAIGIMRRLLRRNPERRLgsserDAEDVKKQP 878
Cdd:cd07864 226 QLELISRlcgspcpavwpDVIKLPYFntmkpkkqyrrrlreefsfIPTPALDLLDHMLTLDPSKRC-----TAEQALNSP 300

                .
gi 47132591 879 F 879
Cdd:cd07864 301 W 301
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
626-863 1.38e-05

Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 48.05  E-value: 1.38e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRPSGELFAIKAlkkgdIVARDEVESLMCEKRILAAVTSAGHPFLVNLFGCF--QTPEHVCFV--- 700
Cdd:cd14037  10 YLAEGGFAHVYLVKTSNGGNRAALKR-----VYVNDEHDLNVCKREIEIMKRLSGHKNIVGYIDSSanRSGNGVYEVlll 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 701 MEYSAGG---DLMLHIHSDVFSEPR--AIFYSACvvLGLQFLHEHK--IVYRDLKLDNLLLDTEGYVKIADFGLC----- 768
Cdd:cd14037  85 MEYCKGGgviDLMNQRLQTGLTESEilKIFCDVC--EAVAAMHYLKppLIHRDLKVENVLISDSGNYKLCDFGSAttkil 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 769 ----KEGMGYGDRTSTFCGTPEFLAPEVLtDT----SYTRAVDWWGLGVLLYEMLVGESPFpgddEEEVFDSIVNDEVRY 840
Cdd:cd14037 163 ppqtKQGVTYVEEDIKKYTTLQYRAPEMI-DLyrgkPITEKSDIWALGCLLYKLCFYTTPF----EESGQLAILNGNFTF 237
                       250       260
                ....*....|....*....|....*
gi 47132591 841 PRF--LSAEAIGIMRRLLRRNPERR 863
Cdd:cd14037 238 PDNsrYSKRLHKLIRYMLEEDPEKR 262
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
642-863 1.53e-05

Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. ILK contains N-terminal ankyrin repeats, a Pleckstrin Homology (PH) domain, and a C-terminal pseudokinase domain. It is a component of the IPP (ILK/PINCH/Parvin) complex that couples beta integrins to the actin cytoskeleton, and plays important roles in cell adhesion, spreading, invasion, and migration. ILK was initially thought to be an active kinase despite the lack of key conserved residues because of in vitro studies showing that it can phosphorylate certain protein substrates. However, in vivo experiments in Caenorhabditis elegans, Drosophila melanogaster, and mice (ILK-null and knock-in) proved that ILK is not an active kinase. In addition to actin cytoskeleton regulation, ILK also influences the microtubule network and mitotic spindle orientation. The pseudokinase domain of ILK binds several adaptor proteins including the parvins and paxillin. The ILK subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270959 [Multi-domain]  Cd Length: 251  Bit Score: 47.48  E-value: 1.53e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 642 PSGELF---------AIKALKKGDIVAR------DEVESLmcekRILAavtsagHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd14057   7 HSGELWkgrwqgndiVAKILKVRDVTTRisrdfnEEYPRL----RIFS------HPNVLPVLGACNSPPNLVVISQYMPY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDL--MLHIHSD-VFSEPRAIFYSACVVLGLQFLHE-HKIVYRDLKLDNLLLDTEG---YVKIAD--FGLCKEGMGYgdr 777
Cdd:cd14057  77 GSLynVLHEGTGvVVDQSQAVKFALDIARGMAFLHTlEPLIPRHHLNSKHVMIDEDmtaRINMADvkFSFQEPGKMY--- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 778 tstfcgTPEFLAPEVLT---DTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVR--YPRFLSAEAIGIM 852
Cdd:cd14057 154 ------NPAWMAPEALQkkpEDINRRSADMWSFAILLWELVTREVPFADLSNMEIGMKIALEGLRvtIPPGISPHMCKLM 227
                       250
                ....*....|.
gi 47132591 853 RRLLRRNPERR 863
Cdd:cd14057 228 KICMNEDPGKR 238
HR1_PKC-like_2_fungi cd11620
Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of fungal ...
212-279 1.74e-05

Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of fungal Protein Kinase C-like proteins; This subfamily is composed of fungal PKC-like proteins including Pkc1p from Saccharomyces cerevisiae, and Pck1p and Pck2p from Schizosaccharomyces pombe. The yeast PKC-like proteins play a critical role in regulating cell wall biosynthesis and maintaining cell wall integrity. They contain two HR1 domains, C2 and C1 domains, and a kinase domain. This model characterizes the second HR1 domain. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family. The HR1 domains of Pck1p and Pck2p interact with GTP-bound Rho1p and Rho2p.


Pssm-ID: 212010  Cd Length: 72  Bit Score: 43.50  E-value: 1.74e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47132591 212 PDLGA-VELRIEELRHHFRVEHAVAEGAKNVLRLLSAAkaPDRKAVSEAQEKLTESNQKLGLLREALER 279
Cdd:cd11620   1 PLTGAkIQRMLQQLEFKLQVEKQYKEGIEKMARLYQAE--GDKRSIADAENKRVESEQKIQLLKKALKR 67
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
621-828 1.77e-05

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. DYRK4 is a testis-specific kinase with restricted expression to postmeiotic spermatids. It may function during spermiogenesis, however, it is not required for male fertility. DYRK4 has also been detected in a human teratocarcinoma cell line induced to produce postmitotic neurons. It may have a role in neuronal differentiation. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. The DYRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 48.16  E-value: 1.77e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 621 FKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGdivARDEVESLMcEKRILAAVTSA---GHPFLVNLFGCFQTPEHV 697
Cdd:cd14225  45 YEILEVIGKGSFGQVVKALDHKTNEHVAIKIIRNK---KRFHHQALV-EVKILDALRRKdrdNSHNVIHMKEYFYFRNHL 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 698 CFVMEYsAGGDLMLHIHSDVF-----SEPRAIFYSacVVLGLQFLHEHKIVYRDLKLDNLLLDTEGY--VKIADFGL-CK 769
Cdd:cd14225 121 CITFEL-LGMNLYELIKKNNFqgfslSLIRRFAIS--LLQCLRLLYRERIIHCDLKPENILLRQRGQssIKVIDFGSsCY 197
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 47132591 770 EGmgygDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEE 828
Cdd:cd14225 198 EH----QRVYTYIQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYTGYPLFPGENEVE 252
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
627-880 1.87e-05

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP1 harbors a C-terminal Death domain (DD), which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 can also recruit other kinases including MEKK1, MEKK3, and RIP3 through an intermediate domain (ID) that bears a RIP homotypic interaction motif (RHIM). RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accummulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. RIP kinases serve as essential sensors of cellular stress. The RIP1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 47.49  E-value: 1.87e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 627 LGRGHFGKVLLSEFRPSGeLFAIKALKKGDIVARDEvESLMCEKRILaavTSAGHPFLVNLFGCFQTPEHVCFVMEYSAG 706
Cdd:cd14027   1 LDSGGFGKVSLCFHRTQG-LVVLKTVYTGPNCIEHN-EALLEEGKMM---NRLRHSRVVKLLGVILEEGKYSLVMEYMEK 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 707 GDLMlHIHSDVfsePRAIFYSACVVL----GLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFG---------LCKEGMG 773
Cdd:cd14027  76 GNLM-HVLKKV---SVPLSVKGRIILeiieGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGlasfkmwskLTKEEHN 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 774 YGDRTSTFC----GTPEFLAPEVLTD--TSYTRAVDWWGLGVLLYEMLVGESPFPGD-DEEEVFDSIVN----DEVRYPR 842
Cdd:cd14027 152 EQREVDGTAkknaGTLYYMAPEHLNDvnAKPTEKSDVYSFAIVLWAIFANKEPYENAiNEDQIIMCIKSgnrpDVDDITE 231
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 47132591 843 FLSAEAIGIMRRLLRRNPERRLGSSERDAedvKKQPFF 880
Cdd:cd14027 232 YCPREIIDLMKLCWEANPEARPTFPGIEE---KFRPFY 266
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
626-864 2.20e-05

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type I Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of type I receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation through trans-phosphorylation by type II receptors, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. They are inhibited by the immunophilin FKBP12, which is thought to control leaky signaling caused by receptor oligomerization in the absence of ligand. The TGFbR-I subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 47.27  E-value: 2.20e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 626 VLGRGHFGKVLLSEFRpsGELFAIKALKkgdivARDEvESLMCEKRILAAVTsAGHPFLVNLFGCFQTPEHVC----FVM 701
Cdd:cd14056   2 TIGKGRYGEVWLGKYR--GEKVAVKIFS-----SRDE-DSWFRETEIYQTVM-LRHENILGFIAADIKSTGSWtqlwLIT 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 702 EYSAGGDLMLHIHSDVFSEPRA--IFYSACVvlGLQFLH------EHK--IVYRDLKLDNLLLDTEGYVKIADFGLckeG 771
Cdd:cd14056  73 EYHEHGSLYDYLQRNTLDTEEAlrLAYSAAS--GLAHLHteivgtQGKpaIAHRDLKSKNILVKRDGTCCIADLGL---A 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 772 MGYGDRTSTF-------CGTPEFLAPEVLTDT-------SYTRAvDWWGLGVLLYEML--VGESPFPGDDE--------- 826
Cdd:cd14056 148 VRYDSDTNTIdippnprVGTKRYMAPEVLDDSinpksfeSFKMA-DIYSFGLVLWEIArrCEIGGIAEEYQlpyfgmvps 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 47132591 827 ----EEVFDSIVNDEVR---YPRFLSAEAIGIMRRLLRR----NPERRL 864
Cdd:cd14056 227 dpsfEEMRKVVCVEKLRppiPNRWKSDPVLRSMVKLMQEcwseNPHARL 275
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
681-821 4.07e-05

Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK2 is widely expressed and has been shown to be epigenetically silenced in gliomas. It inhibits cell growth by acting as a negative regulator of MEK1-ERK1/2 signaling. WNK2 modulates growth factor-induced cancer cell proliferation, suggesting that it may be a tumor suppressor gene. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. The WNK2-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 46.22  E-value: 4.07e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 681 HPFLVNLFGCFQTPEH----VCFVMEYSAGGDLMLHIHSDVFSEPRaIFYSAC--VVLGLQFLHEHK--IVYRDLK-LDN 751
Cdd:cd14032  59 HPNIVRFYDFWESCAKgkrcIVLVTELMTSGTLKTYLKRFKVMKPK-VLRSWCrqILKGLLFLHTRTppIIHRDLKcDNI 137
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 752 LLLDTEGYVKIADFGLCKegMGYGDRTSTFCGTPEFLAPEvLTDTSYTRAVDWWGLGVLLYEMLVGESPF 821
Cdd:cd14032 138 FITGPTGSVKIGDLGLAT--LKRASFAKSVIGTPEFMAPE-MYEEHYDESVDVYAFGMCMLEMATSEYPY 204
HR1_PKN1_2 cd11630
Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
220-281 4.30e-05

Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N1; PKN1, also called PKNalpha or Protein-kinase C-related kinase 1 (PRK1), is a serine/threonine protein kinase that is activated by the Rho family of small GTPases, and by fatty acids such as arachidonic and linoleic acids. It is expressed ubiquitously and is the most abundant PKN isoform in neurons. PKN1 is implicated in a variety of functions including cytoskeletal reorganization, cardiac cell survival, cell adhesion, and glucose transport, among others. PKN1 contains three HR1 domains, a C2 domain, and a kinase domain. This model characterizes the second HR1 domain of PKN1. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; PKN1 binds the GTPases RhoA, RhoB, and RhoC, and can also interact weakly with Rac.


Pssm-ID: 212020  Cd Length: 78  Bit Score: 42.70  E-value: 4.30e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47132591 220 RIEELRHHFRVEHAVAEGAKNVLRLLSAAKAPDRKAVSEAQEKLTESNQKLGLLREALERRL 281
Cdd:cd11630   9 RIAGLEKQLNIELKVKQGAENMIQTYANGSTKDRKLLQTAQQMLQDSKTKIDIIRMQIRKAM 70
HR1_PKN2_3 cd11635
Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
124-194 6.53e-05

Third Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N2; PKN2, also called PKNgamma or Protein-kinase C-related kinase 2 (PRK2), is a serine/threonine protein kinase and an effector of the small GTPase Rho/Rac. It regulates G2/M cell cycle progression and the exit from cytokinesis. It also phosphorylates hepatitis C virus (HCV) RNA polymerase and thus, plays a role in HCV RNA replication. PKN2 shares a common domain architecture with other PKNs, containing three HR1 domains, a C2 domain, and a kinase domain. In addition, PKN2 contains a proline-rich region in between its C2 and kinase domains and has been shown to associate with SH3 domain containing proteins like NCK and Grb4. This model characterizes the third HR1 domain of PKN2. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; PKN2 specifically binds to RhoA GTPase in a GTP-dependent manner. The HR1 domains of PKN2, together with its C2 domain, also facilitate the recruitment of PKN2 to primordial junctions at nascent cell-cell contacts, where it promotes junctional maturation.


Pssm-ID: 212025  Cd Length: 74  Bit Score: 41.95  E-value: 6.53e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47132591 124 PTCSATNLsRVAGLEKQLAIELKVKQGAENMIQTYSNGSTKDRKLLLTAQQMLQDSKTKIDIIRMQLRRAL 194
Cdd:cd11635   2 PVISPLEL-RMEELRHHFRIESAVAEGAKNVMKLLGSGKVTDRKALSEAQARFNESSQKLDLLKYSLEQRL 71
HR1_PKN2_2 cd11631
Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
220-274 4.99e-04

Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N2; PKN2, also called PKNgamma or Protein-kinase C-related kinase 2 (PRK2), is a serine/threonine protein kinase and an effector of the small GTPase Rho/Rac. It regulates G2/M cell cycle progression and the exit from cytokinesis. It also phosphorylates hepatitis C virus (HCV) RNA polymerase and thus, plays a role in HCV RNA replication. PKN2 shares a common domain architecture with other PKNs, containing three HR1 domains, a C2 domain, and a kinase domain. In addition, PKN2 contains a proline-rich region in between its C2 and kinase domains and has been shown to associate with SH3 domain containing proteins like NCK and Grb4. This model characterizes the second HR1 domain of PKN2. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; PKN2 specifically binds to RhoA GTPase in a GTP-dependent manner. The HR1 domains of PKN2, together with its C2 domain, also facilitate the recruitment of PKN2 to primordial junctions at nascent cell-cell contacts, where it promotes junctional maturation.


Pssm-ID: 212021  Cd Length: 74  Bit Score: 39.68  E-value: 4.99e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 47132591 220 RIEELRHHFRVEHAVAEGAKNVLRLLSAAKAPDRKAVSEAQEKLTESNQKLGLLR 274
Cdd:cd11631  10 RLMALKKQLDIELKVKQGAENMIQMYSNGSSKDRKLLATAQQMLQDSKTKIEVIR 64
HR1_PKN_1 cd11622
First Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ...
137-196 1.42e-03

First Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N; PKN, also called Protein-kinase C-related kinase (PRK), is a serine/threonine protein kinase that can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytoskeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. In some vertebrates, there are three PKN isoforms from different genes (designated PKN1, PKN2, and PKN3), which show different enzymatic properties, tissue distribution, and varied functions. PKN proteins contain three HR1 domains, a C2 domain, and a kinase domain. This model characterizes the first HR1 domain of PKN. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family.


Pssm-ID: 212012  Cd Length: 66  Bit Score: 38.02  E-value: 1.42e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132591 137 LEKQLAIELKVKQGAENMIQtysngSTKDRKLLLTAQQMLQDSKTKIDiirmQLRRALQA 196
Cdd:cd11622  11 IRREIRKELKIKEGAENLRK-----ATTDKKSLAHVESILKKSNRKLE----DLHQELQE 61
HR1_Ste20-like cd11627
Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of ...
218-279 1.83e-03

Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Schizosaccharomyces pombe Ste20-like proteins; This group is composed of predominantly uncharacterized fungal proteins, which contain two known domains: HR1 at the N-terminal region and REM (Ras exchanger motif) at the C-terminal region. One member protein from Schizosaccharomyces pombe is named Ste16 while its gene is called ste20 (a target of rapamycin complex 2 subunit). It is a subunit in the protein kinase TOR complexes in fission yeast. The REM domain is usually found in nucleotide exchange factors for Ras-like small GTPases. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family.


Pssm-ID: 212017 [Multi-domain]  Cd Length: 71  Bit Score: 37.74  E-value: 1.83e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47132591 218 ELRIEELRHHFRVEHAVAEGAKNVLRLLSAAKAPDRK-AVSEAQEKLTESNQKLGLLREALER 279
Cdd:cd11627   4 EQRLEELRGKLEIETKIKDGAENLLQVLDSKNAKEKKdQRARVESELNSSNRKIAQLTSQLEE 66
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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