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Conserved domains on  [gi|1231802383|ref|NP_001341525|]
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glycogen synthase kinase-3 beta isoform 3 [Homo sapiens]

Protein Classification

GSK family serine/threonine-protein kinase( domain architecture ID 10197641)

GSK (glycogen synthase kinase) family serine/threonine-protein kinase 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_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
51-343 0e+00

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: 645.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  51 PQEVSYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDEVYLNL 130
Cdd:cd14137     1 PVEISYTIEKVIGSGSFGVVYQAKLLETGEVVAIKKVLQDKRYKNRELQIMRRLKHPNIVKLKYFFYSSGEKKDEVYLNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 VLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSAKQLVRG 210
Cdd:cd14137    81 VMEYMPETLYRVIRHYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDPETGVLKLCDFGSAKRLVPG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 211 EPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTE 290
Cdd:cd14137   161 EPNVSYICSRYYRAPELIFGATDYTTAIDIWSAGCVLAELLLGQPLFPGESSVDQLVEIIKVLGTPTREQIKAMNPNYTE 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1231802383 291 FKFPQIKAHPWTKVFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDEL 343
Cdd:cd14137   241 FKFPQIKPHPWEKVFPKRTPPDAIDLLSKILVYNPSKRLTALEALAHPFFDEL 293
 
Name Accession Description Interval E-value
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
51-343 0e+00

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: 645.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  51 PQEVSYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDEVYLNL 130
Cdd:cd14137     1 PVEISYTIEKVIGSGSFGVVYQAKLLETGEVVAIKKVLQDKRYKNRELQIMRRLKHPNIVKLKYFFYSSGEKKDEVYLNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 VLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSAKQLVRG 210
Cdd:cd14137    81 VMEYMPETLYRVIRHYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDPETGVLKLCDFGSAKRLVPG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 211 EPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTE 290
Cdd:cd14137   161 EPNVSYICSRYYRAPELIFGATDYTTAIDIWSAGCVLAELLLGQPLFPGESSVDQLVEIIKVLGTPTREQIKAMNPNYTE 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1231802383 291 FKFPQIKAHPWTKVFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDEL 343
Cdd:cd14137   241 FKFPQIKPHPWEKVFPKRTPPDAIDLLSKILVYNPSKRLTALEALAHPFFDEL 293
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
29-366 1.68e-153

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 440.24  E-value: 1.68e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  29 SRDKDGSKVTTVVATPGQGPDRpqevSYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCN 108
Cdd:PTZ00036   45 NAGEDEDEEKMIDNDINRSPNK----SYKLGNIIGNGSFGVVYEAICIDTSEKVAIKKVLQDPQYKNRELLIMKNLNHIN 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 109 IVRLRYFFYSSGEKKDE--VYLNLVLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQN 186
Cdd:PTZ00036  121 IIFLKDYYYTECFKKNEknIFLNVVMEFIPQTVHKYMKHYARNNHALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQN 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 187 LLLDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQL 266
Cdd:PTZ00036  201 LLIDPNTHTLKLCDFGSAKNLLAGQRSVSYICSRFYRAPELMLGATNYTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQL 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 267 VEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKVFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDELRDP 346
Cdd:PTZ00036  281 VRIIQVLGTPTEDQLKEMNPNYADIKFPDVKPKDLKKVFPKGTPDDAINFISQFLKYEPLKRLNPIEALADPFFDDLRDP 360
                         330       340
                  ....*....|....*....|.
gi 1231802383 347 NVKLPNGRDT-PALFNFTTQD 366
Cdd:PTZ00036  361 CIKLPKYIDKlPDLFNFCDAE 381
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
56-340 2.48e-84

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 257.07  E-value: 2.48e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383   56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN-----RELQIMRKLDHCNIVRLRYFFYssgekkDEVYLNL 130
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDrerilREIKILKKLKHPNIVRLYDVFE------DEDKLYL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  131 VLDYVPetvYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTaVLKLCDFGSAKQLVRG 210
Cdd:smart00220  75 VMEYCE---GGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDG-HVKLADFGLARQLDPG 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  211 EPNVSYICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIFPGDsgvDQLVEIIKVLGTPTREQIREMnpnyte 290
Cdd:smart00220 151 EKLTTFVGTPEYMAPEVLLG-KGYGKAVDIWSLGVILYELLTGKPPFPGD---DQLLELFKKIGKPKPPFPPPE------ 220
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1231802383  291 fkfpqikahpwtkvfrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:smart00220 221 ----------------WDISPEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
56-340 1.43e-54

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 179.36  E-value: 1.43e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN------RELQIMRKLDHCNIVRLRYFFYssgekkDEVYLN 129
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKkdknilREIKILKKLNHPNIVRLYDAFE------DKDNLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 LVLDYVPETVYrvARHYSRAKqTLPVIYVKLYMYQLFRSLAyihsfgichrdikpqnllldpdtavlklcdfgsakqlvR 209
Cdd:pfam00069  75 LVLEYVEGGSL--FDLLSEKG-AFSEREAKFIMKQILEGLE--------------------------------------S 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 210 GEPNVSYICSRYYRAPELIfGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGvDQLVEIIkvlgtptreqIREMNPNYT 289
Cdd:pfam00069 114 GSSLTTFVGTPWYMAPEVL-GGNPYGPKVDVWSLGCILYELLTGKPPFPGING-NEIYELI----------IDQPYAFPE 181
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1231802383 290 EFkfpqikahpwtkvfrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:pfam00069 182 LP---------------SNLSEEAKDLLKKLLKKDPSKRLTATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
56-345 3.22e-48

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 170.19  E-value: 3.22e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQD--------KRFKnRELQIMRKLDHCNIVRLryffYSSGEKKDEVY 127
Cdd:COG0515     9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPElaadpearERFR-REARALARLNHPNIVRV----YDVGEEDGRPY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 128 LnlVLDYVP-ETVyrvaRHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKLCDFGSAKQ 206
Cdd:COG0515    84 L--VMEYVEgESL----ADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPD-GRVKLIDFGIARA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 207 LVRGEPNVS--YICSRYYRAPELIFGAT-DYTSsiDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREqire 283
Cdd:COG0515   157 LGGATLTQTgtVVGTPGYMAPEQARGEPvDPRS--DVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSE---- 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 284 mnpnytefkfpqikahpwtkvFRPRTPPEAIALCSRLLEYTPTARLtpleACAHSFFDELRD 345
Cdd:COG0515   231 ---------------------LRPDLPPALDAIVLRALAKDPEERY----QSAAELAAALRA 267
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
60-263 1.76e-24

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 104.88  E-value: 1.76e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKlcDS--GELVAIKkVLQD---------KRFKnRELQIMRKLDHCNIVRLryffYSSGEKKDEVYL 128
Cdd:NF033483   13 ERIGRGGMAEVYLAK--DTrlDRDVAVK-VLRPdlardpefvARFR-REAQSAASLSHPNIVSV----YDVGEDGGIPYI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 129 nlVLDYVP-ETVyrvaRHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQL 207
Cdd:NF033483   85 --VMEYVDgRTL----KDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRV-KVTDFGIARAL 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1231802383 208 vrGEPNVSY----ICSRYYRAPELIFGAT-DYTSsiDVWSAGCVLAELLLGQPIFPGDSGV 263
Cdd:NF033483  158 --SSTTMTQtnsvLGTVHYLSPEQARGGTvDARS--DIYSLGIVLYEMLTGRPPFDGDSPV 214
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
77-323 7.72e-16

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 79.50  E-value: 7.72e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383   77 DSGELVAIKKVLQD--------KRFKnRELQIMRKLDHCNIVRLryffYSSGEKKDEvYLNLVLDYVPEtvyRVARHYSR 148
Cdd:TIGR03903    1 MTGHEVAIKLLRTDapeeehqrARFR-RETALCARLYHPNIVAL----LDSGEAPPG-LLFAVFEYVPG---RTLREVLA 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  149 AKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDP--DTAVLKLCDFG-----------SAKQLVR-GEpnv 214
Cdd:TIGR03903   72 ADGALPAGETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQtgVRPHAKVLDFGigtllpgvrdaDVATLTRtTE--- 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  215 sYICSRYYRAPELIFGATdYTSSIDVWSAGCVLAELLLGQPIFPGDSgvdqLVEIIKvlgtptreqiREMNPNytEFKFP 294
Cdd:TIGR03903  149 -VLGTPTYCAPEQLRGEP-VTPNSDLYAWGLIFLECLTGQRVVQGAS----VAEILY----------QQLSPV--DVSLP 210
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1231802383  295 Q-IKAHPWTKVFR------PR---TPPEAIALCSRLLEY 323
Cdd:TIGR03903  211 PwIAGHPLGQVLRkalnkdPRqraASAPALAERFRALEL 249
 
Name Accession Description Interval E-value
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
51-343 0e+00

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: 645.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  51 PQEVSYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDEVYLNL 130
Cdd:cd14137     1 PVEISYTIEKVIGSGSFGVVYQAKLLETGEVVAIKKVLQDKRYKNRELQIMRRLKHPNIVKLKYFFYSSGEKKDEVYLNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 VLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSAKQLVRG 210
Cdd:cd14137    81 VMEYMPETLYRVIRHYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDPETGVLKLCDFGSAKRLVPG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 211 EPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTE 290
Cdd:cd14137   161 EPNVSYICSRYYRAPELIFGATDYTTAIDIWSAGCVLAELLLGQPLFPGESSVDQLVEIIKVLGTPTREQIKAMNPNYTE 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1231802383 291 FKFPQIKAHPWTKVFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDEL 343
Cdd:cd14137   241 FKFPQIKPHPWEKVFPKRTPPDAIDLLSKILVYNPSKRLTALEALAHPFFDEL 293
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
29-366 1.68e-153

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 440.24  E-value: 1.68e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  29 SRDKDGSKVTTVVATPGQGPDRpqevSYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCN 108
Cdd:PTZ00036   45 NAGEDEDEEKMIDNDINRSPNK----SYKLGNIIGNGSFGVVYEAICIDTSEKVAIKKVLQDPQYKNRELLIMKNLNHIN 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 109 IVRLRYFFYSSGEKKDE--VYLNLVLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQN 186
Cdd:PTZ00036  121 IIFLKDYYYTECFKKNEknIFLNVVMEFIPQTVHKYMKHYARNNHALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQN 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 187 LLLDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQL 266
Cdd:PTZ00036  201 LLIDPNTHTLKLCDFGSAKNLLAGQRSVSYICSRFYRAPELMLGATNYTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQL 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 267 VEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKVFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDELRDP 346
Cdd:PTZ00036  281 VRIIQVLGTPTEDQLKEMNPNYADIKFPDVKPKDLKKVFPKGTPDDAINFISQFLKYEPLKRLNPIEALADPFFDDLRDP 360
                         330       340
                  ....*....|....*....|.
gi 1231802383 347 NVKLPNGRDT-PALFNFTTQD 366
Cdd:PTZ00036  361 CIKLPKYIDKlPDLFNFCDAE 381
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
56-340 3.89e-106

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: 312.63  E-value: 3.89e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN---RELQIMRKL----DHCNIVRLRYFFYSSGEKkdevYL 128
Cdd:cd05118     1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHPKaalREIKLLKHLndveGHPNIVKLLDVFEHRGGN----HL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 129 NLVLDYVPETVYRVARHYSRakqTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSAKQLV 208
Cdd:cd05118    77 CLVFELMGMNLYELIKDYPR---GLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELGQLKLADFGLARSFT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 209 RGEPNVsYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTptreqiremnpny 288
Cdd:cd05118   154 SPPYTP-YVATRWYRAPEVLLGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVRLLGT------------- 219
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 289 tefkfpqikahpwtkvfrprtpPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd05118   220 ----------------------PEALDLLSKMLKYDPAKRITASQALAHPYF 249
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
56-347 3.17e-89

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: 272.09  E-value: 3.17e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLqdKRFKN--------RELQIMRKLDHCNIVRLRYFFYS-SGEKKDEV 126
Cdd:cd07834     2 YELLKPIGSGAYGVVCSAYDKRTGRKVAIKKIS--NVFDDlidakrilREIKILRHLKHENIIGLLDILRPpSPEEFNDV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 127 YLnlVLDYVPETVYRVARhysrAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQ 206
Cdd:cd07834    80 YI--VTELMETDLHKVIK----SPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVN-SNCDLKICDFGLARG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 207 LVRGEPNV---SYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQI-R 282
Cdd:cd07834   153 VDPDEDKGfltEYVVTRWYRAPELLLSSKKYTKAIDIWSVGCIFAELLTRKPLFPGRDYIDQLNLIVEVLGTPSEEDLkF 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1231802383 283 EMNPNYTEF--KFPQIKAHPWTKVFrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDELRDPN 347
Cdd:cd07834   233 ISSEKARNYlkSLPKKPKKPLSEVF-PGASPEAIDLLEKMLVFNPKKRITADEALAHPYLAQLHDPE 298
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
56-340 2.04e-86

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: 263.57  E-value: 2.04e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRfKN-------RELQIMRKLDHCNIVRLRYFFYSsgekKDEVYL 128
Cdd:cd07829     1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIRLDNE-EEgipstalREISLLKELKHPNIVKLLDVIHT----ENKLYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 129 nlVLDYVPETVyrvaRHY-SRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQL 207
Cdd:cd07829    76 --VFEYCDQDL----KKYlDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLIN-RDGVLKLADFGLARAF 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 208 vrGEPNVSY---ICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREM 284
Cdd:cd07829   149 --GIPLRTYtheVVTLWYRAPEILLGSKHYSTAVDIWSVGCIFAELITGKPLFPGDSEIDQLFKIFQILGTPTEESWPGV 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1231802383 285 N--PNYTeFKFPQIKAHPWTKVFrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd07829   227 TklPDYK-PTFPKWPKNDLEKVL-PRLDPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
56-340 2.48e-84

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 257.07  E-value: 2.48e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383   56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN-----RELQIMRKLDHCNIVRLRYFFYssgekkDEVYLNL 130
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDrerilREIKILKKLKHPNIVRLYDVFE------DEDKLYL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  131 VLDYVPetvYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTaVLKLCDFGSAKQLVRG 210
Cdd:smart00220  75 VMEYCE---GGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDG-HVKLADFGLARQLDPG 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  211 EPNVSYICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIFPGDsgvDQLVEIIKVLGTPTREQIREMnpnyte 290
Cdd:smart00220 151 EKLTTFVGTPEYMAPEVLLG-KGYGKAVDIWSLGVILYELLTGKPPFPGD---DQLLELFKKIGKPKPPFPPPE------ 220
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1231802383  291 fkfpqikahpwtkvfrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:smart00220 221 ----------------WDISPEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
56-340 3.06e-81

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: 250.32  E-value: 3.06e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKL-------DHCNIVRLRYFFyssgekKDEVYL 128
Cdd:cd07832     2 YKILGRIGEGAHGIVFKAKDRETGETVALKKVALRKLEGGIPNQALREIkalqacqGHPYVVKLRDVF------PHGTGF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 129 NLVLDYVPETVYRVARHYSRAkqtLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKqLV 208
Cdd:cd07832    76 VLVFEYMLSSLSEVLRDEERP---LTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLIS-STGVLKIADFGLAR-LF 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 209 RGEPNVSY---ICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMN 285
Cdd:cd07832   151 SEEDPRLYshqVATRWYRAPELLYGSRKYDEGVDLWAVGCIFAELLNGSPLFPGENDIEQLAIVLRTLGTPNEKTWPELT 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1231802383 286 --PNYTEFKFPQIKAHPWTKVFrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd07832   231 slPDYNKITFPESKGIRLEEIF-PDCSPEAIDLLKGLLVYNPKKRLSAEEALRHPYF 286
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
61-340 1.33e-80

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: 248.77  E-value: 1.33e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  61 VIGNGSFGVVYQAKLCDSGELVAIKKVLQ---DKRFKN---RELQIMRKLDHCNIVRLRYFFYSSGEkkdevyLNLVLDY 134
Cdd:cd07833     8 VVGEGAYGVVLKCRNKATGEIVAIKKFKEsedDEDVKKtalREVKVLRQLRHENIVNLKEAFRRKGR------LYLVFEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 135 VPETVYRVARHYSRAkqtLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKLCDFGSAKQLvRGEPNV 214
Cdd:cd07833    82 VERTLLELLEASPGG---LPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSES-GVLKLCDFGFARAL-TARPAS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 215 ---SYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGT-PTREQIREM-NPNYT 289
Cdd:cd07833   157 pltDYVATRWYRAPELLVGDTNYGKPVDVWAIGCIMAELLDGEPLFPGDSDIDQLYLIQKCLGPlPPSHQELFSsNPRFA 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1231802383 290 EFKFPQIKaHPWTKVFRPRT--PPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd07833   237 GVAFPEPS-QPESLERRYPGkvSSPALDFLKACLRMDPKERLTCDELLQHPYF 288
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
56-340 2.09e-80

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: 248.22  E-value: 2.09e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQdkRFKN-------RELQIMRKL-DHCNIVRLRYFFYSSGEkkdevy 127
Cdd:cd07830     1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKMKK--KFYSweecmnlREVKSLRKLnEHPNIVKLKEVFRENDE------ 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 128 LNLVLDYVPETVYRVARhySRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTaVLKLCDFGSAKQL 207
Cdd:cd07830    73 LYFVFEYMEGNLYQLMK--DRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPE-VVKIADFGLAREI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 208 VRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIRE---- 283
Cdd:cd07830   150 RSRPPYTDYVSTRWYRAPEILLRSTSYSSPVDIWALGCIMAELYTLRPLFPGSSEIDQLYKICSVLGTPTKQDWPEgykl 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 284 ---MNpnyteFKFPQIKAHPWTKVFrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd07830   230 askLG-----FRFPQFAPTSLHQLI-PNASPEAIDLIKDMLRWDPKKRPTASQALQHPYF 283
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
56-340 9.98e-79

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: 244.40  E-value: 9.98e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN---------RELQIMRKLDHCNIVRLRYFFyssGEKKdev 126
Cdd:cd07841     2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERKEAkdginftalREIKLLQELKHPNIIGLLDVF---GHKS--- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 127 YLNLVLDYVP---ETVYRvarhysRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKLCDFGS 203
Cdd:cd07841    76 NINLVFEFMEtdlEKVIK------DKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASD-GVLKLADFGL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 204 AKQLvrGEPNVSYIC---SRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQ 280
Cdd:cd07841   149 ARSF--GSPNRKMTHqvvTRWYRAPELLFGARHYGVGVDMWSVGCIFAELLLRVPFLPGDSDIDQLGKIFEALGTPTEEN 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 281 IREMN--PNYTEFKFpqIKAHPWTKVFrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd07841   227 WPGVTslPDYVEFKP--FPPTPLKQIF-PAASDDALDLLQRLLTLNPNKRITARQALEHPYF 285
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
62-340 3.97e-75

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: 234.77  E-value: 3.97e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKVlqdkRFKN----------RELQIMRKLDHCNIVRLRYFFYSSGEKKDEVYLNLV 131
Cdd:cd07840     7 IGEGTYGQVYKARNKKTGELVALKKI----RMENekegfpitaiREIKLLQKLDHPNVVRLKEIVTSKGSAKYKGSIYMV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 132 LDYVPETVYRVARHYSrAKQTLPviYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKLCDFGSAKQLVRgE 211
Cdd:cd07840    83 FEYMDHDLTGLLDNPE-VKFTES--QIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINND-GVLKLADFGLARPYTK-E 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 212 PNVSY---ICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTRE---QIREMn 285
Cdd:cd07840   158 NNADYtnrVITLWYRPPELLLGATRYGPEVDMWSVGCILAELFTGKPIFQGKTELEQLEKIFELCGSPTEEnwpGVSDL- 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1231802383 286 PNYTEFKFPQIKAHPWTKVFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd07840   237 PWFENLKPKKPYKRRLREVFKNVIDPSALDLLDKLLTLDPKKRISADQALQHEYF 291
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
62-347 4.22e-73

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: 231.29  E-value: 4.22e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKVLQdkRFKN--------RELQIMRKL-DHCNIVRLRYFFYSSGEKkdEVYLnlVL 132
Cdd:cd07852    15 LGKGAYGIVWKAIDKKTGEVVALKKIFD--AFRNatdaqrtfREIMFLQELnDHPNIIKLLNVIRAENDK--DIYL--VF 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 DYVPETVYRVARhysraKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLVRGEP 212
Cdd:cd07852    89 EYMETDLHAVIR-----ANILEDIHKQYIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRV-KLADFGLARSLSQLEE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 213 NVS------YICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNP 286
Cdd:cd07852   163 DDEnpvltdYVATRWYRAPEILLGSTRYTKGVDMWSVGCILGEMLLGKPLFPGTSTLNQLEKIIEVIGRPSAEDIESIQS 242
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1231802383 287 NYTE---FKFPQIKAHPWTKVFrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDELRDPN 347
Cdd:cd07852   243 PFAAtmlESLPPSRPKSLDELF-PKASPDALDLLKKLLVFNPNKRLTAEEALRHPYVAQFHNPA 305
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
55-362 3.37e-68

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: 218.39  E-value: 3.37e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  55 SYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKV------LQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDEVYL 128
Cdd:cd07855     6 RYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIpnafdvVTTAKRTLRELKILRHFKHDNIIAIRDILRPKVPYADFKDV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 129 NLVLDYVPETVYRVARhysrAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKLCDFGSAKQLV 208
Cdd:cd07855    86 YVVLDLMESDLHHIIH----SDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNEN-CELKIGDFGMARGLC 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 209 RGEPN-----VSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIRE 283
Cdd:cd07855   161 TSPEEhkyfmTEYVATRWYRAPELMLSLPEYTQAIDMWSVGCIFAEMLGRRQLFPGKNYVHQLQLILTVLGTPSQAVINA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 284 MNP----NYTEfKFPQIKAHPWTKVFrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDELRDPNvklpNGRDTPAL 359
Cdd:cd07855   241 IGAdrvrRYIQ-NLPNKQPVPWETLY-PKADQQALDLLSQMLRFDPSERITVAEALQHPFLAKYHDPD----DEPDCAPP 314

                  ...
gi 1231802383 360 FNF 362
Cdd:cd07855   315 FDF 317
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
56-347 4.04e-68

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: 218.33  E-value: 4.04e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVlqdKRFKN--------RELQIMRKLDHCNIVRLRYFFYS-SGEKKDEV 126
Cdd:cd07849     7 YQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKI---SPFEHqtyclrtlREIKILLRFKHENIIGILDIQRPpTFESFKDV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 127 YLnlVLDYVPETVYRVARhysraKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQ 206
Cdd:cd07849    84 YI--VQELMETDLYKLIK-----TQHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLN-TNCDLKICDFGLARI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 207 LVRGEPN----VSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTRE--- 279
Cdd:cd07849   156 ADPEHDHtgflTEYVATRWYRAPEIMLNSKGYTKAIDIWSVGCILAEMLSNRPLFPGKDYLHQLNLILGILGTPSQEdln 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1231802383 280 -QIREMNPNYTEfKFPQIKAHPWTKVFrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDELRDPN 347
Cdd:cd07849   236 cIISLKARNYIK-SLPFKPKVPWNKLF-PNADPKALDLLDKMLTFNPHKRITVEEALAHPYLEQYHDPS 302
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
62-340 4.68e-68

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: 216.39  E-value: 4.68e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN------RELQIMRKLDHCNIVRLRYFFYSsgEKKdevyLNLVLDYV 135
Cdd:cd07835     7 IGEGTYGVVYKARDKLTGEIVALKKIRLETEDEGvpstaiREISLLKELNHPNIVRLLDVVHS--ENK----LYLVFEFL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 136 PETVyrvaRHY--SRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQLvrGEPN 213
Cdd:cd07835    81 DLDL----KKYmdSSPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLID-TEGALKLADFGLARAF--GVPV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 214 VSY---ICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQ---IREMnPN 287
Cdd:cd07835   154 RTYtheVVTLWYRAPEILLGSKHYSTPVDIWSVGCIFAEMVTRRPLFPGDSEIDQLFRIFRTLGTPDEDVwpgVTSL-PD 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1231802383 288 YTEfKFPQIKAHPWTKVFrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd07835   233 YKP-TFPKWARQDLSKVV-PSLDEDGLDLLSQMLVYDPAKRISAKAALQHPYF 283
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
56-362 3.19e-67

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: 216.08  E-value: 3.19e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVlqDKRFKN--------RELQIMRKLDHCNIVRLRYFFYSSG-EKKDEV 126
Cdd:cd07858     7 YVPIKPIGRGAYGIVCSAKNSETNEKVAIKKI--ANAFDNridakrtlREIKLLRHLDHENVIAIKDIMPPPHrEAFNDV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 127 YLnlVLDYVPETVYRVARhysrAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAvLKLCDFGSAK- 205
Cdd:cd07858    85 YI--VYELMDTDLHQIIR----SSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCD-LKICDFGLARt 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 206 QLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREM- 284
Cdd:cd07858   158 TSEKGDFMTEYVVTRWYRAPELLLNCSEYTTAIDVWSVGCIFAELLGRKPLFPGKDYVHQLKLITELLGSPSEEDLGFIr 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 285 NPNYTEF--KFPQIKAHPWTKVFrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDELRDPNVKLPNgrDTPALFNF 362
Cdd:cd07858   238 NEKARRYirSLPYTPRQSFARLF-PHANPLAIDLLEKMLVFDPSKRITVEEALAHPYLASLHDPSDEPVC--QTPFSFDF 314
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
48-347 3.63e-64

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: 208.30  E-value: 3.63e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  48 PDRPQEVSYtdtkvIGNGSFGVVYQAKLCDSGELVAIKKVLQDkrFKN--------RELQIMRKLDHCNIVRLRYFFY-- 117
Cdd:cd07851    14 PDRYQNLSP-----VGSGAYGQVCSAFDTKTGRKVAIKKLSRP--FQSaihakrtyRELRLLKHMKHENVIGLLDVFTpa 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 118 SSGEKKDEVYLnlVLDYVPETVYRVARHysrakQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAvLK 197
Cdd:cd07851    87 SSLEDFQDVYL--VTHLMGADLNNIVKC-----QKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCE-LK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 198 LCDFGSAKQLvrGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPT 277
Cdd:cd07851   159 ILDFGLARHT--DDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGKTLFPGSDHIDQLKRIMNLVGTPD 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1231802383 278 REQIREMNP----NYTEfKFPQIKAHPWTKVFrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDELRDPN 347
Cdd:cd07851   237 EELLKKISSesarNYIQ-SLPQMPKKDFKEVF-SGANPLAIDLLEKMLVLDPDKRITAAEALAHPYLAEYHDPE 308
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
62-340 5.92e-64

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: 205.58  E-value: 5.92e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKVlqDKRFKN-------RELQIMRKL-DHCNIVRLRYFFYSSGEKKdevyLNLVLD 133
Cdd:cd07831     7 IGEGTFSEVLKAQSRKTGKYYAIKCM--KKHFKSleqvnnlREIQALRRLsPHPNILRLIEVLFDRKTGR----LALVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 134 YVPETVYRVARhySRaKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTavLKLCDFGSAKQLVRGEPN 213
Cdd:cd07831    81 LMDMNLYELIK--GR-KRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDDI--LKLADFGSCRGIYSKPPY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 214 VSYICSRYYRAPELIFgaTD--YTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNP-NYTE 290
Cdd:cd07831   156 TEYISTRWYRAPECLL--TDgyYGPKMDIWAVGCVFFEILSLFPLFPGTNELDQIAKIHDVLGTPDAEVLKKFRKsRHMN 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1231802383 291 FKFPQIKAHPWTKVFrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd07831   234 YNFPSKKGTGLRKLL-PNASAEGLDLLKKLLAYDPDERITAKQALRHPYF 282
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
62-342 3.56e-62

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: 202.21  E-value: 3.56e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN------RELQIMRKLDHCNIVRLRYFFysSGEKKDEVYLnlVLDYV 135
Cdd:cd07845    15 IGEGTYGIVYRARDTTSGEIVALKKVRMDNERDGipisslREITLLLNLRHPNIVELKEVV--VGKHLDSIFL--VMEYC 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 136 PETVyrvARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKqlVRGEPNVS 215
Cdd:cd07845    91 EQDL---ASLLDNMPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLT-DKGCLKIADFGLAR--TYGLPAKP 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 216 Y---ICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTrEQI----REMnPNY 288
Cdd:cd07845   165 MtpkVVTLWYRAPELLLGCTTYTTAIDMWAVGCILAELLAHKPLLPGKSEIEQLDLIIQLLGTPN-ESIwpgfSDL-PLV 242
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1231802383 289 TEFKFPQikaHPWTKVfRPRTP--PEA-IALCSRLLEYTPTARLTPLEACAHSFFDE 342
Cdd:cd07845   243 GKFTLPK---QPYNNL-KHKFPwlSEAgLRLLNFLLMYDPKKRATAEEALESSYFKE 295
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
62-340 4.46e-61

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: 199.43  E-value: 4.46e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDS--GELVAIKKVLQDKRFKN-------RELQIMRKLDHCNIVRLRYFFYSSGEKKdeVYLnlVL 132
Cdd:cd07842     8 IGRGTYGRVYKAKRKNGkdGKEYAIKKFKGDKEQYTgisqsacREIALLRELKHENVVSLVEVFLEHADKS--VYL--LF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 DYVPETVYRVARHYSRAKQT-LPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLL---DPDTAVLKLCDFGSA---- 204
Cdd:cd07842    84 DYAEHDLWQIIKFHRQAKRVsIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVmgeGPERGVVKIGDLGLArlfn 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 205 ---KQLVRGEPNVSYIcsrYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSG---------VDQLVEIIKV 272
Cdd:cd07842   164 aplKPLADLDPVVVTI---WYRAPELLLGARHYTKAIDIWAIGCIFAELLTLEPIFKGREAkikksnpfqRDQLERIFEV 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1231802383 273 LGTPTREQ---IREMnPNYTEF-------KFPQIKAHPWTKVFRPRTpPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd07842   241 LGTPTEKDwpdIKKM-PEYDTLksdtkasTYPNSLLAKWMHKHKKPD-SQGFDLLRKLLEYDPTKRITAEEALEHPYF 316
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
56-340 6.43e-61

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: 198.03  E-value: 6.43e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQ---DKRFKN---RELQIMRKLDHCNIVRLRYFFyssgEKKDEVYLn 129
Cdd:cd07846     3 YENLGLVGEGSYGMVMKCRHKETGQIVAIKKFLEsedDKMVKKiamREIKMLKQLRHENLVNLIEVF----RRKKRWYL- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 lVLDYVPETVYRVARHYSRAkqtLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPdTAVLKLCDFGSAKQLVR 209
Cdd:cd07846    78 -VFEFVDHTVLDDLEKYPNG---LDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQ-SGVVKLCDFGFARTLAA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 210 -GEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGT--PTREQIREMNP 286
Cdd:cd07846   153 pGEVYTDYVATRWYRAPELLVGDTKYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDQLYHIIKCLGNliPRHQELFQKNP 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1231802383 287 NYTEFKFPQIK-AHPWTKVFrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd07846   233 LFAGVRLPEVKeVEPLERRY-PKLSGVVIDLAKKCLHIDPDKRPSCSELLHHEFF 286
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
55-341 4.61e-60

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: 196.21  E-value: 4.61e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  55 SYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKV---LQDKRFKN---RELQIMRKLDHCN-IVRLryFFYSSGEKKDEVY 127
Cdd:cd07837     2 AYEKLEKIGEGTYGKVYKARDKNTGKLVALKKTrleMEEEGVPStalREVSLLQMLSQSIyIVRL--LDVEHVEENGKPL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 128 LNLVLDYVPETVYRVARHYSRAKQT-LPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSAKQ 206
Cdd:cd07837    80 LYLVFEYLDTDLKKFIDSYGRGPHNpLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQKGLLKIADLGLGRA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 207 LVRgePNVSY---ICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIre 283
Cdd:cd07837   160 FTI--PIKSYtheIVTLWYRAPEVLLGSTHYSTPVDMWSVGCIFAEMSRKQPLFPGDSELQQLLHIFRLLGTPNEEVW-- 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 284 mnPNYTEFK----FPQIKAHPWTKVFrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFD 341
Cdd:cd07837   236 --PGVSKLRdwheYPQWKPQDLSRAV-PDLEPEGVDLLTKMLAYDPAKRISAKAALQHPYFD 294
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
62-340 3.54e-59

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: 193.49  E-value: 3.54e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN------RELQIMRKLDHCNIVRLRYFFYSsgEKKdevyLNLVLDYV 135
Cdd:cd07860     8 IGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGvpstaiREISLLKELNHPNIVKLLDVIHT--ENK----LYLVFEFL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 136 PETVYRVARhySRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLvrGEPNVS 215
Cdd:cd07860    82 HQDLKKFMD--ASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAI-KLADFGLARAF--GVPVRT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 216 Y---ICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQ---IREMnPNYT 289
Cdd:cd07860   157 YtheVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVwpgVTSM-PDYK 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1231802383 290 EfKFPQIKAHPWTKVFrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd07860   236 P-SFPKWARQDFSKVV-PPLDEDGRDLLSQMLHYDPNKRISAKAALAHPFF 284
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
62-340 1.12e-58

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: 192.44  E-value: 1.12e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN------RELQIMRKLDHCNIVRLRYFFYssGEKKDEVYLnlVLDYV 135
Cdd:cd07843    13 IEEGTYGVVYRARDKKTGEIVALKKLKMEKEKEGfpitslREINILLKLQHPNIVTVKEVVV--GSNLDKIYM--VMEYV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 136 PETVYRVARHYsraKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQLvrGEPNVS 215
Cdd:cd07843    89 EHDLKSLMETM---KQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLN-NRGILKICDFGLAREY--GSPLKP 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 216 Y---ICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREqiremnpNYTEF- 291
Cdd:cd07843   163 YtqlVVTLWYRAPELLLGAKEYSTAIDMWSVGCIFAELLTKKPLFPGKSEIDQLNKIFKLLGTPTEK-------IWPGFs 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1231802383 292 KFPQIKAHPWTK--------VFRPRTPPEA-IALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd07843   236 ELPGAKKKTFTKypynqlrkKFPALSLSDNgFDLLNRLLTYDPAKRISAEDALKHPYF 293
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
56-347 1.64e-58

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: 193.39  E-value: 1.64e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDS--GELVAIKKV-------LQDKRfKNRELQIMRKL-DHCNIVRL---RYFFYSsgeK 122
Cdd:cd07857     2 YELIKELGQGAYGIVCSARNAETseEETVAIKKItnvfskkILAKR-ALRELKLLRHFrGHKNITCLydmDIVFPG---N 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 123 KDEVYLnlvldYVPETVYRVARhYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAvLKLCDFG 202
Cdd:cd07857    78 FNELYL-----YEELMEADLHQ-IIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCE-LKICDFG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 203 SAKQL----VRGEPNVS-YICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPT 277
Cdd:cd07857   151 LARGFsenpGENAGFMTeYVATRWYRAPEIMLSFQSYTKAIDVWSVGCILAELLGRKPVFKGKDYVDQLNQILQVLGTPD 230
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1231802383 278 REQIREMNP----NYTeFKFPQIKAHPWTKVFrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDELRDPN 347
Cdd:cd07857   231 EETLSRIGSpkaqNYI-RSLPNIPKKPFESIF-PNANPLALDLLEKLLAFDPTKRISVEEALEHPYLAIWHDPD 302
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
62-340 3.11e-58

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: 191.05  E-value: 3.11e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKVLQD------KRFKNRELQIMRKLDHCNIVRLRYFFyssgEKKDEvyLNLVLDYV 135
Cdd:cd07847     9 IGEGSYGVVFKCRNRETGQIVAIKKFVESeddpviKKIALREIRMLKQLKHPNLVNLIEVF----RRKRK--LHLVFEYC 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 136 PETVYRVARHYSRAkqtLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKLCDFGSAKQLVRGEPNVS 215
Cdd:cd07847    83 DHTVLNELEKNPRG---VPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQ-GQIKLCDFGFARILTGPGDDYT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 216 -YICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLG--TPTREQIREMNPNYTEFK 292
Cdd:cd07847   159 dYVATRWYRAPELLVGDTQYGPPVDVWAIGCVFAELLTGQPLWPGKSDVDQLYLIRKTLGdlIPRHQQIFSTNQFFKGLS 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1231802383 293 FPQIKA-HPWTKVFrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd07847   239 IPEPETrEPLESKF-PNISSPALSFLKGCLQMDPTERLSCEELLEHPYF 286
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
56-345 6.41e-58

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 190.80  E-value: 6.41e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN------RELQIMRKLDHCNIVRLRYFFYSsgEKKdevyLN 129
Cdd:PLN00009    4 YEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEDEGvpstaiREISLLKEMQHGNIVRLQDVVHS--EKR----LY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 LVLDYVPETVYRVARHYSRAKQTLPVIyvKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSAKQLvr 209
Cdd:PLN00009   78 LVFEYLDLDLKKHMDSSPDFAKNPRLI--KTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTNALKLADFGLARAF-- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 210 GEPNVSY---ICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMN- 285
Cdd:PLN00009  154 GIPVRTFtheVVTLWYRAPEILLGSRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIFRILGTPNEETWPGVTs 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1231802383 286 -PNYTEfKFPQIKAHPWTKVFrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDELRD 345
Cdd:PLN00009  234 lPDYKS-AFPKWPPKDLATVV-PTLEPAGVDLLSKMLRLDPSKRITARAALEHEYFKDLGD 292
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
55-340 6.48e-58

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: 190.38  E-value: 6.48e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  55 SYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN-----RELQIMRKLDHCNIVRLRYFFYSsgEKKdevyLN 129
Cdd:cd07836     1 NFKQLEKLGEGTYATVYKGRNRTTGEIVALKEIHLDAEEGTpstaiREISLMKELKHENIVRLHDVIHT--ENK----LM 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 LVLDYVPETVYRVARHYSRaKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKLCDFGSAKQLvr 209
Cdd:cd07836    75 LVFEYMDKDLKKYMDTHGV-RGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKR-GELKLADFGLARAF-- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 210 GEPNVSY---ICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMN- 285
Cdd:cd07836   151 GIPVNTFsneVVTLWYRAPDVLLGSRTYSTSIDIWSVGCIMAEMITGRPLFPGTNNEDQLLKIFRIMGTPTESTWPGISq 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1231802383 286 -PNYtEFKFPQIKAHPWTKVFrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd07836   231 lPEY-KPTFPRYPPQDLQQLF-PHADPLGIDLLHRLLQLNPELRISAHDALQHPWF 284
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
55-340 2.19e-57

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: 189.13  E-value: 2.19e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  55 SYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKV-LQDKR---FKN-RELQIMRKLDHCNIVRLRYFFYSsgekkdEVYLN 129
Cdd:cd07844     1 TYKKLDKLGEGSYATVYKGRSKLTGQLVALKEIrLEHEEgapFTAiREASLLKDLKHANIVTLHDIIHT------KKTLT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 LVLDYVPETVYRVARHYSRAkqtLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKqlVR 209
Cdd:cd07844    75 LVFEYLDTDLKQYMDDCGGG---LSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLIS-ERGELKLADFGLAR--AK 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 210 GEPNVSY---ICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGV-DQLVEIIKVLGTPTREQIR--E 283
Cdd:cd07844   149 SVPSKTYsneVVTLWYRPPDVLLGSTEYSTSLDMWGVGCIFYEMATGRPLFPGSTDVeDQLHKIFRVLGTPTEETWPgvS 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1231802383 284 MNPNYTEFKFPQIKAHPWTKVFrPR--TPPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd07844   229 SNPEFKPYSFPFYPPRPLINHA-PRldRIPHGEELALKFLQYEPKKRISAAEAMKHPYF 286
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
55-340 2.47e-57

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: 188.80  E-value: 2.47e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  55 SYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDK------RFKNRELQIMRKLDHCNIVRLRYFFYSsgEKKdevyL 128
Cdd:cd07839     1 KYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDddegvpSSALREICLLKELKHKNIVRLYDVLHS--DKK----L 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 129 NLVLDYVPETVyrvARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQLv 208
Cdd:cd07839    75 TLVFEYCDQDL---KKYFDSCNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLIN-KNGELKLADFGLARAF- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 209 rGEPNVSY---ICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELL-LGQPIFPGDSGVDQLVEIIKVLGTPTREQIREM 284
Cdd:cd07839   150 -GIPVRCYsaeVVTLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELAnAGRPLFPGNDVDDQLKRIFRLLGTPTEESWPGV 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1231802383 285 N--PNYTEF-KFPQIKAhpWTKVFrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd07839   229 SklPDYKPYpMYPATTS--LVNVV-PKLNSTGRDLLQNLLVCNPVQRISAEEALQHPYF 284
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
55-340 5.76e-57

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: 188.68  E-value: 5.76e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  55 SYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQdKRFKN-------RELQIMRKLDHCNIVRLRYFFYS----SGEKK 123
Cdd:cd07866     9 DYEILGKLGEGTFGEVYKARQIKTGRVVALKKILM-HNEKDgfpitalREIKILKKLKHPNVVPLIDMAVErpdkSKRKR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 124 DEVYLnlVLDYVPETVYRVArHYSRAKQTLPVIyvKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGS 203
Cdd:cd07866    88 GSVYM--VTPYMDHDLSGLL-ENPSVKLTESQI--KCYMLQLLEGINYLHENHILHRDIKAANILID-NQGILKIADFGL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 204 AKQLVRGEPNVSY------------ICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIK 271
Cdd:cd07866   162 ARPYDGPPPNPKGgggggtrkytnlVVTRWYRPPELLLGERRYTTAVDIWGIGCVFAEMFTRRPILQGKSDIDQLHLIFK 241
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1231802383 272 VLGTPTREQIremnPNYTefKFPQIKAHPWTKVfRPRT--------PPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd07866   242 LCGTPTEETW----PGWR--SLPGCEGVHSFTN-YPRTleerfgklGPEGLDLLSKLLSLDPYKRLTASDALEHPYF 311
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
56-340 8.92e-57

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: 189.22  E-value: 8.92e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKK-VLQDKR-FKN--RELQIMRKLDHCNIVRLRYFFYSSGEK-----KDEV 126
Cdd:cd07854     7 YMDLRPLGCGSNGLVFSAVDSDCDKRVAVKKiVLTDPQsVKHalREIKIIRRLDHDNIVKVYEVLGPSGSDltedvGSLT 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 127 YLN---LVLDYVPETVYRVARHysrakQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGS 203
Cdd:cd07854    87 ELNsvyIVQEYMETDLANVLEQ-----GPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTEDLVLKIGDFGL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 204 AKQLvrgEPNVSY-------ICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQL---VEIIKVL 273
Cdd:cd07854   162 ARIV---DPHYSHkgylsegLVTKWYRSPRLLLSPNNYTKAIDMWAAGCIFAEMLTGKPLFAGAHELEQMqliLESVPVV 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1231802383 274 GTPTREQIREMNPNYTEFKFPQIKaHPWTKVFrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd07854   239 REEDRNELLNVIPSFVRNDGGEPR-RPLRDLL-PGVNPEALDFLEQILTFNPMDRLTAEEALMHPYM 303
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
56-368 1.78e-56

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: 187.78  E-value: 1.78e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLqdKRFKN--------RELQIMRKLDHCNIVRLRYFFYSSGEkkdEVY 127
Cdd:cd07856    12 YSDLQPVGMGAFGLVCSARDQLTGQNVAVKKIM--KPFSTpvlakrtyRELKLLKHLRHENIISLSDIFISPLE---DIY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 128 LnlVLDYVPETVYRVARHYSRAKQtlpviYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKql 207
Cdd:cd07856    87 F--VTELLGTDLHRLLTSRPLEKQ-----FIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVN-ENCDLKICDFGLAR-- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 208 VRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREM-NP 286
Cdd:cd07856   157 IQDPQMTGYVSTRYYRAPEIMLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNQFSIITELLGTPPDDVINTIcSE 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 287 NYTEF--KFPQIKAHPWTKVFrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDELRDPNvklpngrDTP---ALFN 361
Cdd:cd07856   237 NTLRFvqSLPKRERVPFSEKF-KNADPDAIDLLEKMLVFDPKKRISAAEALAHPYLAPYHDPT-------DEPvadEKFD 308

                  ....*..
gi 1231802383 362 FTTQDAN 368
Cdd:cd07856   309 WSFNDAD 315
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
62-341 4.11e-56

Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK2 is a tetrameric protein with two catalytic (alpha) and two regulatory (beta) subunits. It is constitutively active and ubiquitously expressed, and is found in the cytoplasm, nucleus, as well as in the plasma membrane. It phosphorylates a wide variety of substrates including gylcogen synthase, cell cycle proteins, nuclear proteins (e.g. DNA topoisomerase II), and ion channels (e.g. ENaC), among others. It may be considered a master kinase controlling the activity or lifespan of many other kinases and exerting its effect over cell fate, gene expression, protein synthesis and degradation, and viral infection. CK2 is implicated in every stage of the cell cycle and is required for cell cycle progression. It plays crucial roles in cell differentiation, proliferation, and survival, and is thus implicated in cancer. CK2 is not an oncogene by itself but elevated CK2 levels create an environment that enhances the survival of tumor cells. The CK2 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: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 186.21  E-value: 4.11e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIK--KVLQDKRFkNRELQIMRKL-DHCNIVRLryffYSSGEKKDEVYLNLVLDYVPET 138
Cdd:cd14132    26 IGRGKYSEVFEGINIGNNEKVVIKvlKPVKKKKI-KREIKILQNLrGGPNIVKL----LDVVKDPQSKTPSLIFEYVNNT 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 139 VYRVARhysrakQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSAkqlvrgE---PNVS 215
Cdd:cd14132   101 DFKTLY------PTLTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDHEKRKLRLIDWGLA------EfyhPGQE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 216 YIC---SRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLG-QPIFPGDSGVDQLVEIIKVLGtpTREQIREMN------ 285
Cdd:cd14132   169 YNVrvaSRYYKGPELLVDYQYYDYSLDMWSLGCMLASMIFRkEPFFHGHDNYDQLVKIAKVLG--TDDLYAYLDkygiel 246
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 286 PNYTEFKFPQIKAHPWTKVFRPRT----PPEAIALCSRLLEYTPTARLTPLEACAHSFFD 341
Cdd:cd14132   247 PPRLNDILGRHSKKPWERFVNSENqhlvTPEALDLLDKLLRYDHQERITAKEAMQHPYFD 306
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
56-347 9.79e-56

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: 186.31  E-value: 9.79e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKV---LQDKRFKNR---ELQIMRKLDHCNIVRLRYFFYSSGEKKDEVYLN 129
Cdd:cd07880    17 YRDLKQVGSGAYGTVCSALDRRTGAKVAIKKLyrpFQSELFAKRayrELRLLKHMKHENVIGLLDVFTPDLSLDRFHDFY 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 LVLDYVPETVYRVARHysrakQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAvLKLCDFGSAKQlvR 209
Cdd:cd07880    97 LVMPFMGTDLGKLMKH-----EKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCE-LKILDFGLARQ--T 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 210 GEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNP--- 286
Cdd:cd07880   169 DSEMTGYVVTRWYRAPEVILNWMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQLMEIMKVTGTPSKEFVQKLQSeda 248
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 287 -NYTEfKFPQIKAHPWTKVFrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDELRDPN 347
Cdd:cd07880   249 kNYVK-KLPRFRKKDFRSLL-PNANPLAVNVLEKMLVLDAESRITAAEALAHPYFEEFHDPE 308
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
56-340 2.20e-55

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: 183.63  E-value: 2.20e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVlqdkRFKN----------RELQIMRKLD---HCNIVRLRYFFYSSgEK 122
Cdd:cd07838     1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKV----RVPLseegiplstiREIALLKQLEsfeHPNVVRLLDVCHGP-RT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 123 KDEVYLNLVLDYVPETVYRVARHYSraKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFG 202
Cdd:cd07838    76 DRELKLTLVFEHVDQDLATYLDKCP--KPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQV-KLADFG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 203 SAKQLVRGEPNVSYICSRYYRAPELIFGATdYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQir 282
Cdd:cd07838   153 LARIYSFEMALTSVVVTLWYRAPEVLLQSS-YATPVDMWSVGCIFAELFNRRPLFRGSSEADQLGKIFDVIGLPSEEE-- 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1231802383 283 emnpnytefkFPQIKAHPWTKvFRPRTP-----------PEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd07838   230 ----------WPRNSALPRSS-FPSYTPrpfksfvpeidEEGLDLLKKMLTFNPHKRISAFEALQHPYF 287
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
60-340 2.44e-55

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: 184.29  E-value: 2.44e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNR---ELQIMRKL------DHCNIVRLRYFFYSSGekkdevYLNL 130
Cdd:cd14210    19 SVLGKGSFGQVVKCLDHKTGQLVAIKIIRNKKRFHQQalvEVKILKHLndndpdDKHNIVRYKDSFIFRG------HLCI 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 VLDYVPETVYRVARhySRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLL-DPDTAVLKLCDFGSAKQLvr 209
Cdd:cd14210    93 VFELLSINLYELLK--SNNFQGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLkQPSKSSIKVIDFGSSCFE-- 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 210 GEPNVSYICSRYYRAPELIFGAtDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYT 289
Cdd:cd14210   169 GEKVYTYIQSRFYRAPEVILGL-PYDTAIDMWSLGCILAELYTGYPLFPGENEEEQLACIMEVLGVPPKSLIDKASRRKK 247
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1231802383 290 EFK---FPQIKAHPWTKVFRPRT----------PPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd14210   248 FFDsngKPRPTTNSKGKKRRPGSkslaqvlkcdDPSFLDFLKKCLRWDPSERMTPEEALQHPWI 311
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
56-347 5.89e-55

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: 184.34  E-value: 5.89e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKV---LQDKRFKNR---ELQIMRKLDHCNIVRLRYFFYSSGEKKDEVYLN 129
Cdd:cd07879    17 YTSLKQVGSGAYGSVCSAIDKRTGEKVAIKKLsrpFQSEIFAKRayrELTLLKHMQHENVIGLLDVFTSAVSGDEFQDFY 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 LVLDYVPETVYRV-ARHYSRAKqtlpviyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAvLKLCDFGSAKQlv 208
Cdd:cd07879    97 LVMPYMQTDLQKImGHPLSEDK-------VQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCE-LKILDFGLARH-- 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 209 RGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMN--- 285
Cdd:cd07879   167 ADAEMTGYVVTRWYRAPEVILNWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQILKVTGVPGPEFVQKLEdka 246
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1231802383 286 -PNYTEfKFPQIKAHPWTKVFrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDELRDPN 347
Cdd:cd07879   247 aKSYIK-SLPKYPRKDFSTLF-PKASPQAVDLLEKMLELDVDKRLTATEALEHPYFDSFRDAD 307
Pkinase pfam00069
Protein kinase domain;
56-340 1.43e-54

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 179.36  E-value: 1.43e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN------RELQIMRKLDHCNIVRLRYFFYssgekkDEVYLN 129
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKkdknilREIKILKKLNHPNIVRLYDAFE------DKDNLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 LVLDYVPETVYrvARHYSRAKqTLPVIYVKLYMYQLFRSLAyihsfgichrdikpqnllldpdtavlklcdfgsakqlvR 209
Cdd:pfam00069  75 LVLEYVEGGSL--FDLLSEKG-AFSEREAKFIMKQILEGLE--------------------------------------S 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 210 GEPNVSYICSRYYRAPELIfGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGvDQLVEIIkvlgtptreqIREMNPNYT 289
Cdd:pfam00069 114 GSSLTTFVGTPWYMAPEVL-GGNPYGPKVDVWSLGCILYELLTGKPPFPGING-NEIYELI----------IDQPYAFPE 181
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1231802383 290 EFkfpqikahpwtkvfrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:pfam00069 182 LP---------------SNLSEEAKDLLKKLLKKDPSKRLTATQALQHPWF 217
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
51-347 7.36e-54

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: 181.79  E-value: 7.36e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  51 PQEvsYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKV------LQDKRFKNRELQIMRKLDHCNIVRLRYFFY--SSGEK 122
Cdd:cd07878    14 PER--YQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLsrpfqsLIHARRTYRELRLLKHMKHENVIGLLDVFTpaTSIEN 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 123 KDEVYLnlVLDYVPETVYRVARHysrakQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAvLKLCDFG 202
Cdd:cd07878    92 FNEVYL--VTNLMGADLNNIVKC-----QKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCE-LRILDFG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 203 SAKQlvRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIR 282
Cdd:cd07878   164 LARQ--ADDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLKGKALFPGNDYIDQLKRIMEVVGTPSPEVLK 241
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1231802383 283 EMNPNYTEFKF---PQIKAHPWTKVFRPRTpPEAIALCSRLLEYTPTARLTPLEACAHSFFDELRDPN 347
Cdd:cd07878   242 KISSEHARKYIqslPHMPQQDLKKIFRGAN-PLAIDLLEKMLVLDSDKRISASEALAHPYFSQYHDPE 308
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
56-340 3.52e-53

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: 177.07  E-value: 3.52e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNR---ELQIMRKL------DHCNIVRLRYFFYSsgekKDEV 126
Cdd:cd14133     1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKIIKNNKDYLDQsldEIRLLELLnkkdkaDKYHIVRLKDVFYF----KNHL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 127 YL-------NLvLDYVPETVYrvarhysrakQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLL-DPDTAVLKL 198
Cdd:cd14133    77 CIvfellsqNL-YEFLKQNKF----------QYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLaSYSRCQIKI 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 199 CDFGSAKQLVRGEpnVSYICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTR 278
Cdd:cd14133   146 IDFGSSCFLTQRL--YSYIQSRYYRAPEVILG-LPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIGIPPA 222
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 279 EQIREMNPNYTEFkfpqikahpwtkvfrprtppeaIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd14133   223 HMLDQGKADDELF----------------------VDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
56-343 4.21e-53

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: 179.59  E-value: 4.21e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKV------LQDKRFKNRELQIMRKLDHCNIVRLRYFFY--SSGEKKDeVY 127
Cdd:cd07859     2 YKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKIndvfehVSDATRILREIKLLRLLRHPDIVEIKHIMLppSRREFKD-IY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 128 LnlVLDYVPETVYRVARhysrAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAvLKLCDFGSAKQL 207
Cdd:cd07859    81 V--VFELMESDLHQVIK----ANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCK-LKICDFGLARVA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 208 VRGEPN----VSYICSRYYRAPELIfGA--TDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQI 281
Cdd:cd07859   154 FNDTPTaifwTDYVATRWYRAPELC-GSffSKYTPAIDIWSIGCIFAEVLTGKPLFPGKNVVHQLDLITDLLGTPSPETI 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1231802383 282 -REMNPNYTEF--KFPQIKAHPWTKVFrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDEL 343
Cdd:cd07859   233 sRVRNEKARRYlsSMRKKQPVPFSQKF-PNADPLALRLLERLLAFDPKDRPTAEEALADPYFKGL 296
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
56-339 4.78e-53

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: 176.90  E-value: 4.78e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKkVLQDKRFKN-------RELQIMRKLDHCNIVRLRYFFyssgEKKDEVYL 128
Cdd:cd05117     2 YELGKVLGRGSFGVVRLAVHKKTGEEYAVK-IIDKKKLKSedeemlrREIEILKRLDHPNIVKLYEVF----EDDKNLYL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 129 nlVLDYVP--ETVYRVARhysraKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDP--DTAVLKLCDFGSA 204
Cdd:cd05117    77 --VMELCTggELFDRIVK-----KGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASkdPDSPIKIIDFGLA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 205 KQLVRGEPNVSYICSRYYRAPElIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSgvdqLVEIIkvlgtptrEQIREM 284
Cdd:cd05117   150 KIFEEGEKLKTVCGTPYYVAPE-VLKGKGYGKKCDIWSLGVILYILLCGYPPFYGET----EQELF--------EKILKG 216
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1231802383 285 NPNyteFKFPqikahPWTKVfrprtPPEAIALCSRLLEYTPTARLTPLEACAHSF 339
Cdd:cd05117   217 KYS---FDSP-----EWKNV-----SEEAKDLIKRLLVVDPKKRLTAAEALNHPW 258
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
61-340 5.89e-53

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: 177.50  E-value: 5.89e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  61 VIGNGSFGVVYQAKLCDSGELVAIKKVLQD------KRFKNRELQIMRKLDHCNIVRLRYFFYSSGEkkdevyLNLVLDY 134
Cdd:cd07848     8 VVGEGAYGVVLKCRHKETKEIVAIKKFKDSeeneevKETTLRELKMLRTLKQENIVELKEAFRRRGK------LYLVFEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 135 VPETVYRVARHYSRAkqtLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTaVLKLCDFGSAKQLVRG-EPN 213
Cdd:cd07848    82 VEKNMLELLEEMPNG---VPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHND-VLKLCDFGFARNLSEGsNAN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 214 VS-YICSRYYRAPELIFGATdYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREM--NPNYTE 290
Cdd:cd07848   158 YTeYVATRWYRSPELLLGAP-YGKAVDMWSVGCILGELSDGQPLFPGESEIDQLFTIQKVLGPLPAEQMKLFysNPRFHG 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 291 FKFPQIkAHPWT--KVFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd07848   237 LRFPAV-NHPQSleRRYLGILSGVLLDLMKNLLKLNPTDRYLTEQCLNHPAF 287
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
55-258 9.70e-52

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: 173.48  E-value: 9.70e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  55 SYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKV-LQDKRFKN-----RELQIMRKLDHCNIVRlrYFfyssGEKKDEVYL 128
Cdd:cd06606     1 RWKKGELLGKGSFGSVYLALNLDTGELMAVKEVeLSGDSEEElealeREIRILSSLKHPNIVR--YL----GTERTENTL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 129 NLVLDYVPE-TVyrvaRHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKLCDFGSAKQL 207
Cdd:cd06606    75 NIFLEYVPGgSL----ASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSD-GVVKLADFGCAKRL 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1231802383 208 VR---GEPNVSYICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIFP 258
Cdd:cd06606   150 AEiatGEGTKSLRGTPYWMAPEVIRG-EGYGRAADIWSLGCTVIEMATGKPPWS 202
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
55-340 1.14e-51

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: 173.99  E-value: 1.14e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  55 SYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKR----FKN-RELQIMRKLDHCNIVRLRYFFYSSGEkkdevyLN 129
Cdd:cd07870     1 SYLNLEKLGEGSYATVYKGISRINGQLVALKVISMKTEegvpFTAiREASLLKGLKHANIVLLHDIIHTKET------LT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 LVLDYVPETVyrvARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQlvR 209
Cdd:cd07870    75 FVFEYMHTDL---AQYMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLIS-YLGELKLADFGLARA--K 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 210 GEPNVSY---ICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGV-DQLVEIIKVLGTPTRE------ 279
Cdd:cd07870   149 SIPSQTYsseVVTLWYRPPDVLLGATDYSSALDIWGAGCIFIEMLQGQPAFPGVSDVfEQLEKIWTVLGVPTEDtwpgvs 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1231802383 280 QIREMNPNYTEFKFPQIKAHPWTKVFRprtPPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd07870   229 KLPNYKPEWFLPCKPQQLRVVWKRLSR---PPKAEDLASQMLMMFPKDRISAQDALLHPYF 286
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
56-330 4.05e-51

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: 171.62  E-value: 4.05e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQD--------KRFKnRELQIMRKLDHCNIVRLryffYSSGEKKDEVY 127
Cdd:cd14014     2 YRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPElaedeefrERFL-REARALARLSHPNIVRV----YDVGEDDGRPY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 128 LnlVLDYVP-ETVyrvaRHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQ 206
Cdd:cd14014    77 I--VMEYVEgGSL----ADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRV-KLTDFGIARA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 207 LVRGEPNVS--YICSRYYRAPELIFGAT-DYTSsiDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREqire 283
Cdd:cd14014   150 LGDSGLTQTgsVLGTPAYMAPEQARGGPvDPRS--DIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSP---- 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1231802383 284 mnpnytefkfpqikahpwtkvFRPRTPPEAIALCSRLLEYTPTARLT 330
Cdd:cd14014   224 ---------------------LNPDVPPALDAIILRALAKDPEERPQ 249
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
48-347 4.59e-51

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: 174.46  E-value: 4.59e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  48 PDRPQEVSytdtkVIGNGSFGVVYQAKLCDSGELVAIKK-------VLQDKRfKNRELQIMRKLDHCNIVRLRYFFY--S 118
Cdd:cd07877    16 PERYQNLS-----PVGSGAYGSVCAAFDTKTGLRVAVKKlsrpfqsIIHAKR-TYRELRLLKHMKHENVIGLLDVFTpaR 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 119 SGEKKDEVYLnlVLDYVPETVYRVARHysrakQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAvLKL 198
Cdd:cd07877    90 SLEEFNDVYL--VTHLMGADLNNIVKC-----QKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCE-LKI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 199 CDFGSAKQlvRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTR 278
Cdd:cd07877   162 LDFGLARH--TDDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVGTPGA 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1231802383 279 EQIREMNP----NYTEfKFPQIKAHPWTKVFRPRTpPEAIALCSRLLEYTPTARLTPLEACAHSFFDELRDPN 347
Cdd:cd07877   240 ELLKKISSesarNYIQ-SLTQMPKMNFANVFIGAN-PLAVDLLEKMLVLDSDKRITAAQALAHAYFAQYHDPD 310
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
60-340 4.75e-51

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 173.79  E-value: 4.75e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKVlQDKRFKN-------------------RELQIMRKLDHCNIVRLRYFFYSSG 120
Cdd:PTZ00024   15 AHLGEGTYGKVEKAYDTLTGKIVAIKKV-KIIEISNdvtkdrqlvgmcgihfttlRELKIMNEIKHENIMGLVDVYVEGD 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 121 ekkdevYLNLVLDYVPETVYRVARhysrAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCD 200
Cdd:PTZ00024   94 ------FINLVMDIMASDLKKVVD----RKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFIN-SKGICKIAD 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 201 FGSAKQ-----LVRGEPNVSYICSR----------YYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQ 265
Cdd:PTZ00024  163 FGLARRygyppYSDTLSKDETMQRReemtskvvtlWYRAPELLMGAEKYHFAVDMWSVGCIFAELLTGKPLFPGENEIDQ 242
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1231802383 266 LVEIIKVLGTPTRE---QIREMnPNYTEFKFPQIKAhpwTKVFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:PTZ00024  243 LGRIFELLGTPNEDnwpQAKKL-PLYTEFTPRKPKD---LKTIFPNASDDAIDLLQSLLKLNPLERISAKEALKHEYF 316
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
55-352 5.86e-51

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: 172.49  E-value: 5.86e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  55 SYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVlqdkRFKN---------RELQIMRKLDHCNIVRLRYFFYSsgekkdE 125
Cdd:cd07873     3 TYIKLDKLGEGTYATVYKGRSKLTDNLVALKEI----RLEHeegapctaiREVSLLKDLKHANIVTLHDIIHT------E 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 126 VYLNLVLDYVPETVyrvARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAK 205
Cdd:cd07873    73 KSLTLVFEYLDKDL---KQYLDDCGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLIN-ERGELKLADFGLAR 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 206 qlVRGEPNVSY---ICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIR 282
Cdd:cd07873   149 --AKSIPTKTYsneVVTLWYRPPDILLGSTDYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEQLHFIFRILGTPTEETWP 226
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 283 EM--NPNYTEFKFPQIKAHPWTKvFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDELRDPNVKLPN 352
Cdd:cd07873   227 GIlsNEEFKSYNYPKYRADALHN-HAPRLDSDGADLLSKLLQFEGRKRISAEEAMKHPYFHSLGERIHKLPD 297
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
55-340 2.90e-50

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: 170.58  E-value: 2.90e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  55 SYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVlqdkRFKN---------RELQIMRKLDHCNIVRLRYFFYSsgekkdE 125
Cdd:cd07871     6 TYVKLDKLGEGTYATVFKGRSKLTENLVALKEI----RLEHeegapctaiREVSLLKNLKHANIVTLHDIIHT------E 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 126 VYLNLVLDYVPETVyrvaRHY-SRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSA 204
Cdd:cd07871    76 RCLTLVFEYLDSDL----KQYlDNCGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLIN-EKGELKLADFGLA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 205 KqlVRGEPNVSY---ICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQI 281
Cdd:cd07871   151 R--AKSVPTKTYsneVVTLWYRPPDVLLGSTEYSTPIDMWGVGCILYEMATGRPMFPGSTVKEELHLIFRLLGTPTEETW 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 282 REMNPNyTEFK---FPQIKAHPwTKVFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd07871   229 PGVTSN-EEFRsylFPQYRAQP-LINHAPRLDTDGIDLLSSLLLYETKSRISAEAALRHSYF 288
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
62-250 1.69e-49

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: 166.29  E-value: 1.69e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN-----RELQIMRKLDHCNIVRlryfFYSSGEKKDEVYLnlVLDYVP 136
Cdd:cd00180     1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKLleellREIEILKKLNHPNIVK----LYDVFETENFLYL--VMEYCE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 137 E-TVYRVARhysRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQLVRGEPNVS 215
Cdd:cd00180    75 GgSLKDLLK---ENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLD-SDGTVKLADFGLAKDLDSDDSLLK 150
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1231802383 216 YIC--SRYYRAPELIFGATDYTSSIDVWSAGCVLAEL 250
Cdd:cd00180   151 TTGgtTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL 187
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
56-340 9.93e-49

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1; 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. Mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A was previously called minibrain kinase homolog (MNBH) or dual-specificity YAK1-related kinase. It phosphorylates various substrates and is involved in many cellular events. It phosphorylates and inhibits the transcription factors, nuclear factor of activated T cells (NFAT) and forkhead in rhabdomyosarcoma (FKHR). It regulates neuronal differentiation by targetting CREB (cAMP response element-binding protein). It also targets many endocytic proteins including dynamin and amphiphysin and may play a role in the endocytic pathway. The gene encoding DYRK1A is located in the DSCR (Down syndrome critical region) of human chromosome 21 and DYRK1A has been implicated in the pathogenesis of DS. DYRK1B, also called minibrain-related kinase (MIRK), is highly expressed in muscle and 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. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK1 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: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 167.88  E-value: 9.93e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNR---ELQIMRKLDH------CNIVRL-RYFFYSSgekkde 125
Cdd:cd14226    15 YEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIKNKKAFLNQaqiEVRLLELMNKhdtenkYYIVRLkRHFMFRN------ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 126 vYLNLVLDYVPETVYRVARHYSRAKQTLPVIYVklYMYQLFRSLAYIHS--FGICHRDIKPQNLLL-DPDTAVLKLCDFG 202
Cdd:cd14226    89 -HLCLVFELLSYNLYDLLRNTNFRGVSLNLTRK--FAQQLCTALLFLSTpeLSIIHCDLKPENILLcNPKRSAIKIIDFG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 203 SAKQLvrGEPNVSYICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIr 282
Cdd:cd14226   166 SSCQL--GQRIYQYIQSRFYRSPEVLLG-LPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGMPPVHML- 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 283 EMNPNYTEF--KFP----QIKAHPWTKVFRP-------------------RTPPEA----------IALCSRLLEYTPTA 327
Cdd:cd14226   242 DQAPKARKFfeKLPdgtyYLKKTKDGKKYKPpgsrklheilgvetggpggRRAGEPghtvedylkfKDLILRMLDYDPKT 321
                         330
                  ....*....|...
gi 1231802383 328 RLTPLEACAHSFF 340
Cdd:cd14226   322 RITPAEALQHSFF 334
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
56-340 1.61e-48

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher eukaryotes; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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. CDK1/cyclin A2 has also been implicated as an important regulator of S phase events. The CDK1/cyclin B complex is critical for G2 to M phase transition. It induces mitosis by activating nuclear enzymes that regulate chromatin condensation, nuclear membrane degradation, mitosis-specific microtubule and cytoskeletal reorganization. CDK1 also associates with cyclin E and plays a role in the entry into S phase. CDK1 transcription is stable throughout the cell cycle but is modulated in some pathological conditions. It may play a role in regulating apoptosis under these conditions. In breast cancer cells, HER2 can mediate apoptosis by inactivating CDK1. Activation of CDK1 may contribute to HIV-1 induced apoptosis as well as neuronal apoptosis in neurodegenerative diseases. 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: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 165.67  E-value: 1.61e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVlqdkRFKN----------RELQIMRKLDHCNIVRLRYFFYssgekkDE 125
Cdd:cd07861     2 YTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKI----RLESeeegvpstaiREISLLKELQHPNIVCLEDVLM------QE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 126 VYLNLVLDYVPetvYRVARHYS--RAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGS 203
Cdd:cd07861    72 NRLYLVFEFLS---MDLKKYLDslPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLID-NKGVIKLADFGL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 204 AKQLvrGEPNVSY---ICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQ 280
Cdd:cd07861   148 ARAF--GIPVRVYtheVVTLWYRAPEVLLGSPRYSTPVDIWSIGTIFAEMATKKPLFHGDSEIDQLFRIFRILGTPTEDI 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 281 IREMN--PNYTEfKFPQIKAHPWTKVFrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd07861   226 WPGVTslPDYKN-TFPKWKKGSLRTAV-KNLDEDGLDLLEKMLIYDPAKRISAKKALVHPYF 285
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
56-345 3.22e-48

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 170.19  E-value: 3.22e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQD--------KRFKnRELQIMRKLDHCNIVRLryffYSSGEKKDEVY 127
Cdd:COG0515     9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPElaadpearERFR-REARALARLNHPNIVRV----YDVGEEDGRPY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 128 LnlVLDYVP-ETVyrvaRHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKLCDFGSAKQ 206
Cdd:COG0515    84 L--VMEYVEgESL----ADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPD-GRVKLIDFGIARA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 207 LVRGEPNVS--YICSRYYRAPELIFGAT-DYTSsiDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREqire 283
Cdd:COG0515   157 LGGATLTQTgtVVGTPGYMAPEQARGEPvDPRS--DVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSE---- 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 284 mnpnytefkfpqikahpwtkvFRPRTPPEAIALCSRLLEYTPTARLtpleACAHSFFDELRD 345
Cdd:COG0515   231 ---------------------LRPDLPPALDAIVLRALAKDPEERY----QSAAELAAALRA 267
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
56-301 5.75e-48

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: 163.46  E-value: 5.75e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIK----KVLQDKRFKN--RELQIMRKLDHCNIVRLRYFFyssgEKKDevYLN 129
Cdd:cd14003     2 YELGKTLGEGSFGKVKLARHKLTGEKVAIKiidkSKLKEEIEEKikREIEIMKLLNHPNIIKLYEVI----ETEN--KIY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 LVLDYVPE-TVYrvarHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTaVLKLCDFGSAKQLV 208
Cdd:cd14003    76 LVMEYASGgELF----DYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNG-NLKIIDFGLSNEFR 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 209 RGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSgVDQLVEIIKVlGTPT---------RE 279
Cdd:cd14003   151 GGSLLKTFCGTPAYAAPEVLLGRKYDGPKADVWSLGVILYAMLTGYLPFDDDN-DSKLFRKILK-GKYPipshlspdaRD 228
                         250       260
                  ....*....|....*....|....
gi 1231802383 280 QIREM-NPNYTE-FKFPQIKAHPW 301
Cdd:cd14003   229 LIRRMlVVDPSKrITIEEILNHPW 252
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
60-339 8.29e-48

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: 163.03  E-value: 8.29e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN-------RELQIMRKLDHCNIVRLRYFFYssgekkDEVYLNLVL 132
Cdd:cd14007     6 KPLGKGKFGNVYLAREKKSGFIVALKVISKSQLQKSglehqlrREIEIQSHLRHPNILRLYGYFE------DKKRIYLIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 DYVPE-TVY---RVARHYSRAKqtlpviyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQLV 208
Cdd:cd14007    80 EYAPNgELYkelKKQKRFDEKE-------AAKYIYQLALALDYLHSKNIIHRDIKPENILLG-SNGELKLADFGWSVHAP 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 209 RGEPNVsyICSRY-YRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVlgtptreqiremnpn 287
Cdd:cd14007   152 SNRRKT--FCGTLdYLPPEMVEG-KEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNV--------------- 213
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 288 ytEFKFPqikahpwtkvfrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSF 339
Cdd:cd14007   214 --DIKFP------------SSVSPEAKDLISKLLQKDPSKRLSLEQVLNHPW 251
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
48-344 1.28e-47

Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NLK is an atypical mitogen-activated protein kinase (MAPK) that is not regulated by a MAPK kinase. It functions downstream of the MAPK kinase kinase Tak1, which also plays a role in activating the JNK and p38 MAPKs. The Tak1/NLK pathways are regulated by Wnts, a family of secreted proteins that is critical in the control of asymmetric division and cell polarity. NLK can phosphorylate transcription factors from the TCF/LEF family, inhibiting their ability to activate the transcription of target genes. In prostate cancer cells, NLK is involved in regulating androgen receptor-mediated transcription and its expression is altered during cancer progression. MAPKs are important mediators of cellular responses to extracellular signals. The NLK 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: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 166.07  E-value: 1.28e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  48 PDRPqevsytdtkvIGNGSFGVVYQAKLCDSGELVAIKK---VLQD----KRFKnRELQIMRKLDHCNIVR--------- 111
Cdd:cd07853     4 PDRP----------IGYGAFGVVWSVTDPRDGKRVALKKmpnVFQNlvscKRVF-RELKMLCFFKHDNVLSaldilqpph 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 112 LRYFfyssgekkDEVYLnlVLDYVPETVYRVARhysrAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDP 191
Cdd:cd07853    73 IDPF--------EEIYV--VTELMQSDLHKIIV----SPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNS 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 192 DtAVLKLCDFGSAKqlvRGEPNVSY-----ICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQL 266
Cdd:cd07853   139 N-CVLKICDFGLAR---VEEPDESKhmtqeVVTQYYRAPEILMGSRHYTSAVDIWSVGCIFAELLGRRILFQAQSPIQQL 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 267 VEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKVFRPRTPP---EAIALCSRLLEYTPTARLTPLEACAHSFFDEL 343
Cdd:cd07853   215 DLITDLLGTPSLEAMRSACEGARAHILRGPHKPPSLPVLYTLSSQathEAVHLLCRMLVFDPDKRISAADALAHPYLDEG 294

                  .
gi 1231802383 344 R 344
Cdd:cd07853   295 R 295
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
62-340 3.64e-47

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: 161.15  E-value: 3.64e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIK-----KVLQDKRFKN--RELQIMRKLDHCNIVRLRYFFyssgekKDEVYLNLVLDY 134
Cdd:cd05123     1 LGKGSFGKVLLVRKKDTGKLYAMKvlrkkEIIKRKEVEHtlNERNILERVNHPFIVKLHYAF------QTEEKLYLVLDY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 135 VP--ETVYRVARHysrakQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQLVRGEP 212
Cdd:cd05123    75 VPggELFSHLSKE-----GRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLD-SDGHIKLTDFGLAKELSSDGD 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 213 NVSYIC-SRYYRAPELIFGAtDYTSSIDVWSAGCVLAELLLGQPIFPGDSgVDQLVEIIKvlgtptreqiremnpnYTEF 291
Cdd:cd05123   149 RTYTFCgTPEYLAPEVLLGK-GYGKAVDWWSLGVLLYEMLTGKPPFYAEN-RKEIYEKIL----------------KSPL 210
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 292 KFPqikahpwtkvfrPRTPPEAIALCSRLLEYTPTARLTPLEAC---AHSFF 340
Cdd:cd05123   211 KFP------------EYVSPEAKSLISGLLQKDPTKRLGSGGAEeikAHPFF 250
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
62-339 3.78e-47

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: 161.24  E-value: 3.78e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKV----LQDKRFKN--RELQIMRKLDHCNIVRLRYFfyssgeKKDEVYLNLVLDYV 135
Cdd:cd14009     1 IGRGSFATVWKGRHKQTGEVVAIKEIsrkkLNKKLQENleSEIAILKSIKHPNIVRLYDV------QKTEDFIYLVLEYC 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 136 petvyrvA----RHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLL--DPDTAVLKLCDFGSAKQLvr 209
Cdd:cd14009    75 -------AggdlSQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLstSGDDPVLKIADFGFARSL-- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 210 gEPN--VSYIC-SRYYRAPELIFGAtDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVdQLVEIIKvlgtptreqiremnP 286
Cdd:cd14009   146 -QPAsmAETLCgSPLYMAPEILQFQ-KYDAKADLWSVGAILFEMLVGKPPFRGSNHV-QLLRNIE--------------R 208
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1231802383 287 NYTEFKFPQikahpwtkvfRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSF 339
Cdd:cd14009   209 SDAVIPFPI----------AAQLSPDCKDLLRRLLRRDPAERISFEEFFAHPF 251
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
56-340 6.36e-47

Catalytic domain of the Dual-specificity protein kinase, YAK1; 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 proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 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: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 162.80  E-value: 6.36e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKkVLQDKRFKNR----ELQIMRKL-------DHCNIVRLR-YFFYSSgekk 123
Cdd:cd14212     1 YLVLDLLGQGTFGQVVKCQDLKTNKLVAVK-VLKNKPAYFRqamlEIAILTLLntkydpeDKHHIVRLLdHFMHHG---- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 124 devYLNLVLDYVPETVYRVARhySRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLL-DPDTAVLKLCDFG 202
Cdd:cd14212    76 ---HLCIVFELLGVNLYELLK--QNQFRGLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLvNLDSPEIKLIDFG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 203 SA---KQLVrgepnVSYICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTRE 279
Cdd:cd14212   151 SAcfeNYTL-----YTYIQSRFYRSPEVLLG-LPYSTAIDMWSLGCIAAELFLGLPLFPGNSEYNQLSRIIEMLGMPPDW 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 280 QIR--------------EMNPNYTEFKFPQ-------IKAHPWTKVFRPRTPPEAIALC--------------------- 317
Cdd:cd14212   225 MLEkgkntnkffkkvakSGGRSTYRLKTPEefeaennCKLEPGKRYFKYKTLEDIIMNYpmkkskkeqidkemetrlafi 304
                         330       340
                  ....*....|....*....|....*.
gi 1231802383 318 ---SRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd14212   305 dflKGLLEYDPKKRWTPDQALNHPFI 330
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
56-340 3.45e-46

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: 158.91  E-value: 3.45e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKV----LQDKRFKNRELQIMRKLDHCNIVRlryfFYSSGEKKDEVYLnlV 131
Cdd:cd05122     2 FEILEKIGKGGFGVVYKARHKKTGQIVAIKKInlesKEKKESILNEIAILKKCKHPNIVK----YYGSYLKKDELWI--V 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 132 LDYVPE-TVYRVARHYsraKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKLCDFGSAKQLVRG 210
Cdd:cd05122    76 MEFCSGgSLKDLLKNT---NKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSD-GEVKLIDFGLSAQLSDG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 211 EPNVSYICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIFpGDSGVDQLVEIIKVLGTPtreqiremnpnyte 290
Cdd:cd05122   152 KTRNTFVGTPYWMAPEVIQG-KPYGFKADIWSLGITAIEMAEGKPPY-SELPPMKALFLIATNGPP-------------- 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1231802383 291 fKFPQIKAhpWTKVFRprtppEAIALCsrlLEYTPTARLTPLEACAHSFF 340
Cdd:cd05122   216 -GLRNPKK--WSKEFK-----DFLKKC---LQKDPEKRPTAEQLLKHPFI 254
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
55-343 7.29e-46

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: 159.77  E-value: 7.29e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  55 SYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVlqdkRFKN---------RELQIMRKLDHCNIVRLRYFFYSSGEkkde 125
Cdd:cd07872     7 TYIKLEKLGEGTYATVFKGRSKLTENLVALKEI----RLEHeegapctaiREVSLLKDLKHANIVTLHDIVHTDKS---- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 126 vyLNLVLDYVPETVyrvARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAK 205
Cdd:cd07872    79 --LTLVFEYLDKDL---KQYMDDCGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLIN-ERGELKLADFGLAR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 206 qlVRGEPNVSY---ICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIR 282
Cdd:cd07872   153 --AKSVPTKTYsneVVTLWYRPPDVLLGSSEYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDELHLIFRLLGTPTEETWP 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1231802383 283 EMNPN--YTEFKFPQIKAHPWTKvFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDEL 343
Cdd:cd07872   231 GISSNdeFKNYNFPKYKPQPLIN-HAPRLDTEGIELLTKFLQYESKKRISAEEAMKHAYFRSL 292
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
52-340 5.41e-45

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK9, together with a cyclin partner (cyclin T1, T2a, T2b, or K), is the main component of distinct positive transcription elongation factors (P-TEFb), which function as Ser2 C-terminal domain kinases of RNA polymerase II. P-TEFb participates in multiple steps of gene expression including transcription elongation, mRNA synthesis, processing, export, and translation. It also plays a role in mediating cytokine induced transcription networks such as IL6-induced STAT3 signaling. In addition, the CDK9/cyclin T2a complex promotes muscle differentiation and enhances the function of some myogenic regulatory factors. 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 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: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 157.15  E-value: 5.41e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  52 QEVS-YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN------RELQIMRKLDHCNIVRLRYFFYS--SGEK 122
Cdd:cd07865     9 DEVSkYEKLAKIGQGTFGEVFKARHRKTGQIVALKKVLMENEKEGfpitalREIKILQLLKHENVVNLIEICRTkaTPYN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 123 KDEVYLNLVLDYVPetvYRVARHYSRA--KQTLPVIyvKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKLCD 200
Cdd:cd07865    89 RYKGSIYLVFEFCE---HDLAGLLSNKnvKFTLSEI--KKVMKMLLNGLYYIHRNKILHRDMKAANILITKD-GVLKLAD 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 201 FGSAKQLV---RGEPN--VSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGT 275
Cdd:cd07865   163 FGLARAFSlakNSQPNryTNRVVTLWYRPPELLLGERDYGPPIDMWGAGCIMAEMWTRSPIMQGNTEQHQLTLISQLCGS 242
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1231802383 276 PTRE---QIREMnPNYTEFKFPQ-----IKAHPWTKVfrprTPPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd07865   243 ITPEvwpGVDKL-ELFKKMELPQgqkrkVKERLKPYV----KDPYALDLIDKLLVLDPAKRIDADTALNHDFF 310
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
56-346 9.78e-44

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: 154.88  E-value: 9.78e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDkrFKN--------RELQIMRKLDHCNIVRLRYFFY--SSGEKKDE 125
Cdd:cd07850     2 YQNLKPIGSGAQGIVCAAYDTVTGQNVAIKKLSRP--FQNvthakrayRELVLMKLVNHKNIIGLLNVFTpqKSLEEFQD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 126 VYLnlVLDYVPETVYRVarhysrakqtlpvIYVKL-------YMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKL 198
Cdd:cd07850    80 VYL--VMELMDANLCQV-------------IQMDLdhermsyLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSD-CTLKI 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 199 CDFGSAKQLVRGEPNVSYICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTR 278
Cdd:cd07850   144 LDFGLARTAGTSFMMTPYVVTRYYRAPEVILG-MGYKENVDIWSVGCIMGEMIRGTVLFPGTDHIDQWNKIIEQLGTPSD 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 279 EQIREMNP---NYTEFKfPQIKAHPWTKVF------------RPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDEL 343
Cdd:cd07850   223 EFMSRLQPtvrNYVENR-PKYAGYSFEELFpdvlfppdseehNKLKASQARDLLSKMLVIDPEKRISVDDALQHPYINVW 301

                  ...
gi 1231802383 344 RDP 346
Cdd:cd07850   302 YDP 304
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
56-291 9.85e-44

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: 152.41  E-value: 9.85e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQ----DKRFKN--RELQIMRKLDHCNIVRLryffYSSGEKKDEVylN 129
Cdd:cd14002     3 YHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPKrgksEKELRNlrQEIEILRKLNHPNIIEM----LDSFETKKEF--V 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 LVLDYVPETVYRVARhysrAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQL-- 207
Cdd:cd14002    77 VVTEYAQGELFQILE----DDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVV-KLCDFGFARAMsc 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 208 -------VRGEPnvsyicsrYYRAPELIfGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSgVDQLVEIIkvlgtpTREQ 280
Cdd:cd14002   152 ntlvltsIKGTP--------LYMAPELV-QEQPYDHTADLWSLGCILYELFVGQPPFYTNS-IYQLVQMI------VKDP 215
                         250
                  ....*....|....
gi 1231802383 281 IR---EMNPNYTEF 291
Cdd:cd14002   216 VKwpsNMSPEFKSF 229
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
62-302 1.38e-42

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: 149.63  E-value: 1.38e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIK----KVLQDKRF--------KN------RELQIMRKLDHCNIVRLRYFFYSsgEKK 123
Cdd:cd14008     1 LGRGSFGKVKLALDTETGQLYAIKifnkSRLRKRREgkndrgkiKNalddvrREIAIMKKLDHPNIVRLYEVIDD--PES 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 124 DEVYLnlVLDYVP--ETVYRVARHYSRAkqtLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTaVLKLCDF 201
Cdd:cd14008    79 DKLYL--VLEYCEggPVMELDSGDRVPP---LPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADG-TVKISDF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 202 GSAKQLVRGEPNVS-YICSRYYRAPELI-FGATDY-TSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKV-LGTPT 277
Cdd:cd14008   153 GVSEMFEDGNDTLQkTAGTPAFLAPELCdGDSKTYsGKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQnDEFPI 232
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1231802383 278 REQI---------REMNPNYTE-FKFPQIKAHPWT 302
Cdd:cd14008   233 PPELspelkdllrRMLEKDPEKrITLKEIKEHPWV 267
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
56-339 1.56e-42

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: 150.72  E-value: 1.56e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN------RELQIMRKLDHCNIVRLRYFFY----SSGEKKDE 125
Cdd:cd07864     9 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGfpitaiREIKILRQLNHRSVVNLKEIVTdkqdALDFKKDK 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 126 VYLNLVLDYVPETVYRVAR----HYSRAkqtlpviYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDF 201
Cdd:cd07864    89 GAFYLVFEYMDHDLMGLLEsglvHFSED-------HIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLN-NKGQIKLADF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 202 GSAKQLVRGE--PNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTre 279
Cdd:cd07864   161 GLARLYNSEEsrPYTNKVITLWYRPPELLLGEERYGPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRLCGSPC-- 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1231802383 280 qiREMNPNYTefKFPQIKAHPWTKVFRPR-------TPPEAIALCSRLLEYTPTARLTPLEACAHSF 339
Cdd:cd07864   239 --PAVWPDVI--KLPYFNTMKPKKQYRRRlreefsfIPTPALDLLDHMLTLDPSKRCTAEQALNSPW 301
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
56-340 1.77e-42

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: 150.11  E-value: 1.77e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVlqdkRFKN----------RELQIMRKL---DHCNIVRLRYFFYSSGEK 122
Cdd:cd07863     2 YEPVAEIGVGAYGTVYKARDPHSGHFVALKSV----RVQTnedglplstvREVALLKRLeafDHPNIVRLMDVCATSRTD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 123 KdEVYLNLVLDYVPETVyrvaRHY-SRAKQT-LPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCD 200
Cdd:cd07863    78 R-ETKVTLVFEHVDQDL----RTYlDKVPPPgLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQV-KLAD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 201 FGSAKQLVRGEPNVSYICSRYYRAPELIFGATdYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQ 280
Cdd:cd07863   152 FGLARIYSCQMALTPVVVTLWYRAPEVLLQST-YATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPEDD 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 281 IrEMNPNYTEFKFPQIKAHPWTKVFrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd07863   231 W-PRDVTLPRGAFSPRGPRPVQSVV-PEIEESGAQLLLEMLTFNPHKRISAFRALQHPFF 288
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
54-340 1.19e-41

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: 146.93  E-value: 1.19e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  54 VSYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKV----LQDKRFKNR---ELQIMRKLDHCNIVRlryfFYSSGEKKDEV 126
Cdd:cd14099     1 KRYRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVpkssLTKPKQREKlksEIKIHRSLKHPNIVK----FHDCFEDEENV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 127 YLnlVLDYVP-ETVyrvaRHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAK 205
Cdd:cd14099    77 YI--LLELCSnGSL----MELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNV-KIGDFGLAA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 206 QL---------VRGEPNvsYIcsryyrAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSgvdqlVEIikvlgtp 276
Cdd:cd14099   150 RLeydgerkktLCGTPN--YI------APEVLEKKKGHSFEVDIWSLGVILYTLLVGKPPFETSD-----VKE------- 209
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1231802383 277 TREQIREmnpnyTEFKFPQikahpwtkvfRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd14099   210 TYKRIKK-----NEYSFPS----------HLSISDEAKDLIRSMLQPDPTKRPSLDEILSHPFF 258
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
55-343 3.27e-41

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: 147.15  E-value: 3.27e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  55 SYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKV-LQDKRFKN----RELQIMRKLDHCNIVRLRYFFYSSGEkkdevyLN 129
Cdd:cd07869     6 SYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIrLQEEEGTPftaiREASLLKGLKHANIVLLHDIIHTKET------LT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 LVLDYVPETVyrvARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKqlVR 209
Cdd:cd07869    80 LVFEYVHTDL---CQYMDKHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLIS-DTGELKLADFGLAR--AK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 210 GEPNVSY---ICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGV-DQLVEIIKVLGTPTREQIREMN 285
Cdd:cd07869   154 SVPSHTYsneVVTLWYRPPDVLLGSTEYSTCLDMWGVGCIFVEMIQGVAAFPGMKDIqDQLERIFLVLGTPNEDTWPGVH 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1231802383 286 --PNYTEFKFPQIKA----HPWTKVfrpRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDEL 343
Cdd:cd07869   234 slPHFKPERFTLYSPknlrQAWNKL---SYVNHAEDLASKLLQCFPKNRLSAQAALSHEYFSDL 294
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
62-340 1.09e-39

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: 141.59  E-value: 1.09e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKL-------CDSGELVAIKKVL---QDKRFKNrELQIMRKLDHC-NIVRLRYFFyssgEKKDEVYLnl 130
Cdd:cd14019     9 IGEGTFSSVYKAEDklhdlydRNKGRLVALKHIYptsSPSRILN-ELECLERLGGSnNVSGLITAF----RNEDQVVA-- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 VLDYVPETVYRvarHYSRakqTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSAkQLVRG 210
Cdd:cd14019    82 VLPYIEHDDFR---DFYR---KMSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNRETGKGVLVDFGLA-QREED 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 211 EPNVSYIC--SRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQ-PIFPGDSGVDQLVEIIKVLGTptreqiremnpn 287
Cdd:cd14019   155 RPEQRAPRagTRGFRAPEVLFKCPHQTTAIDIWSAGVILLSILSGRfPFFFSSDDIDALAEIATIFGS------------ 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1231802383 288 ytefkfpqikahpwtkvfrprtpPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd14019   223 -----------------------DEAYDLLDKLLELDPSKRITAEEALKHPFF 252
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
56-255 1.11e-39

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: 141.59  E-value: 1.11e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNR------ELQIMRKLDHCNIVRLRYFFyssgekKDEVYLN 129
Cdd:cd06627     2 YQLGDLIGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKSDlksvmgEIDLLKKLNHPNIVKYIGSV------KTKDSLY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 LVLDYVPE-TVYRVARHYSRAKQTLpviyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLdPDTAVLKLCDFGSAKQLV 208
Cdd:cd06627    76 IILEYVENgSLASIIKKFGKFPESL----VAVYIYQVLEGLAYLHEQGVIHRDIKGANILT-TKDGLVKLADFGVATKLN 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1231802383 209 RGEPN-VSYICSRYYRAPELIFGATDYTSSiDVWSAGCVLAELLLGQP 255
Cdd:cd06627   151 EVEKDeNSVVGTPYWMAPEVIEMSGVTTAS-DIWSVGCTVIELLTGNP 197
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
56-340 3.61e-39

Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PRP4 phosphorylates a number of factors involved in the formation of active spliceosomes, which catalyze pre-mRNA splicing. It phosphorylates PRP6 and PRP31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), during spliceosomal complex formation. In fission yeast, PRP4 phosphorylates the splicing factor PRP1 (U5-102 kD in mammals). Thus, PRP4 plays a key role in regulating spliceosome assembly and pre-mRNA splicing. It also plays an important role in mitosis by acting as a spindle assembly checkpoint kinase that is required for chromosome alignment and the recruitment of the checkpoint proteins MPS1, MAD1, and MAD2 at kinetochores. The PRP4 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: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 141.98  E-value: 3.61e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAK-LCDSGELVAIKKVLQD---KRFKNRELQIMRKLD--------HCniVRL-RYFFYSSgek 122
Cdd:cd14135     2 YRVYGYLGKGVFSNVVRARdLARGNQEVAIKIIRNNelmHKAGLKELEILKKLNdadpddkkHC--IRLlRHFEHKN--- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 123 kdevYLNLVLDYVPETVYRVARHYSRaKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFG 202
Cdd:cd14135    77 ----HLCLVFESLSMNLREVLKKYGK-NVGLNIKAVRSYAQQLFLALKHLKKCNILHADIKPDNILVNEKKNTLKLCDFG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 203 SAKQLVRGEPnVSYICSRYYRAPELIFGAtDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIR 282
Cdd:cd14135   152 SASDIGENEI-TPYLVSRFYRAPEIILGL-PYDYPIDMWSVGCTLYELYTGKILFPGKTNNHMLKLMMDLKGKFPKKMLR 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 283 E---MNPNYTE---FKFPQIKAH---PWTKVFRPRTPPEAIA----------------------LCSRLLEYTPTARLTP 331
Cdd:cd14135   230 KgqfKDQHFDEnlnFIYREVDKVtkkEVRRVMSDIKPTKDLKtlligkqrlpdedrkkllqlkdLLDKCLMLDPEKRITP 309

                  ....*....
gi 1231802383 332 LEACAHSFF 340
Cdd:cd14135   310 NEALQHPFI 318
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
51-338 9.24e-39

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: 139.84  E-value: 9.24e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  51 PQEVS--YTDTKVIGNGSFGVV---YQAKLCdsgELVAIKKVlqDKRFK--------------NRELQIMRKLDHCNIVR 111
Cdd:cd14084     1 PKELRkkYIMSRTLGSGACGEVklaYDKSTC---KKVAIKII--NKRKFtigsrreinkprniETEIEILKKLSHPCIIK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 112 LRYFFyssgEKKDEVYLnlVLDYVP--ETVYRVarhysRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLL 189
Cdd:cd14084    76 IEDFF----DAEDDYYI--VLELMEggELFDRV-----VSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLL 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 190 --DPDTAVLKLCDFGSAKQLVR--------GEPNvsyicsryYRAPELI--FGATDYTSSIDVWSAGCVLAELLLGQPIF 257
Cdd:cd14084   145 ssQEEECLIKITDFGLSKILGEtslmktlcGTPT--------YLAPEVLrsFGTEGYTRAVDCWSLGVILFICLSGYPPF 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 258 PGDSGvdqlveiikvlGTPTREQIREmnpnyTEFKFpqikAHPWTKvfrpRTPPEAIALCSRLLEYTPTARLTPLEACAH 337
Cdd:cd14084   217 SEEYT-----------QMSLKEQILS-----GKYTF----IPKAWK----NVSEEAKDLVKKMLVVDPSRRPSIEEALEH 272

                  .
gi 1231802383 338 S 338
Cdd:cd14084   273 P 273
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
56-288 1.21e-38

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: 139.13  E-value: 1.21e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKV------LQDKRFKNRELQIMRKLDHCNIVRlryfFYSSGEKKDevYLN 129
Cdd:cd08215     2 YEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIdlsnmsEKEREEALNEVKLLSKLKHPNIVK----YYESFEENG--KLC 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 LVLDYVPE-TVYRVARHYSRAKQTLP---VIYvklYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKLCDFGSAK 205
Cdd:cd08215    76 IVMEYADGgDLAQKIKKQKKKGQPFPeeqILD---WFVQICLALKYLHSRKILHRDLKTQNIFLTKD-GVVKLGDFGISK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 206 QLvrgEPNVSYICSR----YYRAPELIFGAtDYTSSIDVWSAGCVLAELLLGQPIFPGDSgVDQLVEIIkvlgtpTREQI 281
Cdd:cd08215   152 VL---ESTTDLAKTVvgtpYYLSPELCENK-PYNYKSDIWALGCVLYELCTLKHPFEANN-LPALVYKI------VKGQY 220

                  ....*..
gi 1231802383 282 REMNPNY 288
Cdd:cd08215   221 PPIPSQY 227
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
56-340 2.88e-38

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: 140.22  E-value: 2.88e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNR---ELQIM---RKLDH---CNIVRLR-YFFYSSgekkde 125
Cdd:cd14225    45 YEILEVIGKGSFGQVVKALDHKTNEHVAIKIIRNKKRFHHQalvEVKILdalRRKDRdnsHNVIHMKeYFYFRN------ 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 126 vYLNLVLDYVPETVYRVARHYSRakQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDP-DTAVLKLCDFGSA 204
Cdd:cd14225   119 -HLCITFELLGMNLYELIKKNNF--QGFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQrGQSSIKVIDFGSS 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 205 ---KQLVrgepnVSYICSRYYRAPELIFGATdYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQI 281
Cdd:cd14225   196 cyeHQRV-----YTYIQSRFYRSPEVILGLP-YSMAIDMWSLGCILAELYTGYPLFPGENEVEQLACIMEVLGLPPPELI 269
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 282 REMNPNYTEFK---FPQIKAHPWTKVFRPRTPPEAIAL----------CSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd14225   270 ENAQRRRLFFDskgNPRCITNSKGKKRRPNSKDLASALktsdplfldfIRRCLEWDPSKRMTPDEALQHEWI 341
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
60-301 5.70e-38

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: 137.00  E-value: 5.70e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN-------RELQIMRKLDHCNIVRLrYFFYSsgekkDEVYLNLVL 132
Cdd:cd14081     7 KTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKEsvlmkveREIAIMKLIEHPNVLKL-YDVYE-----NKKYLYLVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 DYVP--ETVyrvarHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLVRG 210
Cdd:cd14081    81 EYVSggELF-----DYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNI-KIADFGMASLQPEG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 211 EPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSgVDQLVEIIKV--------LGTPTREQIR 282
Cdd:cd14081   155 SLLETSCGSPHYACPEVIKGEKYDGRKADIWSCGVILYALLVGALPFDDDN-LRQLLEKVKRgvfhiphfISPDAQDLLR 233
                         250       260
                  ....*....|....*....|..
gi 1231802383 283 EM---NPNyTEFKFPQIKAHPW 301
Cdd:cd14081   234 RMlevNPE-KRITIEEIKKHPW 254
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
62-286 5.08e-37

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: 134.20  E-value: 5.08e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCdsGELVAIKKV----LQDKRFK--NRELQIMRKLDHCNIVRLRyffyssGEKKDEVYLNLVLDYV 135
Cdd:cd13999     1 IGSGSFGEVYKGKWR--GTDVAIKKLkvedDNDELLKefRREVSILSKLRHPNIVQFI------GACLSPPPLCIVTEYM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 136 PE-TVYRVARhysRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQLVRGEPNV 214
Cdd:cd13999    73 PGgSLYDLLH---KKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLD-ENFTVKIADFGLSRIKNSTTEKM 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1231802383 215 SYICSRY-YRAPElIFGATDYTSSIDVWSAGCVLAELLLGQPIFPgdsGVDQLVEIIKVLGTPTREQIREMNP 286
Cdd:cd13999   149 TGVVGTPrWMAPE-VLRGEPYTEKADVYSFGIVLWELLTGEVPFK---ELSPIQIAAAVVQKGLRPPIPPDCP 217
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
56-346 1.76e-36

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: 135.93  E-value: 1.76e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVlqDKRFKN--------RELQIMRKLDHCNIVRLRYFF--YSSGEKKDE 125
Cdd:cd07876    23 YQQLKPIGSGAQGIVCAAFDTVLGINVAVKKL--SRPFQNqthakrayRELVLLKCVNHKNIISLLNVFtpQKSLEEFQD 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 126 VYLnlVLDYVPETVYRVArHYSRAKQTLPVIyvklyMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKLCDFGSAK 205
Cdd:cd07876   101 VYL--VMELMDANLCQVI-HMELDHERMSYL-----LYQMLCGIKHLHSAGIIHRDLKPSNIVVKSD-CTLKILDFGLAR 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 206 QLVRGEPNVSYICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMN 285
Cdd:cd07876   172 TACTNFMMTPYVVTRYYRAPEVILG-MGYKENVDIWSVGCIMGELVKGSVIFQGTDHIDQWNKVIEQLGTPSAEFMNRLQ 250
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1231802383 286 P---NYTEFKfPQIKAHPWTKVFRPRTPP-----------EAIALCSRLLEYTPTARLTPLEACAHSFFDELRDP 346
Cdd:cd07876   251 PtvrNYVENR-PQYPGISFEELFPDWIFPseserdklktsQARDLLSKMLVIDPDKRISVDEALRHPYITVWYDP 324
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
60-255 2.92e-36

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: 132.81  E-value: 2.92e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKV-LQD---KRFKN--RELQIMRKLDHCNIVRlryfFYSSGEKKDEVYLnlVLD 133
Cdd:cd06626     6 NKIGEGTFGKVYTAVNLDTGELMAMKEIrFQDndpKTIKEiaDEMKVLEGLDHPNLVR----YYGVEVHREEVYI--FME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 134 YVPE-TVYRVARHysraKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQLVRG-- 210
Cdd:cd06626    80 YCQEgTLEELLRH----GRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLD-SNGLIKLGDFGSAVKLKNNtt 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1231802383 211 ----EPNVSYICSRYYRAPELIFGA--TDYTSSIDVWSAGCVLAELLLGQP 255
Cdd:cd06626   155 tmapGEVNSLVGTPAYMAPEVITGNkgEGHGRAADIWSLGCVVLEMATGKR 205
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
60-277 3.68e-36

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: 132.53  E-value: 3.68e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKVL---QDKRFK------NRELQIMRKLDHCNIVRLRyffyssGEKKDEVYLNL 130
Cdd:cd06632     6 QLLGSGSFGSVYEGFNGDTGDFFAVKEVSlvdDDKKSResvkqlEQEIALLSKLRHPNIVQYY------GTEREEDNLYI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 VLDYVPE-TVYRVARHYSRAKQtlPVIyvKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLVR 209
Cdd:cd06632    80 FLEYVPGgSIHKLLQRYGAFEE--PVI--RLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVV-KLADFGMAKHVEA 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1231802383 210 GEPNVSYICSRYYRAPELIFGA-TDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPT 277
Cdd:cd06632   155 FSFAKSFKGSPYWMAPEVIMQKnSGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGNSGELPP 223
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
62-339 4.91e-36

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: 132.03  E-value: 4.91e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQA-KLCDSGELVAIKKVLQDKRFKN------RELQIMRKLDHCNIVRLRYFFYssgekkDEVYLNLVLDY 134
Cdd:cd14121     3 LGSGTYATVYKAyRKSGAREVVAVKCVSKSSLNKAstenllTEIELLKKLKHPHIVELKDFQW------DEEHIYLIMEY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 135 VPETVYRvarHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLL-DPDTAVLKLCDFGSAKQLVRGEPN 213
Cdd:cd14121    77 CSGGDLS---RFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLsSRYNPVLKLADFGFAQHLKPNDEA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 214 VSYICSRYYRAPELIFGATdYTSSIDVWSAGCVLAELLLGQPIFPGDSgvdqLVEIIkvlgtptrEQIREMNPnytefkf 293
Cdd:cd14121   154 HSLRGSPLYMAPEMILKKK-YDARVDLWSVGVILYECLFGRAPFASRS----FEELE--------EKIRSSKP------- 213
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1231802383 294 pqIKAHPwtkvfRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSF 339
Cdd:cd14121   214 --IEIPT-----RPELSADCRDLLLRLLQRDPDRRISFEEFFAHPF 252
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
56-301 5.39e-36

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: 132.31  E-value: 5.39e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSG--ELVAIK-----KVLQD--KRFKNRELQIMRKLDHCNIVRlryfFYSSGEKKDEV 126
Cdd:cd14080     2 YRLGKTIGEGSYSKVKLAEYTKSGlkEKVACKiidkkKAPKDflEKFLPRELEILRKLRHPNIIQ----VYSIFERGSKV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 127 YLnlVLDYvpetvyrvARH-----YSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDF 201
Cdd:cd14080    78 FI--FMEY--------AEHgdlleYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNV-KLSDF 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 202 GSAKQLVRGEPNV---SYICSRYYRAPELIFGaTDYTSSI-DVWSAGCVLAELLLGQPIFpGDSGVDQLVEII--KVLGT 275
Cdd:cd14080   147 GFARLCPDDDGDVlskTFCGSAAYAAPEILQG-IPYDPKKyDIWSLGVILYIMLCGSMPF-DDSNIKKMLKDQqnRKVRF 224
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1231802383 276 PTR---------EQIREM-NPNYTE-FKFPQIKAHPW 301
Cdd:cd14080   225 PSSvkklspeckDLIDQLlEPDPTKrATIEEILNHPW 261
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
62-340 1.03e-35

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: 132.08  E-value: 1.03e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAK-LCDSGELVAIKKVLQDKRFKN------RELQIMRKLD---HCNIVRLryFFYSSGEKKD-EVYLNL 130
Cdd:cd07862     9 IGEGAYGKVFKARdLKNGGRFVALKRVRVQTGEEGmplstiREVAVLRHLEtfeHPNVVRL--FDVCTVSRTDrETKLTL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 VLDYVPETVyrvARHYSRAKQT-LPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQLVR 209
Cdd:cd07862    87 VFEHVDQDL---TTYLDKVPEPgVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVT-SSGQIKLADFGLARIYSF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 210 GEPNVSYICSRYYRAPELIFGATdYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIremnPNyt 289
Cdd:cd07862   163 QMALTSVVVTLWYRAPEVLLQSS-YATPVDLWSVGCIFAEMFRRKPLFRGSSDVDQLGKILDVIGLPGEEDW----PR-- 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 290 EFKFPQIKAHPwtkvfRPRTPPEAI---------ALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd07862   236 DVALPRQAFHS-----KSAQPIEKFvtdidelgkDLLLKCLTFNPAKRISAYSALSHPYF 290
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
60-340 4.60e-35

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: 130.03  E-value: 4.60e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKkVLqDKRF-----K----NRELQIMRKLDHCNIVRLRYFFyssgekKDEVYLNL 130
Cdd:cd05581     7 KPLGEGSYSTVVLAKEKETGKEYAIK-VL-DKRHiikekKvkyvTIEKEVLSRLAHPGIVKLYYTF------QDESKLYF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 VLDYVP--ETVYRVARHYSrakqtLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAvLKLCDFGSAKQLV 208
Cdd:cd05581    79 VLEYAPngDLLEYIRKYGS-----LDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMH-IKITDFGTAKVLG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 209 RGEPNV------------------SYICSRYYRAPELIfGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEII 270
Cdd:cd05581   153 PDSSPEstkgdadsqiaynqaraaSFVGTAEYVSPELL-NEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIV 231
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1231802383 271 KVlgtptreqiremnpnytEFKFPqikahpwtkvfrPRTPPEAIALCSRLLEYTPTARLTPLEAC------AHSFF 340
Cdd:cd05581   232 KL-----------------EYEFP------------ENFPPDAKDLIQKLLVLDPSKRLGVNENGgydelkAHPFF 278
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
56-346 1.25e-34

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: 130.98  E-value: 1.25e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVlqDKRFKN--------RELQIMRKLDHCNIVRLRYFF--YSSGEKKDE 125
Cdd:cd07874    19 YQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKL--SRPFQNqthakrayRELVLMKCVNHKNIISLLNVFtpQKSLEEFQD 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 126 VYLNL-VLDYVPETVYRVARHYSRakqtlpviyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKLCDFGSA 204
Cdd:cd07874    97 VYLVMeLMDANLCQVIQMELDHER---------MSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSD-CTLKILDFGLA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 205 KQLVRGEPNVSYICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREM 284
Cdd:cd07874   167 RTAGTSFMMTPYVVTRYYRAPEVILG-MGYKENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIEQLGTPCPEFMKKL 245
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1231802383 285 NP---NYTEFKfPQIKAHPWTKVFRPRTPP-----------EAIALCSRLLEYTPTARLTPLEACAHSFFDELRDP 346
Cdd:cd07874   246 QPtvrNYVENR-PKYAGLTFPKLFPDSLFPadsehnklkasQARDLLSKMLVIDPAKRISVDEALQHPYINVWYDP 320
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
56-340 2.07e-34

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: 129.61  E-value: 2.07e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN---RELQIMRKLD--------HCniVRLRYFFyssgEKKD 124
Cdd:cd14134    14 YKILRLLGEGTFGKVLECWDRKRKRYVAVKIIRNVEKYREaakIEIDVLETLAekdpngksHC--VQLRDWF----DYRG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 125 EVYLnlVLDYVPETVYRVARHYSRakQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVL-------- 196
Cdd:cd14134    88 HMCI--VFELLGPSLYDFLKKNNY--GPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLVDSDYVKvynpkkkr 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 197 ----------KLCDFGSAkQLVRgEPNVSYICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQL 266
Cdd:cd14134   164 qirvpkstdiKLIDFGSA-TFDD-EYHSSIVSTRHYRAPEVILG-LGWSYPCDVWSIGCILVELYTGELLFQTHDNLEHL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 267 VEIIKVLGTPTREQIREM-------NPNYTEFKFPQ-------IKAHPWT-KVFRPRTPPEAIALC---SRLLEYTPTAR 328
Cdd:cd14134   241 AMMERILGPLPKRMIRRAkkgakyfYFYHGRLDWPEgsssgrsIKRVCKPlKRLMLLVDPEHRLLFdliRKMLEYDPSKR 320
                         330
                  ....*....|..
gi 1231802383 329 LTPLEACAHSFF 340
Cdd:cd14134   321 ITAKEALKHPFF 332
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
61-277 9.76e-34

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: 126.49  E-value: 9.76e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  61 VIGNGSFGVVYQAKLCDSGELVAIKKVL-------QDKRFKN------RELQIMRKLDHCNIVRlrYFfyssGEKKDEVY 127
Cdd:cd06628     7 LIGSGSFGSVYLGMNASSGELMAVKQVElpsvsaeNKDRKKSmldalqREIALLRELQHENIVQ--YL----GSSSDANH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 128 LNLVLDYVPE-TVYRVARHYSRAKQTLpviyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQ 206
Cdd:cd06628    81 LNIFLEYVPGgSVATLLNNYGAFEESL----VRNFVRQILKGLNYLHNRGIIHRDIKGANILVD-NKGGIKISDFGISKK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 207 L-------VRGEPNVSYICSRYYRAPELIfGATDYTSSIDVWSAGCVLAELLLGQPIFPgdsGVDQLVEIIKV--LGTPT 277
Cdd:cd06628   156 LeanslstKNNGARPSLQGSVFWMAPEVV-KQTSYTRKADIWSLGCLVVEMLTGTHPFP---DCTQMQAIFKIgeNASPT 231
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
62-340 2.65e-33

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: 125.41  E-value: 2.65e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKV-LQDKRFKNR------ELQIMRKLDHCNIVRlryFFYS-SGEKKdevyLNLVLD 133
Cdd:cd05579     1 ISRGAYGRVYLAKKKSTGDLYAIKVIkKRDMIRKNQvdsvlaERNILSQAQNPFVVK---LYYSfQGKKN----LYLVME 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 134 YVPE-TVYRVARHYSRakqtLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKLCDFGSAKQ-LVRGE 211
Cdd:cd05579    74 YLPGgDLYSLLENVGA----LDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDAN-GHLKLTDFGLSKVgLVRRQ 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 212 PNVSY---------------ICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIFPGDSgvdqlVEIIkvlgtp 276
Cdd:cd05579   149 IKLSIqkksngapekedrriVGTPDYLAPEILLG-QGHGKTVDWWSLGVILYEFLVGIPPFHAET-----PEEI------ 216
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1231802383 277 treqiremnpnytefkFPQIKAH--PWTKVfrPRTPPEAIALCSRLLEYTPTARLTPL---EACAHSFF 340
Cdd:cd05579   217 ----------------FQNILNGkiEWPED--PEVSDEAKDLISKLLTPDPEKRLGAKgieEIKNHPFF 267
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
56-337 2.70e-33

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: 124.90  E-value: 2.70e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN--------RELQIMRKLDHCNIVRLRYFFyssgEKKDEVY 127
Cdd:cd14098     2 YQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKVAGNdknlqlfqREINILKSLEHPGIVRLIDWY----EDDQHIY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 128 LnlVLDYVP--ETVYRVARHYSRAKQTLPVIYVklymyQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAV-LKLCDFGSA 204
Cdd:cd14098    78 L--VMEYVEggDLMDFIMAWGAIPEQHARELTK-----QILEAMAYTHSMGITHRDLKPENILITQDDPViVKISDFGLA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 205 KQLVRGEPNVSYICSRYYRAPELIFGAT-----DYTSSIDVWSAGCVLAELLLGQPIFPGDSGvDQLVEIIKVlGTPTRE 279
Cdd:cd14098   151 KVIHTGTFLVTFCGTMAYLAPEILMSKEqnlqgGYSNLVDMWSVGCLVYVMLTGALPFDGSSQ-LPVEKRIRK-GRYTQP 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1231802383 280 QIREMNpnytefkfpqikahpwtkvfrprTPPEAIALCSRLLEYTPTARLTPLEACAH 337
Cdd:cd14098   229 PLVDFN-----------------------ISEEAIDFILRLLDVDPEKRMTAAQALDH 263
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
62-301 2.92e-33

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: 124.68  E-value: 2.92e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKkVLQDKRFKN---------RELQIMRKLDHCNIVRLRYFFYssGEKKDEVYLnlVL 132
Cdd:cd14119     1 LGEGSYGKVKEVLDTETLCRRAVK-ILKKRKLRRipngeanvkREIQILRRLNHRNVIKLVDVLY--NEEKQKLYM--VM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 DYVPETVYRVARhySRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKLCDFGSAKQLVRGEP 212
Cdd:cd14119    76 EYCVGGLQEMLD--SAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTD-GTLKISDFGVAEALDLFAE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 213 NvsYICSRYY-----RAPELIFGATDYTS-SIDVWSAGCVLAELLLGQPIFPGDSgVDQLVEII--------KVLGTPTR 278
Cdd:cd14119   153 D--DTCTTSQgspafQPPEIANGQDSFSGfKVDIWSAGVTLYNMTTGKYPFEGDN-IYKLFENIgkgeytipDDVDPDLQ 229
                         250       260
                  ....*....|....*....|....*.
gi 1231802383 279 EQIREM---NPNyTEFKFPQIKAHPW 301
Cdd:cd14119   230 DLLRGMlekDPE-KRFTIEQIRQHPW 254
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
56-337 3.40e-33

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: 127.56  E-value: 3.40e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHC---------NIVR-LRYFFYSSgekkde 125
Cdd:cd14224    67 YEVLKVIGKGSFGQVVKAYDHKTHQHVALKMVRNEKRFHRQAAEEIRILEHLkkqdkdntmNVIHmLESFTFRN------ 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 126 vYLNLVLDYVPETVYRVARhysRAK-QTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPD-TAVLKLCDFGS 203
Cdd:cd14224   141 -HICMTFELLSMNLYELIK---KNKfQGFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQgRSGIKVIDFGS 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 204 A---KQLVrgepnVSYICSRYYRAPELIFGAtDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTrEQ 280
Cdd:cd14224   217 ScyeHQRI-----YTYIQSRFYRAPEVILGA-RYGMPIDMWSFGCILAELLTGYPLFPGEDEGDQLACMIELLGMPP-QK 289
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 281 IREMNPNYTEFKFPqiKAHP------------------WTKVFRPRTPPEA---------------IALCSRLLEYTPTA 327
Cdd:cd14224   290 LLETSKRAKNFISS--KGYPryctvttlpdgsvvlnggRSRRGKMRGPPGSkdwvtalkgcddplfLDFLKRCLEWDPAA 367
                         330
                  ....*....|
gi 1231802383 328 RLTPLEACAH 337
Cdd:cd14224   368 RMTPSQALRH 377
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
56-346 3.58e-33

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: 127.08  E-value: 3.58e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVlqDKRFKN--------RELQIMRKLDHCNIVRLRYFF--YSSGEKKDE 125
Cdd:cd07875    26 YQNLKPIGSGAQGIVCAAYDAILERNVAIKKL--SRPFQNqthakrayRELVLMKCVNHKNIIGLLNVFtpQKSLEEFQD 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 126 VYLNL-VLDYVPETVYRVARHYSRakqtlpviyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKLCDFGSA 204
Cdd:cd07875   104 VYIVMeLMDANLCQVIQMELDHER---------MSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSD-CTLKILDFGLA 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 205 KQLVRGEPNVSYICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREM 284
Cdd:cd07875   174 RTAGTSFMMTPYVVTRYYRAPEVILG-MGYKENVDIWSVGCIMGEMIKGGVLFPGTDHIDQWNKVIEQLGTPCPEFMKKL 252
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1231802383 285 NP---NYTEFKfPQIKAHPWTKVFRPRTPP-----------EAIALCSRLLEYTPTARLTPLEACAHSFFDELRDP 346
Cdd:cd07875   253 QPtvrTYVENR-PKYAGYSFEKLFPDVLFPadsehnklkasQARDLLSKMLVIDASKRISVDEALQHPYINVWYDP 327
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
56-337 1.15e-32

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: 123.20  E-value: 1.15e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKkVLQDKRFKNR------ELQIMRKLDHCNIVRLryffYSSGEKKDEVYLn 129
Cdd:cd14095     2 YDIGRVIGDGNFAVVKECRDKATDKEYALK-IIDKAKCKGKehmienEVAILRRVKHPNIVQL----IEEYDTDTELYL- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 lVLDYVPE----TVYRVARHYSRAKqtlpviyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPD---TAVLKLCDFG 202
Cdd:cd14095    76 -VMELVKGgdlfDAITSSTKFTERD-------ASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHedgSKSLKLADFG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 203 SAKQLVrgEPnVSYIC-SRYYRAPElIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGV-DQLVEIIKvLGtptreq 280
Cdd:cd14095   148 LATEVK--EP-LFTVCgTPTYVAPE-ILAETGYGLKVDIWAAGVITYILLCGFPPFRSPDRDqEELFDLIL-AG------ 216
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1231802383 281 iremnpnytEFKFPQikahP-WTKVfrprtPPEAIALCSRLLEYTPTARLTPLEACAH 337
Cdd:cd14095   217 ---------EFEFLS----PyWDNI-----SDSAKDLISRMLVVDPEKRYSAGQVLDH 256
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
56-340 7.30e-32

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: 120.78  E-value: 7.30e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKV-LQDKRFKN--RELQIMRKLDHCNIVRlryfFYSSGEKKDEVYLnlVL 132
Cdd:cd06614     2 YKNLEKIGEGASGEVYKATDRATGKEVAIKKMrLRKQNKELiiNEILIMKECKHPNIVD----YYDSYLVGDELWV--VM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 DY-----VPETVYrvarhYSRAKQTLPVI-YVklyMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQ 206
Cdd:cd06614    76 EYmdggsLTDIIT-----QNPVRMNESQIaYV---CREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSV-KLADFGFAAQ 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 207 LVRGEPN-VSYICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKvLGTPtreQIREmn 285
Cdd:cd06614   147 LTKEKSKrNSVVGTPYWMAPEVIKR-KDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRALFLITT-KGIP---PLKN-- 219
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1231802383 286 pnytefkfpqikAHPWTKVFRprtppEAIALCsrlLEYTPTARLTPLEACAHSFF 340
Cdd:cd06614   220 ------------PEKWSPEFK-----DFLNKC---LVKDPEKRPSAEELLQHPFL 254
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
60-340 7.97e-32

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: 123.16  E-value: 7.97e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKVLQD---KR----FKNRELQIMRKLDHCNIVRLRYFFyssgekKDEVYLNLVL 132
Cdd:cd05573     7 KVIGRGAFGEVWLVRDKDTGQVYAMKILRKSdmlKReqiaHVRAERDILADADSPWIVRLHYAF------QDEDHLYLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 DYVP--ETVYRVARhysraKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLVRG 210
Cdd:cd05573    81 EYMPggDLMNLLIK-----YDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHI-KLADFGLCTKMNKS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 211 EPNVSYICSRY------------------------------YRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIFPGD 260
Cdd:cd05573   155 GDRESYLNDSVntlfqdnvlarrrphkqrrvraysavgtpdYIAPEVLRG-TGYGPECDWWSLGVILYEMLYGFPPFYSD 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 261 SgvdqLVEiikvlgtpTREQIreMNPNyTEFKFPQikahpwtkvfRPRTPPEAIALCSRLLEyTPTARLTPLE-ACAHSF 339
Cdd:cd05573   234 S----LVE--------TYSKI--MNWK-ESLVFPD----------DPDVSPEAIDLIRRLLC-DPEDRLGSAEeIKAHPF 287

                  .
gi 1231802383 340 F 340
Cdd:cd05573   288 F 288
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
56-330 1.10e-31

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: 120.51  E-value: 1.10e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKV-------LQDKRFKnRELQIMRKLDHCNIVRlryfFYssGEKKDEVYL 128
Cdd:cd14069     3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVdmkrapgDCPENIK-KEVCIQKMLSHKNVVR----FY--GHRREGEFQ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 129 NLVLDYVP--ETVYRVARHYSrakqtLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQ 206
Cdd:cd14069    76 YLFLEYASggELFDKIEPDVG-----MPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLD-ENDNLKISDFGLATV 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 207 L-VRGEPNV--SYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQpifpgdsgvdqlveiikvlgTPTrEQIRE 283
Cdd:cd14069   150 FrYKGKERLlnKMCGTLPYVAPELLAKKKYRAEPVDVWSCGIVLFAMLAGE--------------------LPW-DQPSD 208
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1231802383 284 MNPNYTEFKFPQ-IKAHPWTKVfrprtPPEAIALCSRLLEYTPTARLT 330
Cdd:cd14069   209 SCQEYSDWKENKkTYLTPWKKI-----DTAALSLLRKILTENPNKRIT 251
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
54-254 4.01e-31

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: 119.41  E-value: 4.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  54 VSYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKV--------LQDKRFK------NRELQIMRKLDHCNIVRlryffYSS 119
Cdd:cd06629     1 FKWVKGELIGKGTYGRVYLAMNATTGEMLAVKQVelpktssdRADSRQKtvvdalKSEIDTLKDLDHPNIVQ-----YLG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 120 GEKKDEvYLNLVLDYVPE-TVYRVARHYSRAKQTLpviyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKL 198
Cdd:cd06629    76 FEETED-YFSIFLEYVPGgSIGSCLRKYGKFEEDL----VRFFTRQILDGLAYLHSKGILHRDLKADNILVDLE-GICKI 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 199 CDFGSAKQ---LVRGEPNVSYICSRYYRAPELIFGATD-YTSSIDVWSAGCVLAELLLGQ 254
Cdd:cd06629   150 SDFGISKKsddIYGNNGATSMQGSVFWMAPEVIHSQGQgYSAKVDIWSLGCVVLEMLAGR 209
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
59-257 8.78e-31

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: 118.84  E-value: 8.78e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  59 TKVIGNGSFGVVYQAKLCDSGELVAIK-----KVLQDKRFK--NRELQIMRKLDHCNIVRLRYFFyssgekKDEVYLNLV 131
Cdd:cd05580     6 LKTLGTGSFGRVRLVKHKDSGKYYALKilkkaKIIKLKQVEhvLNEKRILSEVRHPFIVNLLGSF------QDDRNLYMV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 132 LDYVP--ETVyrvarHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKLCDFGSAKQLvr 209
Cdd:cd05580    80 MEYVPggELF-----SLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSD-GHIKITDFGFAKRV-- 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1231802383 210 gePNVSY-IC-SRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIF 257
Cdd:cd05580   152 --KDRTYtLCgTPEYLAPEIILS-KGHGKAVDWWALGILIYEMLAGYPPF 198
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
62-329 9.89e-31

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: 118.10  E-value: 9.89e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNR-------ELQIMRKLDHCNIVRL-RYFfyssgekKDEVYLNLVLD 133
Cdd:cd05572     1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIVQTRqqehifsEKEILEECNSPFIVKLyRTF-------KDKKYLYMLME 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 134 YVPE----TVYRVARHYSRAKqtlpviyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQLVR 209
Cdd:cd05572    74 YCLGgelwTILRDRGLFDEYT-------ARFYTACVVLAFEYLHSRGIIYRDLKPENLLLD-SNGYVKLVDFGFAKKLGS 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 210 GEPNVSYICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIFPGDSGvDQLVeiikvlgtpTREQIREMNPNYt 289
Cdd:cd05572   146 GRKTWTFCGTPEYVAPEIILN-KGYDFSVDYWSLGILLYELLTGRPPFGGDDE-DPMK---------IYNIILKGIDKI- 213
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1231802383 290 efKFPQIKahpwtkvfrprtPPEAIALCSRLLEYTPTARL 329
Cdd:cd05572   214 --EFPKYI------------DKNAKNLIKQLLRRNPEERL 239
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
62-340 1.05e-30

Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L6 is also called CDK8-like and was previously referred to as CDK11. However, this is a confusing nomenclature as CDC2L6 is distinct from CDC2L1, which is represented by the two protein products from its gene, called CDK11(p110) and CDK11(p58), as well as the caspase-processed CDK11(p46). CDK11(p110), CDK11(p58), and CDK11(p46)do not belong to this subfamily. CDC2L6 is an associated protein of Mediator, a multiprotein complex that provides a platform to connect transcriptional and chromatin regulators and cofactors, in order to activate and mediate RNA polymerase II transcription. CDC2L6 is localized mainly in the nucleus amd exerts an opposing effect to CDK8 in VP16-dependent transcriptional activation by being a negative regulator. 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 CDC2L6 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: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 119.40  E-value: 1.05e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGEL--VAIKKVLQD--KRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKdevyLNLVLDYVPE 137
Cdd:cd07867    10 VGRGTYGHVYKAKRKDGKDEkeYALKQIEGTgiSMSACREIALLRELKHPNVIALQKVFLSHSDRK----VWLLFDYAEH 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 138 TVYRVARHYSRAKQT-----LPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLL---DPDTAVLKLCDFGSA----- 204
Cdd:cd07867    86 DLWHIIKFHRASKANkkpmqLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgeGPERGRVKIADMGFArlfns 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 205 --KQLVRGEPnvsYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIF---------PGDSGVDQLVEIIKVL 273
Cdd:cd07867   166 plKPLADLDP---VVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELLTSEPIFhcrqediktSNPFHHDQLDRIFSVM 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 274 GTPTR---EQIREMnPNYTEFK----------------FPQIKAHPWTKVFrprtppeaiALCSRLLEYTPTARLTPLEA 334
Cdd:cd07867   243 GFPADkdwEDIRKM-PEYPTLQkdfrrttyansslikyMEKHKVKPDSKVF---------LLLQKLLTMDPTKRITSEQA 312

                  ....*.
gi 1231802383 335 CAHSFF 340
Cdd:cd07867   313 LQDPYF 318
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
61-340 1.20e-30

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: 117.74  E-value: 1.20e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  61 VIGNGSFGVVYQAKLCDSGELVAIK-----KVLQDKRFKN--RELQIMRKLDHCNIVRLRYFFyssgekKDEVYLNLVLD 133
Cdd:cd05578     7 VIGKGSFGKVCIVQKKDTKKMFAMKymnkqKCIEKDSVRNvlNELEILQELEHPFLVNLWYSF------QDEEDMYMVVD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 134 YVPETVYRVarHYSRaKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLVRGEPN 213
Cdd:cd05578    81 LLLGGDLRY--HLQQ-KVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHV-HITDFNIATKLTDGTLA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 214 VSYICSRYYRAPElIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSgvdqlveiikvlgTPTREQIREMnpnytefkf 293
Cdd:cd05578   157 TSTSGTKPYMAPE-VFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEIHS-------------RTSIEEIRAK--------- 213
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1231802383 294 pQIKAHPwtkVFRPRTPPEAIALCSRLLEYTPTARLTPLEAC-AHSFF 340
Cdd:cd05578   214 -FETASV---LYPAGWSEEAIDLINKLLERDPQKRLGDLSDLkNHPYF 257
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
56-301 1.35e-30

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: 117.78  E-value: 1.35e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDK-------RFKNRELQIMRKLDHCNIVRlryfFYSSGEKKDEVYL 128
Cdd:cd14162     2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVSKKKapedylqKFLPREIEVIKGLKHPNLIC----FYEAIETTSRVYI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 129 NL-------VLDYVpetvyrvarhysRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAvLKLCDF 201
Cdd:cd14162    78 IMelaengdLLDYI------------RKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNN-LKITDF 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 202 GSAK---QLVRGEPNVS--YICSRYYRAPELIFG-ATDYTSSiDVWSAGCVLAELLLGQPIFpGDSGVDQLVEII----- 270
Cdd:cd14162   145 GFARgvmKTKDGKPKLSetYCGSYAYASPEILRGiPYDPFLS-DIWSMGVVLYTMVYGRLPF-DDSNLKVLLKQVqrrvv 222
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1231802383 271 ----KVLGTPTREQIREM-NPNYTEFKFPQIKAHPW 301
Cdd:cd14162   223 fpknPTVSEECKDLILRMlSPVKKRITIEEIKRDPW 258
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
55-253 1.79e-30

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: 117.45  E-value: 1.79e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  55 SYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQD-----------KRFKNRELQIMRKL-DHCNIVRLRYFFyssgek 122
Cdd:cd13993     1 RYQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLYKSgpnskdgndfqKLPQLREIDLHRRVsRHPNIITLHDVF------ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 123 KDEVYLNLVLDYVPETVYRVARHYSRAKQTLPVIyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFG 202
Cdd:cd13993    75 ETEVAIYIVLEYCPNGDLFEAITENRIYVGKTEL-IKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDEGTVKLCDFG 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1231802383 203 SAKQlVRGEPNVSyICSRYYRAPELI-----FGATDYTSSIDVWSAGCVLAELLLG 253
Cdd:cd13993   154 LATT-EKISMDFG-VGSEFYMAPECFdevgrSLKGYPCAAGDIWSLGIILLNLTFG 207
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
56-260 2.01e-30

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: 117.37  E-value: 2.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKV----LQDKRFKN---RELQIMRKLDHCNIVRlrYF--FYSSGEkkdev 126
Cdd:cd08224     2 YEIEKKIGKGQFSVVYRARCLLDGRLVALKKVqifeMMDAKARQdclKEIDLLQQLNHPNIIK--YLasFIENNE----- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 127 yLNLVLDYVPE-TVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKLCDFG--- 202
Cdd:cd08224    75 -LNIVLELADAgDLSRLIKHFKKQKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITAN-GVVKLGDLGlgr 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1231802383 203 -------SAKQLVrGEPnvsyicsrYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIFPGD 260
Cdd:cd08224   153 ffsskttAAHSLV-GTP--------YYMSPERIRE-QGYDFKSDIWSLGCLLYEMAALQSPFYGE 207
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
62-339 2.20e-30

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: 117.39  E-value: 2.20e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFK-NRELQIMRKLDHCNIVRlryfFYSSGEKKDevYLNLVLDYVP---- 136
Cdd:cd14010     8 IGRGKHSVVYKGRRKGTIEFVAIKCVDKSKRPEvLNEVRLTHELKHPNVLK----FYEWYETSN--HLWLVVEYCTggdl 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 137 ETVYRVARHysrakqtLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAK----------Q 206
Cdd:cd14010    82 ETLLRQDGN-------LPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLD-GNGTLKLSDFGLARregeilkelfG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 207 LVRGEPNVSYIC-------SRYYRAPELIFGATDYTSSiDVWSAGCVLAELLLGQPIFPGDSgVDQLVEiikvlgtptre 279
Cdd:cd14010   154 QFSDEGNVNKVSkkqakrgTPYYMAPELFQGGVHSFAS-DLWALGCVLYEMFTGKPPFVAES-FTELVE----------- 220
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 280 QIREMNPNytefkfpqikahPWTKVFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSF 339
Cdd:cd14010   221 KILNEDPP------------PPPPKVSSKPSPDFKSLLKGLLEKDPAKRLSWDELVKHPF 268
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
56-339 2.20e-30

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: 118.71  E-value: 2.20e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKkVLQDKRFKNRELQIMRKLDHC---------NIVRLRYFFyssgekKDEV 126
Cdd:cd14211     1 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIK-ILKNHPSYARQGQIEVSILSRlsqenadefNFVRAYECF------QHKN 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 127 YLNLVLDYVPETVYRVARHysRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLL-DPDTAV--LKLCDFGS 203
Cdd:cd14211    74 HTCLVFEMLEQNLYDFLKQ--NKFSPLPLKYIRPILQQVLTALLKLKSLGLIHADLKPENIMLvDPVRQPyrVKVIDFGS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 204 AKQLVRGEPNvSYICSRYYRAPELIFGATdYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTP------- 276
Cdd:cd14211   152 ASHVSKAVCS-TYLQSRYYRAPEIILGLP-FCEAIDMWSLGCVIAELFLGWPLYPGSSEYDQIRYISQTQGLPaehllna 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 277 ----TREQIREMNPNY------------TEFKFPQIKAHPW--------TKVFRPRTPP------------EAIALCSRL 320
Cdd:cd14211   230 atktSRFFNRDPDSPYplwrlktpeeheAETGIKSKEARKYifnclddmAQVNGPSDLEgsellaekadrrEFIDLLKRM 309
                         330
                  ....*....|....*....
gi 1231802383 321 LEYTPTARLTPLEACAHSF 339
Cdd:cd14211   310 LTIDQERRITPGEALNHPF 328
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
62-340 2.53e-30

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK8 can act 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 (RNAP II)-dependent transcription. CDK8 phosphorylates cyclin H, a subunit of the general transcription factor TFIIH, which results in the inhibition of TFIIH-dependent phosphorylation of the C-terminal domain of RNAP II, facilitating the inhibition of transcription. It has also been shown to promote transcription by a mechanism that is likely to involve RNAP II phosphorylation. CDK8 also functions as a stimulus-specific positive coregulator of p53 transcriptional responses. 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 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: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 118.62  E-value: 2.53e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGEL--VAIKKVLQD--KRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKdevyLNLVLDYVPE 137
Cdd:cd07868    25 VGRGTYGHVYKAKRKDGKDDkdYALKQIEGTgiSMSACREIALLRELKHPNVISLQKVFLSHADRK----VWLLFDYAEH 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 138 TVYRVARHYSRAKQT-----LPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLL---DPDTAVLKLCDFGSA----- 204
Cdd:cd07868   101 DLWHIIKFHRASKANkkpvqLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgeGPERGRVKIADMGFArlfns 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 205 --KQLVRGEPnvsYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIF---------PGDSGVDQLVEIIKVL 273
Cdd:cd07868   181 plKPLADLDP---VVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELLTSEPIFhcrqediktSNPYHHDQLDRIFNVM 257
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1231802383 274 GTPTR---EQIREMNPNYTEFK------FPQIKAHPWTKVFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd07868   258 GFPADkdwEDIKKMPEHSTLMKdfrrntYTNCSLIKYMEKHKVKPDSKAFHLLQKLLTMDPIKRITSEQAMQDPYF 333
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
60-271 7.74e-30

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: 115.34  E-value: 7.74e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383   60 KVIGNGSFGVVYQAKL----CDSGELVAIKKVLQDKRFKN-----RELQIMRKLDHCNIVRLryffYSSGEKKDEVYLnl 130
Cdd:smart00221   5 KKLGEGAFGEVYKGTLkgkgDGKEVEVAVKTLKEDASEQQieeflREARIMRKLDHPNIVKL----LGVCTEEEPLMI-- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  131 VLDYVPetvYRVARHY--SRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLV 208
Cdd:smart00221  79 VMEYMP---GGDLLDYlrKNRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVV-KISDFGLSRDLY 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1231802383  209 RGEpnvsyicsrYYR-----------APELIFGATdYTSSIDVWSAGCVLAELL-LGQPIFPGDSgVDQLVEIIK 271
Cdd:smart00221 155 DDD---------YYKvkggklpirwmAPESLKEGK-FTSKSDVWSFGVLLWEIFtLGEEPYPGMS-NAEVLEYLK 218
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
57-271 1.13e-29

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 114.94  E-value: 1.13e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383   57 TDTKVIGNGSFGVVYQAKL----CDSGELVAIKKVLQDKRFKN-----RELQIMRKLDHCNIVRLRYFFYSSGEkkdevy 127
Cdd:smart00219   2 TLGKKLGEGAFGEVYKGKLkgkgGKKKVEVAVKTLKEDASEQQieeflREARIMRKLDHPNVVKLLGVCTEEEP------ 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  128 LNLVLDYVPetvYRVARHYSRAKQ-TLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTaVLKLCDFGSAKQ 206
Cdd:smart00219  76 LYIVMEYME---GGDLLSYLRKNRpKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENL-VVKISDFGLSRD 151
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1231802383  207 LVRGEpnvsyicsrYYR-----------APELIFGATdYTSSIDVWSAGCVLAELL-LGQPIFPGDSgVDQLVEIIK 271
Cdd:smart00219 152 LYDDD---------YYRkrggklpirwmAPESLKEGK-FTSKSDVWSFGVLLWEIFtLGEQPYPGMS-NEEVLEYLK 217
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
60-301 1.50e-29

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: 114.81  E-value: 1.50e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN-------RELQIMRKLDHCNIVRLRYFFYSsgekKDEVYLnlVL 132
Cdd:cd14663     6 RTLGEGTFAKVKFARNTKTGESVAIKIIDKEQVAREgmveqikREIAIMKLLRHPNIVELHEVMAT----KTKIFF--VM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 DYVP--ETVYRVArhysrAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKLCDFG-SA-KQLV 208
Cdd:cd14663    80 ELVTggELFSKIA-----KNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDED-GNLKISDFGlSAlSEQF 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 209 RGEPNVSYIC-SRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKV-------LGTPTREQ 280
Cdd:cd14663   154 RQDGLLHTTCgTPNYVAPEVLARRGYDGAKADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKGefeyprwFSPGAKSL 233
                         250       260
                  ....*....|....*....|....
gi 1231802383 281 IREM---NPNyTEFKFPQIKAHPW 301
Cdd:cd14663   234 IKRIldpNPS-TRITVEQIMASPW 256
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
60-305 5.60e-29

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: 113.46  E-value: 5.60e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKK--VLQDKRFKN---RELQIMRKLDHCNIVRLRYFFYSSGEkkdevyLNLVLDY 134
Cdd:cd06623     7 KVLGQGSSGVVYKVRHKPTGKIYALKKihVDGDEEFRKqllRELKTLRSCESPYVVKCYGAFYKEGE------ISIVLEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 135 VP----ETVYRVARHysrakqtLPVIYVKLYMYQLFRSLAYIHSF-GICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLVR 209
Cdd:cd06623    81 MDggslADLLKKVGK-------IPEPVLAYIARQILKGLDYLHTKrHIIHRDIKPSNLLINSKGEV-KIADFGISKVLEN 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 210 G-EPNVSYICSRYYRAPELIFGATDYTSSiDVWSAGCVLAELLLGQ-P-IFPGDSGVDQLVEIIkVLGTPTREQIREMNP 286
Cdd:cd06623   153 TlDQCNTFVGTVTYMSPERIQGESYSYAA-DIWSLGLTLLECALGKfPfLPPGQPSFFELMQAI-CDGPPPSLPAEEFSP 230
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1231802383 287 NYTEF------KFP-------QIKAHPWTKVF 305
Cdd:cd06623   231 EFRDFisaclqKDPkkrpsaaELLQHPFIKKA 262
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
60-340 3.29e-28

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: 111.42  E-value: 3.29e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIK-----KVLQDKRFKNRELQ---IMRKLDHCNIVRLRYFFYSsgekKDevYLNLV 131
Cdd:cd05611     2 KPISKGAFGSVYLAKKRSTGDYFAIKvlkksDMIAKNQVTNVKAEraiMMIQGESPYVAKLYYSFQS----KD--YLYLV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 132 LDYVP----ETVYRVArhysrakQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQL 207
Cdd:cd05611    76 MEYLNggdcASLIKTL-------GGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLID-QTGHLKLTDFGLSRNG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 208 VRGEPNVSYICSRYYRAPELIFGATDyTSSIDVWSAGCVLAELLLGQPIFPGDSgVDQLVEIIkvlgtpTREQIremnpN 287
Cdd:cd05611   148 LEKRHNKKFVGTPDYLAPETILGVGD-DKMSDWWSLGCVIFEFLFGYPPFHAET-PDAVFDNI------LSRRI-----N 214
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1231802383 288 YTEFKFPQIKahpwtkvfrprtpPEAIALCSRLLEYTPTARLTP---LEACAHSFF 340
Cdd:cd05611   215 WPEEVKEFCS-------------PEAVDLINRLLCMDPAKRLGAngyQEIKSHPFF 257
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
62-286 5.53e-28

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: 110.83  E-value: 5.53e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLcDSGELVAIKKV-----LQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKdevylnLVLDYVP 136
Cdd:cd14066     1 IGSGGFGTVYKGVL-ENGTVVAVKRLnemncAASKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKL------LVYEYMP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 137 E-TVYRVARHySRAKQTLPV-----IYVklymyQLFRSLAYIHSFG---ICHRDIKPQNLLLDPDTaVLKLCDFGSAKQL 207
Cdd:cd14066    74 NgSLEDRLHC-HKGSPPLPWpqrlkIAK-----GIARGLEYLHEECpppIIHGDIKSSNILLDEDF-EPKLTDFGLARLI 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 208 VRGEPNVSYICSRY---YRAPELIFGATdYTSSIDVWSAGCVLAELLLGQP---IFPGDSGVDQLVEIIKVLGTPTREQI 281
Cdd:cd14066   147 PPSESVSKTSAVKGtigYLAPEYIRTGR-VSTKSDVYSFGVVLLELLTGKPavdENRENASRKDLVEWVESKGKEELEDI 225

                  ....*
gi 1231802383 282 REMNP 286
Cdd:cd14066   226 LDKRL 230
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
60-251 9.26e-28

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: 110.46  E-value: 9.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKV-LQDKRFKN----RELQIMRKLDHCNIVRlryfFYSSGEKKDEVYLNLVLdY 134
Cdd:cd13996    12 ELLGSGGFGSVYKVRNKVDGVTYAIKKIrLTEKSSASekvlREVKALAKLNHPNIVR----YYTAWVEEPPLYIQMEL-C 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 135 VPETVY-RVARHYSRAKQTLPVIYvkLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSAKQLVRGEP- 212
Cdd:cd13996    87 EGGTLRdWIDRRNSSSKNDRKLAL--ELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDDLQVKIGDFGLATSIGNQKRe 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1231802383 213 --------------NVSYICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAELL 251
Cdd:cd13996   165 lnnlnnnnngntsnNSVGIGTPLYASPEQLDG-ENYNEKADIYSLGIILFEML 216
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
62-340 1.78e-27

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: 109.32  E-value: 1.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVV--YQAKLCDSGELVAIKKV------LQDKRFKNR---ELQIMRKLDHCNIVRLRYFFYSSGEKkdevyLNL 130
Cdd:cd13994     1 IGKGATSVVriVTKKNPRSGVLYAVKEYrrrddeSKRKDYVKRltsEYIISSKLHHPNIVKVLDLCQDLHGK-----WCL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 VLDYVPE-TVYRVARhysrAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKLCDFGSAKQL-V 208
Cdd:cd13994    76 VMEYCPGgDLFTLIE----KADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDED-GVLKLTDFGTAEVFgM 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 209 RGEPNVSYIC----SRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGqpIFPGDSGVDQlveiikvlgtptreqirem 284
Cdd:cd13994   151 PAEKESPMSAglcgSEPYMAPEVFTSGSYDGRAVDVWSCGIVLFALFTG--RFPWRSAKKS------------------- 209
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1231802383 285 NPNYTEFKFPQIKAHPWTKVFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd13994   210 DSAYKAYEKSGDFTNGPYEPIENLLPSECRRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
61-255 1.97e-27

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: 108.89  E-value: 1.97e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  61 VIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN--RELQIMRKLDHCNIVRlryfFYSSGEKKDEVYLnlVLDY-VPE 137
Cdd:cd06612    10 KLGEGSYGSVYKAIHKETGQVVAIKVVPVEEDLQEiiKEISILKQCDSPYIVK----YYGSYFKNTDLWI--VMEYcGAG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 138 TVYRVARHYSRakqTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLVR--GEPNvS 215
Cdd:cd06612    84 SVSDIMKITNK---TLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQA-KLADFGVSGQLTDtmAKRN-T 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1231802383 216 YICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQP 255
Cdd:cd06612   159 VIGTPFWMAPEVIQE-IGYNNKADIWSLGITAIEMAEGKP 197
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
55-312 2.84e-27

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: 110.95  E-value: 2.84e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  55 SYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNR---ELQIMRKL-----DHCNIVRlryfFYSSGEKKDev 126
Cdd:cd14228    16 SYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQgqiEVSILSRLssenaDEYNFVR----SYECFQHKN-- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 127 YLNLVLDYVPETVYRVARHYSRAKqtLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLL-DP--DTAVLKLCDFGS 203
Cdd:cd14228    90 HTCLVFEMLEQNLYDFLKQNKFSP--LPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLvDPvrQPYRVKVIDFGS 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 204 AKQLVRGEPNvSYICSRYYRAPELIFGATdYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTrEQIRE 283
Cdd:cd14228   168 ASHVSKAVCS-TYLQSRYYRAPEIILGLP-FCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQGLPA-EYLLS 244
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1231802383 284 MNPNYTEF--KFPQIKAHPWtkvfRPRTPPE 312
Cdd:cd14228   245 AGTKTSRFfnRDPNLGYPLW----RLKTPEE 271
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
62-253 4.06e-27

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: 108.24  E-value: 4.06e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKkvLQDK--------RFKnRELQIMRKLDHCNIVRLryffYSSGEKKDEVYLnlVLD 133
Cdd:cd14078    11 IGSGGFAKVKLATHILTGEKVAIK--IMDKkalgddlpRVK-TEIEALKNLSHQHICRL----YHVIETDNKIFM--VLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 134 YVP--ETVyrvarHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAvLKLCDFG-SAKQLVRG 210
Cdd:cd14078    82 YCPggELF-----DYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQN-LKLIDFGlCAKPKGGM 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1231802383 211 EPNVSYIC-SRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLG 253
Cdd:cd14078   156 DHHLETCCgSPAYAAPELIQGKPYIGSEADVWSMGVLLYALLCG 199
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
60-340 4.42e-27

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: 108.20  E-value: 4.42e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKVLQD---KRFKN--RELQIMRKLDHCNIVRLRYFFYSSGEkkdevyLNLVLDY 134
Cdd:cd06605     7 GELGEGNGGVVSKVRHRPSGQIMAVKVIRLEideALQKQilRELDVLHKCNSPYIVGFYGAFYSEGD------ISICMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 135 VPETvyRVARHYSRAKqTLPVIYVKLYMYQLFRSLAYIHS-FGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLVRGEPN 213
Cdd:cd06605    81 MDGG--SLDKILKEVG-RIPERILGKIAVAVVKGLIYLHEkHKIIHRDVKPSNILVNSRGQV-KLCDFGVSGQLVDSLAK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 214 vSYICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQpiFPGD-SGVDQLVEIIKVLgtptrEQIREMNPnytefk 292
Cdd:cd06605   157 -TFVGTRSYMAPERISG-GKYTVKSDIWSLGLSLVELATGR--FPYPpPNAKPSMMIFELL-----SYIVDEPP------ 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1231802383 293 fPQIKAHPWTKVFRprtppEAIALCsrlLEYTPTARLTPLEACAHSFF 340
Cdd:cd06605   222 -PLLPSGKFSPDFQ-----DFVSQC---LQKDPTERPSYKELMEHPFI 260
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
55-312 7.62e-27

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: 109.79  E-value: 7.62e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  55 SYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNR---ELQIMRKL-----DHCNIVRLryffYSSGEKKDev 126
Cdd:cd14227    16 TYEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQgqiEVSILARLstesaDDYNFVRA----YECFQHKN-- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 127 YLNLVLDYVPETVYRVARHYSRAKqtLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLL-DPDTAV--LKLCDFGS 203
Cdd:cd14227    90 HTCLVFEMLEQNLYDFLKQNKFSP--LPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLvDPSRQPyrVKVIDFGS 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 204 AKQLVRGEPNvSYICSRYYRAPELIFGATdYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTrEQIRE 283
Cdd:cd14227   168 ASHVSKAVCS-TYLQSRYYRAPEIILGLP-FCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQGLPA-EYLLS 244
                         250       260
                  ....*....|....*....|....*....
gi 1231802383 284 MNPNYTEFkFPQIKAHPWtKVFRPRTPPE 312
Cdd:cd14227   245 AGTKTTRF-FNRDTDSPY-PLWRLKTPED 271
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
55-299 9.33e-27

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: 108.96  E-value: 9.33e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  55 SYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNR---ELQIMRKL-----DHCNIVRLRYFFyssgekKDEV 126
Cdd:cd14229     1 TYEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILKNHPSYARQgqiEVGILARLsnenaDEFNFVRAYECF------QHRN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 127 YLNLVLDYVPETVYRVARHYSRAKqtLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLL-DP--DTAVLKLCDFGS 203
Cdd:cd14229    75 HTCLVFEMLEQNLYDFLKQNKFSP--LPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMLvDPvrQPYRVKVIDFGS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 204 AKQLVRGEPNvSYICSRYYRAPELIFGATdYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQI-- 281
Cdd:cd14229   153 ASHVSKTVCS-TYLQSRYYRAPEIILGLP-FCEAIDMWSLGCVIAELFLGWPLYPGALEYDQIRYISQTQGLPGEQLLnv 230
                         250       260
                  ....*....|....*....|....*..
gi 1231802383 282 ---------REMNPNYTEFKFPQIKAH 299
Cdd:cd14229   231 gtktsrffcRETDAPYSSWRLKTLEEH 257
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
56-339 1.13e-26

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: 106.96  E-value: 1.13e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKkVLQDKRFKNRE------LQIMRKLDHCNIVRLryffYSSGEKKDEVYLn 129
Cdd:cd14185     2 YEIGRTIGDGNFAVVKECRHWNENQEYAMK-IIDKSKLKGKEdmieseILIIKSLSHPNIVKL----FEVYETEKEIYL- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 lVLDYVP---------ETVyRVARHYSrakqtlpviyvKLYMYQLFRSLAYIHSFGICHRDIKPQNLLL--DPD-TAVLK 197
Cdd:cd14185    76 -ILEYVRggdlfdaiiESV-KFTEHDA-----------ALMIIDLCEALVYIHSKHIVHRDLKPENLLVqhNPDkSTTLK 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 198 LCDFGSAKQLVRgePNVSYICSRYYRAPElIFGATDYTSSIDVWSAGCVLAELLLGQPIFPG-DSGVDQLVEIIKVlgtp 276
Cdd:cd14185   143 LADFGLAKYVTG--PIFTVCGTPTYVAPE-ILSEKGYGLEVDMWAAGVILYILLCGFPPFRSpERDQEELFQIIQL---- 215
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1231802383 277 treqiremnpNYTEFKFPQikahpWTKVfrprtPPEAIALCSRLLEYTPTARLTPLEACAHSF 339
Cdd:cd14185   216 ----------GHYEFLPPY-----WDNI-----SEAAKDLISRLLVVDPEKRYTAKQVLQHPW 258
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
60-255 1.43e-26

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: 106.67  E-value: 1.43e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYqakLC---DSGELVAIKKVLQD----------KRFKNrELQIMRKLDHCNIVRlrYFfyssGEKKDEV 126
Cdd:cd06625     6 KLLGQGAFGQVY---LCydaDTGRELAVKQVEIDpinteaskevKALEC-EIQLLKNLQHERIVQ--YY----GCLQDEK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 127 YLNLVLDYVPE-TVYRVARHYSRAKQTLpviyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAK 205
Cdd:cd06625    76 SLSIFMEYMPGgSVKDEIKAYGALTENV----TRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNV-KLGDFGASK 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1231802383 206 QL-----------VRGEPnvsyicsrYYRAPELIFGAtDYTSSIDVWSAGCVLAELLLGQP 255
Cdd:cd06625   151 RLqticsstgmksVTGTP--------YWMSPEVINGE-GYGRKADIWSVGCTVVEMLTTKP 202
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
60-257 2.99e-26

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: 107.40  E-value: 2.99e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKkVLQDK--RFKNRELQIM-------RKLDHCNIVRLRYFFyssgEKKDEVYLnl 130
Cdd:cd05575     1 KVIGKGSFGKVLLARHKAEGKLYAVK-VLQKKaiLKRNEVKHIMaernvllKNVKHPFLVGLHYSF----QTKDKLYF-- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 VLDYVP--ETVYRVA--RHYSRAKqtlpviyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQ 206
Cdd:cd05575    74 VLDYVNggELFFHLQreRHFPEPR-------ARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHV-VLTDFGLCKE 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 207 LVRGEPNVSYIC-SRYYRAPELIFgATDYTSSIDVWSAGCVLAELLLGQPIF 257
Cdd:cd05575   146 GIEPSDTTSTFCgTPEYLAPEVLR-KQPYDRTVDWWCLGAVLYEMLYGLPPF 196
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
60-271 3.26e-26

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: 105.70  E-value: 3.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKV------LQDKRFKNRELQIMRKLDHCNIVRlryffyssgekkdevYLNLVLD 133
Cdd:cd08217     6 ETIGKGSFGTVRKVRRKSDGKILVWKEIdygkmsEKEKQQLVSEVNILRELKHPNIVR---------------YYDRIVD 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 134 YVPETVY------------RVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFG-----ICHRDIKPQNLLLDPDTAVl 196
Cdd:cd08217    71 RANTTLYivmeyceggdlaQLIKKCKKENQYIPEEFIWKIFTQLLLALYECHNRSvgggkILHRDLKPANIFLDSDNNV- 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1231802383 197 KLCDFGSAKQLvrGEPNV---SYICSRYYRAPELIFGATdYTSSIDVWSAGCVLAELLLGQPIFPGdSGVDQLVEIIK 271
Cdd:cd08217   150 KLGDFGLARVL--SHDSSfakTYVGTPYYMSPELLNEQS-YDEKSDIWSLGCLIYELCALHPPFQA-ANQLELAKKIK 223
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
56-339 4.04e-26

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: 105.76  E-value: 4.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAkLCDSGELVAIKKV-LQDKR------FKNrELQIMRKLDHC-NIVRLryFFYSSGEKKDEVY 127
Cdd:cd14131     3 YEILKQLGKGGSSKVYKV-LNPKKKIYALKRVdLEGADeqtlqsYKN-EIELLKKLKGSdRIIQL--YDYEVTDEDDYLY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 128 LnlVLDYVPETVYRVARhySRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLdpdtaV---LKLCDFGSA 204
Cdd:cd14131    79 M--VMECGEIDLATILK--KKRPKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLL-----VkgrLKLIDFGIA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 205 KQLVRGEPNV---SYICSRYYRAPELIFGaTDYTSSI----------DVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIk 271
Cdd:cd14131   150 KAIQNDTTSIvrdSQVGTLNYMSPEAIKD-TSASGEGkpkskigrpsDVWSLGCILYQMVYGKTPFQHITNPIAKLQAI- 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1231802383 272 vlgtptreqireMNPNYtEFKFPQIkahpwtkvfrprTPPEAIALCSRLLEYTPTARLTPLEACAHSF 339
Cdd:cd14131   228 ------------IDPNH-EIEFPDI------------PNPDLIDVMKRCLQRDPKKRPSIPELLNHPF 270
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
56-301 4.07e-26

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: 105.17  E-value: 4.07e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKV----LQDKRFKN--RELQIMRKLDHCNIVRLryffYSSGEKKDEVYLn 129
Cdd:cd14071     2 YDIERTIGKGNFAVVKLARHRITKTEVAIKIIdksqLDEENLKKiyREVQIMKMLNHPHIIKL----YQVMETKDMLYL- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 lVLDYVP--ETVYRVARH----YSRAKQTLpviyvklymYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGS 203
Cdd:cd14071    77 -VTEYASngEIFDYLAQHgrmsEKEARKKF---------WQILSAVEYCHKRHIVHRDLKAENLLLDANMNI-KIADFGF 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 204 AKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSgVDQLVEiiKVLGTPTR----- 278
Cdd:cd14071   146 SNFFKPGELLKTWCGSPPYAAPEVFEGKEYEGPQLDIWSLGVVLYVLVCGALPFDGST-LQTLRD--RVLSGRFRipffm 222
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1231802383 279 ----EQ-IREM---NPNyTEFKFPQIKAHPW 301
Cdd:cd14071   223 stdcEHlIRRMlvlDPS-KRLTIEQIKKHKW 252
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
71-340 5.77e-26

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: 105.51  E-value: 5.77e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  71 YQAKLCD-SGELVAIKKVLQDKRFKNRELQIMRKLD-HCNIVRLRYFFYSSgekkdeVYLNLVL---------DYVPETV 139
Cdd:cd14093    31 FAVKIIDiTGEKSSENEAEELREATRREIEILRQVSgHPNIIELHDVFESP------TFIFLVFelcrkgelfDYLTEVV 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 140 yRVARhysraKQTlpviyvKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLVRGEpNVSYIC- 218
Cdd:cd14093   105 -TLSE-----KKT------RRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNV-KISDFGFATRLDEGE-KLRELCg 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 219 SRYYRAPELI-----FGATDYTSSIDVWSAGCVLAELLLGQPIFpgdsgvdqlveiikvlgtPTREQI----REMNPNYt 289
Cdd:cd14093   171 TPGYLAPEVLkcsmyDNAPGYGKEVDMWACGVIMYTLLAGCPPF------------------WHRKQMvmlrNIMEGKY- 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1231802383 290 EFKFPQikahpWTKVfrPRTPPEAIalcSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd14093   232 EFGSPE-----WDDI--SDTAKDLI---SKLLVVDPKKRLTAEEALEHPFF 272
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
60-337 5.79e-26

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: 105.04  E-value: 5.79e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFK-------NRELQIMRKLDHCNIVRLRYFFYssgekkDEVYLNLVL 132
Cdd:cd14116    11 RPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKagvehqlRREVEIQSHLRHPNILRLYGYFH------DATRVYLIL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 DYVPE-TVYRVARHYSRAKQTLPVIYVKlymyQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKLCDFG------SAK 205
Cdd:cd14116    85 EYAPLgTVYRELQKLSKFDEQRTATYIT----ELANALSYCHSKRVIHRDIKPENLLLGSA-GELKIADFGwsvhapSSR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 206 QlvrgepnvSYICSRY-YRAPELIFGATdYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVlgtptreqirem 284
Cdd:cd14116   160 R--------TTLCGTLdYLPPEMIEGRM-HDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRV------------ 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1231802383 285 npnytEFKFPqikahpwtkvfrPRTPPEAIALCSRLLEYTPTARLTPLEACAH 337
Cdd:cd14116   219 -----EFTFP------------DFVTEGARDLISRLLKHNPSQRPMLREVLEH 254
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
56-337 9.37e-26

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: 104.39  E-value: 9.37e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDK--------RFKnRELQIMRKLDHCNIVRLRYFFyssgEKKDEVY 127
Cdd:cd14073     3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKiedeqdmvRIR-REIEIMSSLNHPHIIRIYEVF----ENKDKIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 128 LnlVLDYVPE-TVYrvarHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQ 206
Cdd:cd14073    78 I--VMEYASGgELY----DYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNA-KIADFGLSNL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 207 LVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSgvdqlveiIKVLgtptREQIREmnp 286
Cdd:cd14073   151 YSKDKLLQTFCGSPLYASPEIVNGTPYQGPEVDCWSLGVLLYTLVYGTMPFDGSD--------FKRL----VKQISS--- 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1231802383 287 nytefkfpqikahpwTKVFRPRTPPEAIALCSRLLEYTPTARLTPLEACAH 337
Cdd:cd14073   216 ---------------GDYREPTQPSDASGLIRWMLTVNPKRRATIEDIANH 251
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
62-339 1.13e-25

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: 105.20  E-value: 1.13e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQA-KLCDSGELVAikKVLQDKRFKNRELQ-------IMRKLDHCNIVRLRYFFyssgekKDEVYLNLVLD 133
Cdd:cd14086     9 LGKGAFSVVRRCvQKSTGQEFAA--KIINTKKLSARDHQklerearICRLLKHPNIVRLHDSI------SEEGFHYLVFD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 134 YVP-----ETVyrVAR-HYSRAKQTLpviyvklYMYQLFRSLAYIHSFGICHRDIKPQNLLL---DPDTAVlKLCDFGSA 204
Cdd:cd14086    81 LVTggelfEDI--VAReFYSEADASH-------CIQQILESVNHCHQNGIVHRDLKPENLLLaskSKGAAV-KLADFGLA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 205 KQLVRGEPNVSYICSRY-YRAPELIfGATDYTSSIDVWSAGCVLAELLLGQPIFpGDSGVDQLVEIIKVlgtptreqire 283
Cdd:cd14086   151 IEVQGDQQAWFGFAGTPgYLSPEVL-RKDPYGKPVDIWACGVILYILLVGYPPF-WDEDQHRLYAQIKA----------- 217
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1231802383 284 mnpnyTEFKFPqikAHPWTKVfrprtPPEAIALCSRLLEYTPTARLTPLEACAHSF 339
Cdd:cd14086   218 -----GAYDYP---SPEWDTV-----TPEAKDLINQMLTVNPAKRITAAEALKHPW 260
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
60-340 1.25e-25

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: 105.56  E-value: 1.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLC---DSGELVAIKkVLQDKRFKNR-------ELQIMRKLDHCNIVRLRYFFYSSGEkkdevyLN 129
Cdd:cd05582     1 KVLGQGSFGKVFLVRKItgpDAGTLYAMK-VLKKATLKVRdrvrtkmERDILADVNHPFIVKLHYAFQTEGK------LY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 LVLDYVP--ETVYRVARHYSRAKQTlpviyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQL 207
Cdd:cd05582    74 LILDFLRggDLFTRLSKEVMFTEED-----VKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHI-KLTDFGLSKES 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 208 VRGEPNVSYIC-SRYYRAPELIfGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKV-LGTP---TREQ-- 280
Cdd:cd05582   148 IDHEKKAYSFCgTVEYMAPEVV-NRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAkLGMPqflSPEAqs 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 281 -IREM---NPN----YTEFKFPQIKAHP------WTKVFRPRTPPEAIALCSRL-------LEYTP-TARLT---PLEAC 335
Cdd:cd05582   227 lLRALfkrNPAnrlgAGPDGVEEIKRHPffatidWNKLYRKEIKPPFKPAVSRPddtfyfdPEFTSrTPKDSpgvPPSAN 306

                  ....*
gi 1231802383 336 AHSFF 340
Cdd:cd05582   307 AHQLF 311
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
62-272 1.44e-25

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: 103.50  E-value: 1.44e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVA---IKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFyssgekKDEVYLNLVLDYV--P 136
Cdd:cd14006     1 LGRGRFGVVKRCIEKATGREFAakfIPKRDKKKEAVLREISILNQLQHPRIIQLHEAY------ESPTELVLILELCsgG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 137 ETVYRVARHYSRAKQTlpviyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAV-LKLCDFGSAKQLVRGEPNVS 215
Cdd:cd14006    75 ELLDRLAERGSLSEEE-----VRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPSPqIKIIDFGLARKLNPGEELKE 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1231802383 216 YICSRYYRAPELI-----FGATdytssiDVWSAGcVLAELLL-GQPIFPGDSGVDQLVEIIKV 272
Cdd:cd14006   150 IFGTPEFVAPEIVngepvSLAT------DMWSIG-VLTYVLLsGLSPFLGEDDQETLANISAC 205
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
56-301 1.89e-25

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: 103.50  E-value: 1.89e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKkVLQDKRFKN--------RELQIMRKLDHCNIVRLryffYSSGEKKDEVY 127
Cdd:cd14079     4 YILGKTLGVGSFGKVKLAEHELTGHKVAVK-ILNRQKIKSldmeekirREIQILKLFRHPHIIRL----YEVIETPTDIF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 128 LnlVLDYVP--ETV-YRVARHYSRAKQTlpviyvKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSA 204
Cdd:cd14079    79 M--VMEYVSggELFdYIVQKGRLSEDEA------RRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNV-KIADFGLS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 205 KQLVRGE--------PNvsyicsryYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFpGDSGVDQLVEIIKV---- 272
Cdd:cd14079   150 NIMRDGEflktscgsPN--------YAAPEVISGKLYAGPEVDVWSCGVILYALLCGSLPF-DDEHIPNLFKKIKSgiyt 220
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1231802383 273 ----LGTPTREQIREM---NPnYTEFKFPQIKAHPW 301
Cdd:cd14079   221 ipshLSPGARDLIKRMlvvDP-LKRITIPEIRQHPW 255
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
62-350 4.19e-25

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: 102.99  E-value: 4.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKvLQDKRFKNR--------ELQIMRKLDHCNIVRLRYFFyssgEKKDEVYLNLVLD 133
Cdd:cd05577     1 LGRGGFGEVCACQVKATGKMYACKK-LDKKRIKKKkgetmalnEKIILEKVSSPFIVSLAYAF----ETKDKLCLVLTLM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 134 YVPETVYRVARHYSRAKQTLPVIYvklYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLVRGEPN 213
Cdd:cd05577    76 NGGDLKYHIYNVGTRGFSEARAIF---YAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHV-RISDLGLAVEFKGGKKI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 214 VSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFpgdsgvDQLVEIIKvlgtptREQIREMNPNyTEFKF 293
Cdd:cd05577   152 KGRVGTHGYMAPEVLQKEVAYDFSVDWFALGCMLYEMIAGRSPF------RQRKEKVD------KEELKRRTLE-MAVEY 218
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 294 PQikahpwtkvfrpRTPPEAIALCSRLLEYTPTARLTPLEACA-----HSFFDELRDPNVKL 350
Cdd:cd05577   219 PD------------SFSPEARSLCEGLLQKDPERRLGCRGGSAdevkeHPFFRSLNWQRLEA 268
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
60-259 4.84e-25

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: 102.62  E-value: 4.84e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKL---CDSGELVAIKKVLQDKRFKNR-----ELQIMRKLDHCNIVRLryffYSSGEKKDEVYlnLV 131
Cdd:cd00192     1 KKLGEGAFGEVYKGKLkggDGKTVDVAVKTLKEDASESERkdflkEARVMKKLGHPNVVRL----LGVCTEEEPLY--LV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 132 LDYVPE----TVYRVARHYSRA--KQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKLCDFGSAK 205
Cdd:cd00192    75 MEYMEGgdllDFLRKSRPVFPSpePSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGED-LVVKISDFGLSR 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1231802383 206 QLVRGEpnvsyicsrYYR------------APELIFGATdYTSSIDVWSAGCVLAELL-LGQPIFPG 259
Cdd:cd00192   154 DIYDDD---------YYRkktggklpirwmAPESLKDGI-FTSKSDVWSFGVLLWEIFtLGATPYPG 210
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
56-291 5.32e-25

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: 102.94  E-value: 5.32e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN-----RELQIMRKLDHC---NIVRlryfFYSSGEKKDEVY 127
Cdd:cd06917     3 YRRLELVGRGSYGAVYRGYHVKTGRVVALKVLNLDTDDDDvsdiqKEVALLSQLKLGqpkNIIK----YYGSYLKGPSLW 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 128 LnlVLDYVPETVYRVarhYSRAkQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQL 207
Cdd:cd06917    79 I--IMDYCEGGSIRT---LMRA-GPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVT-NTGNVKLCDFGVAASL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 208 VRGEPNVS-YICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFpgdSGVDQLVEIIKVLGT-PTREQIREMN 285
Cdd:cd06917   152 NQNSSKRStFVGTPYWMAPEVITEGKYYDTKADIWSLGITTYEMATGNPPY---SDVDALRAVMLIPKSkPPRLEGNGYS 228

                  ....*.
gi 1231802383 286 PNYTEF 291
Cdd:cd06917   229 PLLKEF 234
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
62-255 5.38e-25

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: 102.38  E-value: 5.38e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKV-LQDK---RFKNRELQIMRKLDHCNIVRlryfFYSSGEKKDevYLNLVLDYVP- 136
Cdd:cd06613     8 IGSGTYGDVYKARNIATGELAAVKVIkLEPGddfEIIQQEISMLKECRHPNIVA----YFGSYLRRD--KLWIVMEYCGg 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 137 ---ETVYRVARHYSRakqtlPVI-YVklyMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLVR--G 210
Cdd:cd06613    82 gslQDIYQVTGPLSE-----LQIaYV---CRETLKGLAYLHSTGKIHRDIKGANILLTEDGDV-KLADFGVSAQLTAtiA 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1231802383 211 EPNvSYICSRYYRAPELIFGA--TDYTSSIDVWSAGCVLAELLLGQP 255
Cdd:cd06613   153 KRK-SFIGTPYWMAPEVAAVErkGGYDGKCDIWALGITAIELAELQP 198
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
61-257 5.49e-25

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: 102.77  E-value: 5.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  61 VIGNGSFGVVYQAKLCDSGELVAIK--KVLQDKRFK-NRELQIMRKL-DHCNIVRLRYFFYSSGEKKDEVYLNLVLDYVP 136
Cdd:cd06608    13 VIGEGTYGKVYKARHKKTGQLAAIKimDIIEDEEEEiKLEINILRKFsNHPNIATFYGAFIKKDPPGGDDQLWLVMEYCG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 137 E-TVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQL--VRGEPN 213
Cdd:cd06608    93 GgSVTDLVKGLRKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEV-KLVDFGVSAQLdsTLGRRN 171
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1231802383 214 vSYICSRYYRAPELI----FGATDYTSSIDVWSAGCVLAELLLGQPIF 257
Cdd:cd06608   172 -TFIGTPYWMAPEVIacdqQPDASYDARCDVWSLGITAIELADGKPPL 218
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
62-258 5.56e-25

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: 102.91  E-value: 5.56e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKK--VLQDKRFKNR-----ELQIMRKLDHCNIVRLRyffyssgEKKDEVYLN----- 129
Cdd:cd13989     1 LGSGGFGYVTLWKHQDTGEYVAIKKcrQELSPSDKNRerwclEVQIMKKLNHPNVVSAR-------DVPPELEKLspndl 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 --LVLDYVPETVYRvaRHYSRAKQT--LPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDP--DTAVLKLCDFGS 203
Cdd:cd13989    74 plLAMEYCSGGDLR--KVLNQPENCcgLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQggGRVIYKLIDLGY 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1231802383 204 AKQLVRGEPNVSYICSRYYRAPELiFGATDYTSSIDVWSAGCVLAELLLG-QPIFP 258
Cdd:cd13989   152 AKELDQGSLCTSFVGTLQYLAPEL-FESKKYTCTVDYWSFGTLAFECITGyRPFLP 206
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
58-246 7.99e-25

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: 101.97  E-value: 7.99e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  58 DTKVIGNGSFG-VVYQAKLcdSGELVAIKKVLQD-KRFKNRELQIMRKLD-HCNIVRlrYFfyssGEKKDEVYLNLVLDY 134
Cdd:cd13982     5 SPKVLGYGSEGtIVFRGTF--DGRPVAVKRLLPEfFDFADREVQLLRESDeHPNVIR--YF----CTEKDRQFLYIALEL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 135 VPETVYRVARHYSRAKQTL-PVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAV----LKLCDFGSAKQLVR 209
Cdd:cd13982    77 CAASLQDLVESPRESKLFLrPGLEPVRLLRQIASGLAHLHSLNIVHRDLKPQNILISTPNAHgnvrAMISDFGLCKKLDV 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1231802383 210 GEPnvSYIC------SRYYRAPELIFGATDY--TSSIDVWSAGCV 246
Cdd:cd13982   157 GRS--SFSRrsgvagTSGWIAPEMLSGSTKRrqTRAVDIFSLGCV 199
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
60-255 8.25e-25

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: 102.12  E-value: 8.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN----------RELQIMRKLDHCNIVRLRyffyssGEKKDEVYLN 129
Cdd:cd06630     6 PLLGTGAFSSCYQARDVKTGTLMAVKQVSFCRNSSSeqeevveairEEIRMMARLNHPNIVRML------GATQHKSHFN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 LVLDYVPE-TVYRVARHYSRAKQTLpviyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSAKQLV 208
Cdd:cd06630    80 IFVEWMAGgSVASLLSKYGAFSENV----IINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGQRLRIADFGAAARLA 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 209 R-----GEPNVSYICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQP 255
Cdd:cd06630   156 SkgtgaGEFQGQLLGTIAFMAPEVLRG-EQYGRSCDVWSVGCVIIEMATAKP 206
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
60-321 1.01e-24

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: 103.08  E-value: 1.01e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKVLQ-DKRFKNR------ELQIMRKLDHCNIVRLRYFFyssgekKDEVYLNLVL 132
Cdd:cd05599     7 KVIGRGAFGEVRLVRKKDTGHVYAMKKLRKsEMLEKEQvahvraERDILAEADNPWVVKLYYSF------QDEENLYLIM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 DYVP--ETVYRVARhysraKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLVRG 210
Cdd:cd05599    81 EFLPggDMMTLLMK-----KDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHI-KLSDFGLCTGLKKS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 211 EPNVSYICSRYYRAPElIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIkvlgtptreqiremnpNYTE 290
Cdd:cd05599   155 HLAYSTVGTPDYIAPE-VFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIM----------------NWRE 217
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1231802383 291 -FKFPQikahpwtkvfRPRTPPEAIALCSRLL 321
Cdd:cd05599   218 tLVFPP----------EVPISPEAKDLIERLL 239
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
56-301 1.12e-24

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: 102.51  E-value: 1.12e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQA-KLCDSGELVAIKKV---------LQDKRFKN--RELQIMRKLDHCNIVRLRYFFYSsgekk 123
Cdd:cd14096     3 YRLINKIGEGAFSNVYKAvPLRNTGKPVAIKVVrkadlssdnLKGSSRANilKEVQIMKRLSHPNIVKLLDFQES----- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 124 dEVYLNLVLDYVP--ETVYRVARH-YSRAKQTLPVIYvklymyQLFRSLAYIHSFGICHRDIKPQNLLL----------- 189
Cdd:cd14096    78 -DEYYYIVLELADggEIFHQIVRLtYFSEDLSRHVIT------QVASAVKYLHEIGVVHRDIKPENLLFepipfipsivk 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 190 -----DPDTAV----------------LKLCDFGSAKQLvrGEPNVSYICSRY-YRAPElIFGATDYTSSIDVWSAGCVL 247
Cdd:cd14096   151 lrkadDDETKVdegefipgvggggigiVKLADFGLSKQV--WDSNTKTPCGTVgYTAPE-VVKDERYSKKVDMWALGCVL 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1231802383 248 AELLLGQPIFPGDSgVDQLVEIIK----VLGTPTREQIR-----------EMNPNyTEFKFPQIKAHPW 301
Cdd:cd14096   228 YTLLCGFPPFYDES-IETLTEKISrgdyTFLSPWWDEISksakdlishllTVDPA-KRYDIDEFLAHPW 294
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
60-263 1.76e-24

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 104.88  E-value: 1.76e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKlcDS--GELVAIKkVLQD---------KRFKnRELQIMRKLDHCNIVRLryffYSSGEKKDEVYL 128
Cdd:NF033483   13 ERIGRGGMAEVYLAK--DTrlDRDVAVK-VLRPdlardpefvARFR-REAQSAASLSHPNIVSV----YDVGEDGGIPYI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 129 nlVLDYVP-ETVyrvaRHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQL 207
Cdd:NF033483   85 --VMEYVDgRTL----KDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRV-KVTDFGIARAL 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1231802383 208 vrGEPNVSY----ICSRYYRAPELIFGAT-DYTSsiDVWSAGCVLAELLLGQPIFPGDSGV 263
Cdd:NF033483  158 --SSTTMTQtnsvLGTVHYLSPEQARGGTvDARS--DIYSLGIVLYEMLTGRPPFDGDSPV 214
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
57-367 2.53e-24

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: 101.61  E-value: 2.53e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  57 TDTKVIGNGSFGVVYQAKLCDSGELVAIKKVlqDKRFK-NRELQIMRKLD-HCNIVRLRYFFYssgekkDEVYLNLVLDY 134
Cdd:cd14092     9 LREEALGDGSFSVCRKCVHKKTGQEFAVKIV--SRRLDtSREVQLLRLCQgHPNIVKLHEVFQ------DELHTYLVMEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 135 VP--ETVYRVARHYSRAKQTLPVIyvklyMYQLFRSLAYIHSFGICHRDIKPQNLLL--DPDTAVLKLCDFGSAKQLVRG 210
Cdd:cd14092    81 LRggELLERIRKKKRFTESEASRI-----MRQLVSAVSFMHSKGVVHRDLKPENLLFtdEDDDAEIKIVDFGFARLKPEN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 211 EPNVSYICSRYYRAPELIFGATD---YTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKvlgtptreQIREmnpn 287
Cdd:cd14092   156 QPLKTPCFTLPYAAPEVLKQALStqgYDESCDLWSLGVILYTMLSGQVPFQSPSRNESAAEIMK--------RIKS---- 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 288 yTEFKFpqiKAHPWTKVfrprtPPEAIALCSRLLEYTPTARLTPLEACAHSFFDE--------LRDPNVKLPNGRDTPAL 359
Cdd:cd14092   224 -GDFSF---DGEEWKNV-----SSEAKSLIQGLLTVDPSKRLTMSELRNHPWLQGssspsstpLMTPGVLSSSAAAVSTA 294

                  ....*...
gi 1231802383 360 FNfTTQDA 367
Cdd:cd14092   295 LR-ATFDA 301
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
55-257 2.58e-24

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: 100.87  E-value: 2.58e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  55 SYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVL-----QDKRFKNrELQIMRKL-DHCNIVRLRYFFYSSGEKKDEVYL 128
Cdd:cd13985     1 RYQVTKQLGEGGFSYVYLAHDVNTGRRYALKRMYfndeeQLRVAIK-EIEIMKRLcGHPNIVQYYDSAILSSEGRKEVLL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 129 nlVLDYVPETVYRVARhySRAKQTLPVIYVKLYMYQLFRSLAYIHSFG--ICHRDIKPQNLLLDpDTAVLKLCDFGSA-- 204
Cdd:cd13985    80 --LMEYCPGSLVDILE--KSPPSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFS-NTGRFKLCDFGSAtt 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1231802383 205 --KQLVRGEpNVSYICS---RY----YRAPELI--FGATDYTSSIDVWSAGCVLAELLLGQPIF 257
Cdd:cd13985   155 ehYPLERAE-EVNIIEEeiqKNttpmYRAPEMIdlYSKKPIGEKADIWALGCLLYKLCFFKLPF 217
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
62-271 3.86e-24

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: 99.79  E-value: 3.86e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKV-LQDKRFKNR-----ELQIMRKLDHCNIVRlryfFYSSGEKKDEvyLNLVLDYV 135
Cdd:cd08529     8 LGKGSFGVVYKVVRKVDGRVYALKQIdISRMSRKMReeaidEARVLSKLNSPYVIK----YYDSFVDKGK--LNIVMEYA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 136 PE-TVYRVARhySRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQL------- 207
Cdd:cd08529    82 ENgDLHSLIK--SQRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNV-KIGDLGVAKILsdttnfa 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1231802383 208 --VRGEPnvsyicsrYYRAPELIFGATdYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIK 271
Cdd:cd08529   159 qtIVGTP--------YYLSPELCEDKP-YNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVR 215
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
60-337 3.97e-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: 100.18  E-value: 3.97e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKV-------LQDKRFKNrELQIMRKLDHCNIVRLRYFFyssgEKKDEVY----- 127
Cdd:cd14082     9 EVLGSGQFGIVYGGKHRKTGRDVAIKVIdklrfptKQESQLRN-EVAILQQLSHPGVVNLECMF----ETPERVFvvmek 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 128 -----LNLVLdyvpetvyrvarhySRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAV--LKLCD 200
Cdd:cd14082    84 lhgdmLEMIL--------------SSEKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPFpqVKLCD 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 201 FGSAKQLVRGEPNVSYICSRYYRAPElIFGATDYTSSIDVWSAGCVLAELLLGQpiFPGDSGVDqlveiikvlgtpTREQ 280
Cdd:cd14082   150 FGFARIIGEKSFRRSVVGTPAYLAPE-VLRNKGYNRSLDMWSVGVIIYVSLSGT--FPFNEDED------------INDQ 214
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1231802383 281 IREmnpnyTEFKFPqikAHPWTKVfrprtPPEAIALCSRLLEYTPTARLTPLEACAH 337
Cdd:cd14082   215 IQN-----AAFMYP---PNPWKEI-----SPDAIDLINNLLQVKMRKRYSVDKSLSH 258
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
49-348 4.13e-24

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: 101.27  E-value: 4.13e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  49 DRPQEVsYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN-------RELQIMRKLDHCNIVRlryffYSSGE 121
Cdd:cd06633    17 DDPEEI-FVDLHEIGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNekwqdiiKEVKFLQQLKHPNTIE-----YKGCY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 122 KKDEVYLnLVLDYVPETVYRVARHYSRAKQTLPVIYVklyMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDF 201
Cdd:cd06633    91 LKDHTAW-LVMEYCLGSASDLLEVHKKPLQEVEIAAI---THGALQGLAYLHSHNMIHRDIKAGNILLT-EPGQVKLADF 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 202 GSAKqlvRGEPNVSYICSRYYRAPELIFGATD--YTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIikvlgtptre 279
Cdd:cd06633   166 GSAS---IASPANSFVGTPYWMAPEVILAMDEgqYDGKVDIWSLGITCIELAERKPPLFNMNAMSALYHI---------- 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1231802383 280 qiremnpnyTEFKFPQIKAHPWTKVFRprtppeaiALCSRLLEYTPTARLTPLEACAHSFFDELRDPNV 348
Cdd:cd06633   233 ---------AQNDSPTLQSNEWTDSFR--------GFVDYCLQKIPQERPSSAELLRHDFVRRERPPRV 284
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
54-255 6.90e-24

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: 99.43  E-value: 6.90e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  54 VSYTDTKVIGNGSFGVVYqAKLCDSGELVAIKKVLQDKRFKNR----------ELQIMRKLDHCNIVRlrYFfyssGEKK 123
Cdd:cd06631     1 IQWKKGNVLGKGAYGTVY-CGLTSTGQLIAVKQVELDTSDKEKaekeyeklqeEVDLLKTLKHVNIVG--YL----GTCL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 124 DEVYLNLVLDYVPE-TVYRVARHYSrakqTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPdTAVLKLCDFG 202
Cdd:cd06631    74 EDNVVSIFMEFVPGgSIASILARFG----ALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMP-NGVIKLIDFG 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1231802383 203 SAKQL---------------VRGEPnvsyicsrYYRAPELIfGATDYTSSIDVWSAGCVLAELLLGQP 255
Cdd:cd06631   149 CAKRLcinlssgsqsqllksMRGTP--------YWMAPEVI-NETGHGRKSDIWSIGCTVFEMATGKP 207
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
56-289 8.74e-24

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: 98.88  E-value: 8.74e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKV------LQDKRFKNRELQIMRKLDHCNIVRlryfFYSSGEKKDEVYLn 129
Cdd:cd08225     2 YEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIdltkmpVKEKEASKKEVILLAKMKHPNIVT----FFASFQENGRLFI- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 lVLDYVP--ETVYRVARHYS---RAKQTLPviyvklYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSA 204
Cdd:cd08225    77 -VMEYCDggDLMKRINRQRGvlfSEDQILS------WFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVAKLGDFGIA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 205 KQLvRGEPNVSYIC--SRYYRAPElIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSgVDQLVeiIKVlgtpTREQIR 282
Cdd:cd08225   150 RQL-NDSMELAYTCvgTPYYLSPE-ICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNN-LHQLV--LKI----CQGYFA 220

                  ....*..
gi 1231802383 283 EMNPNYT 289
Cdd:cd08225   221 PISPNFS 227
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
61-260 8.75e-24

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: 99.38  E-value: 8.75e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  61 VIGNGSFGVVYQAKLCdsGELVAIKKVlqDKRFKNR--------ELQIMRkLDHCNIVRLryFFYSSGEKKDEvyLNLVL 132
Cdd:cd13979    10 PLGSGGFGSVYKATYK--GETVAVKIV--RRRRKNRasrqsfwaELNAAR-LRHENIVRV--LAAETGTDFAS--LGLII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 DYVPETVYRVARHYSRAKQtLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKLCDFGSAKQLvrGEP 212
Cdd:cd13979    81 MEYCGNGTLQQLIYEGSEP-LPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQ-GVCKLCDFGCSVKL--GEG 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1231802383 213 NV-----SYICSRY-YRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIFPGD 260
Cdd:cd13979   157 NEvgtprSHIGGTYtYRAPELLKG-ERVTPKADIYSFGITLWQMLTRELPYAGL 209
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
62-257 1.69e-23

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: 98.21  E-value: 1.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGEL-VAIK-----KVLQDKRFKNRELQIMRKLDHCNIVRLryffYSSGEKKDEVYLnlVLDYV 135
Cdd:cd14120     1 IGHGAFAVVFKGRHRKKPDLpVAIKcitkkNLSKSQNLLGKEIKILKELSHENVVAL----LDCQETSSSVYL--VMEYC 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 136 PetvYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLL--------DPDTAVLKLCDFGSAKQL 207
Cdd:cd14120    75 N---GGDLADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLshnsgrkpSPNDIRLKIADFGFARFL 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1231802383 208 VRGEPNVSYICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIF 257
Cdd:cd14120   152 QDGMMAATLCGSPMYMAPEVIMS-LQYDAKADLWSIGTIVYQCLTGKAPF 200
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
60-352 1.75e-23

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: 99.65  E-value: 1.75e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKkVLQDKRFKNRELQ---------IMRKLDHCNIVRLRYFFYSSgekkDEVYLnl 130
Cdd:cd05604     2 KVIGKGSFGKVLLAKRKRDGKYYAVK-VLQKKVILNRKEQkhimaernvLLKNVKHPFLVGLHYSFQTT----DKLYF-- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 VLDYVP--ETVYRVARhysraKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLkLCDFGSAKQLV 208
Cdd:cd05604    75 VLDFVNggELFFHLQR-----ERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIV-LTDFGLCKEGI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 209 RGEPNVSYIC-SRYYRAPELIFgATDYTSSIDVWSAGCVLAELLLGQPIFpgdsgvdqlveiikvlgtpTREQIREMNPN 287
Cdd:cd05604   149 SNSDTTTTFCgTPEYLAPEVIR-KQPYDNTVDWWCLGSVLYEMLYGLPPF-------------------YCRDTAEMYEN 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 288 ytefkfpqIKAHPWTkvFRPRTPPEAIALCSRLLEYTPTARLTP----LEACAHSFFDELR-------------DPNVKL 350
Cdd:cd05604   209 --------ILHKPLV--LRPGISLTAWSILEELLEKDRQLRLGAkedfLEIKNHPFFESINwtdlvqkkipppfNPNVNG 278

                  ..
gi 1231802383 351 PN 352
Cdd:cd05604   279 PD 280
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
60-251 1.77e-23

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: 98.79  E-value: 1.77e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRElQIMR------KLDHCNIVRlryFFYSSGE--------KKDE 125
Cdd:cd14048    12 QCLGRGGFGVVFEAKNKVDDCNYAVKRIRLPNNELARE-KVLRevralaKLDHPGIVR---YFNAWLErppegwqeKMDE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 126 VYLNLVLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKLCDFGSAK 205
Cdd:cd14048    88 VYLYIQMQLCRKENLKDWMNRRCTMESRELFVCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLD-DVVKVGDFGLVT 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1231802383 206 QLVRGEPNVSY-------------ICSRYYRAPELIFGATdYTSSIDVWSAGCVLAELL 251
Cdd:cd14048   167 AMDQGEPEQTVltpmpayakhtgqVGTRLYMSPEQIHGNQ-YSEKVDIFALGLILFELI 224
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
48-340 2.18e-23

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: 97.90  E-value: 2.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  48 PDRPQEvSYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVlqDKRFKNR------ELQIMRKLDHCNIVRlryfFYSSGE 121
Cdd:cd06648     2 PGDPRS-DLDNFVKIGEGSTGIVCIATDKSTGRQVAVKKM--DLRKQQRrellfnEVVIMRDYQHPNIVE----MYSSYL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 122 KKDEVYLnlVLDYVPE-TVYRVARHYSRAKQTLPVIYVklymyQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCD 200
Cdd:cd06648    75 VGDELWV--VMEFLEGgALTDIVTHTRMNEEQIATVCR-----AVLKALSFLHSQGVIHRDIKSDSILLTSDGRV-KLSD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 201 FGSAKQLVRGEPN-VSYICSRYYRAPELIfGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLveiikvlgtptrE 279
Cdd:cd06648   147 FGFCAQVSKEVPRrKSLVGTPYWMAPEVI-SRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAM------------K 213
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1231802383 280 QIREMNPnytefkfPQIKAHpwtkvfrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd06648   214 RIRDNEP-------PKLKNL-------HKVSPRLRSFLDRMLVRDPAQRATAAELLNHPFL 260
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
62-311 2.57e-23

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: 98.01  E-value: 2.57e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN-------RELQIMRKLDHCNIVRLRYFFYssgekkDEVYLNLVLDY 134
Cdd:cd14117    14 LGKGKFGNVYLAREKQSKFIVALKVLFKSQIEKEgvehqlrREIEIQSHLRHPNILRLYNYFH------DRKRIYLILEY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 135 VPE-TVYRVARHYSRAKQTlpviYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPdTAVLKLCDFG---SAKQLVRg 210
Cdd:cd14117    88 APRgELYKELQKHGRFDEQ----RTATFMEELADALHYCHEKKVIHRDIKPENLLMGY-KGELKIADFGwsvHAPSLRR- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 211 epnvSYICSRY-YRAPELIFGATdYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKV-------LGTPTREQIR 282
Cdd:cd14117   162 ----RTMCGTLdYLPPEMIEGRT-HDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVdlkfppfLSDGSRDLIS 236
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1231802383 283 EMNPNYTEFKFP--QIKAHPWTKVFRPRTPP 311
Cdd:cd14117   237 KLLRYHPSERLPlkGVMEHPWVKANSRRVLP 267
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
60-257 2.62e-23

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: 99.27  E-value: 2.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKkVLQDKRFKNRELQ---------IMRKLDHCNIVRLRYFFYSSgEKkdevyLNL 130
Cdd:cd05603     1 KVIGKGSFGKVLLAKRKCDGKFYAVK-VLQKKTILKKKEQnhimaernvLLKNLKHPFLVGLHYSFQTS-EK-----LYF 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 VLDYVP--ETVYrvarHYSRAKQTLPViYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLkLCDFGSAKQLV 208
Cdd:cd05603    74 VLDYVNggELFF----HLQRERCFLEP-RARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVV-LTDFGLCKEGM 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1231802383 209 RGEPNVSYIC-SRYYRAPElIFGATDYTSSIDVWSAGCVLAELLLGQPIF 257
Cdd:cd05603   148 EPEETTSTFCgTPEYLAPE-VLRKEPYDRTVDWWCLGAVLYEMLYGLPPF 196
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
62-290 2.78e-23

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: 97.45  E-value: 2.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKVL------QDKRFKNRELQIMRKL-DHCNIVRLryffYSSGEKKDEVYLNL---- 130
Cdd:cd13997     8 IGSGSFSEVFKVRSKVDGCLYAVKKSKkpfrgpKERARALREVEAHAALgQHPNIVRY----YSSWEEGGHLYIQMelce 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 --VLDYVPETVYRVARhysrakqtLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKLCDFGSAKQLV 208
Cdd:cd13997    84 ngSLQDALEELSPISK--------LSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNK-GTCKIGDFGLATRLE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 209 RGePNVSYICSRYYrAPELIFGATDYTSSIDVWSAGCVLAELLLGQ-----------------PIFPGDSGVDQLVEIIK 271
Cdd:cd13997   155 TS-GDVEEGDSRYL-APELLNENYTHLPKADIFSLGVTVYEAATGEplprngqqwqqlrqgklPLPPGLVLSQELTRLLK 232
                         250
                  ....*....|....*....
gi 1231802383 272 VLgtptreqireMNPNYTE 290
Cdd:cd13997   233 VM----------LDPDPTR 241
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
56-264 3.30e-23

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: 97.77  E-value: 3.30e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGEL-VAIK-----KVLQDKRFKNRELQIMRKLDHCNIVRLryffYSSGEKKDEVYLn 129
Cdd:cd14202     4 FSRKDLIGHGAFAVVFKGRHKEKHDLeVAVKcinkkNLAKSQTLLGKEIKILKELKHENIVAL----YDFQEIANSVYL- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 lVLDYVPETVYRvarHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLL--------DPDTAVLKLCDF 201
Cdd:cd14202    79 -VMEYCNGGDLA---DYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLsysggrksNPNNIRIKIADF 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1231802383 202 GSAKQLvRGEPNVSYIC-SRYYRAPELIFgATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVD 264
Cdd:cd14202   155 GFARYL-QNNMMAATLCgSPMYMAPEVIM-SQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQD 216
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
61-340 3.61e-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: 97.43  E-value: 3.61e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  61 VIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN-----RELQIMRKLDHCNIVRlryfFYSSGEKKDEVYLnlVLDYV 135
Cdd:cd06610     8 VIGSGATAVVYAAYCLPKKEKVAIKRIDLEKCQTSmdelrKEIQAMSQCNHPNVVS----YYTSFVVGDELWL--VMPLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 136 PE-TVYRVARH-YSRAKQTLPVIYVKLYmyQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLVRGEPN 213
Cdd:cd06610    82 SGgSLLDIMKSsYPRGGLDEAIIATVLK--EVLKGLEYLHSNGQIHRDVKAGNILLGEDGSV-KIADFGVSASLATGGDR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 214 VS-----YICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKvlGTPTREQIREMNPNY 288
Cdd:cd06610   159 TRkvrktFVGTPCWMAPEVMEQVRGYDFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLQ--NDPPSLETGADYKKY 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 289 tefkfpqikahpwTKVFRprtppEAIALCsrlLEYTPTARLTPLEACAHSFF 340
Cdd:cd06610   237 -------------SKSFR-----KMISLC---LQKDPSKRPTAEELLKHKFF 267
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
56-270 5.57e-23

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: 97.47  E-value: 5.57e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQ-------IMRKLDHCNIVRLRYFFyssgekKDEVYL 128
Cdd:cd14209     3 FDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKLKQVEhtlnekrILQAINFPFLVKLEYSF------KDNSNL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 129 NLVLDYVP--ETVyrvarHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQ 206
Cdd:cd14209    77 YMVMEYVPggEMF-----SHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLID-QQGYIKVTDFGFAKR 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1231802383 207 lVRGEpnVSYIC-SRYYRAPELIFgATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVdQLVEII 270
Cdd:cd14209   151 -VKGR--TWTLCgTPEYLAPEIIL-SKGYNKAVDWWALGVLIYEMAAGYPPFFADQPI-QIYEKI 210
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
55-257 5.99e-23

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: 96.53  E-value: 5.99e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  55 SYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNR-------ELQIMRKLDHCNIVRLRYFFyssgEKKDEVY 127
Cdd:cd14189     2 SYCKGRLLGKGGFARCYEMTDLATNKTYAVKVIPHSRVAKPHqrekivnEIELHRDLHHKHVVKFSHHF----EDAENIY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 128 LNLVLdyvpeTVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQL 207
Cdd:cd14189    78 IFLEL-----CSRKSLAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFIN-ENMELKVGDFGLAARL 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1231802383 208 VRGEPNVSYIC-SRYYRAPELIFGATDYTSSiDVWSAGCVLAELLLGQPIF 257
Cdd:cd14189   152 EPPEQRKKTICgTPNYLAPEVLLRQGHGPES-DVWSLGCVMYTLLCGNPPF 201
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
56-338 6.67e-23

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: 96.69  E-value: 6.67e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKV-LQDKRFKNR-----ELQIMRKLDHCNIVRLRYFFYssgekkDEVYLN 129
Cdd:cd08530     2 FKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVnLGSLSQKERedsvnEIRLLASVNHPNIIRYKEAFL------DGNRLC 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 LVLDYVPE-TVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLL-DPDtaVLKLCDFGSAKQL 207
Cdd:cd08530    76 IVMEYAPFgDLSKLISKRKKKRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLsAGD--LVKIGDLGISKVL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 208 VRGEPNvSYICSRYYRAPElIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVeiiKVLGTptreqiremnpn 287
Cdd:cd08530   154 KKNLAK-TQIGTPLYAAPE-VWKGRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQELRY---KVCRG------------ 216
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1231802383 288 ytefKFPQIKahpwtkvfrPRTPPEAIALCSRLLEYTPTARLTPLEACAHS 338
Cdd:cd08530   217 ----KFPPIP---------PVYSQDLQQIIRSLLQVNPKKRPSCDKLLQSP 254
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
62-251 6.94e-23

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: 96.35  E-value: 6.94e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLcdSGELVAIKKV--LQDKRFKNRELQIMRKLDHCNIVRLryffYSSGEKKDEVYLnlVLDYVPE-T 138
Cdd:cd14058     1 VGRGSFGVVCKARW--RNQIVAVKIIesESEKKAFEVEVRQLSRVDHPNIIKL----YGACSNQKPVCL--VMEYAEGgS 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 139 VYRVArHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFG---ICHRDIKPQNLLLDPDTAVLKLCDFGSAKQLVRGEPNVS 215
Cdd:cd14058    73 LYNVL-HGKEPKPIYTAAHAMSWALQCAKGVAYLHSMKpkaLIHRDLKPPNLLLTNGGTVLKICDFGTACDISTHMTNNK 151
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1231802383 216 yiCSRYYRAPElIFGATDYTSSIDVWSAGCVLAELL 251
Cdd:cd14058   152 --GSAAWMAPE-VFEGSKYSEKCDVFSWGIILWEVI 184
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
60-343 9.25e-23

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: 97.77  E-value: 9.25e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKV-------LQDKRFKNRELQIMRKLDHCNIVRLRYFFyssgekKDEVYLNLVL 132
Cdd:cd05601     7 NVIGRGHFGEVQVVKEKATGDIYAMKVLkksetlaQEEVSFFEEERDIMAKANSPWITKLQYAF------QDSENLYLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 DYVP--ETVYRVARHYSRAKQTLpviyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQLVR- 209
Cdd:cd05601    81 EYHPggDLLSLLSRYDDIFEESM----ARFYLAELVLAIHSLHSMGYVHRDIKPENILID-RTGHIKLADFGSAAKLSSd 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 210 ---------GEPNvsyicsryYRAPELI-----FGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIkvlgt 275
Cdd:cd05601   156 ktvtskmpvGTPD--------YIAPEVLtsmngGSKGTYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIM----- 222
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1231802383 276 ptreqiremnpNYTEF-KFPQikahpwtkvfRPRTPPEAIALCSRLLEyTPTARLTPLEACAHSFFDEL 343
Cdd:cd05601   223 -----------NFKKFlKFPE----------DPKVSESAVDLIKGLLT-DAKERLGYEGLCCHPFFSGI 269
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
55-290 9.31e-23

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: 95.96  E-value: 9.31e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  55 SYTDTKVIGNGSFG--VVYQAKLCDSgeLVAIKKV----LQDKRFKN--RELQIMRKLDHCNIVRLRYFFYssgekkDEV 126
Cdd:cd08221     1 HYIPVRVLGRGAFGeaVLYRKTEDNS--LVVWKEVnlsrLSEKERRDalNEIDILSLLNHDNIITYYNHFL------DGE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 127 YLNLVLDYVPE-TVYRVARHYSRakQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAK 205
Cdd:cd08221    73 SLFIEMEYCNGgNLHDKIAQQKN--QLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLT-KADLVKLGDFGISK 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 206 QL-VRGEPNVSYICSRYYRAPELIFGATdYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKvlgtptrEQIREM 284
Cdd:cd08221   150 VLdSESSMAESIVGTPYYMSPELVQGVK-YNFKSDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVQ-------GEYEDI 221

                  ....*.
gi 1231802383 285 NPNYTE 290
Cdd:cd08221   222 DEQYSE 227
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
60-337 1.75e-22

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: 95.43  E-value: 1.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIG---NGSFGVVYQAKlcdSGELVAIKkVLQDKRFKNRELQI-MRKLDHCNIVRLRYFFYSSGEKKDevYLNLVLDYV 135
Cdd:cd14089     7 QVLGlgiNGKVLECFHKK---TGEKFALK-VLRDNPKARREVELhWRASGCPHIVRIIDVYENTYQGRK--CLLVVMECM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 136 P--ETVYRVARHYSRA---KQTLPViyvklyMYQLFRSLAYIHSFGICHRDIKPQNLLL---DPDtAVLKLCDFGSAKQL 207
Cdd:cd14089    81 EggELFSRIQERADSAfteREAAEI------MRQIGSAVAHLHSMNIAHRDLKPENLLYsskGPN-AILKLTDFGFAKET 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 208 VRGEPNVSYICSRYYRAPElIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVdqlveiikVLGTPTREQIREmnpn 287
Cdd:cd14089   154 TTKKSLQTPCYTPYYVAPE-VLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGL--------AISPGMKKRIRN---- 220
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1231802383 288 yTEFKFPqikaHP-WTKVFRprtppEAIALCSRLLEYTPTARLTPLEACAH 337
Cdd:cd14089   221 -GQYEFP----NPeWSNVSE-----EAKDLIRGLLKTDPSERLTIEEVMNH 261
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
56-259 1.81e-22

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: 95.28  E-value: 1.81e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVlqDKRFKN--------RELQIMRKLDHCNIVRLryffYSSGEKKDEVY 127
Cdd:cd14072     2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKII--DKTQLNpsslqklfREVRIMKILNHPNIVKL----FEVIETEKTLY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 128 LNL-------VLDYVPeTVYRVARHYSRAKqtlpviyvklyMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCD 200
Cdd:cd14072    76 LVMeyasggeVFDYLV-AHGRMKEKEARAK-----------FRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNI-KIAD 142
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1231802383 201 FGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPG 259
Cdd:cd14072   143 FGFSNEFTPGNKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDG 201
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
60-343 2.09e-22

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: 96.51  E-value: 2.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKkVLQdkrfknRELQIMRKLDHCNIVRLRYF-----------FYSSGEKKDEVYL 128
Cdd:cd05570     1 KVLGKGSFGKVMLAERKKTDELYAIK-VLK------KEVIIEDDDVECTMTEKRVLalanrhpfltgLHACFQTEDRLYF 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 129 nlVLDYV---------------PEtvyRVARHYSrAKQTLpviyvklymyqlfrSLAYIHSFGICHRDIKPQNLLLDPDT 193
Cdd:cd05570    74 --VMEYVnggdlmfhiqrarrfTE---ERARFYA-AEICL--------------ALQFLHERGIIYRDLKLDNVLLDAEG 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 194 AVlKLCDFGSAKQLVRGEPNVSYIC-SRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIFPGDsGVDQLVeiikv 272
Cdd:cd05570   134 HI-KIADFGMCKEGIWGGNTTSTFCgTPDYIAPEILRE-QDYGFSVDWWALGVLLYEMLAGQSPFEGD-DEDELF----- 205
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1231802383 273 lgtptrEQIREMNPNYtefkfpqikahpwtkvfrPRT-PPEAIALCSRLLEYTPTARL--TP---LEACAHSFFDEL 343
Cdd:cd05570   206 ------EAILNDEVLY------------------PRWlSREAVSILKGLLTKDPARRLgcGPkgeADIKAHPFFRNI 258
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
56-340 2.12e-22

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: 96.62  E-value: 2.12e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKkVLQDKRFKNR--------ELQIMRKLDHCNIVRLRYFFyssgekKDEVY 127
Cdd:cd05598     3 FEKIKTIGVGAFGEVSLVRKKDTNALYAMK-TLRKKDVLKRnqvahvkaERDILAEADNEWVVKLYYSF------QDKEN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 128 LNLVLDYVP--ETVYRVARhysraKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFG--- 202
Cdd:cd05598    76 LYFVMDYIPggDLMSLLIK-----KGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHI-KLTDFGlct 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 203 -----------SAKQLVrGEPNvsYIcsryyrAPElIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDsgvdqlveiik 271
Cdd:cd05598   150 gfrwthdskyyLAHSLV-GTPN--YI------APE-VLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQ----------- 208
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 272 vlgTPTREQIREMNpNYTEFKFPQikahpwtkvfRPRTPPEAIALCSRLLEyTPTARL---TPLEACAHSFF 340
Cdd:cd05598   209 ---TPAETQLKVIN-WRTTLKIPH----------EANLSPEAKDLILRLCC-DAEDRLgrnGADEIKAHPFF 265
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
61-261 2.61e-22

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: 94.93  E-value: 2.61e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  61 VIGNGSFGVVYQAKLCDSGELVAIK----KVLQDKRFKNR---ELQIMRKLDHCNIVRLRYFFyssgEKKDEVYLNLVLD 133
Cdd:cd14186     8 LLGKGSFACVYRARSLHTGLEVAIKmidkKAMQKAGMVQRvrnEVEIHCQLKHPSILELYNYF----EDSNYVYLVLEMC 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 134 YVPEtvyrVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLVRGEPN 213
Cdd:cd14186    84 HNGE----MSRYLKNRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNI-KIADFGLATQLKMPHEK 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1231802383 214 VSYIC-SRYYRAPElIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDS 261
Cdd:cd14186   159 HFTMCgTPNYISPE-IATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDT 206
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
62-311 2.74e-22

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: 97.02  E-value: 2.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKkvlqdkRFKNRELQIMRKLDHCN-------------IVRLRYFFyssgekKDEVYL 128
Cdd:cd05600    19 VGQGGYGSVFLARKKDTGEICALK------IMKKKVLFKLNEVNHVLterdiltttnspwLVKLLYAF------QDPENV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 129 NLVLDYVPETVYRVARHYSRakqTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAK--- 205
Cdd:cd05600    87 YLAMEYVPGGDFRTLLNNSG---ILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLID-SSGHIKLTDFGLASgtl 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 206 ------------QLVRGEPNV-----------------------SYICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAEL 250
Cdd:cd05600   163 spkkiesmkirlEEVKNTAFLeltakerrniyramrkedqnyanSVVGSPDYMAPEVLRG-EGYDLTVDYWSLGCILFEC 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 251 LLGQPIFPGDSGVDQLVEII---KVLGTPTREQIRE----------------MNPNYTEFKFPQIKAHP------WTKVF 305
Cdd:cd05600   242 LVGFPPFSGSTPNETWANLYhwkKTLQRPVYTDPDLefnlsdeawdlitkliTDPQDRLQSPEQIKNHPffknidWDRLR 321

                  ....*.
gi 1231802383 306 RPRTPP 311
Cdd:cd05600   322 EGSKPP 327
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
56-271 2.92e-22

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: 94.92  E-value: 2.92e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDK------RFKNRELQIMRKLDHCNIVRLRYFFYSSgeKKDEVYLN 129
Cdd:cd14097     3 YTFGRKLGQGSFGVVIEATHKETQTKWAIKKINREKagssavKLLEREVDILKHVNHAHIIHLEEVFETP--KRMYLVME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 LVLDYVPETVYRVARHYSRAKqtlpviyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLL-----DP-DTAVLKLCDFG- 202
Cdd:cd14097    81 LCEDGELKELLLRKGFFSENE-------TRHIIQSLASAVAYLHKNDIVHRDLKLENILVkssiiDNnDKLNIKVTDFGl 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 203 SAKQLVRGEPNVSYIC-SRYYRAPELIfGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGvDQLVEIIK 271
Cdd:cd14097   154 SVQKYGLGEDMLQETCgTPIYMAPEVI-SAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSE-EKLFEEIR 221
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
60-311 3.19e-22

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: 95.78  E-value: 3.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQimrkldhCNIVRLRYF-----------FYSSGEKKDEVYL 128
Cdd:cd05620     1 KVLGKGSFGKVLLAELKGKGEYFAVKALKKDVVLIDDDVE-------CTMVEKRVLalawenpflthLYCTFQTKEHLFF 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 129 nlVLDYVP--ETVYRVarhysRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQ 206
Cdd:cd05620    74 --VMEFLNggDLMFHI-----QDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHI-KIADFGMCKE 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 207 LVRGEPNVSYIC-SRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIFPGDSGvDQLVEIIKVlGTP--------- 276
Cdd:cd05620   146 NVFGDNRASTFCgTPDYIAPEILQG-LKYTFSVDWWSFGVLLYEMLIGQSPFHGDDE-DELFESIRV-DTPhyprwitke 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1231802383 277 ---TREQIREMNPNYTEFKFPQIKAHP------WTKVFRPRTPP 311
Cdd:cd05620   223 skdILEKLFERDPTRRLGVVGNIRGHPffktinWTALEKRELDP 266
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
60-334 3.20e-22

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: 95.13  E-value: 3.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN-----RELQIMRKLDHCNIVRlryfFYSSGEKKDEVYLNLvlDY 134
Cdd:cd14046    12 QVLGKGAFGQVVKVRNKLDGRYYAIKKIKLRSESKNnsrilREVMLLSRLNHQHVVR----YYQAWIERANLYIQM--EY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 135 VPetvyrvarhysraKQTL-PVIYVKLY-----MYQLFR----SLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSA 204
Cdd:cd14046    86 CE-------------KSTLrDLIDSGLFqdtdrLWRLFRqileGLAYIHSQGIIHRDLKPVNIFLDSNGNV-KIGDFGLA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 205 KQ----------------LVRGEPNV---SYICSRYYRAPELIFGATD-YTSSIDVWSAGCVLAELllgqpIFPGDSGvd 264
Cdd:cd14046   152 TSnklnvelatqdinkstSAALGSSGdltGNVGTALYVAPEVQSGTKStYNEKVDMYSLGIIFFEM-----CYPFSTG-- 224
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 265 qlVEIIKVLGtptreQIREMNPNytefkFPQIkahpwtkvFRPRTPPEAIALCSRLLEYTPTARLTPLEA 334
Cdd:cd14046   225 --MERVQILT-----ALRSVSIE-----FPPD--------FDDNKHSKQAKLIRWLLNHDPAKRPSAQEL 274
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
60-343 3.71e-22

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: 95.17  E-value: 3.71e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKV-LQDKRFKNR------ELQIMRKLDHCNIVRLryffYSSGEKKDevYLNLVL 132
Cdd:cd05609     6 KLISNGAYGAVYLVRHRETRQRFAMKKInKQNLILRNQiqqvfvERDILTFAENPFVVSM----YCSFETKR--HLCMVM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 DYVPE-TVYRVARHYSrakqTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLdpdTAV--LKLCDFGSAK---- 205
Cdd:cd05609    80 EYVEGgDCATLLKNIG----PLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLI---TSMghIKLTDFGLSKiglm 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 206 --------------------QLVRGEPNvsyicsryYRAPELIFgATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQ 265
Cdd:cd05609   153 slttnlyeghiekdtrefldKQVCGTPE--------YIAPEVIL-RQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEEL 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 266 LVEIIKVlgtptreqiremnpnytEFKFPQIKAHPwtkvfrprtPPEAIALCSRLLEYTPTARL---TPLEACAHSFFDE 342
Cdd:cd05609   224 FGQVISD-----------------EIEWPEGDDAL---------PDDAQDLITRLLQQNPLERLgtgGAEEVKQHPFFQD 277

                  .
gi 1231802383 343 L 343
Cdd:cd05609   278 L 278
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
60-259 3.80e-22

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: 94.49  E-value: 3.80e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGE----LVAIKKVLQDKRFKN-----RELQIMRKLDHCNIVRLrYFFYSSGEkkdevYLNL 130
Cdd:pfam07714   5 EKLGEGAFGEVYKGTLKGEGEntkiKVAVKTLKEGADEEEredflEEASIMKKLDHPNIVKL-LGVCTQGE-----PLYI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 VLDYVPetvYRVARHYSRA-KQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQLvr 209
Cdd:pfam07714  79 VTEYMP---GGDLLDFLRKhKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVS-ENLVVKISDFGLSRDI-- 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1231802383 210 gEPNVSYICS-------RYYrAPELIFGATdYTSSIDVWSAGCVLAELL-LGQPIFPG 259
Cdd:pfam07714 153 -YDDDYYRKRgggklpiKWM-APESLKDGK-FTSKSDVWSFGVLLWEIFtLGEQPYPG 207
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
55-250 4.93e-22

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: 94.03  E-value: 4.93e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  55 SYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKV-----LQDKRFKNR-ELQIMRKLDHCNIVRlryffYSSGEKKDEVyL 128
Cdd:cd08220     1 KYEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIpveqmTKEERQAALnEVKVLSMLHHPNIIE-----YYESFLEDKA-L 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 129 NLVLDYVPE-TVYRVARhySRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSAKQL 207
Cdd:cd08220    75 MIVMEYAPGgTLFEYIQ--QRKGSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTVVKIGDFGISKIL 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1231802383 208 VRGEPNVSYICSRYYRAPELIFGATdYTSSIDVWSAGCVLAEL 250
Cdd:cd08220   153 SSKSKAYTVVGTPCYISPELCEGKP-YNQKSDIWALGCVLYEL 194
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
56-301 5.92e-22

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: 93.90  E-value: 5.92e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFK---NRELQIMRKLDHCNIVRLRYFFYSSgekkdeVYLNLVL 132
Cdd:cd14665     2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGEKIDenvQREIINHRSLRHPNIVRFKEVILTP------THLAIVM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 DYVP--ETVYRV--ARHYSRAKqtlpviyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAV-LKLCDFGSAKQL 207
Cdd:cd14665    76 EYAAggELFERIcnAGRFSEDE-------ARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAPrLKICDFGYSKSS 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 208 VRGEPNVSYICSRYYRAPELIFgATDYTSSI-DVWSAGCVLAELLLGQ-PIFPGDSGVDQLVEIIKVLGTPTR------- 278
Cdd:cd14665   149 VLHSQPKSTVGTPAYIAPEVLL-KKEYDGKIaDVWSCGVTLYVMLVGAyPFEDPEEPRNFRKTIQRILSVQYSipdyvhi 227
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1231802383 279 --------EQIREMNPNyTEFKFPQIKAHPW 301
Cdd:cd14665   228 specrhliSRIFVADPA-TRITIPEIRNHEW 257
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
53-257 6.00e-22

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: 94.01  E-value: 6.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  53 EVSYTDTK---VIGNGSFGVVYQAKLCDSGELVAIK----KVLQDKRFKNRELQIMRKLDHCNIVRlrYFfyssGEKKDE 125
Cdd:cd06624     4 EYEYDESGervVLGKGTFGVVYAARDLSTQVRIAIKeipeRDSREVQPLHEEIALHSRLSHKNIVQ--YL----GSVSED 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 126 VYLNLVLDYVP----ETVYRvaRHYSRAKQTLPVIyvKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDF 201
Cdd:cd06624    78 GFFKIFMEQVPggslSALLR--SKWGPLKDNENTI--GYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTYSGVVKISDF 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1231802383 202 GSAKQLVRGEPNV-SYICSRYYRAPELI-FGATDYTSSIDVWSAGCVLAELLLGQPIF 257
Cdd:cd06624   154 GTSKRLAGINPCTeTFTGTLQYMAPEVIdKGQRGYGPPADIWSLGCTIIEMATGKPPF 211
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
60-251 6.01e-22

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: 94.37  E-value: 6.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYqakLC-------DSGELVAIKKVLQDKR------FKnRELQIMRKLDHCNIVRLRYFFYSSGEKKdev 126
Cdd:cd05038    10 KQLGEGHFGSVE---LCrydplgdNTGEQVAVKSLQPSGEeqhmsdFK-REIEILRTLDHEYIVKYKGVCESPGRRS--- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 127 yLNLVLDYVPetvYRVARHY---SRAKQTLPVIYvkLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGS 203
Cdd:cd05038    83 -LRLIMEYLP---SGSLRDYlqrHRDQIDLKRLL--LFASQICKGMEYLGSQRYIHRDLAARNILVESEDLV-KISDFGL 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1231802383 204 AKQLVRG-------EPNVSYIcsRYYrAPELIFGATDYTSSiDVWSAGCVLAELL 251
Cdd:cd05038   156 AKVLPEDkeyyyvkEPGESPI--FWY-APECLRESRFSSAS-DVWSFGVTLYELF 206
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
56-301 6.96e-22

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: 93.94  E-value: 6.96e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIK----KVLQDKRFK-NRELQIMRKLDHCNIVRLRYFFyssgEKKDEVYLNL 130
Cdd:cd14167     5 YDFREVLGTGAFSEVVLAEEKRTQKLVAIKciakKALEGKETSiENEIAVLHKIKHPNIVALDDIY----ESGGHLYLIM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 VL-------DYVPETVYRVARHYSRakqtlpviyvklYMYQLFRSLAYIHSFGICHRDIKPQNLL---LDPDTAVLkLCD 200
Cdd:cd14167    81 QLvsggelfDRIVEKGFYTERDASK------------LIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIM-ISD 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 201 FGSAKqlVRGEPNV-SYIC-SRYYRAPElIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKV---LGT 275
Cdd:cd14167   148 FGLSK--IEGSGSVmSTACgTPGYVAPE-VLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAeyeFDS 224
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1231802383 276 PTREQIR-----------EMNPNyTEFKFPQIKAHPW 301
Cdd:cd14167   225 PYWDDISdsakdfiqhlmEKDPE-KRFTCEQALQHPW 260
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
56-342 8.03e-22

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: 93.83  E-value: 8.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVV-----------YQAKLCD--SGELVAIKKVLQDKRFKNRELQIMRKLD-HCNIVRLR-------- 113
Cdd:cd14182     5 YEPKEILGRGVSSVVrrcihkptrqeYAVKIIDitGGGSFSPEEVQELREATLKEIDILRKVSgHPNIIQLKdtyetntf 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 114 YFFYSSGEKKDEVYlnlvlDYVPETVyrvarhysrakqTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDT 193
Cdd:cd14182    85 FFLVFDLMKKGELF-----DYLTEKV------------TLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDM 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 194 AVlKLCDFGSAKQLVRGEpNVSYIC-SRYYRAPELIFGATD-----YTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLV 267
Cdd:cd14182   148 NI-KLTDFGFSCQLDPGE-KLREVCgTPGYLAPEIIECSMDdnhpgYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLR 225
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1231802383 268 EIikvlgtptreqireMNPNYtEFKFPQikahpWTKvfRPRTPPEaiaLCSRLLEYTPTARLTPLEACAHSFFDE 342
Cdd:cd14182   226 MI--------------MSGNY-QFGSPE-----WDD--RSDTVKD---LISRFLVVQPQKRYTAEEALAHPFFQQ 275
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
50-261 8.91e-22

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: 95.14  E-value: 8.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  50 RPQEVSYTDTKVIGNGSFGVVYQAKLCDSGELVAIK---KVLQDKR----FKNRELQIMRkldHCN---IVRLRYFFyss 119
Cdd:cd05596    22 RMNAEDFDVIKVIGRGAFGEVQLVRHKSTKKVYAMKllsKFEMIKRsdsaFFWEERDIMA---HANsewIVQLHYAF--- 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 120 gekKDEVYLNLVLDYVP--ETVYRVARHysrakqTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPdTAVLK 197
Cdd:cd05596    96 ---QDDKYLYMVMDYMPggDLVNLMSNY------DVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDA-SGHLK 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1231802383 198 LCDFGS-----AKQLVRGEPNV---SYIcsryyrAPELIF---GATDYTSSIDVWSAGCVLAELLLGQPIFPGDS 261
Cdd:cd05596   166 LADFGTcmkmdKDGLVRSDTAVgtpDYI------SPEVLKsqgGDGVYGRECDWWSVGVFLYEMLVGDTPFYADS 234
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
53-264 1.02e-21

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: 93.53  E-value: 1.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  53 EVSYTDTKVIGNGSFGVVYQAKLCDSGEL-VAIKKVLQDKRFKN-----RELQIMRKLDHCNIVRLryffYSSGEKKDEV 126
Cdd:cd14201     5 DFEYSRKDLVGHGAFAVVFKGRHRKKTDWeVAIKSINKKNLSKSqillgKEIKILKELQHENIVAL----YDVQEMPNSV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 127 YLnlVLDYVPETVYRvarHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLL--------DPDTAVLKL 198
Cdd:cd14201    81 FL--VMEYCNGGDLA---DYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLsyasrkksSVSGIRIKI 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1231802383 199 CDFGSAKQLVRGEPNVSYICSRYYRAPELIFgATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVD 264
Cdd:cd14201   156 ADFGFARYLQSNMMAATLCGSPMYMAPEVIM-SQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQD 220
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
56-339 1.53e-21

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: 93.08  E-value: 1.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKV-----LQDKRFKNRELQIMRKLDHCNIVRlrYFfyssGEKKDEVYLNL 130
Cdd:cd06609     3 FTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIdleeaEDEIEDIQQEIQFLSQCDSPYITK--YY----GSFLKGSKLWI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 VLDYVPETVyrvARHYSRAkQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLVR- 209
Cdd:cd06609    77 IMEYCGGGS---VLDLLKP-GPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDV-KLADFGVSGQLTSt 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 210 --------GEPnvsyicsrYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIFpgdSGVDQLveiiKVLgtptrEQI 281
Cdd:cd06609   152 mskrntfvGTP--------FWMAPEVIKQ-SGYDEKADIWSLGITAIELAKGEPPL---SDLHPM----RVL-----FLI 210
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1231802383 282 REMNPnytefkfPQIKAHPWTKVFRprtppEAIALCsrlLEYTPTARLTPLEACAHSF 339
Cdd:cd06609   211 PKNNP-------PSLEGNKFSKPFK-----DFVELC---LNKDPKERPSAKELLKHKF 253
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
60-301 1.75e-21

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: 92.48  E-value: 1.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIK--------KVLQDKRFKnrELQIMRKLDHCNIVRLryffYSSGEKKDEVYLNLV 131
Cdd:cd14074     9 ETLGRGHFAVVKLARHVFTGEKVAVKvidktkldDVSKAHLFQ--EVRCMKLVQHPNVVRL----YEVIDTQTKLYLILE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 132 L-------DYVpetvyrvARHYSRAKQTLpviyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSA 204
Cdd:cd14074    83 LgdggdmyDYI-------MKHENGLNEDL----ARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQGLVKLTDFGFS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 205 KQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIF--PGDSgvDQLVEII-------KVLGT 275
Cdd:cd14074   152 NKFQPGEKLETSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILYMLVCGQPPFqeANDS--ETLTMIMdckytvpAHVSP 229
                         250       260
                  ....*....|....*....|....*....
gi 1231802383 276 PTREQIREM---NPNyTEFKFPQIKAHPW 301
Cdd:cd14074   230 ECKDLIRRMlirDPK-KRASLEEIENHPW 257
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
63-340 1.93e-21

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: 93.80  E-value: 1.93e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  63 GNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNR---ELQIMRKL--------DHCNIVRLRYFFYSSGEkkDEVYLNLV 131
Cdd:cd14136    19 GWGHFSTVWLCWDLQNKRFVALKVVKSAQHYTEAaldEIKLLKCVreadpkdpGREHVVQLLDDFKHTGP--NGTHVCMV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 132 LDYVPETVYRVARHYsrAKQTLPVIYVKLYMYQLFRSLAYIHS-FGICHRDIKPQNLLLDPDTAVLKLCDFGSA----KQ 206
Cdd:cd14136    97 FEVLGPNLLKLIKRY--NYRGIPLPLVKKIARQVLQGLDYLHTkCGIIHTDIKPENVLLCISKIEVKIADLGNAcwtdKH 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 207 LvrgepnVSYICSRYYRAPELIFGAtDYTSSIDVWSAGCVLAELLLGQPIFPGDSG------VDQLVEIIKVLGTPTReQ 280
Cdd:cd14136   175 F------TEDIQTRQYRSPEVILGA-GYGTPADIWSTACMAFELATGDYLFDPHSGedysrdEDHLALIIELLGRIPR-S 246
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1231802383 281 IREMNPNYTEF-----KFPQI-KAHPW--TKVFRPR---TPPEAIALCSRL---LEYTPTARLTPLEACAHSFF 340
Cdd:cd14136   247 IILSGKYSREFfnrkgELRHIsKLKPWplEDVLVEKykwSKEEAKEFASFLlpmLEYDPEKRATAAQCLQHPWL 320
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
52-340 2.26e-21

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: 92.19  E-value: 2.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  52 QEVSYTDTKVIGNGSFGVVYQAKLCDSGELVAiKKVLQDKRFKNRELQIMRKLDHCNIVRLrYFFYSSGEKKDEVYLNL- 130
Cdd:cd14109     2 RELYEIGEEDEKRAAQGAPFHVTERSTGRNFL-AQLRYGDPFLMREVDIHNSLDHPNIVQM-HDAYDDEKLAVTVIDNLa 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 -----VLDYVPEtvyrvARHYSRAKQtlpviyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtaVLKLCDFGSAK 205
Cdd:cd14109    80 stielVRDNLLP-----GKDYYTERQ------VAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQDD--KLKLADFGQSR 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 206 QLVRGEPNVSYICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIFPGDSgvdqlveiikvlgtpTREQIRemn 285
Cdd:cd14109   147 RLLRGKLTTLIYGSPEFVSPEIVNS-YPVTLATDMWSVGVLTYVLLGGISPFLGDN---------------DRETLT--- 207
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1231802383 286 pNYTEFKFpQIKAHPWTKVfrprtPPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd14109   208 -NVRSGKW-SFDSSPLGNI-----SDDARDFIKKLLVYIPESRLTVDEALNHPWF 255
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
60-261 3.20e-21

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: 92.50  E-value: 3.20e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKVL--------QDKRFKNrELQIMRKLDHCNIVRLryfFYSSgekKDEVYLNLV 131
Cdd:cd05612     7 KTIGTGTFGRVHLVRDRISEHYYALKVMAipevirlkQEQHVHN-EKRVLKEVSHPFIIRL---FWTE---HDQRFLYML 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 132 LDYVPE----TVYRVARHYSRAKQtlpviyvKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKLCDFGSAKQL 207
Cdd:cd05612    80 MEYVPGgelfSYLRNSGRFSNSTG-------LFYASEIVCALEYLHSKEIVYRDLKPENILLDKE-GHIKLTDFGFAKKL 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 208 VR------GEPNvsyicsryYRAPELIfGATDYTSSIDVWSAGCVLAELLLGQPIFPGDS 261
Cdd:cd05612   152 RDrtwtlcGTPE--------YLAPEVI-QSKGHNKAVDWWALGILIYEMLVGYPPFFDDN 202
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
62-303 3.28e-21

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: 92.79  E-value: 3.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAiKKVLQDKRFKNRE-----LQIMRKLDHCNIVRLRYFFYSSGEkkdevyLNLVLDYVP 136
Cdd:cd06644    20 LGDGAFGKVYKAKNKETGALAA-AKVIETKSEEELEdymveIEILATCNHPYIVKLLGAFYWDGK------LWIMIEFCP 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 137 E-TVYRVARHYSRAKQTlPVIyvKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFG-SAKQLVRGEPNV 214
Cdd:cd06644    93 GgAVDAIMLELDRGLTE-PQI--QVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDI-KLADFGvSAKNVKTLQRRD 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 215 SYICSRYYRAPELIFGAT----DYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVlGTPTREQIREMNPNYTE 290
Cdd:cd06644   169 SFIGTPYWMAPEVVMCETmkdtPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKS-EPPTLSQPSKWSMEFRD 247
                         250
                  ....*....|...
gi 1231802383 291 FKFPQIKAHPWTK 303
Cdd:cd06644   248 FLKTALDKHPETR 260
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
56-267 3.38e-21

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: 91.98  E-value: 3.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVlqDK---------RFKNRELQIMRKLDHCNIVRLrYFFYSSGEKKDEV 126
Cdd:cd14163     2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKII--DKsggpeefiqRFLPRELQIVERLDHKNIIHV-YEMLESADGKIYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 127 YLNL-----VLDYVPEtvyrvarhysraKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTavLKLCDF 201
Cdd:cd14163    79 VMELaedgdVFDCVLH------------GGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGFT--LKLTDF 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1231802383 202 GSAKQLVRGEPNVS--YICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFpGDSGVDQLV 267
Cdd:cd14163   145 GFAKQLPKGGRELSqtFCGSTAYAAPEVLQGVPHDSRKGDIWSMGVVLYVMLCAQLPF-DDTDIPKML 211
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
61-351 3.47e-21

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: 92.60  E-value: 3.47e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  61 VIGNGSFGVVYQAKLCDSGELVAIKKVLQDKrFK----------NRELQIMRKLDHCNIVRLRYFFYSSGekkdevYLNL 130
Cdd:cd14094    10 VIGKGPFSVVRRCIHRETGQQFAVKIVDVAK-FTsspglstedlKREASICHMLKHPHIVELLETYSSDG------MLYM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 VLDYVP------ETVYRVARH--YSRAkqtlpviYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLL--DPDTAVLKLCD 200
Cdd:cd14094    83 VFEFMDgadlcfEIVKRADAGfvYSEA-------VASHYMRQILEALRYCHDNNIIHRDVKPHCVLLasKENSAPVKLGG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 201 FGSAKQLVRGEpnvSYICSR----YYRAPELIfGATDYTSSIDVWSAGCVLAELLLGQPIFpgdsgvdqlveiikvLGTP 276
Cdd:cd14094   156 FGVAIQLGESG---LVAGGRvgtpHFMAPEVV-KREPYGKPVDVWGCGVILFILLSGCLPF---------------YGTK 216
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1231802383 277 TREQIREMNPNYtefkfpQIKAHPWtkvfrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFfdeLRDPNVKLP 351
Cdd:cd14094   217 ERLFEGIIKGKY------KMNPRQW-----SHISESAKDLVRRMLMLDPAERITVYEALNHPW---IKERDRYAY 277
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
60-281 4.55e-21

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: 91.64  E-value: 4.55e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNR---------ELQIMRKLDHCNIVRLRYFFYSSGEKKdevyLNL 130
Cdd:cd06652     8 KLLGQGAFGRVYLCYDADTGRELAVKQVQFDPESPETskevnalecEIQLLKNLLHERIVQYYGCLRDPQERT----LSI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 VLDYVPETVYRvarHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQL--- 207
Cdd:cd06652    84 FMEYMPGGSIK---DQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRD-SVGNVKLGDFGASKRLqti 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1231802383 208 -VRGEPNVSYICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIFpgdSGVDQLVEIIKVLGTPTREQI 281
Cdd:cd06652   160 cLSGTGMKSVTGTPYWMSPEVISG-EGYGRKADIWSVGCTVVEMLTEKPPW---AEFEAMAAIFKIATQPTNPQL 230
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
62-339 4.73e-21

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: 92.10  E-value: 4.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKVLQD-----KRFKNRELQIMRKLDHCNIVRlryfFYSSGEKKDEVYLNLVLDYVP 136
Cdd:cd06621     9 LGEGAGGSVTKCRLRNTKTIFALKTITTDpnpdvQKQILRELEINKSCASPYIVK----YYGAFLDEQDSSIGIAMEYCE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 137 ----ETVYRVARhySRAKQTLPVIYVKLyMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLVRGEP 212
Cdd:cd06621    85 ggslDSIYKKVK--KKGGRIGEKVLGKI-AESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQV-KLCDFGVSGELVNSLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 213 NvSYICSRYYRAPELIFGATdYTSSIDVWSAGCVLAELLLGQPIFPGDSgvDQLVEIIKVLgtptrEQIREMNPnytefk 292
Cdd:cd06621   161 G-TFTGTSYYMAPERIQGGP-YSITSDVWSLGLTLLEVAQNRFPFPPEG--EPPLGPIELL-----SYIVNMPN------ 225
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 293 fPQIKAHP-----WTKVFRprtppEAIALCsrlLEYTPTARLTPLEACAHSF 339
Cdd:cd06621   226 -PELKDEPengikWSESFK-----DFIEKC---LEKDGTRRPGPWQMLAHPW 268
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
60-340 6.65e-21

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: 92.47  E-value: 6.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQA-KLC--DSGELVAIKkVLQ---------DKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEkkdevy 127
Cdd:cd05584     2 KVLGKGGYGKVFQVrKTTgsDKGKIFAMK-VLKkasivrnqkDTAHTKAERNILEAVKHPFIVDLHYAFQTGGK------ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 128 LNLVLDYVP--ETVYRVARhysraKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAK 205
Cdd:cd05584    75 LYLILEYLSggELFMHLER-----EGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHV-KLTDFGLCK 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 206 QLVRGEPNVSYICSRY-YRAPElIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKvlgtptreqirem 284
Cdd:cd05584   149 ESIHDGTVTHTFCGTIeYMAPE-ILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILK------------- 214
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1231802383 285 npnyTEFKFPqikahpwtkvfrPRTPPEAIALCSRLLEYTPTARL--TPLEAC---AHSFF 340
Cdd:cd05584   215 ----GKLNLP------------PYLTNEARDLLKKLLKRNVSSRLgsGPGDAEeikAHPFF 259
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
62-314 8.26e-21

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: 91.54  E-value: 8.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQI-MRKLDHCNIVRLRYFFyssgekKDEVYLNLVLDYVP---- 136
Cdd:cd14091     8 IGKGSYSVCKRCIHKATGKEYAVKIIDKSKRDPSEEIEIlLRYGQHPNIITLRDVY------DDGNSVYLVTELLRggel 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 137 -ETVYRVaRHYSRaKQTLPVIYVklymyqLFRSLAYIHSFGICHRDIKPQNLLL-----DPDTavLKLCDFGSAKQLvRG 210
Cdd:cd14091    82 lDRILRQ-KFFSE-REASAVMKT------LTKTVEYLHSQGVVHRDLKPSNILYadesgDPES--LRICDFGFAKQL-RA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 211 E------PnvsyiCsrY---YRAPElIFGATDYTSSIDVWSAGCVLAELLLGQPIF---PGDSGVDQLVEI----IKVLG 274
Cdd:cd14091   151 EngllmtP-----C--YtanFVAPE-VLKKQGYDAACDIWSLGVLLYTMLAGYTPFasgPNDTPEVILARIgsgkIDLSG 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 275 -------TPTREQIREM---NPN--YTEfkfPQIKAHPWTkVFRPRTPPEAI 314
Cdd:cd14091   223 gnwdhvsDSAKDLVRKMlhvDPSqrPTA---AQVLQHPWI-RNRDSLPQRQL 270
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
61-343 8.34e-21

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: 90.92  E-value: 8.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  61 VIGNGSFGVVYQA-KLC--DSGELVAIK-----KVLQDKRFKNR---ELQIMRKLDHCN-IVRLRYFFYSsgekkdEVYL 128
Cdd:cd05583     1 VLGTGAYGKVFLVrKVGghDAGKLYAMKvlkkaTIVQKAKTAEHtmtERQVLEAVRQSPfLVTLHYAFQT------DAKL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 129 NLVLDYVPETvyRVARH-YSRAKQTLPviYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQL 207
Cdd:cd05583    75 HLILDYVNGG--ELFTHlYQREHFTES--EVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHV-VLTDFGLSKEF 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 208 VRGEPNVSY-ICSRY-YRAPELIFGATD-YTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKvlgtptreQIREM 284
Cdd:cd05583   150 LPGENDRAYsFCGTIeYMAPEVVRGGSDgHDKAVDWWSLGVLTYELLTGASPFTVDGERNSQSEISK--------RILKS 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1231802383 285 NPnytefkfpqikahPWTKVFRprtpPEAIALCSRLLEYTPTARL-----TPLEACAHSFFDEL 343
Cdd:cd05583   222 HP-------------PIPKTFS----AEAKDFILKLLEKDPKKRLgagprGAHEIKEHPFFKGL 268
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
60-341 8.45e-21

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: 91.21  E-value: 8.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKV-----LQDKRFKNrELQIMRKLDHCNIVRLRYFFyssgEKKDEVYLNLVLDY 134
Cdd:cd14166     9 EVLGSGAFSEVYLVKQRSTGKLYALKCIkksplSRDSSLEN-EIAVLKRIKHENIVTLEDIY----ESTTHYYLVMQLVS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 135 VPETVYRV-ARHYSRAKQTLPVIYvklymyQLFRSLAYIHSFGICHRDIKPQNLL-LDPD-TAVLKLCDFGSAKQLVRGE 211
Cdd:cd14166    84 GGELFDRIlERGVYTEKDASRVIN------QVLSAVKYLHENGIVHRDLKPENLLyLTPDeNSKIMITDFGLSKMEQNGI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 212 pnVSYIC-SRYYRAPElIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDsgvdqlveiikvlgTPTR--EQIREmnpNY 288
Cdd:cd14166   158 --MSTACgTPGYVAPE-VLAQKPYSKAVDCWSIGVITYILLCGYPPFYEE--------------TESRlfEKIKE---GY 217
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1231802383 289 TEFKFPqikahpwtkvFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFD 341
Cdd:cd14166   218 YEFESP----------FWDDISESAKDFIRHLLEKNPSKRYTCEKALSHPWII 260
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
54-283 1.11e-20

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: 90.47  E-value: 1.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  54 VSYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNR---------ELQIMRKLDHCNIVRlryfFYSSGEKKD 124
Cdd:cd06653     2 VNWRLGKLLGRGAFGEVYLCYDADTGRELAVKQVPFDPDSQETskevnalecEIQLLKNLRHDRIVQ----YYGCLRDPE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 125 EVYLNLVLDYVPE-TVYRVARHYSRAKQTLpviyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGS 203
Cdd:cd06653    78 EKKLSIFVEYMPGgSVKDQLKAYGALTENV----TRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNV-KLGDFGA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 204 AKQL----VRGEPNVSYICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIFpgdSGVDQLVEIIKVLGTPTRE 279
Cdd:cd06653   153 SKRIqticMSGTGIKSVTGTPYWMSPEVISG-EGYGRKADVWSVACTVVEMLTEKPPW---AEYEAMAAIFKIATQPTKP 228

                  ....
gi 1231802383 280 QIRE 283
Cdd:cd06653   229 QLPD 232
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
60-271 1.15e-20

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: 90.51  E-value: 1.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIK----KVLQDKRFK-NRELQIMRKLDHCNIVRLRYFFyssgEKKDEVYLnlVLDY 134
Cdd:cd14083     9 EVLGTGAFSEVVLAEDKATGKLVAIKcidkKALKGKEDSlENEIAVLRKIKHPNIVQLLDIY----ESKSHLYL--VMEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 135 VP--ETVYRVARHYSRAKQTLPVIyvklyMYQLFRSLAYIHSFGICHRDIKPQNLL---LDPDTAVLkLCDFGSAKqlVR 209
Cdd:cd14083    83 VTggELFDRIVEKGSYTEKDASHL-----IRQVLEAVDYLHSLGIVHRDLKPENLLyysPDEDSKIM-ISDFGLSK--ME 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1231802383 210 GEPNVSYIC-SRYYRAPELIfGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIK 271
Cdd:cd14083   155 DSGVMSTACgTPGYVAPEVL-AQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILK 216
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
62-261 1.19e-20

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 91.80  E-value: 1.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIK-----KVLQDKRFK--NRELQIMRKLDHCNIVRLryffYSSGEKKDEVYLnlVLDY 134
Cdd:PTZ00263   26 LGTGSFGRVRIAKHKGTGEYYAIKclkkrEILKMKQVQhvAQEKSILMELSHPFIVNM----MCSFQDENRVYF--LLEF 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 135 VPETvyRVARHYSRAKQtLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLvrgePNV 214
Cdd:PTZ00263  100 VVGG--ELFTHLRKAGR-FPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHV-KVTDFGFAKKV----PDR 171
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1231802383 215 SY-IC-SRYYRAPELIfGATDYTSSIDVWSAGCVLAELLLGQPIFPGDS 261
Cdd:PTZ00263  172 TFtLCgTPEYLAPEVI-QSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDT 219
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
60-260 1.38e-20

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: 90.47  E-value: 1.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKV----LQDKRFKN---RELQIMRKLDHCNIVRLRYFFYSSGEkkdevyLNLVL 132
Cdd:cd08228     8 KKIGRGQFSEVYRATCLLDRKPVALKKVqifeMMDAKARQdcvKEIDLLKQLNHPNVIKYLDSFIEDNE------LNIVL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 DYVPE-TVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPdTAVLKLCDFGSAKQLVRGE 211
Cdd:cd08228    82 ELADAgDLSQMIKYFKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITA-TGVVKLGDLGLGRFFSSKT 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1231802383 212 PNV-SYICSRYYRAPELIFgATDYTSSIDVWSAGCVLAELLLGQPIFPGD 260
Cdd:cd08228   161 TAAhSLVGTPYYMSPERIH-ENGYNFKSDIWSLGCLLYEMAALQSPFYGD 209
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
55-253 1.55e-20

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: 90.43  E-value: 1.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  55 SYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVL----QDKRFKNRELQIMRKLDHCNIVRL-RYFFYSSGEKKDEVYLn 129
Cdd:cd13986     1 RYRIQRLLGEGGFSFVYLVEDLSTGRLYALKKILchskEDVKEAMREIENYRLFNHPNILRLlDSQIVKEAGGKKEVYL- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 lVLDYVPE-TVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSF---GICHRDIKPQNLLL-DPDTAVLKlcDFGSA 204
Cdd:cd13986    80 -LLPYYKRgSLQDEIERRLVKGTFFPEDRILHIFLGICRGLKAMHEPelvPYAHRDIKPGNVLLsEDDEPILM--DLGSM 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 205 KQ---LVRGEPNVSYI-------CSRYYRAPELiFGA---TDYTSSIDVWSAGCVLAELLLG 253
Cdd:cd13986   157 NPariEIEGRREALALqdwaaehCTMPYRAPEL-FDVkshCTIDEKTDIWSLGCTLYALMYG 217
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
49-255 1.72e-20

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: 90.85  E-value: 1.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  49 DRPQEVsYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN-------RELQIMRKLDHCNIVRLRyffyssGE 121
Cdd:cd06634    11 DDPEKL-FSDLREIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNekwqdiiKEVKFLQKLRHPNTIEYR------GC 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 122 KKDEVYLNLVLDYVPETVYRVARHYSRAKQTLPVIYVklyMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDF 201
Cdd:cd06634    84 YLREHTAWLVMEYCLGSASDLLEVHKKPLQEVEIAAI---THGALQGLAYLHSHNMIHRDVKAGNILLT-EPGLVKLGDF 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1231802383 202 GSAKQLvrgEPNVSYICSRYYRAPELIFGATD--YTSSIDVWSAGCVLAELLLGQP 255
Cdd:cd06634   160 GSASIM---APANSFVGTPYWMAPEVILAMDEgqYDGKVDVWSLGITCIELAERKP 212
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
62-271 1.74e-20

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: 89.84  E-value: 1.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIK-----KVLQD--KRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKkdeVYLNL---- 130
Cdd:cd14165     9 LGEGSYAKVKSAYSERLKCNVAIKiidkkKAPDDfvEKFLPRELEILARLNHKSIIKTYEIFETSDGK---VYIVMelgv 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 ---VLDYVPEtvyRVARHYSRAKQtlpviyvklYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQL 207
Cdd:cd14165    86 qgdLLEFIKL---RGALPEDVARK---------MFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNI-KLTDFGFSKRC 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1231802383 208 VRGEPN----VSYIC-SRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFpGDSGVDQLVEIIK 271
Cdd:cd14165   153 LRDENGrivlSKTFCgSAAYAAPEVLQGIPYDPRIYDIWSLGVILYIMVCGSMPY-DDSNVKKMLKIQK 220
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
56-301 2.06e-20

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: 89.71  E-value: 2.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDK-----RFKNRELQIMRKLDHCNIVRLryffYSSGEKKDEVYLnl 130
Cdd:cd14184     3 YKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKccgkeHLIENEVSILRRVKHPNIIML----IEEMDTPAELYL-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 VLDYVP-----ETVYRVARHYSRAKQTLpviyvklyMYQLFRSLAYIHSFGICHRDIKPQNLLL--DPD-TAVLKLCDFG 202
Cdd:cd14184    77 VMELVKggdlfDAITSSTKYTERDASAM--------VYNLASALKYLHGLCIVHRDIKPENLLVceYPDgTKSLKLGDFG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 203 SAkQLVRGePNVSYICSRYYRAPELIfGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGV-----DQLveIIKVLGTPT 277
Cdd:cd14184   149 LA-TVVEG-PLYTVCGTPTYVAPEII-AETGYGLKVDIWAAGVITYILLCGFPPFRSENNLqedlfDQI--LLGKLEFPS 223
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1231802383 278 ----------REQIREMNPNYTEFKFP--QIKAHPW 301
Cdd:cd14184   224 pywdnitdsaKELISHMLQVNVEARYTaeQILSHPW 259
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
56-249 2.24e-20

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: 89.43  E-value: 2.24e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN-------RELQIMRKLDHCNIVRLRYFFYSsgekkdEVYL 128
Cdd:cd06607     3 FEDLREIGHGSFGAVYYARNKRTSEVVAIKKMSYSGKQSTekwqdiiKEVKFLRQLRHPNTIEYKGCYLR------EHTA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 129 NLVLDY-VPETVYRVARHysraKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQL 207
Cdd:cd06607    77 WLVMEYcLGSASDIVEVH----KKPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLT-EPGTVKLADFGSASLV 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1231802383 208 vrgEPNVSYICSRYYRAPELIFgATD---YTSSIDVWSAG--CV-LAE 249
Cdd:cd06607   152 ---CPANSFVGTPYWMAPEVIL-AMDegqYDGKVDVWSLGitCIeLAE 195
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
60-343 2.64e-20

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: 90.75  E-value: 2.64e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLC---DSGELVAIKkVLQD----KRFKNRELQIMRK--LDHCN----IVRLRYFFyssgekKDEV 126
Cdd:cd05614     6 KVLGTGAYGKVFLVRKVsghDANKLYAMK-VLRKaalvQKAKTVEHTRTERnvLEHVRqspfLVTLHYAF------QTDA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 127 YLNLVLDYVP-----ETVYRvARHYSRAKqtlpviyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLkLCDF 201
Cdd:cd05614    79 KLHLILDYVSggelfTHLYQ-RDHFSEDE-------VRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVV-LTDF 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 202 GSAKQLVRGEPNVSY-ICSRY-YRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKvlgtptre 279
Cdd:cd05614   150 GLSKEFLTEEKERTYsFCGTIeYMAPEIIRGKSGHGKAVDWWSLGILMFELLTGASPFTLEGEKNTQSEVSR-------- 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1231802383 280 QIREMNPnytefKFPqikahpwtkvfrPRTPPEAIALCSRLLEYTPTARLTPLEACA-----HSFFDEL 343
Cdd:cd05614   222 RILKCDP-----PFP------------SFIGPVARDLLQKLLCKDPKKRLGAGPQGAqeikeHPFFKGL 273
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
55-343 2.90e-20

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: 89.70  E-value: 2.90e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  55 SYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKvLQDKRFKNR--------ELQIMRKLDHCNIVRLRYFFyssgEKKDEV 126
Cdd:cd05630     1 TFRQYRVLGKGGFGEVCACQVRATGKMYACKK-LEKKRIKKRkgeamalnEKQILEKVNSRFVVSLAYAY----ETKDAL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 127 YLNLVLDYVPETVYRVarhYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQ 206
Cdd:cd05630    76 CLVLTLMNGGDLKFHI---YHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLD-DHGHIRISDLGLAVH 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 207 LVRGEPNVSYICSRYYRAPELIFGATdYTSSIDVWSAGCVLAELLLGQPIFpgdsgvDQLVEIIKvlgtptREQ----IR 282
Cdd:cd05630   152 VPEGQTIKGRVGTVGYMAPEVVKNER-YTFSPDWWALGCLLYEMIAGQSPF------QQRKKKIK------REEverlVK 218
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1231802383 283 EMNPNYTEfkfpqikahpwtkvfrpRTPPEAIALCSRLLEYTPTARL-----TPLEACAHSFFDEL 343
Cdd:cd05630   219 EVPEEYSE-----------------KFSPQARSLCSMLLCKDPAERLgcrggGAREVKEHPLFKKL 267
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
60-260 3.34e-20

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: 89.71  E-value: 3.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKV----LQDKRFKN---RELQIMRKLDHCNIVRlryfFYSSGEKKDEvyLNLVL 132
Cdd:cd08229    30 KKIGRGQFSEVYRATCLLDGVPVALKKVqifdLMDAKARAdciKEIDLLKQLNHPNVIK----YYASFIEDNE--LNIVL 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 DYVPE-TVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPdTAVLKLCDFGSAKQL-VRG 210
Cdd:cd08229   104 ELADAgDLSRMIKHFKKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITA-TGVVKLGDLGLGRFFsSKT 182
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1231802383 211 EPNVSYICSRYYRAPELIFgATDYTSSIDVWSAGCVLAELLLGQPIFPGD 260
Cdd:cd08229   183 TAAHSLVGTPYYMSPERIH-ENGYNFKSDIWSLGCLLYEMAALQSPFYGD 231
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
62-351 3.98e-20

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: 89.66  E-value: 3.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKkvLQDKRFKNR------ELQIMRKLDHCNIVRLrYFFYSSGEK----KDEVYLNLV 131
Cdd:cd06659    29 IGEGSTGVVCIAREKHSGRQVAVK--MMDLRKQQRrellfnEVVIMRDYQHPNVVEM-YKSYLVGEElwvlMEYLQGGAL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 132 LDYVPETVYRVARHYSRAKQTLPviyvklymyqlfrSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLVRGE 211
Cdd:cd06659   106 TDIVSQTRLNEEQIATVCEAVLQ-------------ALAYLHSQGVIHRDIKSDSILLTLDGRV-KLSDFGFCAQISKDV 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 212 PN-VSYICSRYYRAPELIfGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLveiikvlgtptrEQIREMNPnyte 290
Cdd:cd06659   172 PKrKSLVGTPYWMAPEVI-SRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAM------------KRLRDSPP---- 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 291 fkfPQIK-AHPWTKVFRPrtppeaiaLCSRLLEYTPTARLTPLEACAHSFFDELRDPNVKLP 351
Cdd:cd06659   235 ---PKLKnSHKASPVLRD--------FLERMLVRDPQERATAQELLDHPFLLQTGLPECLVP 285
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
55-340 4.04e-20

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: 88.84  E-value: 4.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  55 SYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFK-------NRELQIMRKLDHCNIVRLRYFFyssgEKKDEVY 127
Cdd:cd14187     8 RYVRGRFLGKGGFAKCYEITDADTKEVFAGKIVPKSLLLKphqkekmSMEIAIHRSLAHQHVVGFHGFF----EDNDFVY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 128 LnlvldyVPETVYR---VARHYSRAKQTLPviYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSA 204
Cdd:cd14187    84 V------VLELCRRrslLELHKRRKALTEP--EARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEV-KIGDFGLA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 205 KQL-VRGEPNVSYICSRYYRAPElIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKvlgtptreqire 283
Cdd:cd14187   155 TKVeYDGERKKTLCGTPNYIAPE-VLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKK------------ 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1231802383 284 mnpnyTEFKFPQikahpwtkvfrpRTPPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd14187   222 -----NEYSIPK------------HINPVAASLIQKMLQTDPTARPTINELLNDEFF 261
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
57-320 4.70e-20

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: 89.35  E-value: 4.70e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  57 TDTKVIGNGSFGVVYQAKLCDSGELVAIKKV------LQDKRFKnRELQIMRKLDHC-NIVRlryfFYSSGEKKDEVYLN 129
Cdd:cd06616     9 KDLGEIGRGAFGTVNKMLHKPSGTIMAVKRIrstvdeKEQKRLL-MDLDVVMRSSDCpYIVK----FYGALFREGDCWIC 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 LVL-DYVPETVYRVArhYSRAKQTLPVIYVKLYMYQLFRSLAYI-HSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQL 207
Cdd:cd06616    84 MELmDISLDKFYKYV--YEVLDSVIPEEILGKIAVATVKALNYLkEELKIIHRDVKPSNILLD-RNGNIKLCDFGISGQL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 208 VRGEPNVSYICSRYYRAPELI--FGATD-YTSSIDVWSAGCVLAELLLGQPIFPG-DSGVDQLVEIIKvlGTPTR---EQ 280
Cdd:cd06616   161 VDSIAKTRDAGCRPYMAPERIdpSASRDgYDVRSDVWSLGITLYEVATGKFPYPKwNSVFDQLTQVVK--GDPPIlsnSE 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1231802383 281 IREMNPNYTEF-------------KFPQIKAHPWTKVFRPRTPPEAIALCSRL 320
Cdd:cd06616   239 EREFSPSFVNFvnlclikdeskrpKYKELLKHPFIKMYEERNVDVAAYVQKIL 291
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
56-340 5.02e-20

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: 88.87  E-value: 5.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKV-----------LQDKRFKN-RELQIMRKL-DHCNIVRLRYFFYSSG-- 120
Cdd:cd14181    12 YDPKEVIGRGVSSVVRRCVHRHTGQEFAVKIIevtaerlspeqLEEVRSSTlKEIHILRQVsGHPSIITLIDSYESSTfi 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 121 ------EKKDEVYlnlvlDYVPETVyrvarhysrakqTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTA 194
Cdd:cd14181    92 flvfdlMRRGELF-----DYLTEKV------------TLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLD-DQL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 195 VLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATD-----YTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEI 269
Cdd:cd14181   154 HIKLSDFGFSCHLEPGEKLRELCGTPGYLAPEILKCSMDethpgYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMI 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1231802383 270 ikvlgtptreqireMNPNYtEFKFPQikahpWTKvfRPRTPPEAIalcSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd14181   234 --------------MEGRY-QFSSPE-----WDD--RSSTVKDLI---SRLLVVDPEIRLTAEQALQHPFF 279
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
55-301 5.42e-20

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: 88.60  E-value: 5.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  55 SYTDTKVIGNGSFGVVYQAKLCDSGELVAIK-----KVLQDKRFKNR-------ELQIM---RKLDHCNIVRLRYFFyss 119
Cdd:cd14004     1 DYTILKEMGEGAYGQVNLAIYKSKGKEVVIKfifkeRILVDTWVRDRklgtvplEIHILdtlNKRSHPNIVKLLDFF--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 120 gEKKDEVYLNLV--------LDYVpETVYRVARHYSRAkqtlpvIYVklymyQLFRSLAYIHSFGICHRDIKPQNLLLDP 191
Cdd:cd14004    78 -EDDEFYYLVMEkhgsgmdlFDFI-ERKPNMDEKEAKY------IFR-----QVADAVKHLHDQGIVHRDIKDENVILDG 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 192 DTAVlKLCDFGSAKQLVRGePNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQ-PIFPGDSGVDQLVEII 270
Cdd:cd14004   145 NGTI-KLIDFGSAAYIKSG-PFDTFVGTIDYAAPEVLRGNPYGGKEQDIWALGVLLYTLVFKEnPFYNIEEILEADLRIP 222
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1231802383 271 KVLGTPTREQIREM-NPNYTE-FKFPQIKAHPW 301
Cdd:cd14004   223 YAVSEDLIDLISRMlNRDVGDrPTIEELLTDPW 255
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
62-258 7.01e-20

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: 88.87  E-value: 7.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNR-----ELQIMRKLDHCNIVRLRYffyssgekkdevylnlvldyVP 136
Cdd:cd14038     2 LGTGGFGNVLRWINQETGEQVAIKQCRQELSPKNRerwclEIQIMKRLNHPNVVAARD--------------------VP 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 137 ETVYRVArhysraKQTLPVIYVKL--------YMYQL------------------FRSLAYIHSFGICHRDIKPQNLLLD 190
Cdd:cd14038    62 EGLQKLA------PNDLPLLAMEYcqggdlrkYLNQFenccglregailtllsdiSSALRYLHENRIIHRDLKPENIVLQ 135
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1231802383 191 PDTAVL--KLCDFGSAKQLVRGEPNVSYICSRYYRAPELIfGATDYTSSIDVWSAGCVLAELLLG-QPIFP 258
Cdd:cd14038   136 QGEQRLihKIIDLGYAKELDQGSLCTSFVGTLQYLAPELL-EQQKYTVTVDYWSFGTLAFECITGfRPFLP 205
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
56-251 7.36e-20

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: 88.32  E-value: 7.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRlrYFFYSSGEkkdevylnlvlDYV 135
Cdd:cd14047     8 FKEIELIGSGGFGQVFKAKHRIDGKTYAIKRVKLNNEKAEREVKALAKLDHPNIVR--YNGCWDGF-----------DYD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 136 PETVY----RVARHY-------------------SRAKQTLPVIYVKLYmYQLFRSLAYIHSFGICHRDIKPQNLLLDpD 192
Cdd:cd14047    75 PETSSsnssRSKTKClfiqmefcekgtleswiekRNGEKLDKVLALEIF-EQITKGVEYIHSKKLIHRDLKPSNIFLV-D 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1231802383 193 TAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELiFGATDYTSSIDVWSAGCVLAELL 251
Cdd:cd14047   153 TGKVKIGDFGLVTSLKNDGKRTKSKGTLSYMSPEQ-ISSQDYGKEVDIYALGLILFELL 210
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
60-340 8.96e-20

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: 88.95  E-value: 8.96e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIK----KVLQDKR------FKNRELQIMRkldHCNIVRLRYFFyssgEKKDevYLN 129
Cdd:cd05571     1 KVLGKGTFGKVILCREKATGELYAIKilkkEVIIAKDevahtlTENRVLQNTR---HPFLTSLKYSF----QTND--RLC 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 LVLDYVP--ETVYrvarHYSRAKqTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQL 207
Cdd:cd05571    72 FVMEYVNggELFF----HLSRER-VFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHI-KITDFGLCKEE 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 208 VR-GEPNVSYICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQ-PIFPGDSgvDQLVEIIKVlgtptreqiremn 285
Cdd:cd05571   146 ISyGATTKTFCGTPEYLAPEVLED-NDYGRAVDWWGLGVVMYEMMCGRlPFYNRDH--EVLFELILM------------- 209
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 286 pnyTEFKFPqikahpwtkvfrPRTPPEAIALCSRLLEYTPTARL-----TPLEACAHSFF 340
Cdd:cd05571   210 ---EEVRFP------------STLSPEAKSLLAGLLKKDPKKRLgggprDAKEIMEHPFF 254
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
49-348 1.03e-19

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: 88.95  E-value: 1.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  49 DRPQEVsYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN-------RELQIMRKLDHCNIVRLRyffyssGE 121
Cdd:cd06635    21 EDPEKL-FSDLREIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNekwqdiiKEVKFLQRIKHPNSIEYK------GC 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 122 KKDEVYLNLVLDYVPETVYRVARHYsraKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDF 201
Cdd:cd06635    94 YLREHTAWLVMEYCLGSASDLLEVH---KKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLT-EPGQVKLADF 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 202 GSAKQLvrgEPNVSYICSRYYRAPELIFGATD--YTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIikvlgtptre 279
Cdd:cd06635   170 GSASIA---SPANSFVGTPYWMAPEVILAMDEgqYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHI---------- 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1231802383 280 qiremnpnyTEFKFPQIKAHPWTKVFRprtppeaiALCSRLLEYTPTARLTPLEACAHSFFDELRDPNV 348
Cdd:cd06635   237 ---------AQNESPTLQSNEWSDYFR--------NFVDSCLQKIPQDRPTSEELLKHMFVLRERPETV 288
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
62-254 1.06e-19

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: 87.16  E-value: 1.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLcdSGELVAIKKVlqdKRFKNRELQIMRKLDHCNIVRLRyffyssGEKKDEVYLNLVLDYVPE-TVY 140
Cdd:cd14059     1 LGSGAQGAVFLGKF--RGEEVAVKKV---RDEKETDIKHLRKLNHPNIIKFK------GVCTQAPCYCILMEYCPYgQLY 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 141 RVARhysRAKQTLPVIYVKLYMyQLFRSLAYIHSFGICHRDIKPQNLLLDPDTaVLKLCDFGSAKQLVRGEPNVSYICSR 220
Cdd:cd14059    70 EVLR---AGREITPSLLVDWSK-QIASGMNYLHLHKIIHRDLKSPNVLVTYND-VLKISDFGTSKELSEKSTKMSFAGTV 144
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1231802383 221 YYRAPELIFGATdYTSSIDVWSAGCVLAELLLGQ 254
Cdd:cd14059   145 AWMAPEVIRNEP-CSEKVDIWSFGVVLWELLTGE 177
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
56-253 1.10e-19

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: 87.52  E-value: 1.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN---RELQIMRKLDHCNIVRLRYFFYSSgekkdeVYLNLVL 132
Cdd:cd14662     2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIERGLKIDEnvqREIINHRSLRHPNIIRFKEVVLTP------THLAIVM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 DYVP--ETVYRV--ARHYSRAKqtlpviyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAV-LKLCDFGSAKQL 207
Cdd:cd14662    76 EYAAggELFERIcnAGRFSEDE-------ARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAPrLKICDFGYSKSS 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1231802383 208 VRGEPNVSYICSRYYRAPElIFGATDYTSSI-DVWSAGCVLAELLLG 253
Cdd:cd14662   149 VLHSQPKSTVGTPAYIAPE-VLSRKEYDGKVaDVWSCGVTLYVMLVG 194
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
61-251 1.21e-19

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: 88.03  E-value: 1.21e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  61 VIGNGSFGVVyqaKLC-------DSGELVAIKKVLQD----KRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKdevyLN 129
Cdd:cd05081    11 QLGKGNFGSV---ELCrydplgdNTGALVAVKQLQHSgpdqQRDFQREIQILKALHSDFIVKYRGVSYGPGRRS----LR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 LVLDYVPETVYRvaRHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQL-- 207
Cdd:cd05081    84 LVMEYLPSGCLR--DFLQRHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHV-KIADFGLAKLLpl 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1231802383 208 -----VRGEPNVSYIcsrYYRAPELIFGATdYTSSIDVWSAGCVLAELL 251
Cdd:cd05081   161 dkdyyVVREPGQSPI---FWYAPESLSDNI-FSRQSDVWSFGVVLYELF 205
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
56-260 1.50e-19

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: 87.22  E-value: 1.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVlqDKR---------FKNRELQIMRKLDHCNIVRLRYFFYSSGEKkdeV 126
Cdd:cd14164     2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIV--DRRraspdfvqkFLPRELSILRRVNHPNIVQMFECIEVANGR---L 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 127 YLnlvldyVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSAKQ 206
Cdd:cd14164    77 YI------VMEAAATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDRKIKIADFGFARF 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1231802383 207 lVRGEPNVS--YICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGD 260
Cdd:cd14164   151 -VEDYPELSttFCGSRAYTPPEVILGTPYDPKKYDVWSLGVVLYVMVTGTMPFDET 205
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
56-257 1.84e-19

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: 87.65  E-value: 1.84e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKvLQDKRFKNR--------ELQIMRKLDHCNIVRLRYFFyssgEKKDEVY 127
Cdd:cd05607     4 FYEFRVLGKGGFGEVCAVQVKNTGQMYACKK-LDKKRLKKKsgekmallEKEILEKVNSPFIVSLAYAF----ETKTHLC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 128 LNLVLDYVPETVYRVarhYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQL 207
Cdd:cd05607    79 LVMSLMNGGDLKYHI---YNVGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLD-DNGNCRLSDLGLAVEV 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1231802383 208 VRGEPNVSYICSRYYRAPElIFGATDYTSSIDVWSAGCVLAELLLGQPIF 257
Cdd:cd05607   155 KEGKPITQRAGTNGYMAPE-ILKEESYSYPVDWFAMGCSIYEMVAGRTPF 203
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
62-301 2.05e-19

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: 87.03  E-value: 2.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVyqaKLCDSGE---LVAIKkVLQDKRFKN----------------------------RELQIMRKLDHCNIV 110
Cdd:cd14118     2 IGKGSYGIV---KLAYNEEdntLYAMK-ILSKKKLLKqagffrrppprrkpgalgkpldpldrvyREIAILKKLDHPNVV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 111 RLRYFFyssgEKKDEVYLNLVLDYVPE-TVYRV----------ARHYSRakqtlpviyvklymyQLFRSLAYIHSFGICH 179
Cdd:cd14118    78 KLVEVL----DDPNEDNLYMVFELVDKgAVMEVptdnplseetARSYFR---------------DIVLGIEYLHYQKIIH 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 180 RDIKPQNLLLDPDTAVlKLCDFGSAKQLVRGEPNVSYIC-SRYYRAPELIFGATDYTS--SIDVWSAGCVLAELLLGQPI 256
Cdd:cd14118   139 RDIKPSNLLLGDDGHV-KIADFGVSNEFEGDDALLSSTAgTPAFMAPEALSESRKKFSgkALDIWAMGVTLYCFVFGRCP 217
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1231802383 257 FPgDSGVDQLVEIIK----------VLGTPTREQIREM---NPNyTEFKFPQIKAHPW 301
Cdd:cd14118   218 FE-DDHILGLHEKIKtdpvvfpddpVVSEQLKDLILRMldkNPS-ERITLPEIKEHPW 273
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
55-336 2.06e-19

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: 86.79  E-value: 2.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  55 SYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVlqDKR--------FKN--RELQIMRKLDHCNIVRLryffYSSGEKKD 124
Cdd:cd14070     3 SYLIGRKLGEGSFAKVREGLHAVTGEKVAIKVI--DKKkakkdsyvTKNlrREGRIQQMIRHPNITQL----LDILETEN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 125 EVYLNLVLDYVPETVYRVARhysraKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFG-- 202
Cdd:cd14070    77 SYYLVMELCPGGNLMHRIYD-----KKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNI-KLIDFGls 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 203 -SAKQLVRGEPNVSYICSRYYRAPELIfGATDYTSSIDVWSAGCVLAELLLGQPIFPgdsgvdqlVEIIKVLGTPTREQI 281
Cdd:cd14070   151 nCAGILGYSDPFSTQCGSPAYAAPELL-ARKKYGPKVDVWSIGVNMYAMLTGTLPFT--------VEPFSLRALHQKMVD 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1231802383 282 REMNPnytefkfpqikahpwtkvFRPRTPPEAIALCSRLLEYTPTARLTPLEACA 336
Cdd:cd14070   222 KEMNP------------------LPTDLSPGAISFLRSLLEPDPLKRPNIKQALA 258
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
55-250 2.17e-19

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: 86.59  E-value: 2.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  55 SYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQdkRFKNRELQImRKLD----------HCNIVRlryfFYSSGEKKD 124
Cdd:cd14050     2 CFTILSKLGEGSFGEVFKVRSREDGKLYAVKRSRS--RFRGEKDRK-RKLEeverheklgeHPNCVR----FIKAWEEKG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 125 EVYLNLvldyvpETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKLCDFGSA 204
Cdd:cd14050    75 ILYIQT------ELCDTSLQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKD-GVCKLGDFGLV 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1231802383 205 KQLvrGEPNVSYIC---SRYYrAPELIFGatDYTSSIDVWSAGCVLAEL 250
Cdd:cd14050   148 VEL--DKEDIHDAQegdPRYM-APELLQG--SFTKAADIFSLGITILEL 191
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
151-340 2.25e-19

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK3 is predominantly expressed in mature spermatozoa, and might play a role in the fertilization process. 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 CLK3 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: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 88.14  E-value: 2.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 151 QTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLL---DPDT---------------AVLKLCDFGSAKqlVRGEP 212
Cdd:cd14214   112 QPYPLPHIRHMAYQLCHALKFLHENQLTHTDLKPENILFvnsEFDTlynesksceeksvknTSIRVADFGSAT--FDHEH 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 213 NVSYICSRYYRAPELIFgATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREM-------- 284
Cdd:cd14214   190 HTTIVATRHYRPPEVIL-ELGWAQPCDVWSLGCILFEYYRGFTLFQTHENREHLVMMEKILGPIPSHMIHRTrkqkyfyk 268
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1231802383 285 -----NPNYTEFKFPQIKAHPwTKVFRPRTPPEAIA---LCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd14214   269 gslvwDENSSDGRYVSENCKP-LMSYMLGDSLEHTQlfdLLRRMLEFDPALRITLKEALLHPFF 331
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
62-337 2.38e-19

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: 86.51  E-value: 2.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKV----LQDKRFKNRELQIMRKLDHCNIVRLryffYSSGEKKDEVYlnLVLDYVP- 136
Cdd:cd14103     1 LGRGKFGTVYRCVEKATGKELAAKFIkcrkAKDREDVRNEIEIMNQLRHPRLLQL----YDAFETPREMV--LVMEYVAg 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 137 -ETVYRVARHysraKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLL-LDPDTAVLKLCDFGSAKQLVRGEPnV 214
Cdd:cd14103    75 gELFERVVDD----DFELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILcVSRTGNQIKIIDFGLARKYDPDKK-L 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 215 SYIC-SRYYRAPELI-FGATDYTSsiDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVlgtptreqiremNPNYTEFK 292
Cdd:cd14103   150 KVLFgTPEFVAPEVVnYEPISYAT--DMWSVGVICYVLLSGLSPFMGDNDAETLANVTRA------------KWDFDDEA 215
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1231802383 293 FPQIKahpwtkvfrprtpPEAIALCSRLLEYTPTARLTPLEACAH 337
Cdd:cd14103   216 FDDIS-------------DEAKDFISKLLVKDPRKRMSAAQCLQH 247
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
60-251 2.90e-19

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: 86.99  E-value: 2.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVV----YQAKLCDSGELVAIKKVLQDK----RFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKdevyLNLV 131
Cdd:cd14205    10 QQLGKGNFGSVemcrYDPLQDNTGEVVAVKKLQHSTeehlRDFEREIEILKSLQHDNIVKYKGVCYSAGRRN----LRLI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 132 LDYVPetvYRVARHY-SRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLVRG 210
Cdd:cd14205    86 MEYLP---YGSLRDYlQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRV-KIGDFGLTKVLPQD 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1231802383 211 -------EPNVSYIcsrYYRAPELIfGATDYTSSIDVWSAGCVLAELL 251
Cdd:cd14205   162 keyykvkEPGESPI---FWYAPESL-TESKFSVASDVWSFGVVLYELF 205
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
56-257 3.27e-19

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: 86.22  E-value: 3.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFK-------NRELQIMRKLDHCNIVRLRYFFyssgEKKDEVYL 128
Cdd:cd14188     3 YCRGKVLGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVSKphqrekiDKEIELHRILHHKHVVQFYHYF----EDKENIYI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 129 nlVLDYVPEtvyRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQLV 208
Cdd:cd14188    79 --LLEYCSR---RSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFIN-ENMELKVGDFGLAARLE 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1231802383 209 RGEPNVSYIC-SRYYRAPElIFGATDYTSSIDVWSAGCVLAELLLGQPIF 257
Cdd:cd14188   153 PLEHRRRTICgTPNYLSPE-VLNKQGHGCESDIWALGCVMYTMLLGRPPF 201
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
60-340 3.69e-19

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: 86.64  E-value: 3.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKvLQDKRFKNR--------ELQIMRKLDHCNIVRLRYFFyssgEKKDEVYLNLV 131
Cdd:cd05605     6 RVLGKGGFGEVCACQVRATGKMYACKK-LEKKRIKKRkgeamalnEKQILEKVNSRFVVSLAYAY----ETKDALCLVLT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 132 LDYVPETVYRVarhYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQLVRGE 211
Cdd:cd05605    81 IMNGGDLKFHI---YNMGNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLD-DHGHVRISDLGLAVEIPEGE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 212 PNVSYICSRYYRAPELIfGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSgvdqlvEIIKvlgtptREQ----IREMNPN 287
Cdd:cd05605   157 TIRGRVGTVGYMAPEVV-KNERYTFSPDWWGLGCLIYEMIEGQAPFRARK------EKVK------REEvdrrVKEDQEE 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1231802383 288 YTEfKFpqikahpwtkvfrprtPPEAIALCSRLLEYTPTARL-----TPLEACAHSFF 340
Cdd:cd05605   224 YSE-KF----------------SEEAKSICSQLLQKDPKTRLgcrgeGAEDVKSHPFF 264
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
61-343 3.80e-19

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: 87.24  E-value: 3.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  61 VIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQ-------IMRKLDHCNIVRLRYFFYSSGEkkdevyLNLVLD 133
Cdd:cd05585     1 VIGKGSFGKVMQVRKKDTSRIYALKTIRKAHIVSRSEVThtlaertVLAQVDCPFIVPLKFSFQSPEK------LYLVLA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 134 YVP--ETVYRVARH----YSRAKqtlpviyvkLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPdTAVLKLCDFGSAKQL 207
Cdd:cd05585    75 FINggELFHHLQREgrfdLSRAR---------FYTAELLCALECLHKFNVIYRDLKPENILLDY-TGHIALCDFGLCKLN 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 208 VRGEPNVSYIC-SRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIFPgDSGVDQLVEiiKVLGTPTReqiremnp 286
Cdd:cd05585   145 MKDDDKTNTFCgTPEYLAPELLLG-HGYTKAVDWWTLGVLLYEMLTGLPPFY-DENTNEMYR--KILQEPLR-------- 212
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 287 nytefkfpqikahpwtkvFRPRTPPEAIALCSRLLEYTPTARL---TPLEACAHSFFDEL 343
Cdd:cd05585   213 ------------------FPDGFDRDAKDLLIGLLNRDPTKRLgynGAQEIKNHPFFDQI 254
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
55-301 3.91e-19

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: 86.38  E-value: 3.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  55 SYTDTKVIGNGSFGVV-----YQAKLCDSGELVAIKKVLQDKRFKN-------RELQIMRKLDHCNIVRLRYFFYSSGek 122
Cdd:cd14076     2 PYILGRTLGEGEFGKVklgwpLPKANHRSGVQVAIKLIRRDTQQENcqtskimREINILKGLTHPNIVRLLDVLKTKK-- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 123 kdevYLNLVLDYVPETV---YRVARHYSRAKQTlpviyVKLYMyQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLkLC 199
Cdd:cd14076    80 ----YIGIVLEFVSGGElfdYILARRRLKDSVA-----CRLFA-QLISGVAYLHKKGVVHRDLKLENLLLDKNRNLV-IT 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 200 DFGSAKQLVRGEPNV-SYIC-SRYYRAPELIFGATDYT-SSIDVWSAGCVLAELLLGQPIF---PGDSGVDQLVEIIK-V 272
Cdd:cd14076   149 DFGFANTFDHFNGDLmSTSCgSPCYAAPELVVSDSMYAgRKADIWSCGVILYAMLAGYLPFdddPHNPNGDNVPRLYRyI 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1231802383 273 LGTP----------TREQIREM---NPNYtEFKFPQIKAHPW 301
Cdd:cd14076   229 CNTPlifpeyvtpkARDLLRRIlvpNPRK-RIRLSAIMRHAW 269
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
56-269 5.64e-19

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: 85.72  E-value: 5.64e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKV---LQDKRFKNRELQIMRKLDHCNIVrlryFFYSSGEKKDEVYLNLVL 132
Cdd:cd14108     4 YDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIpvrAKKKTSARRELALLAELDHKSIV----RFHDAFEKRRVVIIVTEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 dYVPETVYRVARhysraKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLL-DPDTAVLKLCDFGSAKQLVRGE 211
Cdd:cd14108    80 -CHEELLERITK-----RPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMaDQKTDQVRICDFGNAQELTPNE 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1231802383 212 PNVSYICSRYYRAPElIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEI 269
Cdd:cd14108   154 PQYCKYGTPEFVAPE-IVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNI 210
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
48-291 6.08e-19

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: 85.75  E-value: 6.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  48 PDRpqevSYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKV-LQDKRFKN---RELQIMRKLDHCNIVRlryfFYSSGEKK 123
Cdd:cd06647     5 PKK----KYTRFEKIGQGASGTVYTAIDVATGQEVAIKQMnLQQQPKKEliiNEILVMRENKNPNIVN----YLDSYLVG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 124 DEVYLNL-------VLDYVPETVYRVARHYSRAKQTLpviyvklymyqlfRSLAYIHSFGICHRDIKPQNLLLDPDTAVl 196
Cdd:cd06647    77 DELWVVMeylaggsLTDVVTETCMDEGQIAAVCRECL-------------QALEFLHSNQVIHRDIKSDNILLGMDGSV- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 197 KLCDFGSAKQLVRGEPNVS-YICSRYYRAPELIfGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVeIIKVLGT 275
Cdd:cd06647   143 KLTDFGFCAQITPEQSKRStMVGTPYWMAPEVV-TRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALY-LIATNGT 220
                         250
                  ....*....|....*.
gi 1231802383 276 PTREQIREMNPNYTEF 291
Cdd:cd06647   221 PELQNPEKLSAIFRDF 236
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
46-281 6.61e-19

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: 85.52  E-value: 6.61e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  46 QGPDRPqeVSYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNR---------ELQIMRKLDHCNIVRlryfF 116
Cdd:cd06651     1 KSPSAP--INWRRGKLLGQGAFGRVYLCYDVDTGRELAAKQVQFDPESPETskevsalecEIQLLKNLQHERIVQ----Y 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 117 YSSGEKKDEVYLNLVLDYVPE-TVYRVARHYSRAKQTLpviyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAV 195
Cdd:cd06651    75 YGCLRDRAEKTLTIFMEYMPGgSVKDQLKAYGALTESV----TRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNV 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 196 lKLCDFGSAKQL----VRGEPNVSYICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIFpgdSGVDQLVEIIK 271
Cdd:cd06651   151 -KLGDFGASKRLqticMSGTGIRSVTGTPYWMSPEVISG-EGYGRKADVWSLGCTVVEMLTEKPPW---AEYEAMAAIFK 225
                         250
                  ....*....|
gi 1231802383 272 VLGTPTREQI 281
Cdd:cd06651   226 IATQPTNPQL 235
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
62-323 8.22e-19

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: 8.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVA-------IKKVLQDKRFknRELQIMRKLDHCNIVRLRYFFYSSGE------KKDEVYL 128
Cdd:cd06650    13 LGAGNGGVVFKVSHKPSGLVMArklihleIKPAIRNQII--RELQVLHECNSPYIVGFYGAFYSDGEisicmeHMDGGSL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 129 NLVLD---YVPETVYrvarhysrAKQTLPVIyvklymyqlfRSLAYI-HSFGICHRDIKPQNLLLDpDTAVLKLCDFGSA 204
Cdd:cd06650    91 DQVLKkagRIPEQIL--------GKVSIAVI----------KGLTYLrEKHKIMHRDVKPSNILVN-SRGEIKLCDFGVS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 205 KQLVRGEPNvSYICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQ-PIFPGDSGVDQLVEIIKVLGTPTREQIRe 283
Cdd:cd06650   152 GQLIDSMAN-SFVGTRSYMSPERLQG-THYSVQSDIWSMGLSLVEMAVGRyPIPPPDAKELELMFGCQVEGDAAETPPR- 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1231802383 284 mnpnytefkfPQIKAHPWTKVFRPRTPPEAIAlcsRLLEY 323
Cdd:cd06650   229 ----------PRTPGRPLSSYGMDSRPPMAIF---ELLDY 255
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
62-273 8.97e-19

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: 85.24  E-value: 8.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLcDSGELVAIKKVL------QDKRFKnRELQIMRKLDHCNIVRLRYFFYSSGEKKdevylnLVLDYV 135
Cdd:cd14664     1 IGRGGAGTVYKGVM-PNGTLVAVKRLKgegtqgGDHGFQ-AEIQTLGMIRHRNIVRLRGYCSNPTTNL------LVYEYM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 136 PETVYRVARHySRAKQTLPVIYVKLYMYQL--FRSLAYIH---SFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLVRG 210
Cdd:cd14664    73 PNGSLGELLH-SRPESQPPLDWETRQRIALgsARGLAYLHhdcSPLIIHRDVKSNNILLDEEFEA-HVADFGLAKLMDDK 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1231802383 211 EPNVSYIC--SRYYRAPELIF-GATDYTSsiDVWSAGCVLAELLLGQ-PI--FPGDSGVDqLVEIIKVL 273
Cdd:cd14664   151 DSHVMSSVagSYGYIAPEYAYtGKVSEKS--DVYSYGVVLLELITGKrPFdeAFLDDGVD-IVDWVRGL 216
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
60-352 9.81e-19

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: 85.90  E-value: 9.81e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQ---IMRKL-----DHCNIVRLRYFFYSsgekkdEVYLNLV 131
Cdd:cd05592     1 KVLGKGSFGKVMLAELKGTNQYFAIKALKKDVVLEDDDVEctmIERRVlalasQHPFLTHLFCTFQT------ESHLFFV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 132 LDYVP--ETVYRVARH----YSRAKqtlpviyvkLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAK 205
Cdd:cd05592    75 MEYLNggDLMFHIQQSgrfdEDRAR---------FYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHI-KIADFGMCK 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 206 QLVRGEPNVSYIC-SRYYRAPELIFGATdYTSSIDVWSAGCVLAELLLGQPIFPGDsGVDQLVEIIkvlgtptreqireM 284
Cdd:cd05592   145 ENIYGENKASTFCgTPDYIAPEILKGQK-YNQSVDWWSFGVLLYEMLIGQSPFHGE-DEDELFWSI-------------C 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 285 NpnytefkfpqikahpwTKVFRPRT-PPEAIALCSRLLEYTPTARL-TPLEAC----AHSFFD-------ELRD------ 345
Cdd:cd05592   210 N----------------DTPHYPRWlTKEAASCLSLLLERNPEKRLgVPECPAgdirDHPFFKtidwdklERREidppfk 273

                  ....*..
gi 1231802383 346 PNVKLPN 352
Cdd:cd05592   274 PKVKSAN 280
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
60-257 9.84e-19

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: 86.22  E-value: 9.84e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKkVLQDKRF--KNRELQIM-------RKLDHCNIVRLRYFFYSSgekkDEVYLnl 130
Cdd:cd05602    13 KVIGKGSFGKVLLARHKSDEKFYAVK-VLQKKAIlkKKEEKHIMsernvllKNVKHPFLVGLHFSFQTT----DKLYF-- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 VLDYVP--ETVYrvarHYSRAKQTLPViYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLkLCDFGSAKQLV 208
Cdd:cd05602    86 VLDYINggELFY----HLQRERCFLEP-RARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIV-LTDFGLCKENI 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1231802383 209 RGEPNVSYIC-SRYYRAPELIFgATDYTSSIDVWSAGCVLAELLLGQPIF 257
Cdd:cd05602   160 EPNGTTSTFCgTPEYLAPEVLH-KQPYDRTVDWWCLGAVLYEMLYGLPPF 208
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
61-337 1.11e-18

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: 84.89  E-value: 1.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  61 VIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFK---NRELQIMRKLDHCNIVRLRYFFyssgEKKDEVYLNLVLDYVPE 137
Cdd:cd14087     8 LIGRGSFSRVVRVEHRVTRQPYAIKMIETKCRGRevcESELNVLRRVRHTNIIQLIEVF----ETKERVYMVMELATGGE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 138 TVYRVARHYSRAKQTLPVIyvkLYMyqLFRSLAYIHSFGICHRDIKPQNLLL---DPDTAVLkLCDFGSAKQLVRGEPN- 213
Cdd:cd14087    84 LFDRIIAKGSFTERDATRV---LQM--VLDGVKYLHGLGITHRDLKPENLLYyhpGPDSKIM-ITDFGLASTRKKGPNCl 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 214 VSYIC-SRYYRAPELIFgATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVlgtptreqiremnpNYTefk 292
Cdd:cd14087   158 MKTTCgTPEYIAPEILL-RKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRA--------------KYS--- 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1231802383 293 fpqIKAHPWtkvfrPRTPPEAIALCSRLLEYTPTARLTPLEACAH 337
Cdd:cd14087   220 ---YSGEPW-----PSVSNLAKDFIDRLLTVNPGERLSATQALKH 256
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
56-271 1.38e-18

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: 84.48  E-value: 1.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKV------LQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEkkdevyLN 129
Cdd:cd08218     2 YVRIKKIGEGSFGKALLVKSKEDGKQYVIKEIniskmsPKEREESRKEVAVLSKMKHPNIVQYQESFEENGN------LY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 LVLDYVpETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKLCDFGSAKQL-V 208
Cdd:cd08218    76 IVMDYC-DGGDLYKRINAQRGVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKD-GIIKLGDFGIARVLnS 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1231802383 209 RGEPNVSYICSRYYRAPElIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIK 271
Cdd:cd08218   154 TVELARTCIGTPYYLSPE-ICENKPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKIIR 215
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
60-247 1.40e-18

Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GAK, also called auxilin-2, contains an N-terminal kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of PTEN-like, clathrin-binding, and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor. It also interacts with the androgen receptor, acting as a transcriptional coactivator, and its expression is significantly increased with the progression of prostate cancer. The GAK 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: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 84.87  E-value: 1.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN----RELQIMRKLD-HCNIVRlryfFYS--------SGEKKDEV 126
Cdd:cd14036     6 RVIAEGGFAFVYEAQDVGTGKEYALKRLLSNEEEKNkaiiQEINFMKKLSgHPNIVQ----FCSaasigkeeSDQGQAEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 127 YL--NLVLDYVPETVYRVarhysRAKQTLPVIYVKLYMYQLFRSLAYIH--SFGICHRDIKPQNLLLDPDTAVlKLCDFG 202
Cdd:cd14036    82 LLltELCKGQLVDFVKKV-----EAPGPFSPDTVLKIFYQTCRAVQHMHkqSPPIIHRDLKIENLLIGNQGQI-KLCDFG 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 203 SAKQLV-----------RG--EPNVSYICSRYYRAPELIFGATDY--TSSIDVWSAGCVL 247
Cdd:cd14036   156 SATTEAhypdyswsaqkRSlvEDEITRNTTPMYRTPEMIDLYSNYpiGEKQDIWALGCIL 215
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
59-354 1.80e-18

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: 85.09  E-value: 1.80e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  59 TKVIGNGSFGVVYQAKLCDSGELVAIKkVLQDKRFKNRELQIMRKLDHC-NIVRLRyffyssgekkdEVYLNL-----VL 132
Cdd:cd14170     7 SQVLGLGINGKVLQIFNKRTQEKFALK-MLQDCPKARREVELHWRASQCpHIVRIV-----------DVYENLyagrkCL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 DYVPETV---YRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPD--TAVLKLCDFGSAKQL 207
Cdd:cd14170    75 LIVMECLdggELFSRIQDRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKrpNAILKLTDFGFAKET 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 208 VRGEPNVSYICSRYYRAPElIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVdqlveiikVLGTPTREQIRemnpn 287
Cdd:cd14170   155 TSHNSLTTPCYTPYYVAPE-VLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGL--------AISPGMKTRIR----- 220
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1231802383 288 YTEFKFPQIKahpWTKVfrprtPPEAIALCSRLLEYTPTARLTPLEACAHSFFDE-LRDPNVKLPNGR 354
Cdd:cd14170   221 MGQYEFPNPE---WSEV-----SEEVKMLIRNLLKTEPTQRMTITEFMNHPWIMQsTKVPQTPLHTSR 280
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
60-259 1.82e-18

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: 85.36  E-value: 1.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQimrkldhCNIVRLRYF-----------FYSSGEKKDEVYL 128
Cdd:cd05619    11 KMLGKGSFGKVFLAELKGTNQFFAIKALKKDVVLMDDDVE-------CTMVEKRVLslawehpflthLFCTFQTKENLFF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 129 nlVLDYVP--ETVYRVArhySRAKQTLPviYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQ 206
Cdd:cd05619    84 --VMEYLNggDLMFHIQ---SCHKFDLP--RATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHI-KIADFGMCKE 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1231802383 207 LVRGEPNVSYIC-SRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIFPG 259
Cdd:cd05619   156 NMLGDAKTSTFCgTPDYIAPEILLG-QKYNTSVDWWSFGVLLYEMLIGQSPFHG 208
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
62-310 2.11e-18

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: 84.41  E-value: 2.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKV-------LQDKRFknrELQIMRKLDHCNIVRLRYFFYSsgEKKDEVYLNL---- 130
Cdd:cd06611    13 LGDGAFGKVYKAQHKETGLFAAAKIIqieseeeLEDFMV---EIDILSECKHPNIVGLYEAYFY--ENKLWILIEFcdgg 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 VLDYVPETVYRVarhysrakqtLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFG-SAKQLVR 209
Cdd:cd06611    88 ALDSIMLELERG----------LTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDV-KLADFGvSAKNKST 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 210 GEPNVSYICSRYYRAPELIFGATD----YTSSIDVWSAGCVLAELLLGQPifPgDSGVDQLVEIIKVLGT--PTREQIRE 283
Cdd:cd06611   157 LQKRDTFIGTPYWMAPEVVACETFkdnpYDYKADIWSLGITLIELAQMEP--P-HHELNPMRVLLKILKSepPTLDQPSK 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1231802383 284 MNPNYTEF------KFPQIKA-------HPWTKVFRPRTP 310
Cdd:cd06611   234 WSSSFNDFlksclvKDPDDRPtaaellkHPFVSDQSDNKA 273
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
162-330 2.85e-18

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: 83.89  E-value: 2.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 162 MYQLFRSLAYIHSFGICHRDIKPQNLLLDP--DTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPElIFGATDYTSSID 239
Cdd:cd14172   109 MRDIGTAIQYLHSMNIAHRDVKPENLLYTSkeKDAVLKLTDFGFAKETTVQNALQTPCYTPYYVAPE-VLGPEKYDKSCD 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 240 VWSAGCVLAELLLGQPIFPGDSGvdqlveiiKVLGTPTREQIRemnpnYTEFKFPqikAHPWTKVfrprtPPEAIALCSR 319
Cdd:cd14172   188 MWSLGVIMYILLCGFPPFYSNTG--------QAISPGMKRRIR-----MGQYGFP---NPEWAEV-----SEEAKQLIRH 246
                         170
                  ....*....|.
gi 1231802383 320 LLEYTPTARLT 330
Cdd:cd14172   247 LLKTDPTERMT 257
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
62-351 2.94e-18

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: 84.01  E-value: 2.94e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKV------LQDKRFKNrELQIMRKLDHC-NIVRlryfFYSSGEKKDEVYLNL-VLD 133
Cdd:cd06617     9 LGRGAYGVVDKMRHVPTGTIMAVKRIratvnsQEQKRLLM-DLDISMRSVDCpYTVT----FYGALFREGDVWICMeVMD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 134 yvpETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHS-FGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLVRGEP 212
Cdd:cd06617    84 ---TSLDKFYKKVYDKGLTIPEDILGKIAVSIVKALEYLHSkLSVIHRDVKPSNVLINRNGQV-KLCDFGISGYLVDSVA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 213 NVSYICSRYYRAPELIFGATD---YTSSIDVWSAGCVLAELLLGQpiFPGDSgvdqlveiikvLGTPTrEQIREMnpnyT 289
Cdd:cd06617   160 KTIDAGCKPYMAPERINPELNqkgYDVKSDVWSLGITMIELATGR--FPYDS-----------WKTPF-QQLKQV----V 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 290 EFKFPQIKAHPWTkvfrprtpPEAIALCSRLLEYTPTARLTPLEACAHSFFDELRDPNVKLP 351
Cdd:cd06617   222 EEPSPQLPAEKFS--------PEFQDFVNKCLKKNYKERPNYPELLQHPFFELHLSKNTDVA 275
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
56-300 3.45e-18

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: 85.06  E-value: 3.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKkVLQDKRFKNR--------ELQIMRKLDHCNIVRLRYFFyssgEKKDEVY 127
Cdd:cd05626     3 FVKIKTLGIGAFGEVCLACKVDTHALYAMK-TLRKKDVLNRnqvahvkaERDILAEADNEWVVKLYYSF----QDKDNLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 128 LnlVLDYVP--ETVYRVARhysraKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFG--- 202
Cdd:cd05626    78 F--VMDYIPggDMMSLLIR-----MEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHI-KLTDFGlct 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 203 ------SAKQLVRG--------EPN-------------------------------VSYICSRYYRAPELIFgATDYTSS 237
Cdd:cd05626   150 gfrwthNSKYYQKGshirqdsmEPSdlwddvsncrcgdrlktleqratkqhqrclaHSLVGTPNYIAPEVLL-RKGYTQL 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1231802383 238 IDVWSAGCVLAELLLGQPIFpgdsgvdqlveiikVLGTPTREQIREMNPNYTEFKFPQIKAHP 300
Cdd:cd05626   229 CDWWSVGVILFEMLVGQPPF--------------LAPTPTETQLKVINWENTLHIPPQVKLSP 277
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
56-206 3.85e-18

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 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: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 83.28  E-value: 3.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKkvLQDKRFKN----RELQIMRKLDHCN-IVRLRYFfyssGEKKDEVYlnL 130
Cdd:cd14016     2 YKLVKKIGSGSFGEVYLGIDLKTGEEVAIK--IEKKDSKHpqleYEAKVYKLLQGGPgIPRLYWF----GQEGDYNV--M 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 VLDYVPETVYRVARHYSRA---KQTLPViyvklyMYQLFRSLAYIHSFGICHRDIKPQNLL--LDPDTAVLKLCDFGSAK 205
Cdd:cd14016    74 VMDLLGPSLEDLFNKCGRKfslKTVLML------ADQMISRLEYLHSKGYIHRDIKPENFLmgLGKNSNKVYLIDFGLAK 147

                  .
gi 1231802383 206 Q 206
Cdd:cd14016   148 K 148
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
56-259 3.91e-18

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: 83.08  E-value: 3.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLcDSGELVAIKKVLQDkRFKN--------RELQIMRKLDHCNIVRLRYFFyssgEKKDEVY 127
Cdd:cd14161     5 YEFLETLGKGTYGRVKKARD-SSGRLVAIKSIRKD-RIKDeqdllhirREIEIMSSLNHPHIISVYEVF----ENSSKIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 128 LnlVLDYVPE-TVYrvarHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAkQ 206
Cdd:cd14161    79 I--VMEYASRgDLY----DYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNI-KIADFGLS-N 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1231802383 207 LVRGEPNVSYIC-SRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPG 259
Cdd:cd14161   151 LYNQDKFLQTYCgSPLYASPEIVNGRPYIGPEVDSWSLGVLLYILVHGTMPFDG 204
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
62-257 4.55e-18

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: 83.70  E-value: 4.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLcdSGELVAIKKV-------LQD--KRFkNRELQIMRKLDHCNIVRLryFFYSSGEKKdevyLNLVL 132
Cdd:cd14158    23 LGEGGFGVVFKGYI--NDKNVAVKKLaamvdisTEDltKQF-EQEIQVMAKCQHENLVEL--LGYSCDGPQ----LCLVY 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 DYVPETvyRVARHYSRAKQTLPVIYVKL--YMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQLVRG 210
Cdd:cd14158    94 TYMPNG--SLLDRLACLNDTPPLSWHMRckIAQGTANGINYLHENNHIHRDIKSANILLD-ETFVPKISDFGLARASEKF 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1231802383 211 EPNV---SYICSRYYRAPELIFGatDYTSSIDVWSAGCVLAELLLGQPIF 257
Cdd:cd14158   171 SQTImteRIVGTTAYMAPEALRG--EITPKSDIFSFGVVLLEIITGLPPV 218
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
62-333 5.87e-18

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: 82.76  E-value: 5.87e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKVLQDK-RFKN--RELQIMRKLDHC-NIVRLRYFFYSSgekkDEVYLnLVLDYVPe 137
Cdd:cd13987     1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPStKLKDflREYNISLELSVHpHIIKTYDVAFET----EDYYV-FAQEYAP- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 138 tvYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQN-LLLDPDTAVLKLCDFGSAKQLVRGEPNVSY 216
Cdd:cd13987    75 --YGDLFSIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENvLLFDKDCRRVKLCDFGLTRRVGSTVKRVSG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 217 ICSryYRAPEL--IFGATDYT--SSIDVWSAGCVLAELLLGQpiFPGDSGVDqlveiikvlgtptreqireMNPNYTEF- 291
Cdd:cd13987   153 TIP--YTAPEVceAKKNEGFVvdPSIDVWAFGVLLFCCLTGN--FPWEKADS-------------------DDQFYEEFv 209
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1231802383 292 KFPQIKAHPWTKVFRPRTpPEAIALCSRLLEYTPTARLTPLE 333
Cdd:cd13987   210 RWQKRKNTAVPSQWRRFT-PKALRMFKKLLAPEPERRCSIKE 250
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
62-271 5.94e-18

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: 82.63  E-value: 5.94e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQ---IMRKLDHCNIVRLRYFFyssgEKKDEVYLNLVLDYVPET 138
Cdd:cd14107    10 IGRGTFGFVKRVTHKGNGECCAAKFIPLRSSTRARAFQerdILARLSHRRLTCLLDQF----ETRKTLILILELCSSEEL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 139 VYRVARhysraKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLL-DPDTAVLKLCDFGSAKQLVRGEPNVSYI 217
Cdd:cd14107    86 LDRLFL-----KGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMvSPTREDIKICDFGFAQEITPSEHQFSKY 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1231802383 218 CSRYYRAPELIfGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIK 271
Cdd:cd14107   161 GSPEFVAPEIV-HQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAE 213
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
56-301 7.21e-18

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: 83.02  E-value: 7.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIK----KVLQDKR-FKNRELQIMRKLDHCNIVRLRYFFyssgEKKDEVYLNL 130
Cdd:cd14169     5 YELKEKLGEGAFSEVVLAQERGSQRLVALKcipkKALRGKEaMVENEIAVLRRINHENIVSLEDIY----ESPTHLYLAM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 VLDYVPETVYRV-ARHYSRAKQTLPVIYvklymyQLFRSLAYIHSFGICHRDIKPQNLLLDP--DTAVLKLCDFGSAKql 207
Cdd:cd14169    81 ELVTGGELFDRIiERGSYTEKDASQLIG------QVLQAVKYLHQLGIVHRDLKPENLLYATpfEDSKIMISDFGLSK-- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 208 VRGEPNVSYIC-SRYYRAPELIFGATdYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKV---LGTPTREQIRE 283
Cdd:cd14169   153 IEAQGMLSTACgTPGYVAPELLEQKP-YGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILKAeyeFDSPYWDDISE 231
                         250       260
                  ....*....|....*....|....*...
gi 1231802383 284 MNPNY----------TEFKFPQIKAHPW 301
Cdd:cd14169   232 SAKDFirhllerdpeKRFTCEQALQHPW 259
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
60-251 8.12e-18

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: 82.64  E-value: 8.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVV----YQAKLCDSGELVAIKKVLQDKRFKNR-----ELQIMRKLDHCNIVRLRYFFYSSGEKKdevyLNL 130
Cdd:cd05080    10 RDLGEGHFGKVslycYDPTNDGTGEMVAVKALKADCGPQHRsgwkqEIDILKTLYHENIVKYKGCCSEQGGKS----LQL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 VLDYVPETVYR--VARHYSRAKQTLpviyvkLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLV 208
Cdd:cd05080    86 IMEYVPLGSLRdyLPKHSIGLAQLL------LFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLV-KIGDFGLAKAVP 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1231802383 209 RGEpnvsyicsRYYR------------APELIFGATDYTSSiDVWSAGCVLAELL 251
Cdd:cd05080   159 EGH--------EYYRvredgdspvfwyAPECLKEYKFYYAS-DVWSFGVTLYELL 204
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
60-329 8.96e-18

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: 82.73  E-value: 8.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKvLQDKRFKNR--------ELQIMRKLDHCNIVRLRYFFyssgEKKDEVYLNLV 131
Cdd:cd05631     6 RVLGKGGFGEVCACQVRATGKMYACKK-LEKKRIKKRkgeamalnEKRILEKVNSRFVVSLAYAY----ETKDALCLVLT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 132 LDYVPETVYRVarhYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQLVRGE 211
Cdd:cd05631    81 IMNGGDLKFHI---YNMGNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLD-DRGHIRISDLGLAVQIPEGE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 212 PNVSYICSRYYRAPELIfGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGvdqlveiiKVLGTPTREQIREMNPNYTEf 291
Cdd:cd05631   157 TVRGRVGTVGYMAPEVI-NNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKE--------RVKREEVDRRVKEDQEEYSE- 226
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1231802383 292 KFPQikahpwtkvfrprtppEAIALCSRLLEYTPTARL 329
Cdd:cd05631   227 KFSE----------------DAKSICRMLLTKNPKERL 248
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
60-271 9.83e-18

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: 82.74  E-value: 9.83e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLC---DSGELVAIK-----------KVLQDKRFKNRELQIMRKLDHcnIVRLRYFFyssgekKDE 125
Cdd:cd05613     6 KVLGTGAYGKVFLVRKVsghDAGKLYAMKvlkkativqkaKTAEHTRTERQVLEHIRQSPF--LVTLHYAF------QTD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 126 VYLNLVLDYVPETvyRVARHYSRaKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLkLCDFGSAK 205
Cdd:cd05613    78 TKLHLILDYINGG--ELFTHLSQ-RERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVV-LTDFGLSK 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1231802383 206 QLVRGEPNVSY-ICSRY-YRAPELIFGA-TDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIK 271
Cdd:cd05613   154 EFLLDENERAYsFCGTIeYMAPEIVRGGdSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISR 222
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
60-261 1.03e-17

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: 82.87  E-value: 1.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKV-LQDK-RFKN---RELQIMRKldhCN---IVRLRYFFYSSG------EKKDE 125
Cdd:cd06615     7 GELGAGNGGVVTKVLHRPSGLIMARKLIhLEIKpAIRNqiiRELKVLHE---CNspyIVGFYGAFYSDGeisicmEHMDG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 126 VYLNLVLDyvpetvyRVARhysrakqtLPVIYVKLYMYQLFRSLAYI---HSfgICHRDIKPQNLLLDPDTAVlKLCDFG 202
Cdd:cd06615    84 GSLDQVLK-------KAGR--------IPENILGKISIAVLRGLTYLrekHK--IMHRDVKPSNILVNSRGEI-KLCDFG 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 203 SAKQLVRGEPNvSYICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQ-PIFPGDS 261
Cdd:cd06615   146 VSGQLIDSMAN-SFVGTRSYMSPERLQG-THYTVQSDIWSLGLSLVEMAIGRyPIPPPDA 203
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
62-247 1.07e-17

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: 82.92  E-value: 1.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIK-----KVLQDKRFKNRELQIMRKLDHCNIVRLryffYSSGEKKDEVYLNLVLDYVP 136
Cdd:cd13988     1 LGQGATANVFRGRHKKTGDLYAVKvfnnlSFMRPLDVQMREFEVLKKLNHKNIVKL----FAIEEELTTRHKVLVMELCP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 137 -ETVYRVARHYSRAkQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLL--LDPD-TAVLKLCDFGSAKQLVRGEP 212
Cdd:cd13988    77 cGSLYTVLEEPSNA-YGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMrvIGEDgQSVYKLTDFGAARELEDDEQ 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1231802383 213 NVSYICSRYYRAPELIFGAT-------DYTSSIDVWSAGCVL 247
Cdd:cd13988   156 FVSLYGTEEYLHPDMYERAVlrkdhqkKYGATVDLWSIGVTF 197
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
56-261 1.08e-17

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: 82.09  E-value: 1.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVY---QAKLCDSGELVAIKKV----LQ--DKRFKNRELQIMRKLDHCNIVRlryfFYSSGEKKDev 126
Cdd:cd08222     2 YRVVRKLGSGNFGTVYlvsDLKATADEELKVLKEIsvgeLQpdETVDANREAKLLSKLDHPAIVK----FHDSFVEKE-- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 127 YLNLVLDYVP-ETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtaVLKLCDFGSAK 205
Cdd:cd08222    76 SFCIVTEYCEgGDLDDKISEYKKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKNN--VIKVGDFGISR 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1231802383 206 QLVrGEPNV--SYICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIFPGDS 261
Cdd:cd08222   154 ILM-GTSDLatTFTGTPYYMSPEVLKH-EGYNSKSDIWSLGCILYEMCCLKHAFDGQN 209
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
56-340 1.08e-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: 81.90  E-value: 1.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAK-LCDsGELVAIKKVL--QDKRFKN--------RELQIMRK---LDHCNIVRLRYFFyssge 121
Cdd:cd14005     2 YEVGDLLGKGGFGTVYSGVrIRD-GLPVAVKFVPksRVTEWAMingpvpvpLEIALLLKaskPGVPGVIRLLDWY----- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 122 KKDEVYLnLVLDYvPETVYRVArHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDF 201
Cdd:cd14005    76 ERPDGFL-LIMER-PEPCQDLF-DFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLRTGEVKLIDF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 202 GSAkQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSgvdqlvEIIKvlgtptreqi 281
Cdd:cd14005   153 GCG-ALLKDSVYTDFDGTRVYSPPEWIRHGRYHGRPATVWSLGILLYDMLCGDIPFENDE------QILR---------- 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1231802383 282 remnpnytefkfpqikahpWTKVFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd14005   216 -------------------GNVLFRPRLSKECCDLISRCLQFDPSKRPSLEQILSHPWF 255
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
48-340 1.14e-17

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: 82.01  E-value: 1.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  48 PDRPQEVSYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKL-------DHCNIVRLRYFFYSSG 120
Cdd:cd14106     2 TENINEVYTVESTPLGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQDCRNEILHEIavlelckDCPRVVNLHEVYETRS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 121 EkkdevyLNLVLDYVP----ETVYRVARHYSRAKqtlpviyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAV- 195
Cdd:cd14106    82 E------LILILELAAggelQTLLDEEECLTEAD-------VRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFPLg 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 196 -LKLCDFGSAKQLVRGEPNVSYICSRYYRAPElIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDqlveiikvlg 274
Cdd:cd14106   149 dIKLCDFGISRVIGEGEEIREILGTPDYVAPE-ILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDKQE---------- 217
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1231802383 275 tpTREQIREMNPNYTEFKFPQIKahpwtkvfrprtpPEAIALCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd14106   218 --TFLNISQCNLDFPEELFKDVS-------------PLAIDFIKRLLVKDPEKRLTAKECLEHPWL 268
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
56-319 1.22e-17

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: 81.94  E-value: 1.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN-----RELQIMRKLDHCNIVRLRYFFYSSGekkdevYLNL 130
Cdd:cd08219     2 YNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRLPKSSSAvedsrKEAVLLAKMKHPNIVAFKESFEADG------HLYI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 VLDYVPETVYRVARHYSRAKqTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLVR- 209
Cdd:cd08219    76 VMEYCDGGDLMQKIKLQRGK-LFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKV-KLGDFGSARLLTSp 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 210 GEPNVSYICSRYYRAPElIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTreqiremnPNYT 289
Cdd:cd08219   154 GAYACTYVGTPYYVPPE-IWENMPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGSYKPL--------PSHY 224
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1231802383 290 EFKFPQIKahpwTKVFR--PRTPPEAIALCSR 319
Cdd:cd08219   225 SYELRSLI----KQMFKrnPRSRPSATTILSR 252
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
60-251 1.28e-17

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: 81.95  E-value: 1.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKVL-QDKRFKN---RELQIMRKL-DHCNIVRlrYFFYSSGEKKDEVYLNLVLdy 134
Cdd:cd14037     9 KYLAEGGFAHVYLVKTSNGGNRAALKRVYvNDEHDLNvckREIEIMKRLsGHKNIVG--YIDSSANRSGNGVYEVLLL-- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 135 vpetvyrvaRHYSRAKQTLPVIYVKLY-----------MYQLFRSLAYIHSFG--ICHRDIKPQNLLLDpDTAVLKLCDF 201
Cdd:cd14037    85 ---------MEYCKGGGVIDLMNQRLQtglteseilkiFCDVCEAVAAMHYLKppLIHRDLKVENVLIS-DSGNYKLCDF 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 202 GSAK---QLVRGEPNVSYI---CSRY----YRAPELI--FGATDYTSSIDVWSAGCVLAELL 251
Cdd:cd14037   155 GSATtkiLPPQTKQGVTYVeedIKKYttlqYRAPEMIdlYRGKPITEKSDIWALGCLLYKLC 216
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
60-255 1.43e-17

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: 81.98  E-value: 1.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIK--KVLQDKRFK-NRELQIMRKLDHCNIVRLRY--FFYSSGEKKDEvYLNLVLDY 134
Cdd:cd06636    22 EVVGNGTYGQVYKGRHVKTGQLAAIKvmDVTEDEEEEiKLEINMLKKYSHHRNIATYYgaFIKKSPPGHDD-QLWLVMEF 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 135 V-PETVYRVARhySRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQLVR--GE 211
Cdd:cd06636   101 CgAGSVTDLVK--NTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLT-ENAEVKLVDFGVSAQLDRtvGR 177
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1231802383 212 PNvSYICSRYYRAPELIF------GATDYTSsiDVWSAGCVLAELLLGQP 255
Cdd:cd06636   178 RN-TFIGTPYWMAPEVIAcdenpdATYDYRS--DIWSLGITAIEMAEGAP 224
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
56-340 1.46e-17

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK1 plays a role in neuronal differentiation. 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 CLK1/4 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: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 82.59  E-value: 1.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFG-VVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCN---------IVRLRYFFYSSGekkde 125
Cdd:cd14213    14 YEIVDTLGEGAFGkVVECIDHKMGGMHVAVKIVKNVDRYREAARSEIQVLEHLNttdpnstfrCVQMLEWFDHHG----- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 126 vYLNLVLDYVPETVYRVARHYSRakQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLL-LDPDTAV--------- 195
Cdd:cd14213    89 -HVCIVFELLGLSTYDFIKENSF--LPFPIDHIRNMAYQICKSVNFLHHNKLTHTDLKPENILfVQSDYVVkynpkmkrd 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 196 --------LKLCDFGSAKqlVRGEPNVSYICSRYYRAPELIFgATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLV 267
Cdd:cd14213   166 ertlknpdIKVVDFGSAT--YDDEHHSTLVSTRHYRAPEVIL-ALGWSQPCDVWSIGCILIEYYLGFTVFQTHDSKEHLA 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 268 EIIKVLGtPTREQIREMNPNYTEFKFPQI--KAHPWT-KVFRPRTPP-------------EAIALCSRLLEYTPTARLTP 331
Cdd:cd14213   243 MMERILG-PLPKHMIQKTRKRKYFHHDQLdwDEHSSAgRYVRRRCKPlkefmlsqdvdheQLFDLIQKMLEYDPAKRITL 321

                  ....*....
gi 1231802383 332 LEACAHSFF 340
Cdd:cd14213   322 DEALKHPFF 330
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
62-291 1.47e-17

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: 82.00  E-value: 1.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKV-------LQDKRFknrELQIMRKLDHCNIVRLRYFFY-----------SSGEKK 123
Cdd:cd06643    13 LGDGAFGKVYKAQNKETGILAAAKVIdtkseeeLEDYMV---EIDILASCDHPNIVKLLDAFYyennlwiliefCAGGAV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 124 DEVYLNLVLDyVPETVYRVArhysrAKQTLpviyvklymyqlfRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFG- 202
Cdd:cd06643    90 DAVMLELERP-LTEPQIRVV-----CKQTL-------------EALVYLHENKIIHRDLKAGNILFTLDGDI-KLADFGv 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 203 SAKQLVRGEPNVSYICSRYYRAPELIFGATD----YTSSIDVWSAGCVLAELllgQPIFPGDSGVDQLVEIIKVLGT--P 276
Cdd:cd06643   150 SAKNTRTLQRRDSFIGTPYWMAPEVVMCETSkdrpYDYKADVWSLGVTLIEM---AQIEPPHHELNPMRVLLKIAKSepP 226
                         250
                  ....*....|....*
gi 1231802383 277 TREQIREMNPNYTEF 291
Cdd:cd06643   227 TLAQPSRWSPEFKDF 241
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
56-337 1.52e-17

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: 82.18  E-value: 1.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQ--DKRFKNRELQIMRKLDHCNIVRLRYFFyssgEKKDEVYLNLVL- 132
Cdd:cd14085     5 FEIESELGRGATSVVYRCRQKGTQKPYAVKKLKKtvDKKIVRTEIGVLLRLSHPNIIKLKEIF----ETPTEISLVLELv 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 ------DYVPETVYRVARHYSRAkqtlpviyVKlymyQLFRSLAYIHSFGICHRDIKPQNLLL-DP-DTAVLKLCDFGSA 204
Cdd:cd14085    81 tggelfDRIVEKGYYSERDAADA--------VK----QILEAVAYLHENGIVHRDLKPENLLYaTPaPDAPLKIADFGLS 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 205 KqLVRGEPNVSYIC-SRYYRAPELIFGATdYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEiikvlgtptreqiRE 283
Cdd:cd14085   149 K-IVDQQVTMKTVCgTPGYCAPEILRGCA-YGPEVDMWSVGVITYILLCGFEPFYDERGDQYMFK-------------RI 213
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1231802383 284 MNPNYtEFKFPQikahpWTKVfrprtPPEAIALCSRLLEYTPTARLTPLEACAH 337
Cdd:cd14085   214 LNCDY-DFVSPW-----WDDV-----SLNAKDLVKKLIVLDPKKRLTTQQALQH 256
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
62-278 1.53e-17

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: 81.63  E-value: 1.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVV----YQAKlcDSGEL-VAIK-----KVLQDKRFKNRELQIMRKLDHCNIVRLryFFYSSGEKkdevyLNLV 131
Cdd:cd05060     3 LGHGNFGSVrkgvYLMK--SGKEVeVAVKtlkqeHEKAGKKEFLREASVMAQLDHPCIVRL--IGVCKGEP-----LMLV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 132 LDYVPETvyrvARH-YSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLVRG 210
Cdd:cd05060    74 MELAPLG----PLLkYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQA-KISDFGMSRALGAG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 211 epnvsyicSRYYR------------APELIFGATdYTSSIDVWSAGCVLAELL-LGQPIFPGDSGVD--QLVEIIKVLGT 275
Cdd:cd05060   149 --------SDYYRattagrwplkwyAPECINYGK-FSSKSDVWSYGVTLWEAFsYGAKPYGEMKGPEviAMLESGERLPR 219

                  ...
gi 1231802383 276 PTR 278
Cdd:cd05060   220 PEE 222
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
61-259 1.70e-17

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: 81.29  E-value: 1.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  61 VIGNGSFGVVYQAKLcdSGELVAIKKVLQD---------KRFKNrELQIMRKLDHCNIVRLRyffyssGEKKDEVYLNLV 131
Cdd:cd14061     1 VIGVGGFGKVYRGIW--RGEEVAVKAARQDpdedisvtlENVRQ-EARLFWMLRHPNIIALR------GVCLQPPNLCLV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 132 LDYvpetvYR---VARHYsrAKQTLPVIYVKLYMYQLFRSLAYIHSFG---ICHRDIKPQNLLL-------DPDTAVLKL 198
Cdd:cd14061    72 MEY-----ARggaLNRVL--AGRKIPPHVLVDWAIQIARGMNYLHNEApvpIIHRDLKSSNILIleaieneDLENKTLKI 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1231802383 199 CDFGSAKQLVRgEPNVSYICSRYYRAPELIFGATdYTSSIDVWSAGCVLAELLLGQPIFPG 259
Cdd:cd14061   145 TDFGLAREWHK-TTRMSAAGTYAWMAPEVIKSST-FSKASDVWSYGVLLWELLTGEVPYKG 203
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
56-319 1.92e-17

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: 82.08  E-value: 1.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNR----ELQIMRKLDHCNIVRlryfFYSSGEKKDEVYLNL- 130
Cdd:cd06655    21 YTRYEKIGQGASGTVFTAIDVATGQEVAIKQINLQKQPKKEliinEILVMKELKNPNIVN----FLDSFLVGDELFVVMe 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 ------VLDYVPETVYRVARHYSRAKQTLpviyvklymyqlfRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSA 204
Cdd:cd06655    97 ylaggsLTDVVTETCMDEAQIAAVCRECL-------------QALEFLHANQVIHRDIKSDNVLLGMDGSV-KLTDFGFC 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 205 KQLVRGEPNVS-YICSRYYRAPELIFGATdYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVeIIKVLGTPTREQIRE 283
Cdd:cd06655   163 AQITPEQSKRStMVGTPYWMAPEVVTRKA-YGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALY-LIATNGTPELQNPEK 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1231802383 284 MNPNYTEF-------------KFPQIKAHPWTKVFRPRTPPEAIALCSR 319
Cdd:cd06655   241 LSPIFRDFlnrclemdvekrgSAKELLQHPFLKLAKPLSSLTPLILAAK 289
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
61-320 2.00e-17

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: 81.51  E-value: 2.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  61 VIGNGSFGVVYQAKLcdSGELVAIKkVLQDKRFKNR--------------------------ELQIMRKLDHCNIVRLry 114
Cdd:cd14000     1 LLGDGGFGSVYRASY--KGEPVAVK-IFNKHTSSNFanvpadtmlrhlratdamknfrllrqELTVLSHLHHPSIVYL-- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 115 ffYSSGEKKdevyLNLVLDYVPE-TVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLL---LD 190
Cdd:cd14000    76 --LGIGIHP----LMLVLELAPLgSLDHLLQQDSRSFASLGRTLQQRIALQVADGLRYLHSAMIIYRDLKSHNVLvwtLY 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 191 PDTAV-LKLCDFGSAKQLVR-------GEPNvsyicsryYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDsg 262
Cdd:cd14000   150 PNSAIiIKIADYGISRQCCRmgakgseGTPG--------FRAPEIARGNVIYNEKVDVFSFGMLLYEILSGGAPMVGH-- 219
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1231802383 263 vDQLVEIIKVLGtptreQIREMNPNYTEFKFPQIKA---HPWTKvfRPRTPPEAIALCSRL 320
Cdd:cd14000   220 -LKFPNEFDIHG-----GLRPPLKQYECAPWPEVEVlmkKCWKE--NPQQRPTAVTVVSIL 272
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
56-273 2.02e-17

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: 81.58  E-value: 2.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDK-RFK----NRELQIMRKLDHCNIVRLryffYSSGEKKDEVYLnl 130
Cdd:cd14183     8 YKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKcRGKehmiQNEVSILRRVKHPNIVLL----IEEMDMPTELYL-- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 VLDYVP-----ETVYRVARHYSRAKQTLpviyvklyMYQLFRSLAYIHSFGICHRDIKPQNLLL---DPDTAVLKLCDFG 202
Cdd:cd14183    82 VMELVKggdlfDAITSTNKYTERDASGM--------LYNLASAIKYLHSLNIVHRDIKPENLLVyehQDGSKSLKLGDFG 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1231802383 203 SAkQLVRGePNVSYICSRYYRAPELIfGATDYTSSIDVWSAGCVLAELLLGQPIFPGdSGVDQLVEIIKVL 273
Cdd:cd14183   154 LA-TVVDG-PLYTVCGTPTYVAPEII-AETGYGLKVDIWAAGVITYILLCGFPPFRG-SGDDQEVLFDQIL 220
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
60-329 2.25e-17

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: 82.05  E-value: 2.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQimrkldhCNIVRLRYF-----------FYSSGEKKDEVYL 128
Cdd:cd05587     2 MVLGKGSFGKVMLAERKGTDELYAIKILKKDVIIQDDDVE-------CTMVEKRVLalsgkppfltqLHSCFQTMDRLYF 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 129 nlVLDYVP--ETVYRVaRHYSRAKQTLPVIYVKLYMYQLFrslaYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQ 206
Cdd:cd05587    75 --VMEYVNggDLMYHI-QQVGKFKEPVAVFYAAEIAVGLF----FLHSKGIIYRDLKLDNVMLDAEGHI-KIADFGMCKE 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 207 LVRGEPNVSYIC-SRYYRAPELIFgATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGvDQLVeiikvlgtptrEQIREMN 285
Cdd:cd05587   147 GIFGGKTTRTFCgTPDYIAPEIIA-YQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDE-DELF-----------QSIMEHN 213
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1231802383 286 PNYtefkfpqikahpwtkvfrPRT-PPEAIALCSRLLEYTPTARL 329
Cdd:cd05587   214 VSY------------------PKSlSKEAVSICKGLLTKHPAKRL 240
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
62-253 3.19e-17

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: 81.12  E-value: 3.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNR-----ELQIMRKLDHCNIVRlryffysSGEKKDEvyLNLVLDYVP 136
Cdd:cd14039     1 LGTGGFGNVCLYQNQETGEKIAIKSCRLELSVKNKdrwchEIQIMKKLNHPNVVK-------ACDVPEE--MNFLVNDVP 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 137 etvyRVARHYS-----RAKQTLPVIYVKLYMYQLFRSLA-------YIHSFGICHRDIKPQNLLLDPDTA--VLKLCDFG 202
Cdd:cd14039    72 ----LLAMEYCsggdlRKLLNKPENCCGLKESQVLSLLSdigsgiqYLHENKIIHRDLKPENIVLQEINGkiVHKIIDLG 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1231802383 203 SAKQLVRGEPNVSYICSRYYRAPELiFGATDYTSSIDVWSAGCVLAELLLG 253
Cdd:cd14039   148 YAKDLDQGSLCTSFVGTLQYLAPEL-FENKSYTVTVDYWSFGTMVFECIAG 197
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
62-351 3.21e-17

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: 81.24  E-value: 3.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKVlqDKRFKNR------ELQIMRKLDHCNIVRLryffYSSGEKKDEVYLnlVLDYV 135
Cdd:cd06658    30 IGEGSTGIVCIATEKHTGKQVAVKKM--DLRKQQRrellfnEVVIMRDYHHENVVDM----YNSYLVGDELWV--VMEFL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 136 PE-TVYRVARHYSRAKQTLPVIYVklymyQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLVRGEPN- 213
Cdd:cd06658   102 EGgALTDIVTHTRMNEEQIATVCL-----SVLRALSYLHNQGVIHRDIKSDSILLTSDGRI-KLSDFGFCAQVSKEVPKr 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 214 VSYICSRYYRAPELIfGATDYTSSIDVWSAGCVLAELLLGQPIFpgdsgvdqlveiikvLGTPTREQIREMNPNYTefkf 293
Cdd:cd06658   176 KSLVGTPYWMAPEVI-SRLPYGTEVDIWSLGIMVIEMIDGEPPY---------------FNEPPLQAMRRIRDNLP---- 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1231802383 294 PQIK-AHPWTKVFRprtppeaiALCSRLLEYTPTARLTPLEACAHSFFDELRDPNVKLP 351
Cdd:cd06658   236 PRVKdSHKVSSVLR--------GFLDLMLVREPSQRATAQELLQHPFLKLAGPPSCIVP 286
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
61-254 4.23e-17

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: 80.35  E-value: 4.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  61 VIGNGSFGVVYQAKLCDSGELVA-----IKKVLQD--KRFKNrELQIMRKLDHCNIVRlryfFYSSGEKKDEVYLNLVLD 133
Cdd:cd13983     8 VLGRGSFKTVYRAFDTEEGIEVAwneikLRKLPKAerQRFKQ-EIEILKSLKHPNIIK----FYDSWESKSKKEVIFITE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 134 YVPE-TVyrvaRHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFG--ICHRDIKPQNLLLDPDTAVLKLCDFGSAKQL--- 207
Cdd:cd13983    83 LMTSgTL----KQYLKRFKRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFINGNTGEVKIGDLGLATLLrqs 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1231802383 208 ----VRGEPNvsyicsryYRAPELIFGatDYTSSIDVWSAGCVLAELLLGQ 254
Cdd:cd13983   159 faksVIGTPE--------FMAPEMYEE--HYDEKVDIYAFGMCLLEMATGE 199
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
55-339 4.45e-17

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: 80.18  E-value: 4.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  55 SYTDTKVIGNGSFGVVYQAKLCDSGELVAIK----------KVLQDKRFKN---------RELQIMRKLDHCNIVRLRYF 115
Cdd:cd14077     2 NWEFVKTIGAGSMGKVKLAKHIRTGEKCAIKiiprasnaglKKEREKRLEKeisrdirtiREAALSSLLNHPHICRLRDF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 116 FYSSGekkdevYLNLVLDYVPETV---YRVARHYSRAKQTlpviyvKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpD 192
Cdd:cd14077    82 LRTPN------HYYMLFEYVDGGQlldYIISHGKLKEKQA------RKFARQIASALDYLHRNSIVHRDLKIENILIS-K 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 193 TAVLKLCDFG-----SAKQLVRgepnvSYICSRYYRAPELIfGATDYTS-SIDVWSAGCVLAELLLGQPIFpGDSGVDQL 266
Cdd:cd14077   149 SGNIKIIDFGlsnlyDPRRLLR-----TFCGSLYFAAPELL-QAQPYTGpEVDVWSFGVVLYVLVCGKVPF-DDENMPAL 221
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1231802383 267 VEIIKvlgtptreqiremnpnYTEFKFPQikahpWTKVfrprtppEAIALCSRLLEYTPTARLTPLEACAHSF 339
Cdd:cd14077   222 HAKIK----------------KGKVEYPS-----YLSS-------ECKSLISRMLVVDPKKRATLEQVLNHPW 266
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
56-339 4.96e-17

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: 80.44  E-value: 4.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIK------KVLQDK-----RFKNRELQIMRKLDHCNIVRLRYFFyssgeKKD 124
Cdd:cd13990     2 YLLLNLLGKGGFSEVYKAFDLVEQRYVACKihqlnkDWSEEKkqnyiKHALREYEIHKSLDHPRIVKLYDVF-----EID 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 125 EVYLNLVLDYVPETVYRVarhYSRAKQTLPVIYVKLYMYQLFRSLAYI--HSFGICHRDIKPQNLLLDPDTA--VLKLCD 200
Cdd:cd13990    77 TDSFCTVLEYCDGNDLDF---YLKQHKSIPEREARSIIMQVVSALKYLneIKPPIIHYDLKPGNILLHSGNVsgEIKITD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 201 FGSAKQLVRGEPNVSYI-------CSRYYRAPE-LIFGATD--YTSSIDVWSAGCVLAELLLGQPIFpgdsGVDQlveii 270
Cdd:cd13990   154 FGLSKIMDDESYNSDGMeltsqgaGTYWYLPPEcFVVGKTPpkISSKVDVWSVGVIFYQMLYGRKPF----GHNQ----- 224
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1231802383 271 kvlgtpTREQIREMNP--NYTEFKFPqikahpwtkvFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSF 339
Cdd:cd13990   225 ------SQEAILEENTilKATEVEFP----------SKPVVSSEAKDFIRRCLTYRKEDRPDVLQLANDPY 279
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
53-261 5.09e-17

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: 80.02  E-value: 5.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  53 EVSYTDTKVIGNGSFGVVyqaKLCD---SGELVAIKKVlqDKRFKNR-----ELQIMRKLDHCNIVRLRYFFYSSG---- 120
Cdd:cd14113     6 DSFYSEVAELGRGRFSVV---KKCDqrgTKRAVATKFV--NKKLMKRdqvthELGVLQSLQHPQLVGLLDTFETPTsyil 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 121 --EKKDEVYLnlvLDYVPETvyrvarhysrakQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLD--PDTAVL 196
Cdd:cd14113    81 vlEMADQGRL---LDYVVRW------------GNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDqsLSKPTI 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 197 KLCDFGSAKQLvrgepNVSY-----ICSRYYRAPELIFGATDYTSSiDVWSAGCVLAELLLGQPIFPGDS 261
Cdd:cd14113   146 KLADFGDAVQL-----NTTYyihqlLGSPEFAAPEIILGNPVSLTS-DLWSIGVLTYVLLSGVSPFLDES 209
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
52-350 5.10e-17

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: 80.31  E-value: 5.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  52 QEVSYTDTkvIGNGSFGVVYQAKLCDSGELVAIKKVLQD-----KRFKNRELQIMRKLDHCNIVRlryfFYSSGEKKDEV 126
Cdd:cd06619     1 QDIQYQEI--LGHGNGGTVYKAYHLLTRRILAVKVIPLDitvelQKQIMSELEILYKCDSPYIIG----FYGAFFVENRI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 127 YL-NLVLDYVPETVYRvarhySRAKQTLPVIYVKLymyqlFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAK 205
Cdd:cd06619    75 SIcTEFMDGGSLDVYR-----KIPEHVLGRIAVAV-----VKGLTYLWSLKILHRDVKPSNMLVNTRGQV-KLCDFGVST 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 206 QLVRGEPNvSYICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQ---PIFPGDSGVDQLVEIIK--VLGTPTREQ 280
Cdd:cd06619   144 QLVNSIAK-TYVGTNAYMAPERISG-EQYGIHSDVWSLGISFMELALGRfpyPQIQKNQGSLMPLQLLQciVDEDPPVLP 221
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 281 IREMNPNYTEFkfpqikahpwtkvfrprtppeaIALCSRLLeytPTARLTPLEACAHSFFDELRDPNVKL 350
Cdd:cd06619   222 VGQFSEKFVHF----------------------ITQCMRKQ---PKERPAPENLMDHPFIVQYNDGNAEV 266
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
62-286 5.12e-17

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: 79.74  E-value: 5.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLcdSGElVAIKKV-------LQDKRFKNrELQIMRKLDHCNIvrLRYFFYSSgekKDEvyLNLVLDY 134
Cdd:cd14062     1 IGSGSFGTVYKGRW--HGD-VAVKKLnvtdptpSQLQAFKN-EVAVLRKTRHVNI--LLFMGYMT---KPQ--LAIVTQW 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 135 VP-ETVYRvarHysrakqtLPVIYVKLYMYQLF---RSLA----YIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSA-- 204
Cdd:cd14062    70 CEgSSLYK---H-------LHVLETKFEMLQLIdiaRQTAqgmdYLHAKNIIHRDLKSNNIFLHEDLTV-KIGDFGLAtv 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 205 KQLVRGEPNVSYIC-SRYYRAPELI--FGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQlveIIKVLG----TPT 277
Cdd:cd14062   139 KTRWSGSQQFEQPTgSILWMAPEVIrmQDENPYSFQSDVYAFGIVLYELLTGQLPYSHINNRDQ---ILFMVGrgylRPD 215

                  ....*....
gi 1231802383 278 REQIREMNP 286
Cdd:cd14062   216 LSKVRSDTP 224
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
62-263 5.12e-17

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: 81.07  E-value: 5.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKVlqDKRFK---NRELQIMRKLD-HCNIVRLRYFFYssgekkDEVYLNLVLDYVP- 136
Cdd:cd14180    14 LGEGSFSVCRKCRHRQSGQEYAVKII--SRRMEantQREVAALRLCQsHPNIVALHEVLH------DQYHTYLVMELLRg 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 137 -ETVYRVAR--HYSRAKQTlpviyvklymyQLFRSL----AYIHSFGICHRDIKPQNLLL--DPDTAVLKLCDFGSAKQL 207
Cdd:cd14180    86 gELLDRIKKkaRFSESEAS-----------QLMRSLvsavSFMHEAGVVHRDLKPENILYadESDGAVLKVIDFGFARLR 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1231802383 208 VRGEPNVSYIC-SRYYRAPELiFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGV 263
Cdd:cd14180   155 PQGSRPLQTPCfTLQYAAPEL-FSNQGYDESCDLWSLGVILYTMLSGQVPFQSKRGK 210
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
55-259 5.50e-17

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: 80.79  E-value: 5.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  55 SYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKvLQDKRFKNR--------ELQIMRKLDHCNIVRLRYFFyssgEKKDEV 126
Cdd:cd05632     3 TFRQYRVLGKGGFGEVCACQVRATGKMYACKR-LEKKRIKKRkgesmalnEKQILEKVNSQFVVNLAYAY----ETKDAL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 127 YLNLVLDYVPETVYRVarhYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQ 206
Cdd:cd05632    78 CLVLTIMNGGDLKFHI---YNMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLD-DYGHIRISDLGLAVK 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1231802383 207 LVRGEPNVSYICSRYYRAPELIfGATDYTSSIDVWSAGCVLAELLLGQPIFPG 259
Cdd:cd05632   154 IPEGESIRGRVGTVGYMAPEVL-NNQRYTLSPDYWGLGCLIYEMIEGQSPFRG 205
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
60-257 5.63e-17

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: 80.85  E-value: 5.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKVlqDKRFK---NRELQIMRKLD-HCNIVRLRYFFYssgekkDEVYLNLVLDYV 135
Cdd:cd14179    13 KPLGEGSFSICRKCLHKKTNQEYAVKIV--SKRMEantQREIAALKLCEgHPNIVKLHEVYH------DQLHTFLVMELL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 136 P--ETVYRVAR--HYSRAKQTlpviYVklyMYQLFRSLAYIHSFGICHRDIKPQNLLL--DPDTAVLKLCDFGSAK-QLV 208
Cdd:cd14179    85 KggELLERIKKkqHFSETEAS----HI---MRKLVSAVSHMHDVGVVHRDLKPENLLFtdESDNSEIKIIDFGFARlKPP 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1231802383 209 RGEPNVSYICSRYYRAPELiFGATDYTSSIDVWSAGCVLAELLLGQPIF 257
Cdd:cd14179   158 DNQPLKTPCFTLHYAAPEL-LNYNGYDESCDLWSLGVILYTMLSGQVPF 205
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
60-365 6.14e-17

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: 80.81  E-value: 6.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQimrkldhCNIVRLRYF-----------FYSSGEKKDEVYL 128
Cdd:cd05616     6 MVLGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDDDVE-------CTMVEKRVLalsgkppfltqLHSCFQTMDRLYF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 129 nlVLDYVP--ETVYRVaRHYSRAKQTLPVIYVKLYMYQLFrslaYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQ 206
Cdd:cd05616    79 --VMEYVNggDLMYHI-QQVGRFKEPHAVFYAAEIAIGLF----FLQSKGIIYRDLKLDNVMLDSEGHI-KIADFGMCKE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 207 -LVRGEPNVSYICSRYYRAPELIfGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGvDQLVeiikvlgtptrEQIREMN 285
Cdd:cd05616   151 nIWDGVTTKTFCGTPDYIAPEII-AYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDE-DELF-----------QSIMEHN 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 286 PNYtefkfpqikahpwtkvfrPRT-PPEAIALCSRLLEYTPTARLtpleACA---------HSFF-----DELRDPNVKL 350
Cdd:cd05616   218 VAY------------------PKSmSKEAVAICKGLMTKHPGKRL----GCGpegerdikeHAFFryidwEKLERKEIQP 275
                         330       340
                  ....*....|....*....|
gi 1231802383 351 P-----NGRDTPALFNFTTQ 365
Cdd:cd05616   276 PykpkaCGRNAENFDRFFTR 295
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
61-329 6.50e-17

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: 81.20  E-value: 6.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  61 VIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQimrkldhCNIVRLRYF-----------FYSSGEKKDEVYLn 129
Cdd:cd05615    17 VLGKGSFGKVMLAERKGSDELYAIKILKKDVVIQDDDVE-------CTMVEKRVLalqdkppfltqLHSCFQTVDRLYF- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 lVLDYVP--ETVYRVaRHYSRAKQTLPVIYVKLYMYQLFrslaYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQ- 206
Cdd:cd05615    89 -VMEYVNggDLMYHI-QQVGKFKEPQAVFYAAEISVGLF----FLHKKGIIYRDLKLDNVMLDSEGHI-KIADFGMCKEh 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 207 LVRGEPNVSYICSRYYRAPELIfGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGvDQLVeiikvlgtptrEQIREMNP 286
Cdd:cd05615   162 MVEGVTTRTFCGTPDYIAPEII-AYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDE-DELF-----------QSIMEHNV 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1231802383 287 NYtefkfpqikahpwtkvfrPRT-PPEAIALCSRLLEYTPTARL 329
Cdd:cd05615   229 SY------------------PKSlSKEAVSICKGLMTKHPAKRL 254
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
48-351 7.31e-17

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: 80.07  E-value: 7.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  48 PDRPQevSYTDTKV-IGNGSFGVVYQAKLCDSGELVAIKKVlqDKRFKNR------ELQIMRKLDHCNIVRLryffYSSG 120
Cdd:cd06657    15 PGDPR--TYLDNFIkIGEGSTGIVCIATVKSSGKLVAVKKM--DLRKQQRrellfnEVVIMRDYQHENVVEM----YNSY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 121 EKKDEVYLnlVLDYVPE-TVYRVARHYSRAKQTLPVIYVklymyQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLC 199
Cdd:cd06657    87 LVGDELWV--VMEFLEGgALTDIVTHTRMNEEQIAAVCL-----AVLKALSVLHAQGVIHRDIKSDSILLTHDGRV-KLS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 200 DFGSAKQLVRGEPN-VSYICSRYYRAPELIfGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLveiikvlgtptr 278
Cdd:cd06657   159 DFGFCAQVSKEVPRrKSLVGTPYWMAPELI-SRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAM------------ 225
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1231802383 279 EQIREMNPnytefkfPQIK-AHpwtkvfrpRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDELRDPNVKLP 351
Cdd:cd06657   226 KMIRDNLP-------PKLKnLH--------KVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPPSCIVP 284
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
50-270 7.48e-17

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: 81.59  E-value: 7.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  50 RPQEVSYTDTKVIGNGSFG-----------VVYQAKLCDSGELvaIKKvlQDKRFKNRELQIMRKLDHCNIVRLRYFFys 118
Cdd:cd05622    69 RMKAEDYEVVKVIGRGAFGevqlvrhkstrKVYAMKLLSKFEM--IKR--SDSAFFWEERDIMAFANSPWVVQLFYAF-- 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 119 sgekKDEVYLNLVLDYVPE-TVYRVARHYSrakqtLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLK 197
Cdd:cd05622   143 ----QDDRYLYMVMEYMPGgDLVNLMSNYD-----VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLD-KSGHLK 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 198 LCDFGSAKQ-----LVRGEPNVSyicSRYYRAPELIF---GATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEI 269
Cdd:cd05622   213 LADFGTCMKmnkegMVRCDTAVG---TPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKI 289

                  .
gi 1231802383 270 I 270
Cdd:cd05622   290 M 290
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
60-340 7.89e-17

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: 80.44  E-value: 7.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNREL-------QIMRKLDHCNIVRLRYFFYSSGEkkdevyLNLVL 132
Cdd:cd05595     1 KLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVahtvtesRVLQNTRHPFLTALKYAFQTHDR------LCFVM 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 DYVP--ETVYRVARHYSRAKQTlpviyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLVRG 210
Cdd:cd05595    75 EYANggELFFHLSRERVFTEDR-----ARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHI-KITDFGLCKEGITD 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 211 EPNVSYIC-SRYYRAPElIFGATDYTSSIDVWSAGCVLAELLLGQ-PIFPGDSgvDQLVEIIKVlgtptrEQIRemnpny 288
Cdd:cd05595   149 GATMKTFCgTPEYLAPE-VLEDNDYGRAVDWWGLGVVMYEMMCGRlPFYNQDH--ERLFELILM------EEIR------ 213
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1231802383 289 tefkFPQikahpwtkvfrpRTPPEAIALCSRLLEYTPTARL-----TPLEACAHSFF 340
Cdd:cd05595   214 ----FPR------------TLSPEAKSLLAGLLKKDPKQRLgggpsDAKEVMEHRFF 254
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
56-303 7.98e-17

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: 79.51  E-value: 7.98e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDK-----RFKN-----RELQIMRKL----DHCNIVRLRYFFyssgE 121
Cdd:cd14101     2 YTMGNLLGKGGFGTVYAGHRISDGLQVAIKQISRNRvqqwsKLPGvnpvpNEVALLQSVgggpGHRGVIRLLDWF----E 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 122 KKDEVYLNL--------VLDYVPEtvyrvarhysraKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDT 193
Cdd:cd14101    78 IPEGFLLVLerpqhcqdLFDYITE------------RGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDLRT 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 194 AVLKLCDFGSAKqLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSG-VDQLVEIIKV 272
Cdd:cd14101   146 GDIKLIDFGSGA-TLKDSMYTDFDGTRVYSPPEWILYHQYHALPATVWSLGILLYDMVCGDIPFERDTDiLKAKPSFNKR 224
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1231802383 273 LGTPTREQIR---EMNPNyTEFKFPQIKAHPWTK 303
Cdd:cd14101   225 VSNDCRSLIRsclAYNPS-DRPSLEQILLHPWMM 257
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
51-255 8.00e-17

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: 79.69  E-value: 8.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  51 PQEvSYTDTKVIGNGSFGVVYQAKLCDSGELVAIK--KVLQDKRFK--NRELQIMRKLDHCNIVRlrYF-FYSSGEKkde 125
Cdd:cd06646     7 PQH-DYELIQRVGSGTYGDVYKARNLHTGELAAVKiiKLEPGDDFSliQQEIFMVKECKHCNIVA--YFgSYLSREK--- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 126 vyLNLVLDYVPETVYRVARHYSRAKQTLPVIYVklyMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFG-SA 204
Cdd:cd06646    81 --LWICMEYCGGGSLQDIYHVTGPLSELQIAYV---CRETLQGLAYLHSKGKMHRDIKGANILLT-DNGDVKLADFGvAA 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1231802383 205 KQLVRGEPNVSYICSRYYRAPEL--IFGATDYTSSIDVWSAGCVLAELLLGQP 255
Cdd:cd06646   155 KITATIAKRKSFIGTPYWMAPEVaaVEKNGGYNQLCDIWAVGITAIELAELQP 207
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
62-261 9.99e-17

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: 80.31  E-value: 9.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIK----KVLQDKR-----FKNRELQIMRKLDHCN-IVRLRYFFYSSGEkkdevyLNLV 131
Cdd:cd05586     1 IGKGTFGQVYQVRKKDTRRIYAMKvlskKVIVAKKevahtIGERNILVRTALDESPfIVGLKFSFQTPTD------LYLV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 132 LDYVP--ETVYRVARHYSRAKQTlpviyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLVR 209
Cdd:cd05586    75 TDYMSggELFWHLQKEGRFSEDR-----AKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHI-ALCDFGLSKADLT 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1231802383 210 GEPNVSYIC-SRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLG-QPIFPGDS 261
Cdd:cd05586   149 DNKTTNTFCgTTEYLAPEVLLDEKGYTKMVDFWSLGVLVFEMCCGwSPFYAEDT 202
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
62-337 1.57e-16

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: 79.13  E-value: 1.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKVL---QDKRFKNRELQIMRKLDHCNIVRLryffYSSGEKKDEvyLNLVLDYVP-- 136
Cdd:cd14104     8 LGRGQFGIVHRCVETSSKKTYMAKFVKvkgADQVLVKKEISILNIARHRNILRL----HESFESHEE--LVMIFEFISgv 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 137 ---ETVYRVARHYSRAKqtlpviyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTA-VLKLCDFGSAKQLVRGEP 212
Cdd:cd14104    82 difERITTARFELNERE-------IVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRRGsYIKIIEFGQSRQLKPGDK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 213 -NVSYICSRYYrAPElIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDqlveiikvlgtpTREQIREMNPNYTEF 291
Cdd:cd14104   155 fRLQYTSAEFY-APE-VHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQ------------TIENIRNAEYAFDDE 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1231802383 292 KFPQIKAhpwtkvfrprtppEAIALCSRLLEYTPTARLTPLEACAH 337
Cdd:cd14104   221 AFKNISI-------------EALDFVDRLLVKERKSRMTAQEALNH 253
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
56-301 2.68e-16

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: 78.47  E-value: 2.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIK-----KVLQDKRFKNR-------------------------ELQIMRKLD 105
Cdd:cd14199     4 YKLKDEIGKGSYGVVKLAYNEDDNTYYAMKvlskkKLMRQAGFPRRppprgaraapegctqprgpiervyqEIAILKKLD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 106 HCNIVRLRYFFYSSGEkkDEVYLnlvldyVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQ 185
Cdd:cd14199    84 HPNVVKLVEVLDDPSE--DHLYM------VFELVKQGPVMEVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 186 NLLLDPDTAVlKLCDFGSAKQLVRGEPNVS-YICSRYYRAPELIFGATDYTS--SIDVWSAGCVLAELLLGQPIFPgDSG 262
Cdd:cd14199   156 NLLVGEDGHI-KIADFGVSNEFEGSDALLTnTVGTPAFMAPETLSETRKIFSgkALDVWAMGVTLYCFVFGQCPFM-DER 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 263 VDQLVEIIKV--LGTPTREQIRE-----------MNPNyTEFKFPQIKAHPW 301
Cdd:cd14199   234 ILSLHSKIKTqpLEFPDQPDISDdlkdllfrmldKNPE-SRISVPEIKLHPW 284
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
74-264 2.89e-16

Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer T-cell-originated protein 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. TOPK, also called PDZ-binding kinase (PBK), is activated at the early stage of mitosis and plays a critical role in cytokinesis. It partly functions as a mitogen-activated protein kinase (MAPK) kinase and is capable of phosphorylating p38, JNK1, and ERK2. TOPK also plays a role in DNA damage sensing and repair through its phosphorylation of histone H2AX. It contributes to cancer development and progression by downregulating the function of tumor suppressor p53 and reducing cell-cycle regulatory proteins. TOPK is found highly expressed in breast and skin cancer cells. The TOPK 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: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 78.60  E-value: 2.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  74 KLCDSGELVAIKKVLQDkrfknrELQIMRKLDHCNIVRLRYFfysSGEKKDEVYLnlVLDYVPETVY-RVARHYSRAKQT 152
Cdd:cd14001    38 SKCDKGQRSLYQERLKE------EAKILKSLNHPNIVGFRAF---TKSEDGSLCL--AMEYGGKSLNdLIEERYEAGLGP 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 153 LPVIYVKLYMYQLFRSLAYIHSFG-ICHRDIKPQNLLLDPDTAVLKLCDFGSAKQL-----VRGEPNVSYICSRYYRAPE 226
Cdd:cd14001   107 FPAATILKVALSIARALEYLHNEKkILHGDIKSGNVLIKGDFESVKLCDFGVSLPLtenleVDSDPKAQYVGTEPWKAKE 186
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1231802383 227 LIFGATDYTSSIDVWSAGCVLAELL-LGQP-IFPGDSGVD 264
Cdd:cd14001   187 ALEEGGVITDKADIFAYGLVLWEMMtLSVPhLNLLDIEDD 226
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
62-365 3.65e-16

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: 78.55  E-value: 3.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVA-------IKKVLQDKRFknRELQIMRKLDHCNIVRLRYFFYSSGEkkdevyLNLVLDY 134
Cdd:cd06649    13 LGAGNGGVVTKVQHKPSGLIMArklihleIKPAIRNQII--RELQVLHECNSPYIVGFYGAFYSDGE------ISICMEH 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 135 VP----ETVYRVARHysrakqtLPVIYVKLYMYQLFRSLAYI-HSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQLVR 209
Cdd:cd06649    85 MDggslDQVLKEAKR-------IPEEILGKVSIAVLRGLAYLrEKHQIMHRDVKPSNILVN-SRGEIKLCDFGVSGQLID 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 210 GEPNvSYICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQ-PIFPGDSGvdqlvEIIKVLGTPTREqiremnpny 288
Cdd:cd06649   157 SMAN-SFVGTRSYMSPERLQG-THYSVQSDIWSMGLSLVELAIGRyPIPPPDAK-----ELEAIFGRPVVD--------- 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 289 tefkfpQIKAHPWTKVFRPRTPPEAIAlcSRLLEYTPtarltpleacAHSFFDEL----RDPNVKLPNGRDTPALFNFTT 364
Cdd:cd06649   221 ------GEEGEPHSISPRPRPPGRPVS--GHGMDSRP----------AMAIFELLdyivNEPPPKLPNGVFTPDFQEFVN 282

                  .
gi 1231802383 365 Q 365
Cdd:cd06649   283 K 283
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
56-354 3.79e-16

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: 78.15  E-value: 3.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKL-DHCNIVRLRYFfYSSGEkkdEVYLNLVLDY 134
Cdd:cd14175     3 YVVKETIGVGSYSVCKRCVHKATNMEYAVKVIDKSKRDPSEEIEILLRYgQHPNIITLKDV-YDDGK---HVYLVTELMR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 135 VPETVYRVARHYSRAKQTLPVIyvklyMYQLFRSLAYIHSFGICHRDIKPQNLLL-----DPDTavLKLCDFGSAKQLVR 209
Cdd:cd14175    79 GGELLDKILRQKFFSEREASSV-----LHTICKTVEYLHSQGVVHRDLKPSNILYvdesgNPES--LRICDFGFAKQLRA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 210 GEPNVSYIC-SRYYRAPElIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGvDQLVEIIKVLGTPtreqiremnpny 288
Cdd:cd14175   152 ENGLLMTPCyTANFVAPE-VLKRQGYDEGCDIWSLGILLYTMLAGYTPFANGPS-DTPEEILTRIGSG------------ 217
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1231802383 289 tefKFpQIKAHPWTKVfrprtPPEAIALCSRLLEYTPTARLTPLEACAHSFFDElRDpnvKLPNGR 354
Cdd:cd14175   218 ---KF-TLSGGNWNTV-----SDAAKDLVSKMLHVDPHQRLTAKQVLQHPWITQ-KD---KLPQSQ 270
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
62-264 3.87e-16

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: 77.53  E-value: 3.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIK--KVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEkkdevyLNLVLDYVPETV 139
Cdd:cd14065     1 LGKGFFGEVYKVTHRETGKVMVMKelKRFDEQRSFLKEVKLMRRLSHPNILRFIGVCVKDNK------LNFITEYVNGGT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 140 YRvaRHYSRAKQTLPvIYVKLYM-YQLFRSLAYIHSFGICHRDIKPQNLLLDPD----TAVLKlcDFGSAKQLV------ 208
Cdd:cd14065    75 LE--ELLKSMDEQLP-WSQRVSLaKDIASGMAYLHSKNIIHRDLNSKNCLVREAnrgrNAVVA--DFGLAREMPdektkk 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1231802383 209 --RGEPnVSYICSRYYRAPELIFGATdYTSSIDVWSAGCVLAELLLGQPIFP------GDSGVD 264
Cdd:cd14065   150 pdRKKR-LTVVGSPYWMAPEMLRGES-YDEKVDVFSFGIVLCEIIGRVPADPdylprtMDFGLD 211
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
56-254 4.34e-16

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. TTBK1 has been linked to Alzheimer's disease (AD) while TTBK2 is associated with spinocerebellar ataxia type 11 (SCA11). Both AD and SCA11 patients show the presence of neurofibrillary tangles in the brain. The Drosophila TTBK homolog, Asator, is an essential protein that localizes to the mitotic spindle during mitosis and may be involved in regulating microtubule dynamics and function. The TTBK 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: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 77.30  E-value: 4.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIK--KVLQDKRFKNRELQIMRKLDHCnivrlRYF--FYSSGekKDEVYLNLV 131
Cdd:cd14017     2 WKVVKKIGGGGFGEIYKVRDVVDGEEVAMKveSKSQPKQVLKMEVAVLKKLQGK-----PHFcrLIGCG--RTERYNYIV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 132 LDYVPETVYRVARHYSRAKQTLPVIyVKLYMyQLFRSLAYIHSFGICHRDIKPQNLLL---DPDTAVLKLCDFGSAKQLV 208
Cdd:cd14017    75 MTLLGPNLAELRRSQPRGKFSVSTT-LRLGI-QILKAIEDIHEVGFLHRDVKPSNFAIgrgPSDERTVYILDFGLARQYT 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1231802383 209 RGEPNVsyicSRYYRAPELIFGATDYtSSI------------DVWSAGCVLAELLLGQ 254
Cdd:cd14017   153 NKDGEV----ERPPRNAAGFRGTVRY-ASVnahrnkeqgrrdDLWSWFYMLIEFVTGQ 205
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
44-285 4.77e-16

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 80.17  E-value: 4.77e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383   44 PGQ---GPDRPQEvsYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVlQDKRFKNRE-------LQIMRKLDHCNIVRLR 113
Cdd:PTZ00266     2 PGKyddGESRLNE--YEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAI-SYRGLKEREksqlvieVNVMRELKHKNIVRYI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  114 YFFYSSGEKKdevyLNLVLDYVPetvyrvARHYSRAKQTLPVIYVKLYMY-------QLFRSLAYIHSFG-------ICH 179
Cdd:PTZ00266    79 DRFLNKANQK----LYILMEFCD------AGDLSRNIQKCYKMFGKIEEHaivditrQLLHALAYCHNLKdgpngerVLH 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  180 RDIKPQNLLLDPD-------TA---------VLKLCDFGSAKQLvrGEPNVSYIC--SRYYRAPELIFGAT-DYTSSIDV 240
Cdd:PTZ00266   149 RDLKPQNIFLSTGirhigkiTAqannlngrpIAKIGDFGLSKNI--GIESMAHSCvgTPYYWSPELLLHETkSYDDKSDM 226
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1231802383  241 WSAGCVLAELLLGQPIFPGDSGVDQLV-EIIKVLGTPTREQIREMN 285
Cdd:PTZ00266   227 WALGCIIYELCSGKTPFHKANNFSQLIsELKRGPDLPIKGKSKELN 272
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
60-301 4.85e-16

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: 77.78  E-value: 4.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIK----KVLQDKRFK-NRELQIMRKLDHCNIVRLRYFFYSSgekkDEVYLNLVLDY 134
Cdd:cd14168    16 EVLGTGAFSEVVLAEERATGKLFAVKcipkKALKGKESSiENEIAVLRKIKHENIVALEDIYESP----NHLYLVMQLVS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 135 VPETVYR-VARHYSRAKQTLPVIYvklymyQLFRSLAYIHSFGICHRDIKPQNLLL--DPDTAVLKLCDFGSAKQLVRGE 211
Cdd:cd14168    92 GGELFDRiVEKGFYTEKDASTLIR------QVLDAVYYLHRMGIVHRDLKPENLLYfsQDEESKIMISDFGLSKMEGKGD 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 212 PNVSYICSRYYRAPElIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKV-----------LGTPTREQ 280
Cdd:cd14168   166 VMSTACGTPGYVAPE-VLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAdyefdspywddISDSAKDF 244
                         250       260
                  ....*....|....*....|....
gi 1231802383 281 IR---EMNPNyTEFKFPQIKAHPW 301
Cdd:cd14168   245 IRnlmEKDPN-KRYTCEQALRHPW 267
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
62-269 5.08e-16

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: 77.75  E-value: 5.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQI-MRKLDHCNIVRLRYFFyssgekKDEVYLNLVLDYVP--ET 138
Cdd:cd14177    12 IGVGSYSVCKRCIHRATNMEFAVKIIDKSKRDPSEEIEIlMRYGQHPNIITLKDVY------DDGRYVYLVTELMKggEL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 139 VYRVARHYSRAKQTLPVIyvklyMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTA---VLKLCDFGSAKQLvRGEpNVS 215
Cdd:cd14177    86 LDRILRQKFFSEREASAV-----LYTITKTVDYLHCQGVVHRDLKPSNILYMDDSAnadSIRICDFGFAKQL-RGE-NGL 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 216 YICSRY---YRAPELIFgATDYTSSIDVWSAGCVLAELLLGQPIF---PGDSGVDQLVEI 269
Cdd:cd14177   159 LLTPCYtanFVAPEVLM-RQGYDAACDIWSLGVLLYTMLAGYTPFangPNDTPEEILLRI 217
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
59-291 5.72e-16

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: 77.26  E-value: 5.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  59 TKVIGNGSFGVVYQAKLCDSGELVAIK----KVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSsgeKKDEVylnLVLDY 134
Cdd:cd14193     9 EEILGGGRFGQVHKCEEKSSGLKLAAKiikaRSQKEKEEVKNEIEVMNQLNHANLIQLYDAFES---RNDIV---LVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 135 VP--ETVYRVARHYSRAKQTLPVIYVKlymyQLFRSLAYIHSFGICHRDIKPQNLL-LDPDTAVLKLCDFGSAKQLVRGE 211
Cdd:cd14193    83 VDggELFDRIIDENYNLTELDTILFIK----QICEGIQYMHQMYILHLDLKPENILcVSREANQVKIIDFGLARRYKPRE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 212 PNVSYICSRYYRAPELIfgATDYTS-SIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTE 290
Cdd:cd14193   159 KLRVNFGTPEFLAPEVV--NYEFVSfPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILACQWDFEDEEFADISEEAKD 236

                  .
gi 1231802383 291 F 291
Cdd:cd14193   237 F 237
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
56-270 5.94e-16

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: 78.50  E-value: 5.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQ-------DKRFKNRELQIMRKLDHCNIVRLRYFFyssgekKDEVYL 128
Cdd:cd05621    54 YDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKfemikrsDSAFFWEERDIMAFANSPWVVQLFCAF------QDDKYL 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 129 NLVLDYVPE-TVYRVARHYSrakqtLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQ- 206
Cdd:cd05621   128 YMVMEYMPGgDLVNLMSNYD-----VPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLD-KYGHLKLADFGTCMKm 201
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1231802383 207 ----LVRGEPNVSyicSRYYRAPELIF---GATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEII 270
Cdd:cd05621   202 detgMVHCDTAVG---TPDYISPEVLKsqgGDGYYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIM 269
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
60-261 6.27e-16

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: 77.66  E-value: 6.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIK---KVLQDKRFK-NR---ELQIMRKLDHCNIVRLryffYSSGEKKDevYLNLVL 132
Cdd:cd05574     7 KLLGKGDVGRVYLVRLKGTGKLFAMKvldKEEMIKRNKvKRvltEREILATLDHPFLPTL----YASFQTST--HLCFVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 DYVP-ETVYRVARhySRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLkLCDF---------- 201
Cdd:cd05574    81 DYCPgGELFRLLQ--KQPGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIM-LTDFdlskqssvtp 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 202 ---------GSAKQLVRGEPNVSYICSRYYR-----------APELIFGAtDYTSSIDVWSAGCVLAELLLGQPIFPGDS 261
Cdd:cd05574   158 ppvrkslrkGSRRSSVKSIEKETFVAEPSARsnsfvgteeyiAPEVIKGD-GHGSAVDWWTLGILLYEMLYGTTPFKGSN 236
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
60-268 6.61e-16

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: 77.77  E-value: 6.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIK--------KVLQDKRFKnRELQIMRKLDHCNIVRLRYFFyssgekKDEVYLNLV 131
Cdd:cd05597     7 KVIGRGAFGEVAVVKLKSTEKVYAMKilnkwemlKRAETACFR-EERDVLVNGDRRWITKLHYAF------QDENYLYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 132 LDYvpetvyrvarhY---------SRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFG 202
Cdd:cd05597    80 MDY-----------YcggdlltllSKFEDRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHI-RLADFG 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1231802383 203 SAKQLVRGepnvSYICSRY------YRAPELIFGATD----YTSSIDVWSAGCVLAELLLGQPIFPGDSgvdqLVE 268
Cdd:cd05597   148 SCLKLRED----GTVQSSVavgtpdYISPEILQAMEDgkgrYGPECDWWSLGVCMYEMLYGETPFYAES----LVE 215
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
77-323 7.72e-16

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 79.50  E-value: 7.72e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383   77 DSGELVAIKKVLQD--------KRFKnRELQIMRKLDHCNIVRLryffYSSGEKKDEvYLNLVLDYVPEtvyRVARHYSR 148
Cdd:TIGR03903    1 MTGHEVAIKLLRTDapeeehqrARFR-RETALCARLYHPNIVAL----LDSGEAPPG-LLFAVFEYVPG---RTLREVLA 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  149 AKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDP--DTAVLKLCDFG-----------SAKQLVR-GEpnv 214
Cdd:TIGR03903   72 ADGALPAGETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQtgVRPHAKVLDFGigtllpgvrdaDVATLTRtTE--- 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  215 sYICSRYYRAPELIFGATdYTSSIDVWSAGCVLAELLLGQPIFPGDSgvdqLVEIIKvlgtptreqiREMNPNytEFKFP 294
Cdd:TIGR03903  149 -VLGTPTYCAPEQLRGEP-VTPNSDLYAWGLIFLECLTGQRVVQGAS----VAEILY----------QQLSPV--DVSLP 210
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1231802383  295 Q-IKAHPWTKVFR------PR---TPPEAIALCSRLLEY 323
Cdd:TIGR03903  211 PwIAGHPLGQVLRkalnkdPRqraASAPALAERFRALEL 249
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
60-339 8.05e-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: 76.99  E-value: 8.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKVLQDK-RFKNRELQIMRKLDHC----NIVRLRYFFyssgEKKDEVYLNL---- 130
Cdd:cd14174     8 ELLGEGAYAKVQGCVSLQNGKEYAVKIIEKNAgHSRSRVFREVETLYQCqgnkNILELIEFF----EDDTRFYLVFeklr 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 ---VLDYVPETVYRVARHYSRAKQTLPviyvklymyqlfRSLAYIHSFGICHRDIKPQNLLLDPDTAV--LKLCDF--GS 203
Cdd:cd14174    84 ggsILAHIQKRKHFNEREASRVVRDIA------------SALDFLHTKGIAHRDLKPENILCESPDKVspVKICDFdlGS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 204 AKQLVRG-----EPNVSYIC-SRYYRAPELIFGATD----YTSSIDVWSAGCVLAELLLGQPIFPGDSGVD---QLVEII 270
Cdd:cd14174   152 GVKLNSActpitTPELTTPCgSAEYMAPEVVEVFTDeatfYDKRCDLWSLGVILYIMLSGYPPFVGHCGTDcgwDRGEVC 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1231802383 271 KVLGTPTREQIREmnpnyTEFKFPQikaHPWTKVfrprtPPEAIALCSRLLEYTPTARLTPLEACAHSF 339
Cdd:cd14174   232 RVCQNKLFESIQE-----GKYEFPD---KDWSHI-----SSEAKDLISKLLVRDAKERLSAAQVLQHPW 287
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
56-270 8.51e-16

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: 77.97  E-value: 8.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNREL-------QIMRKLDHCNIVRLRYFFyssgekKDEVYL 128
Cdd:cd05629     3 FHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMFKKDQLahvkaerDVLAESDSPWVVSLYYSF------QDAQYL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 129 NLVLDYVP--ETVYRVARHysrakQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFG---- 202
Cdd:cd05629    77 YLIMEFLPggDLMTMLIKY-----DTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHI-KLSDFGlstg 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 203 --------SAKQLVRGEPNVSYICSRY------------------------------------YRAPElIFGATDYTSSI 238
Cdd:cd05629   151 fhkqhdsaYYQKLLQGKSNKNRIDNRNsvavdsinltmsskdqiatwkknrrlmaystvgtpdYIAPE-IFLQQGYGQEC 229
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1231802383 239 DVWSAGCVLAELLLGQPIFPGDSGVDQLVEII 270
Cdd:cd05629   230 DWWSLGAIMFECLIGWPPFCSENSHETYRKII 261
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
56-291 9.36e-16

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: 77.07  E-value: 9.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKV-LQDKRFKN---RELQIMRKLDHCNIVRlryfFYSSGEKKDEVYLNL- 130
Cdd:cd06654    22 YTRFEKIGQGASGTVYTAMDVATGQEVAIRQMnLQQQPKKEliiNEILVMRENKNPNIVN----YLDSYLVGDELWVVMe 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 ------VLDYVPETVYRVARHYSRAKQTLpviyvklymyqlfRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSA 204
Cdd:cd06654    98 ylaggsLTDVVTETCMDEGQIAAVCRECL-------------QALEFLHSNQVIHRDIKSDNILLGMDGSV-KLTDFGFC 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 205 KQLVRGEPNVS-YICSRYYRAPELIFGATdYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVeIIKVLGTPTREQIRE 283
Cdd:cd06654   164 AQITPEQSKRStMVGTPYWMAPEVVTRKA-YGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALY-LIATNGTPELQNPEK 241

                  ....*...
gi 1231802383 284 MNPNYTEF 291
Cdd:cd06654   242 LSAIFRDF 249
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
62-281 1.01e-15

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: 76.39  E-value: 1.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSG-ELVAIKKVL------------QDKRFKN--RELQIMR-KLDHCNIVRlryfFYSSGEKKDE 125
Cdd:cd08528     8 LGSGAFGCVYKVRKKSNGqTLLALKEINmtnpafgrteqeRDKSVGDiiSEVNIIKeQLRHPNIVR----YYKTFLENDR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 126 VYLnlVLDYVPETVYRvaRHYSRAKQ-----TLPVIYvKLYMyQLFRSLAYIH-SFGICHRDIKPQNLLLDPDTAVLkLC 199
Cdd:cd08528    84 LYI--VMELIEGAPLG--EHFSSLKEknehfTEDRIW-NIFV-QMVLALRYLHkEKQIVHRDLKPNNIMLGEDDKVT-IT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 200 DFGSAKQlvrGEPNVSYICSR----YYRAPElIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGT 275
Cdd:cd08528   157 DFGLAKQ---KGPESSKMTSVvgtiLYSCPE-IVQNEPYGEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVEAEYE 232

                  ....*.
gi 1231802383 276 PTREQI 281
Cdd:cd08528   233 PLPEGM 238
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
60-257 1.11e-15

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: 76.31  E-value: 1.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQA---KLCDSGELVAIKKVLQDKRFKNRE--LQ---IMRKLDHCNIVRLryffysSGEKKDE-VYLnl 130
Cdd:cd05056    12 RCIGEGQFGDVYQGvymSPENEKIAVAVKTCKNCTSPSVREkfLQeayIMRQFDHPHIVKL------IGVITENpVWI-- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 VLDYVPetvYRVARHY-SRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLL-DPDTavLKLCDFGSAKQLv 208
Cdd:cd05056    84 VMELAP---LGELRSYlQVNKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVsSPDC--VKLGDFGLSRYM- 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1231802383 209 rgEPNVSYICSR-----YYRAPELIfGATDYTSSIDVWSAG-CVLAELLLG-QPIF 257
Cdd:cd05056   158 --EDESYYKASKgklpiKWMAPESI-NFRRFTSASDVWMFGvCMWEILMLGvKPFQ 210
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
56-307 1.24e-15

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: 76.68  E-value: 1.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKV-LQDKRFKN---RELQIMRKLDHCNIVRlryfFYSSGEKKDEVYLNL- 130
Cdd:cd06656    21 YTRFEKIGQGASGTVYTAIDIATGQEVAIKQMnLQQQPKKEliiNEILVMRENKNPNIVN----YLDSYLVGDELWVVMe 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 ------VLDYVPETVYRVARHYSRAKQTLpviyvklymyqlfRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSA 204
Cdd:cd06656    97 ylaggsLTDVVTETCMDEGQIAAVCRECL-------------QALDFLHSNQVIHRDIKSDNILLGMDGSV-KLTDFGFC 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 205 KQLVRGEPNVS-YICSRYYRAPELIFGATdYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVeIIKVLGTPTREQIRE 283
Cdd:cd06656   163 AQITPEQSKRStMVGTPYWMAPEVVTRKA-YGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALY-LIATNGTPELQNPER 240
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1231802383 284 MNPNYTEF-------------KFPQIKAHPWTKVFRP 307
Cdd:cd06656   241 LSAVFRDFlnrclemdvdrrgSAKELLQHPFLKLAKP 277
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
34-258 1.41e-15

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 77.17  E-value: 1.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  34 GSKVTTVVATPGQGPDRPQEVSYTD-TKVIGNGSFGVVYQAKLCDSGELVAIKKVLQD-----KRFKNRELQIMRKLDHC 107
Cdd:PLN00034   53 SSSSSSSSSASGSAPSAAKSLSELErVNRIGSGAGGTVYKVIHRPTGRLYALKVIYGNhedtvRRQICREIEILRDVNHP 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 108 NIVRLRYFFYSSGEkkdevyLNLVLDYVPETVYRvARHYSRAKQTLPViyvklyMYQLFRSLAYIHSFGICHRDIKPQNL 187
Cdd:PLN00034  133 NVVKCHDMFDHNGE------IQVLLEFMDGGSLE-GTHIADEQFLADV------ARQILSGIAYLHRRHIVHRDIKPSNL 199
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1231802383 188 LLDPDTAVlKLCDFGSAKQLVRG-EPNVSYICSRYYRAPELI-----FGATD-YTSsiDVWSAGCVLAELLLGQpiFP 258
Cdd:PLN00034  200 LINSAKNV-KIADFGVSRILAQTmDPCNSSVGTIAYMSPERIntdlnHGAYDgYAG--DIWSLGVSILEFYLGR--FP 272
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
85-257 1.50e-15

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: 75.86  E-value: 1.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  85 KKVLQDKRfknRELQIMRKLDHCNIVRLRYFFYSSGEKKDEVYLNLVLDYVPetVYRVARHYSRAKqTLPVIYVKLYMYQ 164
Cdd:cd14012    39 KKQIQLLE---KELESLKKLRHPNLVSYLAFSIERRGRSDGWKVYLLTEYAP--GGSLSELLDSVG-SVPLDTARRWTLQ 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 165 LFRSLAYIHSFGICHRDIKPQNLLLDPDTA--VLKLCDFGSAKQLVR--GEPNVSYICSRYYRAPELIFGATDYTSSIDV 240
Cdd:cd14012   113 LLEALEYLHRNGVVHKSLHAGNVLLDRDAGtgIVKLTDYSLGKTLLDmcSRGSLDEFKQTYWLPPELAQGSKSPTRKTDV 192
                         170
                  ....*....|....*..
gi 1231802383 241 WSAGCVLAELLLGQPIF 257
Cdd:cd14012   193 WDLGLLFLQMLFGLDVL 209
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
60-270 1.82e-15

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: 77.36  E-value: 1.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDH------CN-IVRLRYFFyssgekKDEVYLNLVL 132
Cdd:cd05624    78 KVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETACFREERNvlvngdCQwITTLHYAF------QDENYLYLVM 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 DY-VPETVYRVarhYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLVRGE 211
Cdd:cd05624   152 DYyVGGDLLTL---LSKFEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHI-RLADFGSCLKMNDDG 227
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1231802383 212 PNVSYIC--SRYYRAPELIFGATD----YTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEII 270
Cdd:cd05624   228 TVQSSVAvgTPDYISPEILQAMEDgmgkYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIM 292
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
59-337 1.95e-15

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: 75.96  E-value: 1.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  59 TKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSS----GEKKDEVYLNLVLDY 134
Cdd:cd14171    11 TQKLGTGISGPVRVCVKKSTGERFALKILLDRPKARTEVRLHMMCSGHPNIVQIYDVYANSvqfpGESSPRARLLIVMEL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 135 VP--ETVYRVA--RHYSRAKQTLpviyvklYMYQLFRSLAYIHSFGICHRDIKPQNLLL--DPDTAVLKLCDFGSAKqlV 208
Cdd:cd14171    91 MEggELFDRISqhRHFTEKQAAQ-------YTKQIALAVQHCHSLNIAHRDLKPENLLLkdNSEDAPIKLCDFGFAK--V 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 209 RGEPNVSYICSRYYRAPEL--------------IFGATDYT--SSIDVWSAGCVLAELLLGQPIFPGDsgvdqlveiikv 272
Cdd:cd14171   162 DQGDLMTPQFTPYYVAPQVleaqrrhrkersgiPTSPTPYTydKSCDMWSLGVIIYIMLCGYPPFYSE------------ 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1231802383 273 lgTPTREQIREMNPNYT--EFKFPQikaHPWTKVFRPrtppeAIALCSRLLEYTPTARLTPLEACAH 337
Cdd:cd14171   230 --HPSRTITKDMKRKIMtgSYEFPE---EEWSQISEM-----AKDIVRKLLCVDPEERMTIEEVLHH 286
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
61-263 1.95e-15

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: 75.84  E-value: 1.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  61 VIGNGSFGVVYQAKLcdSGELVAIKKVLQDKRFK--------NRELQIMRKLDHCNIVRLRyffyssGEKKDEVYLNLVL 132
Cdd:cd14146     1 IIGVGGFGKVYRATW--KGQEVAVKAARQDPDEDikataesvRQEAKLFSMLRHPNIIKLE------GVCLEEPNLCLVM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 DYV-------PETVYRVARHYSRAKQTLPVIYVKlYMYQLFRSLAYIHS---FGICHRDIKPQNLLL-------DPDTAV 195
Cdd:cd14146    73 EFArggtlnrALAAANAAPGPRRARRIPPHILVN-WAVQIARGMLYLHEeavVPILHRDLKSSNILLlekiehdDICNKT 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1231802383 196 LKLCDFGSAKQLVRgEPNVSYICSRYYRAPELIfGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGV 263
Cdd:cd14146   152 LKITDFGLAREWHR-TTKMSAAGTYAWMAPEVI-KSSLFSKGSDIWSYGVLLWELLTGEVPYRGIDGL 217
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
60-270 2.18e-15

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: 76.38  E-value: 2.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIK-----KVLQDKRF-----KNRELQIMRKldHCNIVRLryffYSSGEKKDEVYLn 129
Cdd:cd05591     1 KVLGKGSFGKVMLAERKGTDEVYAIKvlkkdVILQDDDVdctmtEKRILALAAK--HPFLTAL----HSCFQTKDRLFF- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 lVLDYVP--ETVYRV--ARHYSRAKqtlpviyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAK 205
Cdd:cd05591    74 -VMEYVNggDLMFQIqrARKFDEPR-------ARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHC-KLADFGMCK 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1231802383 206 Q-LVRGEPNVSYICSRYYRAPElIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGvDQLVEII 270
Cdd:cd05591   145 EgILNGKTTTTFCGTPDYIAPE-ILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNE-DDLFESI 208
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
51-255 2.50e-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: 75.47  E-value: 2.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  51 PQEvSYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVL----QDKRFKNRELQIMRKLDHCNIVRlryfFYSSGEKKDEV 126
Cdd:cd06645     9 PQE-DFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKlepgEDFAVVQQEIIMMKDCKHSNIVA----YFGSYLRRDKL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 127 YLNlvLDYVPETVYRVARHYSRAKQTLPVIYVKlymYQLFRSLAYIHSFGICHRDIKPQNLLLdPDTAVLKLCDFGSAKQ 206
Cdd:cd06645    84 WIC--MEFCGGGSLQDIYHVTGPLSESQIAYVS---RETLQGLYYLHSKGKMHRDIKGANILL-TDNGHVKLADFGVSAQ 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 207 LVRG-EPNVSYICSRYYRAPEL--IFGATDYTSSIDVWSAGCVLAELLLGQP 255
Cdd:cd06645   158 ITATiAKRKSFIGTPYWMAPEVaaVERKGGYNQLCDIWAVGITAIELAELQP 209
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
61-260 2.96e-15

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: 75.01  E-value: 2.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  61 VIGNGSFGVVYQAKLCDSGELVAIKKVLQDK-----RFKN-----RELQIMRKLDH--CNIVRLRYFFyssgEKKDEVYL 128
Cdd:cd14100     7 LLGSGGFGSVYSGIRVADGAPVAIKHVEKDRvsewgELPNgtrvpMEIVLLKKVGSgfRGVIRLLDWF----ERPDSFVL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 129 nlVLDYvPETVYRVArHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSAKqLV 208
Cdd:cd14100    83 --VLER-PEPVQDLF-DFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDLNTGELKLIDFGSGA-LL 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 209 RGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGD 260
Cdd:cd14100   158 KDTVYTDFDGTRVYSPPEWIRFHRYHGRSAAVWSLGILLYDMVCGDIPFEHD 209
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
53-252 3.17e-15

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: 74.95  E-value: 3.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  53 EVSYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKV---LQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSgekkdeVYLN 129
Cdd:cd14110     2 EKTYAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIpykPEDKQLVLREYQVLRRLSHPRIAQLHSAYLSP------RHLV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 LVLDYV--PETVYRVARH--YSRAKqtlpviyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAK 205
Cdd:cd14110    76 LIEELCsgPELLYNLAERnsYSEAE-------VTDYLWQILSAVDYLHSRRILHLDLRSENMIIT-EKNLLKIVDLGNAQ 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1231802383 206 QLVRGEPNVSYICSRYY--RAPELIF--GATDYTssiDVWSAGcVLAELLL 252
Cdd:cd14110   148 PFNQGKVLMTDKKGDYVetMAPELLEgqGAGPQT---DIWAIG-VTAFIML 194
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
62-350 3.18e-15

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: 75.17  E-value: 3.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKVL--QDKRFKN---RELQIMRKLDHCNIVRlryfFYSSgekkdevYLN------L 130
Cdd:cd06620    13 LGAGNGGSVSKVLHIPTGTIMAKKVIHidAKSSVRKqilRELQILHECHSPYIVS----FYGA-------FLNennniiI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 VLDYVP----ETVYRVarhysraKQTLPVIYVKLYMYQLFRSLAYIHS-FGICHRDIKPQNLLLDpDTAVLKLCDFGSAK 205
Cdd:cd06620    82 CMEYMDcgslDKILKK-------KGPFPEEVLGKIAVAVLEGLTYLYNvHRIIHRDIKPSNILVN-SKGQIKLCDFGVSG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 206 QLVRGEPNvSYICSRYYRAPELIFGAtDYTSSIDVWSAGCVLAELLLGQpiFP------GDSGVDQLVEIIKVLgtptrE 279
Cdd:cd06620   154 ELINSIAD-TFVGTSTYMSPERIQGG-KYSVKSDVWSLGLSIIELALGE--FPfagsndDDDGYNGPMGILDLL-----Q 224
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 280 QIREMNPnytefkfPQIkahPWTKVFrprtPPEAIALCSRLLEYTPTARLTPLEACAHSFF-DELRDPNVKL 350
Cdd:cd06620   225 RIVNEPP-------PRL---PKDRIF----PKDLRDFVDRCLLKDPRERPSPQLLLDHDPFiQAVRASDVDL 282
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
60-257 3.51e-15

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: 75.85  E-value: 3.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKkVLQDKRFKNRE-----------LQIMRKLDHCNIVRLRYFFYSSGEkkdevyL 128
Cdd:cd14223     6 RIIGRGGFGEVYGCRKADTGKMYAMK-CLDKKRIKMKQgetlalnerimLSLVSTGDCPFIVCMSYAFHTPDK------L 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 129 NLVLDYVP--ETVYRVARH--YSRAKqtlpviyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSA 204
Cdd:cd14223    79 SFILDLMNggDLHYHLSQHgvFSEAE-------MRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHV-RISDLGLA 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1231802383 205 KQLVRGEPNVSyICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIF 257
Cdd:cd14223   151 CDFSKKKPHAS-VGTHGYMAPEVLQKGVAYDSSADWFSLGCMLFKLLRGHSPF 202
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
60-255 3.71e-15

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: 75.14  E-value: 3.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIK--KVLQDKRFK-NRELQIMRKLDHC-NIVRLRYFFYSSGEKKDEVYLNLVLDYV 135
Cdd:cd06637    12 ELVGNGTYGQVYKGRHVKTGQLAAIKvmDVTGDEEEEiKQEINMLKKYSHHrNIATYYGAFIKKNPPGMDDQLWLVMEFC 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 136 -PETVYRVARHYSraKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQLVR--GEP 212
Cdd:cd06637    92 gAGSVTDLIKNTK--GNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLT-ENAEVKLVDFGVSAQLDRtvGRR 168
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1231802383 213 NvSYICSRYYRAPELIfgATD------YTSSIDVWSAGCVLAELLLGQP 255
Cdd:cd06637   169 N-TFIGTPYWMAPEVI--ACDenpdatYDFKSDLWSLGITAIEMAEGAP 214
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
60-257 3.74e-15

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: 75.87  E-value: 3.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKkVLQDKRFKNRE-----------LQIMRKLDHCNIVRLRYFFYSSGEkkdevyL 128
Cdd:cd05633    11 RIIGRGGFGEVYGCRKADTGKMYAMK-CLDKKRIKMKQgetlalnerimLSLVSTGDCPFIVCMTYAFHTPDK------L 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 129 NLVLDYVP--ETVYRVARHYSRAKQTLpviyvKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQ 206
Cdd:cd05633    84 CFILDLMNggDLHYHLSQHGVFSEKEM-----RFYATEIILGLEHMHNRFVVYRDLKPANILLD-EHGHVRISDLGLACD 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1231802383 207 LVRGEPNVSyICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIF 257
Cdd:cd05633   158 FSKKKPHAS-VGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPF 207
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
63-262 4.02e-15

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: 74.22  E-value: 4.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  63 GNGSFGVVYQAKLCDSGELVAIKKVLQdkrfKNRELQIMRKLDHCNIVRlryfFYssGEKKDEVYLNLVLDYVPE-TVYR 141
Cdd:cd14060     2 GGGSFGSVYRAIWVSQDKEVAVKKLLK----IEKEAEILSVLSHRNIIQ----FY--GAILEAPNYGIVTEYASYgSLFD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 142 VARhySRAKQTLPVIYVKLYMYQLFRSLAYIHS---FGICHRDIKPQNLLLDPDtAVLKLCDFGSAKqlVRGEPNVSYIC 218
Cdd:cd14060    72 YLN--SNESEEMDMDQIMTWATDIAKGMHYLHMeapVKVIHRDLKSRNVVIAAD-GVLKICDFGASR--FHSHTTHMSLV 146
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1231802383 219 SRY-YRAPELIFGATdYTSSIDVWSAGCVLAELLLGQPIFPGDSG 262
Cdd:cd14060   147 GTFpWMAPEVIQSLP-VSETCDTYSYGVVLWEMLTREVPFKGLEG 190
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
51-261 4.08e-15

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 76.59  E-value: 4.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  51 PQEVSYTDTKVIGNGSFGVVYQAKLC-DSGELVAIKKV-LQDKR---FKNRELQIMRKLDHCNIVRlRYFFYSSGEKkde 125
Cdd:PTZ00267   64 PREHMYVLTTLVGRNPTTAAFVATRGsDPKEKVVAKFVmLNDERqaaYARSELHCLAACDHFGIVK-HFDDFKSDDK--- 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 126 vyLNLVLDY-----VPETVYRvarhysRAKQTLPV--IYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPdTAVLKL 198
Cdd:PTZ00267  140 --LLLIMEYgsggdLNKQIKQ------RLKEHLPFqeYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMP-TGIIKL 210
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1231802383 199 CDFGSAKQL---VRGEPNVSYICSRYYRAPELiFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDS 261
Cdd:PTZ00267  211 GDFGFSKQYsdsVSLDVASSFCGTPYYLAPEL-WERKRYSKKADMWSLGVILYELLTLHRPFKGPS 275
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
56-340 4.65e-15

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: 75.44  E-value: 4.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSG----ELVAIKKVLQDKRFKNRELQIMRKLD-------HCNIVRLRYFFYSSGEKKD 124
Cdd:cd14215    14 YEIVSTLGEGTFGRVVQCIDHRRGgarvALKIIKNVEKYKEAARLEINVLEKINekdpenkNLCVQMFDWFDYHGHMCIS 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 125 EVYLNL-VLDYVPETVYRvarhysrakqTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLL-LDPDTAV------- 195
Cdd:cd14215    94 FELLGLsTFDFLKENNYL----------PYPIHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILfVNSDYELtynlekk 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 196 ----------LKLCDFGSAKqlVRGEPNVSYICSRYYRAPELIFgATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQ 265
Cdd:cd14215   164 rdersvkstaIRVVDFGSAT--FDHEHHSTIVSTRHYRAPEVIL-ELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNREH 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 266 LVEIIKVLGTPTREQIREM-------------NPNYTEFKFPQIKAHPWTKVFRPRTPP--EAIALCSRLLEYTPTARLT 330
Cdd:cd14215   241 LAMMERILGPIPSRMIRKTrkqkyfyhgrldwDENTSAGRYVRENCKPLRRYLTSEAEEhhQLFDLIESMLEYEPSKRLT 320
                         330
                  ....*....|
gi 1231802383 331 PLEACAHSFF 340
Cdd:cd14215   321 LAAALKHPFF 330
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
60-255 5.63e-15

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: 74.64  E-value: 5.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKkVLQDKRFKNRELQ----IMRKL-DHCNIVRLRYFFYssgeKKDEVY---LNLV 131
Cdd:cd06639    28 ETIGKGTYGKVYKVTNKKDGSLAAVK-ILDPISDVDEEIEaeynILRSLpNHPNVVKFYGMFY----KADQYVggqLWLV 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 132 LDYVPE-TVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLV-- 208
Cdd:cd06639   103 LELCNGgSVTELVKGLLKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGV-KLVDFGVSAQLTsa 181
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1231802383 209 RGEPNVSyICSRYYRAPELIFGATDYTSS----IDVWSAGCVLAELLLGQP 255
Cdd:cd06639   182 RLRRNTS-VGTPFWMAPEVIACEQQYDYSydarCDVWSLGITAIELADGDP 231
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
60-263 5.70e-15

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: 74.31  E-value: 5.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLcdSGELVAIKKVLQD------KRFKN--RELQIMRKLDHCNIVRLRyffyssGEKKDEVYLNLV 131
Cdd:cd14145    12 EIIGIGGFGKVYRAIW--IGDEVAVKAARHDpdedisQTIENvrQEAKLFAMLKHPNIIALR------GVCLKEPNLCLV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 132 LDYVPE-TVYRVARhysrAKQTLPVIYVKlYMYQLFRSLAYIHSFGIC---HRDIKPQNLLL-------DPDTAVLKLCD 200
Cdd:cd14145    84 MEFARGgPLNRVLS----GKRIPPDILVN-WAVQIARGMNYLHCEAIVpviHRDLKSSNILIlekvengDLSNKILKITD 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1231802383 201 FGSAKQLVRgEPNVSYICSRYYRAPELIFGATdYTSSIDVWSAGCVLAELLLGQPIFPGDSGV 263
Cdd:cd14145   159 FGLAREWHR-TTKMSAAGTYAWMAPEVIRSSM-FSKGSDVWSYGVLLWELLTGEVPFRGIDGL 219
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
61-257 7.28e-15

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: 74.01  E-value: 7.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  61 VIGNGSFGVVYQAKLCDSGELVAIKkVLQDKRFKNRE-----------LQIMRKLDHCN-IVRLRYFFYSSgEKkdevyL 128
Cdd:cd05606     1 IIGRGGFGEVYGCRKADTGKMYAMK-CLDKKRIKMKQgetlalnerimLSLVSTGGDCPfIVCMTYAFQTP-DK-----L 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 129 NLVLDYVP--ETVYRVARH--YSRAKqtlpviyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSA 204
Cdd:cd05606    74 CFILDLMNggDLHYHLSQHgvFSEAE-------MRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHV-RISDLGLA 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1231802383 205 KQLVRGEPNVSyICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIF 257
Cdd:cd05606   146 CDFSKKKPHAS-VGTHGYMAPEVLQKGVAYDSSADWFSLGCMLYKLLKGHSPF 197
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
62-301 7.59e-15

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: 74.22  E-value: 7.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIK-----KVLQDKRFKNR-------------------------ELQIMRKLDHCNIVR 111
Cdd:cd14200     8 IGKGSYGVVKLAYNESDDKYYAMKvlskkKLLKQYGFPRRppprgskaaqgeqakplaplervyqEIAILKKLDHVNIVK 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 112 LRYFFYSSGEkkDEVYLnlVLDYVPE-TVYRVARHYSRAKQTlpviyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLD 190
Cdd:cd14200    88 LIEVLDDPAE--DNLYM--VFDLLRKgPVMEVPSDKPFSEDQ-----ARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 191 PDTAVlKLCDFGSAKQLVRGEPNVSYIC-SRYYRAPELIF--GATDYTSSIDVWSAGCVLAELLLGQPIFpgdsgVDQLV 267
Cdd:cd14200   159 DDGHV-KIADFGVSNQFEGNDALLSSTAgTPAFMAPETLSdsGQSFSGKALDVWAMGVTLYCFVYGKCPF-----IDEFI 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1231802383 268 ---------EIIKVLGTPT-REQIREM-------NPNyTEFKFPQIKAHPW 301
Cdd:cd14200   233 lalhnkiknKPVEFPEEPEiSEELKDLilkmldkNPE-TRITVPEIKVHPW 282
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
62-306 8.81e-15

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: 74.11  E-value: 8.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKV---LQDKRFKN--RELQIMRKLDHCNIVRLRYFF-----------YSSGEKKDE 125
Cdd:cd06622     9 LGKGNYGSVYKVLHRPTGVTMAMKEIrleLDESKFNQiiMELDILHKAVSPYIVDFYGAFfiegavymcmeYMDAGSLDK 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 126 VYLNLV-LDYVPETVYRvarhysraKQTLPVIyvklymyQLFRSLAYIHSfgICHRDIKPQNLLLDPDTAVlKLCDFGSA 204
Cdd:cd06622    89 LYAGGVaTEGIPEDVLR--------RITYAVV-------KGLKFLKEEHN--IIHRDVKPTNVLVNGNGQV-KLCDFGVS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 205 KQLVRGEPNVSYICSRYYrAPELI-----FGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVD---QLVEIIKvlGTP 276
Cdd:cd06622   151 GNLVASLAKTNIGCQSYM-APERIksggpNQNPTYTVQSDVWSLGLSILEMALGRYPYPPETYANifaQLSAIVD--GDP 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1231802383 277 TR-----------------EQIREMNPNYtefkfPQIKAHPWTKVFR 306
Cdd:cd06622   228 PTlpsgysddaqdfvakclNKIPNRRPTY-----AQLLEHPWLVKYK 269
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
65-328 1.04e-14

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 74.88  E-value: 1.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  65 GSFGVVYQ-AKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFyssgEKKDEVYLnlvldyvpetVYRVA 143
Cdd:PHA03207  103 GSEGEVFVcTKHGDEQRKKVIVKAVTGGKTPGREIDILKTISHRAIINLIHAY----RWKSTVCM----------VMPKY 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 144 RH----YSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLD-PDTAVLKlcDFGSAKQLvrGEPNVSYIC 218
Cdd:PHA03207  169 KCdlftYVDRSGPLPLEQAITIQRRLLEALAYLHGRGIIHRDVKTENIFLDePENAVLG--DFGAACKL--DAHPDTPQC 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 219 SRY-----YRAPELIfgATD-YTSSIDVWSAGCVLAELLLGQPIFPG---DSGVDQLVEIIKVLGTPTREQIREMNPNYT 289
Cdd:PHA03207  245 YGWsgtleTNSPELL--ALDpYCAKTDIWSAGLVLFEMSVKNVTLFGkqvKSSSSQLRSIIRCMQVHPLEFPQNGSTNLC 322
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1231802383 290 -EFK-FPQIKAHPWT--KVFRPRTPP-EAIALCSRLL----EYTPTAR 328
Cdd:PHA03207  323 kHFKqYAIVLRPPYTipPVIRKYGMHmDVEYLIAKMLtfdqEFRPSAQ 370
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
62-269 1.50e-14

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: 73.51  E-value: 1.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIM-RKLDHCNIVRLRYFfYSSGEKkdeVYLNLVLDYVPETVY 140
Cdd:cd14178    11 IGIGSYSVCKRCVHKATSTEYAVKIIDKSKRDPSEEIEILlRYGQHPNIITLKDV-YDDGKF---VYLVMELMRGGELLD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 141 RVARHYSRAKQTLPVIyvklyMYQLFRSLAYIHSFGICHRDIKPQNLLL-----DPDTavLKLCDFGSAKQLVRGEPNVS 215
Cdd:cd14178    87 RILRQKCFSEREASAV-----LCTITKTVEYLHSQGVVHRDLKPSNILYmdesgNPES--IRICDFGFAKQLRAENGLLM 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1231802383 216 YIC-SRYYRAPElIFGATDYTSSIDVWSAGCVLAELLLGQPIF---PGDSGVDQLVEI 269
Cdd:cd14178   160 TPCyTANFVAPE-VLKRQGYDAACDIWSLGILLYTMLAGFTPFangPDDTPEEILARI 216
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
51-339 1.60e-14

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: 72.93  E-value: 1.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  51 PQE-VSYTDTKviGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNR---ELQIMRKLDHCNIVRLRYFFYSSGekkdev 126
Cdd:cd14111     1 PQKpYTFLDEK--ARGRFGVIRRCRENATGKNFPAKIVPYQAEEKQGvlqEYEILKSLHHERIMALHEAYITPR------ 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 127 YLNLVLDYVP--ETVYRVARHYSRAKQTlpviyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAvLKLCDFGSA 204
Cdd:cd14111    73 YLVLIAEFCSgkELLHSLIDRFRYSEDD-----VVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNA-IKIVDFGSA 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 205 KqlvRGEPNVSYICSRY-----YRAPELIFGATdYTSSIDVWSAGcVLAELLLgqpifpgdSGvdqlveiikvlgtptRE 279
Cdd:cd14111   147 Q---SFNPLSLRQLGRRtgtleYMAPEMVKGEP-VGPPADIWSIG-VLTYIML--------SG---------------RS 198
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 280 QIREMNPNYTEFKFPQIKAHPwTKVFrPRTPPEAIALCSRLLEYTPTARLTPLEACAHSF 339
Cdd:cd14111   199 PFEDQDPQETEAKILVAKFDA-FKLY-PNVSQSASLFLKKVLSSYPWSRPTTKDCFAHAW 256
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
56-251 2.06e-14

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: 72.99  E-value: 2.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKvLQDKRFKNR--------ELQIMRKLDHCNIVRLRYFFyssgEKKDEVY 127
Cdd:cd05608     3 FLDFRVLGKGGFGEVSACQMRATGKLYACKK-LNKKRLKKRkgyegamvEKRILAKVHSRFIVSLAYAF----QTKTDLC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 128 LNLVLDYVPETVYRVaRHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQL 207
Cdd:cd05608    78 LVMTIMNGGDLRYHI-YNVDEENPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNV-RISDLGLAVEL 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1231802383 208 VRGEPNV-SYICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAELL 251
Cdd:cd05608   156 KDGQTKTkGYAGTPGFMAPELLLG-EEYDYSVDYFTLGVTLYEMI 199
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
56-301 2.11e-14

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: 72.30  E-value: 2.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFK---------NRELQIMRKLDHC--NIVRLRYFFyssgEKKD 124
Cdd:cd14102     2 YQVGSVLGSGGFGTVYAGSRIADGLPVAVKHVVKERVTEwgtlngvmvPLEIVLLKKVGSGfrGVIKLLDWY----ERPD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 125 EVylnLVLDYVPETVYRVArHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSA 204
Cdd:cd14102    78 GF---LIVMERPEPVKDLF-DFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDLRTGELKLIDFGSG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 205 KqLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREM 284
Cdd:cd14102   154 A-LLKDTVYTDFDGTRVYSPPEWIRYHRYHGRSATVWSLGVLLYDMVCGDIPFEQDEEILRGRLYFRRRVSPECQQLIKW 232
                         250       260
                  ....*....|....*....|
gi 1231802383 285 NPNYTEFKFP---QIKAHPW 301
Cdd:cd14102   233 CLSLRPSDRPtleQIFDHPW 252
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
60-270 2.53e-14

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: 73.02  E-value: 2.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKK-----VLQDKRFK-----NRELQIMRklDHCNIVRLRYFFYSSGEkkdevyLN 129
Cdd:cd05590     1 RVLGKGSFGKVMLARLKESGRLYAVKVlkkdvILQDDDVEctmteKRILSLAR--NHPFLTQLYCCFQTPDR------LF 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 LVLDYVP--ETVYRV--ARHYSRAKqtlpviyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAK 205
Cdd:cd05590    73 FVMEFVNggDLMFHIqkSRRFDEAR-------ARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHC-KLADFGMCK 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1231802383 206 QLVRGEPNVSYIC-SRYYRAPElIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGvDQLVEII 270
Cdd:cd05590   145 EGIFNGKTTSTFCgTPDYIAPE-ILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENE-DDLFEAI 208
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
48-257 2.61e-14

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 73.48  E-value: 2.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  48 PDRPQEVSYTD---TKVIGNGSFGVVYQAKLCDSG-ELVAIKKVLQDKRFKNR-------ELQIMRKLDHCNIVRLRyff 116
Cdd:PTZ00426   21 PKRKNKMKYEDfnfIRTLGTGSFGRVILATYKNEDfPPVAIKRFEKSKIIKQKqvdhvfsERKILNYINHPFCVNLY--- 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 117 yssGEKKDEVYLNLVLDYVPETVYRVarhYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVL 196
Cdd:PTZ00426   98 ---GSFKDESYLYLVLEFVIGGEFFT---FLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKD-GFI 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 197 KLCDFGSAKQLvrgEPNVSYIC-SRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIF 257
Cdd:PTZ00426  171 KMTDFGFAKVV---DTRTYTLCgTPEYIAPEILLN-VGHGKAADWWTLGIFIYEILVGCPPF 228
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
56-257 2.64e-14

Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein 15; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Vps15 is a large protein consisting of an N-terminal kinase domain, a C-terminal WD-repeat containing domain, and an intermediate bridge domain that contain HEAT repeats. The kinase domain is necessary for the signaling functions of Vps15. Human Vps15 was previously called p150. It associates and regulates Vps34, also called Class III phosphoinositide 3-kinase (PI3K), which catalyzes the phosphorylation of D-myo-phosphatidylinositol (PtdIns). Vps34 is the only PI3K present in yeast. It plays an important role in the regulation of protein and vesicular trafficking and sorting, autophagy, trimeric G-protein signaling, and phagocytosis. The Vps15 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 PI3K.


Pssm-ID: 270882 [Multi-domain]  Cd Length: 278  Bit Score: 72.29  E-value: 2.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKlcDSGELVAIKK-VLQD-----KRFKNR-ELQIMRKLDHCNIVrlryfFYSSGEKKDE-VY 127
Cdd:cd13980     2 YLYDKSLGSTRFLKVARAR--HDEGLVVVKVfVKPDpalplRSYKQRlEEIRDRLLELPNVL-----PFQKVIETDKaAY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 128 LnlVLDYVPETVY-RVA-RHYsrakqtLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLkLCDFGSAK 205
Cdd:cd13980    75 L--IRQYVKYNLYdRIStRPF------LNLIEKKWIAFQLLHALNQCHKRGVCHGDIKTENVLVTSWNWVY-LTDFASFK 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1231802383 206 QLVRGEPN---VSY--------ICsryYRAPELIFGATDY-----------TSSIDVWSAGCVLAELLL-GQPIF 257
Cdd:cd13980   146 PTYLPEDNpadFSYffdtsrrrTC---YIAPERFVDALTLdaeserrdgelTPAMDIFSLGCVIAELFTeGRPLF 217
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
62-359 2.79e-14

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: 73.13  E-value: 2.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIM-RKLDHCNIVRLRYFFyssgEKKDEVYLNLVLDYVPETVY 140
Cdd:cd14176    27 IGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEILlRYGQHPNIITLKDVY----DDGKYVYVVTELMKGGELLD 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 141 RVARHYSRAKQTLPVIyvklyMYQLFRSLAYIHSFGICHRDIKPQNLLL-----DPDTavLKLCDFGSAKQLvRGEPNV- 214
Cdd:cd14176   103 KILRQKFFSEREASAV-----LFTITKTVEYLHAQGVVHRDLKPSNILYvdesgNPES--IRICDFGFAKQL-RAENGLl 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 215 -SYICSRYYRAPElIFGATDYTSSIDVWSAGCVLAELLLGQPIFpGDSGVDQLVEIIKVLGTPtreqiremnpnytefKF 293
Cdd:cd14176   175 mTPCYTANFVAPE-VLERQGYDAACDIWSLGVLLYTMLTGYTPF-ANGPDDTPEEILARIGSG---------------KF 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1231802383 294 pQIKAHPWTKVfrprtPPEAIALCSRLLEYTPTARLTPLEACAHSFF---DELrdPNVKLpNGRDTPAL 359
Cdd:cd14176   238 -SLSGGYWNSV-----SDTAKDLVSKMLHVDPHQRLTAALVLRHPWIvhwDQL--PQYQL-NRQDAPHL 297
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
56-271 2.81e-14

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: 73.54  E-value: 2.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQ-DKRFKNR------ELQIMRKLDHCNIVRLRYFFyssgEKKDEVYL 128
Cdd:cd05625     3 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKkDVLLRNQvahvkaERDILAEADNEWVVRLYYSF----QDKDNLYF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 129 nlVLDYVP--ETVYRVARhysraKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFG---- 202
Cdd:cd05625    79 --VMDYIPggDMMSLLIR-----MGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHI-KLTDFGlctg 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 203 -----------SAKQLVR---------GEPNV------------------------SYICSRYYRAPELIFgATDYTSSI 238
Cdd:cd05625   151 frwthdskyyqSGDHLRQdsmdfsnewGDPENcrcgdrlkplerraarqhqrclahSLVGTPNYIAPEVLL-RTGYTQLC 229
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1231802383 239 DVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIK 271
Cdd:cd05625   230 DWWSVGVILFEMLVGQPPFLAQTPLETQMKVIN 262
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
62-253 3.08e-14

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: 72.16  E-value: 3.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKVlQDKRFKNRELQIMRKLDHCNIVRLryffysSGEKKDEVYLNLVLDYVPE-TVY 140
Cdd:cd13991    14 IGRGSFGEVHRMEDKQTGFQCAVKKV-RLEVFRAEELMACAGLTSPRVVPL------YGAVREGPWVNIFMDLKEGgSLG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 141 RVARHYSRakqtLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSA---------KQLVRGE 211
Cdd:cd13991    87 QLIKEQGC----LPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGSDAFLCDFGHAecldpdglgKSLFTGD 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1231802383 212 pnvsYI-CSRYYRAPELIFGATdYTSSIDVWSAGCVLAELLLG 253
Cdd:cd13991   163 ----YIpGTETHMAPEVVLGKP-CDAKVDVWSSCCMMLHMLNG 200
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
56-272 3.42e-14

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: 72.13  E-value: 3.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAiKKVLQDKRFK-----------NRELQIMRKLDHCNIVRLRYFFyssgEKKD 124
Cdd:cd14105     7 YDIGEELGSGQFAVVKKCREKSTGLEYA-AKFIKKRRSKasrrgvsrediEREVSILRQVLHPNIITLHDVF----ENKT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 125 EVYLNLVL-------DYVPEtvyrvarhysraKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLL---DPDTA 194
Cdd:cd14105    82 DVVLILELvaggelfDFLAE------------KESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLldkNVPIP 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 195 VLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIfgatDYTS---SIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIK 271
Cdd:cd14105   150 RIKLIDFGLAHKIEDGNEFKNIFGTPEFVAPEIV----NYEPlglEADMWSIGVITYILLSGASPFLGDTKQETLANITA 225

                  .
gi 1231802383 272 V 272
Cdd:cd14105   226 V 226
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
62-337 3.88e-14

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: 71.85  E-value: 3.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKVLQ----DKRFKNRELQIMRKLDHCNIVRLRYFFyssgEKKDEVYLNLVLDYVPE 137
Cdd:cd14114    10 LGTGAFGVVHRCTERATGNNFAAKFIMTphesDKETVRKEIQIMNQLHHPKLINLHDAF----EDDNEMVLILEFLSGGE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 138 TVYRVA-RHYSRAKQTlpviyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAV-LKLCDFGSAKQLVRGEPNVS 215
Cdd:cd14114    86 LFERIAaEHYKMSEAE-----VINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKRSNeVKLIDFGLATHLDPKESVKV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 216 YICSRYYRAPELIFGATD--YTssiDVWSAGCVLAELLLGQPIFPGDSGVDQLveiikvlgtptrEQIREMNPNYTEFKF 293
Cdd:cd14114   161 TTGTAEFAAPEIVEREPVgfYT---DMWAVGVLSYVLLSGLSPFAGENDDETL------------RNVKSCDWNFDDSAF 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1231802383 294 PQIKahpwtkvfrprtpPEAIALCSRLLEYTPTARLTPLEACAH 337
Cdd:cd14114   226 SGIS-------------EEAKDFIRKLLLADPNKRMTIHQALEH 256
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
62-307 3.98e-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: 72.02  E-value: 3.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKVlqdKRFKNRE--------LQIMRKLDHC-NIVR-LRYFFYSSGEKKDEVYLNLV 131
Cdd:cd06618    23 IGSGTCGQVYKMRHKKTGHVMAVKQM---RRSGNKEenkrilmdLDVVLKSHDCpYIVKcYGYFITDSDVFICMELMSTC 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 132 LDyvpetvyrvaRHYSRAKQTLPVIYVKLYMYQLFRSLAYI-HSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQLVRG 210
Cdd:cd06618   100 LD----------KLLKRIQGPIPEDILGKMTVSIVKALHYLkEKHGVIHRDVKPSNILLD-ESGNVKLCDFGISGRLVDS 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 211 EPNV-SYICSRYYrAPELIFGAT--DYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPN 287
Cdd:cd06618   169 KAKTrSAGCAAYM-APERIDPPDnpKYDIRADVWSLGISLVELATGQFPYRNCKTEFEVLTKILNEEPPSLPPNEGFSPD 247
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1231802383 288 YTEF-------------KFPQIKAHPWTKVFRP 307
Cdd:cd06618   248 FCSFvdlcltkdhryrpKYRELLQHPFIRRYET 280
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
56-304 4.68e-14

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 71.43  E-value: 4.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIgNGSFGVVYQAKLCDSGELVaIKKVLQDKRFKNREL---QIMRklDHCNIVRLRYFFYSsgeKKDEVylnLVL 132
Cdd:PHA03390   19 VKKLKLI-DGKFGKVSVLKHKPTQKLF-VQKIIKAKNFNAIEPmvhQLMK--DNPNFIKLYYSVTT---LKGHV---LIM 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 DYVP-----ETVyrvarhysRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSAKql 207
Cdd:PHA03390   89 DYIKdgdlfDLL--------KKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRAKDRIYLCDYGLCK-- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 208 VRGEPnvsyicSRY-----YRAPELIFGAtDYTSSIDVWSAGCVLAELLLGQPIFPGDSG----VDQL-------VEIIK 271
Cdd:PHA03390  159 IIGTP------SCYdgtldYFSPEKIKGH-NYDVSFDWWAVGVLTYELLTGKHPFKEDEDeeldLESLlkrqqkkLPFIK 231
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1231802383 272 VLGTPTREQIREM---NPNYTEFKFPQIKAHPWTKV 304
Cdd:PHA03390  232 NVSKNANDFVQSMlkyNINYRLTNYNEIIKHPFLKI 267
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
62-338 4.69e-14

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: 71.72  E-value: 4.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN------RELQIMRKLDHCNIVRLRyffyssGEKKDEVYLNLVLDYV 135
Cdd:cd13978     1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIEerkallKEAEKMERARHSYVLPLL------GVCVERRSLGLVMEYM 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 136 PETVYRVARHysRAKQTLPVIYVKLYMYQLFRSLAYIHSF--GICHRDIKPQNLLLDPDTAVlKLCDFGSAK-------- 205
Cdd:cd13978    75 ENGSLKSLLE--REIQDVPWSLRFRIIHEIALGMNFLHNMdpPLLHHDLKPENILLDNHFHV-KISDFGLSKlgmksisa 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 206 QLVRGEPNVSYicSRYYRAPELI-FGATDYTSSIDVWSAGCVLAELLLGQPIFPgDSGVDQLVEIIKVLGT-PTREQIRE 283
Cdd:cd13978   152 NRRRGTENLGG--TPIYMAPEAFdDFNKKPTSKSDVYSFAIVIWAVLTRKEPFE-NAINPLLIMQIVSKGDrPSLDDIGR 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1231802383 284 MNPNytefkfpqikahpwtkvfrpRTPPEAIALCSRLLEYTPTARLTPLEaCAHS 338
Cdd:cd13978   229 LKQI--------------------ENVQELISLMIRCWDGNPDARPTFLE-CLDR 262
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
61-332 5.34e-14

Catalytic domain of Transforming Growth Factor beta Receptor-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 receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), 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. There are two types of TGFbeta receptors included in this subfamily, I and II, that play different roles in signaling. For signaling to occur, the ligand first binds to the high-affinity type II receptor, which is followed by the recruitment of the low-affinity type I receptor to the complex and its activation through trans-phosphorylation by the type II receptor. The active type I receptor kinase starts 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 the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. Different ligands interact with various combinations of types I and II receptors to elicit a specific signaling pathway. Activins primarily signal through combinations of ACVR1b/ALK7 and ACVR2a/b; myostatin and GDF11 through TGFbR1/ALK4 and ACVR2a/b; BMPs through ACVR1/ALK1 and BMPR2; and TGFbeta through TGFbR1 and TGFbR2. The TGFbR-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: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 71.70  E-value: 5.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  61 VIGNGSFGVVYQAKLcdSGELVAIKKV-LQDKRFKNRELQIMRK--LDHCNIVRlryfFYSSGEKKD--EVYLNLVLDYV 135
Cdd:cd13998     2 VIGKGRFGEVWKASL--KNEPVAVKIFsSRDKQSWFREKEIYRTpmLKHENILQ----FIAADERDTalRTELWLVTAFH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 136 PetvyrvarHYSRAKqtlpviYVKLYM----------YQLFRSLAYIHS--FG-------ICHRDIKPQNLLLDPD-TAV 195
Cdd:cd13998    76 P--------NGSL*D------YLSLHTidwvslcrlaLSVARGLAHLHSeiPGctqgkpaIAHRDLKSKNILVKNDgTCC 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 196 lkLCDFGSAKQL--VRGEP---NVSYICSRYYRAPELIFGATDYTSS-----IDVWSAGCVLAELLlgqpifpgdSGVDQ 265
Cdd:cd13998   142 --IADFGLAVRLspSTGEEdnaNNGQVGTKRYMAPEVLEGAINLRDFesfkrVDIYAMGLVLWEMA---------SRCTD 210
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1231802383 266 LVEIIKVLGTPTREQIREmNPNYTEFKF--------PQIKAHpWTKvfrprtPPEAIALCSRLLE---YTPTARLTPL 332
Cdd:cd13998   211 LFGIVEEYKPPFYSEVPN-HPSFEDMQEvvvrdkqrPNIPNR-WLS------HPGLQSLAETIEEcwdHDAEARLTAQ 280
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
62-339 6.11e-14

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: 71.02  E-value: 6.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQA--KLCDSGELVAIK--KVLQDKRFKNRELQIMRKLDHCNIVRLRYFFyssgekKDEVYLNLVLDYVPE 137
Cdd:cd14112    11 IFRGRFSVIVKAvdSTTETDAHCAVKifEVSDEASEAVREFESLRTLQHENVQRLIAAF------KPSNFAYLVMEKLQE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 138 TV--YRVARHYSRAKQtlpviyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAV-LKLCDFGSAkQLVRGEPNV 214
Cdd:cd14112    85 DVftRFSSNDYYSEEQ------VATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSVRSWqVKLVDFGRA-QKVSKLGKV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 215 SYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGdsgvdqlveiikvlGTPTREQIREmNPNYTEFKFP 294
Cdd:cd14112   158 PVDGDTDWASPEFHNPETPITVQSDIWGLGVLTFCLLSGFHPFTS--------------EYDDEEETKE-NVIFVKCRPN 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1231802383 295 QIkahpwtkvFRPRTpPEAIALCSRLLEYTPTARLTPLEACAHSF 339
Cdd:cd14112   223 LI--------FVEAT-QEALRFATWALKKSPTRRMRTDEALEHRW 258
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
61-264 6.43e-14

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: 71.68  E-value: 6.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  61 VIGNGSFGVVYQAKLCDSGELVAIKKVlqDKRFKNRELQIMRK---LDHC----NIVRLRYFFyssgEKKDEVYLNLVLD 133
Cdd:cd14090     9 LLGEGAYASVQTCINLYTGKEYAVKII--EKHPGHSRSRVFREvetLHQCqghpNILQLIEYF----EDDERFYLVFEKM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 134 YVPETVYRVAR--HYSRAKQTLPViyvklymYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAV--LKLCDF--GSAKQL 207
Cdd:cd14090    83 RGGPLLSHIEKrvHFTEQEASLVV-------RDIASALDFLHDKGIAHRDLKPENILCESMDKVspVKICDFdlGSGIKL 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1231802383 208 VRGE------PNVSYIC-SRYYRAPEL----IFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVD 264
Cdd:cd14090   156 SSTSmtpvttPELLTPVgSAEYMAPEVvdafVGEALSYDKRCDLWSLGVILYIMLCGYPPFYGRCGED 223
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
55-251 6.66e-14

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: 70.93  E-value: 6.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  55 SYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKV-LQDKRFKNR-----ELQIMRKLDHCNIVRLRYFFyssgeKKDEVYL 128
Cdd:cd08223     1 EYQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLnLKNASKRERkaaeqEAKLLSKLKHPNIVSYKESF-----EGEDGFL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 129 NLVLDYVpETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQLV 208
Cdd:cd08223    76 YIVMGFC-EGGDLYTRLKEQKGVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLT-KSNIIKVGDLGIARVLE 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1231802383 209 RGEPNVS-YICSRYYRAPELiFGATDYTSSIDVWSAGCVLAELL 251
Cdd:cd08223   154 SSSDMATtLIGTPYYMSPEL-FSNKPYNHKSDVWALGCCVYEMA 196
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
60-270 8.02e-14

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: 72.36  E-value: 8.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKL-------DHCNIVRLRYFFyssgekKDEVYLNLVL 132
Cdd:cd05623    78 KVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETACFREErdvlvngDSQWITTLHYAF------QDDNNLYLVM 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 DYVPETvyRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLVRGEP 212
Cdd:cd05623   152 DYYVGG--DLLTLLSKFEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHI-RLADFGSCLKLMEDGT 228
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1231802383 213 NVSYIC--SRYYRAPELIFGATD----YTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEII 270
Cdd:cd05623   229 VQSSVAvgTPDYISPEILQAMEDgkgkYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIM 292
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
56-255 8.55e-14

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Heme-Regulated Inhibitor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HRI (or EIF2AK1) contains an N-terminal regulatory heme-binding domain and a C-terminal catalytic kinase domain. It is suppressed under normal conditions by binding of the heme iron, and is activated during heme deficiency. It functions as a critical regulator that ensures balanced synthesis of globins and heme, in order to form stable hemoglobin during erythroid differentiation and maturation. HRI also protects cells and enhances survival under iron-deficient conditions. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The HRI 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: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 71.00  E-value: 8.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN------RELQIMRKLDHCNIVRLRYFFYssgekkDEVYLN 129
Cdd:cd14049     8 FEEIARLGKGGYGKVYKVRNKLDGQYYAIKKILIKKVTKRdcmkvlREVKVLAGLQHPNIVGYHTAWM------EHVQLM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 LVL----------DYVPETvYRVARHYSRAKQTLPVIYVKLYM---YQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVL 196
Cdd:cd14049    82 LYIqmqlcelslwDWIVER-NKRPCEEEFKSAPYTPVDVDVTTkilQQLLEGVTYIHSMGIVHRDLKPRNIFLHGSDIHV 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 197 KLCDFGSAKQLVRGEPNVSYICSRY-------------YRAPELIFGaTDYTSSIDVWSAGCVLAELLlgQP 255
Cdd:cd14049   161 RIGDFGLACPDILQDGNDSTTMSRLnglthtsgvgtclYAAPEQLEG-SHYDFKSDMYSIGVILLELF--QP 229
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
62-281 9.11e-14

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: 70.55  E-value: 9.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKK-----VLQDKRFKNRELQIMRKLDHCNIVRLryffYSSGEKKDEVYLnlVLDYVP 136
Cdd:cd05041     3 IGRGNFGDVYRGVLKPDNTEVAVKTcretlPPDLKRKFLQEARILKQYDHPNIVKL----IGVCVQKQPIMI--VMELVP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 137 ETvyRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGsakqLVRGEPNVSY 216
Cdd:cd05041    77 GG--SLLTFLRKKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVG-ENNVLKISDFG----MSREEEDGEY 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1231802383 217 ICSRYYR-------APE-LIFGAtdYTSSIDVWSAGCVLAELL-LGQPIFPGDSgvdqlveiikvlGTPTREQI 281
Cdd:cd05041   150 TVSDGLKqipikwtAPEaLNYGR--YTSESDVWSFGILLWEIFsLGATPYPGMS------------NQQTREQI 209
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
49-261 9.38e-14

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 72.59  E-value: 9.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  49 DRPQEVSYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKV------LQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEK 122
Cdd:PTZ00283   27 AKEQAKKYWISRVLGSGATGTVLCAKRVSDGEPFAVKVVdmegmsEADKNRAQAEVCCLLNCDFFSIVKCHEDFAKKDPR 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 123 KDE--VYLNLVLDYVPETVYRVA-RHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKLC 199
Cdd:PTZ00283  107 NPEnvLMIALVLDYANAGDLRQEiKSRAKTNRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSN-GLVKLG 185
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1231802383 200 DFGSAKQL---VRGEPNVSYICSRYYRAPElIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDS 261
Cdd:PTZ00283  186 DFGFSKMYaatVSDDVGRTFCGTPYYVAPE-IWRRKPYSKKADMFSLGVLLYELLTLKRPFDGEN 249
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
60-270 1.04e-13

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: 71.65  E-value: 1.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNREL-------QIMRKLDHCNIVRLRYFFyssgEKKDEvyLNLVL 132
Cdd:cd05593    21 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVahtltesRVLKNTRHPFLTSLKYSF----QTKDR--LCFVM 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 DYVP--ETVYRVARHYSRAKQTlpviyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLVRG 210
Cdd:cd05593    95 EYVNggELFFHLSRERVFSEDR-----TRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHI-KITDFGLCKEGITD 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 211 EPNVSYIC-SRYYRAPElIFGATDYTSSIDVWSAGCVLAELLLGQ-PIFPGDSgvDQLVEII 270
Cdd:cd05593   169 AATMKTFCgTPEYLAPE-VLEDNDYGRAVDWWGLGVVMYEMMCGRlPFYNQDH--EKLFELI 227
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
61-254 1.14e-13

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: 70.40  E-value: 1.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  61 VIGNGSFGVVYQAKLcdSGELVAIKKVLQDKRFK--------NRELQIMRKLDHCNIVRLRyffyssGEKKDEVYLNLVL 132
Cdd:cd14148     1 IIGVGGFGKVYKGLW--RGEEVAVKAARQDPDEDiavtaenvRQEARLFWMLQHPNIIALR------GVCLNPPHLCLVM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 DYVPETvyrvARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHS---FGICHRDIKPQNLLL-------DPDTAVLKLCDFG 202
Cdd:cd14148    73 EYARGG----ALNRALAGKKVPPHVLVNWAVQIARGMNYLHNeaiVPIIHRDLKSSNILIlepiendDLSGKTLKITDFG 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 203 SAKQLVRgEPNVSYICSRYYRAPELIfGATDYTSSIDVWSAGCVLAELLLGQ 254
Cdd:cd14148   149 LAREWHK-TTKMSAAGTYAWMAPEVI-RLSLFSKSSDVWSFGVLLWELLTGE 198
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
60-263 1.22e-13

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: 70.44  E-value: 1.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLcdSGELVAIKKVLQD--------KRFKNRELQIMRKLDHCNIVRLRyffyssGEKKDEVYLNLV 131
Cdd:cd14147     9 EVIGIGGFGKVYRGSW--RGELVAVKAARQDpdedisvtAESVRQEARLFAMLAHPNIIALK------AVCLEEPNLCLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 132 LDYVPetvyrvARHYSRA---KQTLPVIYVKlYMYQLFRSLAYIHSFGIC---HRDIKPQNLLL-------DPDTAVLKL 198
Cdd:cd14147    81 MEYAA------GGPLSRAlagRRVPPHVLVN-WAVQIARGMHYLHCEALVpviHRDLKSNNILLlqpiendDMEHKTLKI 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1231802383 199 CDFGSAKQLVRgEPNVSYICSRYYRAPELIFGATdYTSSIDVWSAGCVLAELLLGQPIFPGDSGV 263
Cdd:cd14147   154 TDFGLAREWHK-TTQMSAAGTYAWMAPEVIKAST-FSKGSDVWSFGVLLWELLTGEVPYRGIDCL 216
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
60-283 1.32e-13

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: 70.38  E-value: 1.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIK----KVLQDKRFKNRELQIMRKLDHCNIVRLryffYSSGEKKDEVylNLVLDYV 135
Cdd:cd14192    10 EVLGGGRFGQVHKCTELSTGLTLAAKiikvKGAKEREEVKNEINIMNQLNHVNLIQL----YDAFESKTNL--TLIMEYV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 136 P--ETVYRVarhySRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTA-VLKLCDFGSAKQLVRGEP 212
Cdd:cd14192    84 DggELFDRI----TDESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCVNSTGnQIKIIDFGLARRYKPREK 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1231802383 213 NVSYICSRYYRAPELIfgATDYTS-SIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKV---LGTPTREQIRE 283
Cdd:cd14192   160 LKVNFGTPEFLAPEVV--NYDFVSfPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNCkwdFDAEAFENLSE 232
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
56-339 1.49e-13

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: 70.05  E-value: 1.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNR-----ELQIMRKLDHCNIVRLRYFFyssgEKKDEVYLNL 130
Cdd:cd14088     3 YDLGQVIKTEEFCEIFRAKDKTTGKLYTCKKFLKRDGRKVRkaaknEINILKMVKHPNILQLVDVF----ETRKEYFIFL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 -------VLDYVPETVYrvarhYSRaKQTLPVIYvklymyQLFRSLAYIHSFGICHRDIKPQNLLL--DPDTAVLKLCDF 201
Cdd:cd14088    79 elatgreVFDWILDQGY-----YSE-RDTSNVIR------QVLEAVAYLHSLKIVHRNLKLENLVYynRLKNSKIVISDF 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 202 GSAK---QLVRgEPnvsyiC-SRYYRAPELIfGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLgtpt 277
Cdd:cd14088   147 HLAKlenGLIK-EP-----CgTPEYLAPEVV-GRQRYGRPVDCWAIGVIMYILLSGNPPFYDEAEEDDYENHDKNL---- 215
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 278 reqIREMNPNYTEFKFPQikahpWTKVfrprtPPEAIALCSRLLEYTPTARLTPLEACAHSF 339
Cdd:cd14088   216 ---FRKILAGDYEFDSPY-----WDDI-----SQAAKDLVTRLMEVEQDQRITAEEAISHEW 264
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
62-251 1.63e-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: 70.23  E-value: 1.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKVLQ--DKRFKN--RELQIMRKLDHCNIVRLRYFFYSsgEKKdevyLNLVLDYVPE 137
Cdd:cd14154     1 LGKGFFGQAIKVTHRETGEVMVMKELIRfdEEAQRNflKEVKVMRSLDHPNVLKFIGVLYK--DKK----LNLITEYIPG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 138 -TVYRVARHYSrakQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLkLCDFGSAKQLV--RGEPNV 214
Cdd:cd14154    75 gTLKDVLKDMA---RPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVV-VADFGLARLIVeeRLPSGN 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1231802383 215 SYICSR-------------------YYRAPELIFGaTDYTSSIDVWSAGCVLAELL 251
Cdd:cd14154   151 MSPSETlrhlkspdrkkrytvvgnpYWMAPEMLNG-RSYDEKVDIFSFGIVLCEII 205
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
62-330 1.68e-13

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: 70.34  E-value: 1.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVV----YQAKLCDSGELVAIKKVLQDKRFKN-----RELQIMRKLDHCNIVRLRYFFYSSGEKKdevyLNLVL 132
Cdd:cd05079    12 LGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPESGGNHiadlkKEIEILRNLYHENIVKYKGICTEDGGNG----IKLIM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 DYVPETVYRvaRHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLvrgEP 212
Cdd:cd05079    88 EFLPSGSLK--EYLPRNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQV-KIGDFGLTKAI---ET 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 213 NVSYICSR-------YYRAPELIFGATDYTSSiDVWSAGCVLAELLLgqpifPGDSGVDQLVEIIKVLGtPTREQI---R 282
Cdd:cd05079   162 DKEYYTVKddldspvFWYAPECLIQSKFYIAS-DVWSFGVTLYELLT-----YCDSESSPMTLFLKMIG-PTHGQMtvtR 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1231802383 283 EMNPNYTEFKFPqikahpwtkvfRPRTPPEAI-ALCSRLLEYTPTARLT 330
Cdd:cd05079   235 LVRVLEEGKRLP-----------RPPNCPEEVyQLMRKCWEFQPSKRTT 272
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
53-266 2.07e-13

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: 69.56  E-value: 2.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  53 EVSYTDTKVIGNGSFGVVYQAKLCDSGELVAiKKVLQDKRFKNR-----ELQIMRKLDHCNIVRLryffYSSGEKKDEVY 127
Cdd:cd14190     3 TFSIHSKEVLGGGKFGKVHTCTEKRTGLKLA-AKVINKQNSKDKemvllEIQVMNQLNHRNLIQL----YEAIETPNEIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 128 LnlVLDYVP--ETVYRVARHYSRAKQTLPVIYVKlymyQLFRSLAYIHSFGICHRDIKPQNLLLDPDTA-VLKLCDFGSA 204
Cdd:cd14190    78 L--FMEYVEggELFERIVDEDYHLTEVDAMVFVR----QICEGIQFMHQMRVLHLDLKPENILCVNRTGhQVKIIDFGLA 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1231802383 205 KqlvRGEPN----VSYICSRYYrAPELIfgATDYTS-SIDVWSAGCVLAELLLGQPIFPGDSGVDQL 266
Cdd:cd14190   152 R---RYNPReklkVNFGTPEFL-SPEVV--NYDQVSfPTDMWSMGVITYMLLSGLSPFLGDDDTETL 212
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
62-251 2.09e-13

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: 69.60  E-value: 2.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKVL----QDKRFKNRELQIMRKLDHCNIVRLRYFFYSsgEKKdevyLNLVLDYVPE 137
Cdd:cd14221     1 LGKGCFGQAIKVTHRETGEVMVMKELIrfdeETQRTFLKEVKVMRCLEHPNVLKFIGVLYK--DKR----LNFITEYIKG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 138 TVYR-----VARHYSRAKQtlpVIYVKlymyQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLkLCDFGSAKQLVRGEP 212
Cdd:cd14221    75 GTLRgiiksMDSHYPWSQR---VSFAK----DIASGMAYLHSMNIIHRDLNSHNCLVRENKSVV-VADFGLARLMVDEKT 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1231802383 213 NVSYICSR---------------YYRAPELIFGATdYTSSIDVWSAGCVLAELL 251
Cdd:cd14221   147 QPEGLRSLkkpdrkkrytvvgnpYWMAPEMINGRS-YDEKVDVFSFGIVLCEII 199
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
53-272 3.46e-13

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: 69.26  E-value: 3.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  53 EVSYTDTKVIGNGSFGVVYQAKLCDSGELVAiKKVLQDKRFKN-----------RELQIMRKLDHCNIVRLRYFFyssgE 121
Cdd:cd14195     4 EDHYEMGEELGSGQFAIVRKCREKGTGKEYA-AKFIKKRRLSSsrrgvsreeieREVNILREIQHPNIITLHDIF----E 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 122 KKDEVYLNLVLDYVPETVYRVARhysraKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQN-LLLDPDTAV--LKL 198
Cdd:cd14195    79 NKTDVVLILELVSGGELFDFLAE-----KESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENiMLLDKNVPNprIKL 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1231802383 199 CDFGSAKQLVRGEPNVSYICSRYYRAPELIfgatDYTS---SIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKV 272
Cdd:cd14195   154 IDFGIAHKIEAGNEFKNIFGTPEFVAPEIV----NYEPlglEADMWSIGVITYILLSGASPFLGETKQETLTNISAV 226
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
59-255 5.07e-13

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: 68.88  E-value: 5.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  59 TKVIGNGSFGVVYQAKLCDSGELVAIKkVLQDKRFKNRELQ----IMRKL-DHCNIVRLrYFFYSSGEKKDEVYLNLVLD 133
Cdd:cd06638    23 IETIGKGTYGKVFKVLNKKNGSKAAVK-ILDPIHDIDEEIEaeynILKALsDHPNVVKF-YGMYYKKDVKNGDQLWLVLE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 134 YVPE-TVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQL--VRG 210
Cdd:cd06638   101 LCNGgSVTDLVKGFLKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGV-KLVDFGVSAQLtsTRL 179
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1231802383 211 EPNVSyICSRYYRAPELIFGA----TDYTSSIDVWSAGCVLAELLLGQP 255
Cdd:cd06638   180 RRNTS-VGTPFWMAPEVIACEqqldSTYDARCDVWSLGITAIELGDGDP 227
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
60-340 5.12e-13

Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNT7 is a plant thylakoid-associated kinase that is essential in short- and long-term acclimation responses to cope with various light conditions in order to maintain photosynthetic redox poise for optimal photosynthetic performance. Short-term response involves state transitions over periods of minutes while the long-term response (LTR) occurs over hours to days and involves changing the relative amounts of photosystems I and II. SNT7 acts as a redox sensor and a signal transducer for both responses, which are triggered by the redox state of the plastoquinone (PQ) pool. It is positioned at the top of a phosphorylation cascade that induces state transitions by phosphorylating light-harvesting complex II (LHCII), and triggers the LTR through the phosphorylation of chloroplast proteins. The SNT7 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: 270915 [Multi-domain]  Cd Length: 318  Bit Score: 69.00  E-value: 5.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGEL-----VAIKKVlqdKRFKNREL----QIMRKLDHCNIVRLRYFFYSSGEKKDEVYLNL 130
Cdd:cd14013     1 KKLGEGGFGTVYKGSLLQKDPGgekrrVVLKKA---KEYGEVEIwmneRVRRACPSSCAEFVGAFLDTTSKKFTKPSLWL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 VLDYVPE-TVYRVARHYSRAKQTLPVIY----------------VKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDT 193
Cdd:cd14013    78 VWKYEGDaTLADLMQGKEFPYNLEPIIFgrvlipprgpkrenviIKSIMRQILVALRKLHSTGIVHRDVKPQNIIVSEGD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 194 AVLKLCDFGSAKQLVRGepnVSYICSRY-----YRAPELIFGATDYTSS---------------------IDVWSAGCVL 247
Cdd:cd14013   158 GQFKIIDLGAAADLRIG---INYIPKEFlldprYAPPEQYIMSTQTPSAppapvaaalspvlwqmnlpdrFDMYSAGVIL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 248 AELLLgqPIFPGDSGvdqlveIIKVlgtptREQIREMNPNYTEfkfpqikahpWTKVFRPRTPPEAIA------------ 315
Cdd:cd14013   235 LQMAF--PNLRSDSN------LIAF-----NRQLKQCDYDLNA----------WRMLVEPRASADLREgfeildlddgag 291
                         330       340
                  ....*....|....*....|....*..
gi 1231802383 316 --LCSRLLEYTPTARLTPLEACAHSFF 340
Cdd:cd14013   292 wdLVTKLIRYKPRGRLSASAALAHPYF 318
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
61-261 5.26e-13

Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and Anti-Muellerian Hormone Type II Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR2 and AMHR2 belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors (GDFs), and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. BMPR2 and AMHR2 act primarily as a receptor for BMPs and AMH, respectively. BMPs induce bone and cartilage formation, as well as regulate tooth, kidney, skin, hair, haematopoietic, and neuronal development. Mutations in BMPR2A is associated with familial pulmonary arterial hypertension. AMH is mainly responsible for the regression of Mullerian ducts during male sex differentiation. It is expressed exclusively by somatic cells of the gonads. Mutations in either AMH or AMHR2 cause persistent Mullerian duct syndrome (PMDS), a rare form of male pseudohermaphroditism characterized by the presence of Mullerian derivatives (ovary and tubes) in otherwise normally masculine males. The BMPR2/AMHR2 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: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 68.93  E-value: 5.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  61 VIGNGSFGVVYQAKLcdSGELVAIKKVLQDKR--FKNrELQIMR--KLDHCNIVRlryfFYSSGEKKDEV----YLnLVL 132
Cdd:cd14054     2 LIGQGRYGTVWKGSL--DERPVAVKVFPARHRqnFQN-EKDIYElpLMEHSNILR----FIGADERPTADgrmeYL-LVL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 DYVP-ETVYRVARHYSRAKQTLpviyvkLYMYQ-LFRSLAYIHSF---------GICHRDIKPQNLLLDPDTAVLkLCDF 201
Cdd:cd14054    74 EYAPkGSLCSYLRENTLDWMSS------CRMALsLTRGLAYLHTDlrrgdqykpAIAHRDLNSRNVLVKADGSCV-ICDF 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1231802383 202 GSAKQL-----VRGEPN------VSYICSRYYRAPELIFGATD------YTSSIDVWSAGCVLAELLLGQP-IFPGDS 261
Cdd:cd14054   147 GLAMVLrgsslVRGRPGaaenasISEVGTLRYMAPEVLEGAVNlrdcesALKQVDVYALGLVLWEIAMRCSdLYPGES 224
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
60-264 6.28e-13

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: 68.52  E-value: 6.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKVlqDKRFKNRELQIMRKLD-------HCNIVRLRYFFyssgEKKDEVYL---N 129
Cdd:cd14173     8 EVLGEGAYARVQTCINLITNKEYAVKII--EKRPGHSRSRVFREVEmlyqcqgHRNVLELIEFF----EEEDKFYLvfeK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 LVLDYVPETVYRvARHYSRAKQTLPViyvklymYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAV--LKLCDF--GSAK 205
Cdd:cd14173    82 MRGGSILSHIHR-RRHFNELEASVVV-------QDIASALDFLHNKGIAHRDLKPENILCEHPNQVspVKICDFdlGSGI 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1231802383 206 QLVR-----GEPNVSYIC-SRYYRAPELIFG----ATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVD 264
Cdd:cd14173   154 KLNSdcspiSTPELLTPCgSAEYMAPEVVEAfneeASIYDKRCDLWSLGVILYIMLSGYPPFVGRCGSD 222
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
161-320 6.33e-13

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: 69.26  E-value: 6.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 161 YMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTaVLKLCDFGSAKQLVRGEPNVSYICSRY---YRAPELIFGATdYTSS 237
Cdd:cd14207   185 YSFQVARGMEFLSSRKCIHRDLAARNILLSENN-VVKICDFGLARDIYKNPDYVRKGDARLplkWMAPESIFDKI-YSTK 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 238 IDVWSAGCVLAELL-LGQPIFPGdsgvdqlVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKvfRPRTPPEAIAL 316
Cdd:cd14207   263 SDVWSYGVLLWEIFsLGASPYPG-------VQIDEDFCSKLKEGIRMRAPEFATSEIYQIMLDCWQG--DPNERPRFSEL 333

                  ....
gi 1231802383 317 CSRL 320
Cdd:cd14207   334 VERL 337
PLN03225 PLN03225
Serine/threonine-protein kinase SNT7; Provisional
60-370 6.62e-13

Serine/threonine-protein kinase SNT7; Provisional


Pssm-ID: 215638 [Multi-domain]  Cd Length: 566  Bit Score: 69.82  E-value: 6.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKVLqdKRFK---------NRELQIMrkldhC--NIVRLRYFFY--SSGEKKDEV 126
Cdd:PLN03225  138 KKLGEGAFGVVYKASLVNKQSKKEGKYVL--KKATeygaveiwmNERVRRA-----CpnSCADFVYGFLepVSSKKEDEY 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 127 YL-----------NLVLDyvPETVYRVARHYSRAKQTLP------VIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLL 189
Cdd:PLN03225  211 WLvwryegestlaDLMQS--KEFPYNVEPYLLGKVQDLPkglereNKIIQTIMRQILFALDGLHSTGIVHRDVKPQNIIF 288
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 190 DPDTAVLKLCDFGSAKQLVRGepnVSYICSRY-----YRAPELIFGATDYTSS---------------------IDVWSA 243
Cdd:PLN03225  289 SEGSGSFKIIDLGAAADLRVG---INYIPKEFlldprYAAPEQYIMSTQTPSApsapvatalspvlwqlnlpdrFDIYSA 365
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 244 GcvlaeLLLGQPIFPG---DSGVDQLveiikvlgtptREQIREMNPNYTEfkfpqikahpWTKVFRPRTPPE-------- 312
Cdd:PLN03225  366 G-----LIFLQMAFPNlrsDSNLIQF-----------NRQLKRNDYDLVA----------WRKLVEPRASPDlrrgfevl 419
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1231802383 313 ------AIALCSRLLEYTPTARLTPLEACAHSFFDElRDPNVKLPNGRDTPALFNFTTQDANTG 370
Cdd:PLN03225  420 dldggaGWELLKSMMRFKGRQRISAKAALAHPYFDR-EGLLGLSVMQNLRLQLFRATQQDYGEA 482
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
62-272 8.85e-13

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: 68.06  E-value: 8.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKVlqDKRFKN------------RELQIMRKLDHCNIVRLRYFFyssgEKKDEVYLN 129
Cdd:cd14196    13 LGSGQFAIVKKCREKSTGLEYAAKFI--KKRQSRasrrgvsreeieREVSILRQVLHPNIITLHDVY----ENRTDVVLI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 LVLDYVPETVYRVARhysraKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQN-LLLDPDTAV--LKLCDFGSAKQ 206
Cdd:cd14196    87 LELVSGGELFDFLAQ-----KESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENiMLLDKNIPIphIKLIDFGLAHE 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1231802383 207 LVRGEPNVSYICSRYYRAPELIfgatDYTS---SIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKV 272
Cdd:cd14196   162 IEDGVEFKNIFGTPEFVAPEIV----NYEPlglEADMWSIGVITYILLSGASPFLGDTKQETLANITAV 226
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
62-337 1.06e-12

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: 67.74  E-value: 1.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAiKKVLQDKRFKN-----------RELQIMRKLDHCNIVRLRYFFyssgEKKDEVYLNL 130
Cdd:cd14194    13 LGSGQFAVVKKCREKSTGLQYA-AKFIKKRRTKSsrrgvsredieREVSILKEIQHPNVITLHEVY----ENKTDVILIL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 VL-------DYVPEtvyrvarhysraKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQN-LLLDPDT--AVLKLCD 200
Cdd:cd14194    88 ELvaggelfDFLAE------------KESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENiMLLDRNVpkPRIKIID 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 201 FGSAKQLVRGEPNVSYICSRYYRAPELIfgatDYTS---SIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVlgtpt 277
Cdd:cd14194   156 FGLAHKIDFGNEFKNIFGTPEFVAPEIV----NYEPlglEADMWSIGVITYILLSGASPFLGDTKQETLANVSAV----- 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 278 reqiremnpNYtEFKfpqikahpwtKVFRPRTPPEAIALCSRLLEYTPTARLTPLEACAH 337
Cdd:cd14194   227 ---------NY-EFE----------DEYFSNTSALAKDFIRRLLVKDPKKRMTIQDSLQH 266
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
62-278 1.15e-12

Catalytic domain of an unknown subfamily of 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. This group is composed of uncharacterized proteins with similarity to LIMK and Testicular or testis-specific protein kinase (TESK). 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: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 67.16  E-value: 1.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGElVAIKKVLQDKRFKN---RELQIMRKLDHCNIVRlryffYSSGEKKDEvYLNLVLDYVP-- 136
Cdd:cd14156     1 IGSGFFSKVYKVTHGATGK-VMVVKIYKNDVDQHkivREISLLQKLSHPNIVR-----YLGICVKDE-KLHPILEYVSgg 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 137 --ETVYrvarhysrAKQTLPVIY---VKLYMyQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLK--LCDFGSAKQLVR 209
Cdd:cd14156    74 clEELL--------AREELPLSWrekVELAC-DISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGREavVTDFGLAREVGE 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 210 GEPN-----VSYICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIFP------GDSGVDQLVEIIKVLGTPTR 278
Cdd:cd14156   145 MPANdperkLSLVGSAFWMAPEMLRG-EPYDRKVDVFSFGIVLCEILARIPADPevlprtGDFGLDVQAFKEMVPGCPEP 223
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
60-368 1.30e-12

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: 68.51  E-value: 1.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCN--------IVRLRYFFyssgekKDEVYLNLV 131
Cdd:cd05617    21 RVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFeqassnpfLVGLHSCF------QTTSRLFLV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 132 LDYVP--ETVYRVARhysraKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLVR 209
Cdd:cd05617    95 IEYVNggDLMFHMQR-----QRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHI-KLTDYGMCKEGLG 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 210 GEPNVSYIC-SRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIF------PGDSGVDQLVEIIkvLGTPTREQir 282
Cdd:cd05617   169 PGDTTSTFCgTPNYIAPEILRG-EEYGFSVDWWALGVLMFEMMAGRSPFdiitdnPDMNTEDYLFQVI--LEKPIRIP-- 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 283 emnpnytefKFPQIKAHPWTKVFRPRTPPEAIAlCSRLLEYTptarltplEACAHSFF-----DELRDPNVK---LPNGR 354
Cdd:cd05617   244 ---------RFLSVKASHVLKGFLNKDPKERLG-CQPQTGFS--------DIKSHTFFrsidwDLLEKKQVTppfKPQIT 305
                         330
                  ....*....|....
gi 1231802383 355 DTPALFNFTTQDAN 368
Cdd:cd05617   306 DDYGLENFDTQFTS 319
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
60-267 1.37e-12

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: 67.35  E-value: 1.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLcdSGElVAIK--KVL-----QDKRFKNrELQIMRKLDHCNIVRLRYFFYSSGE-------KKDE 125
Cdd:cd14150     6 KRIGTGSFGTVFRGKW--HGD-VAVKilKVTeptpeQLQAFKN-EMQVLRKTRHVNILLFMGFMTRPNFaiitqwcEGSS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 126 VYLNLvldYVPETVYRVARHYSRAKQTLpviyvklymyqlfRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAK 205
Cdd:cd14150    82 LYRHL---HVTETRFDTMQLIDVARQTA-------------QGMDYLHAKNIIHRDLKSNNIFLHEGLTV-KIGDFGLAT 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1231802383 206 QLVR---GEPNVSYICSRYYRAPELIF--GATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLV 267
Cdd:cd14150   145 VKTRwsgSQQVEQPSGSILWMAPEVIRmqDTNPYSFQSDVYAYGVVLYELMSGTLPYSNINNRDQII 211
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
62-254 1.95e-12

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: 66.89  E-value: 1.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKVLQ--DKRFKN--RELQIMRKLDHCNIVRLRYFFYssgekKDEvYLNLVLDYVPE 137
Cdd:cd14222     1 LGKGFFGQAIKVTHKATGKVMVMKELIRcdEETQKTflTEVKVMRSLDHPNVLKFIGVLY-----KDK-RLNLLTEFIEG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 138 TVYRvarHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLkLCDFGSAKQLVRGEP----- 212
Cdd:cd14222    75 GTLK---DFLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVV-VADFGLSRLIVEEKKkpppd 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1231802383 213 ----------------NVSYICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAElLLGQ 254
Cdd:cd14222   151 kpttkkrtlrkndrkkRYTVVGNPYWMAPEMLNG-KSYDEKVDIFSFGIVLCE-IIGQ 206
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
56-257 1.99e-12

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: 67.78  E-value: 1.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNR-------ELQIMRKLDHCNIVRLryfFYSSGEKKDevyL 128
Cdd:cd05627     4 FESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEqvahiraERDILVEADGAWVVKM---FYSFQDKRN---L 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 129 NLVLDYVP--ETVYRVARhysraKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSA-- 204
Cdd:cd05627    78 YLIMEFLPggDMMTLLMK-----KDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHV-KLSDFGLCtg 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 205 ----------KQLVRGEPN------------------------VSYICSRYYRAPElIFGATDYTSSIDVWSAGCVLAEL 250
Cdd:cd05627   152 lkkahrtefyRNLTHNPPSdfsfqnmnskrkaetwkknrrqlaYSTVGTPDYIAPE-VFMQTGYNKLCDWWSLGVIMYEM 230

                  ....*..
gi 1231802383 251 LLGQPIF 257
Cdd:cd05627   231 LIGYPPF 237
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
97-346 2.03e-12

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 68.10  E-value: 2.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  97 ELQIMRKLDHCNIVRLR-YFFYSSgekkdevYLNLVLDYVPETVYrvarHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSF 175
Cdd:PHA03212  133 EAHILRAINHPSIIQLKgTFTYNK-------FTCLILPRYKTDLY----CYLAAKRNIAICDILAIERSVLRAIQYLHEN 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 176 GICHRDIKPQNLLLDPDTAVLkLCDFGSAKQLVRGEPNvsyicsRYY--------RAPELIfgATD-YTSSIDVWSAGCV 246
Cdd:PHA03212  202 RIIHRDIKAENIFINHPGDVC-LGDFGAACFPVDINAN------KYYgwagtiatNAPELL--ARDpYGPAVDIWSAGIV 272
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 247 LAELLLGQ-PIFPGDsGVD-------QLVEIIKVLGTPTRE-------QIREMNPNYTEFKFPQIKAHP-WTKVFrpRTP 310
Cdd:PHA03212  273 LFEMATCHdSLFEKD-GLDgdcdsdrQIKLIIRRSGTHPNEfpidaqaNLDEIYIGLAKKSSRKPGSRPlWTNLY--ELP 349
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1231802383 311 PEAIALCSRLLEYTPTARLTPLEACAHSFFDELRDP 346
Cdd:PHA03212  350 IDLEYLICKMLAFDAHHRPSAEALLDFAAFQDIPDP 385
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
51-255 2.52e-12

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: 66.62  E-value: 2.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  51 PQEVsYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKV-LQDKRFK----NRELQIMRKLDHCNIVRlryfFYSSGEKKDE 125
Cdd:cd06642     2 PEEL-FTKLERIGKGSFGEVYKGIDNRTKEVVAIKIIdLEEAEDEiediQQEITVLSQCDSPYITR----YYGSYLKGTK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 126 VYLnlVLDYVPETVYRVARHYSRAKQTlpviYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAK 205
Cdd:cd06642    77 LWI--IMEYLGGGSALDLLKPGPLEET----YIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDV-KLADFGVAG 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1231802383 206 QLVRGE-PNVSYICSRYYRAPELIfGATDYTSSIDVWSAGCVLAELLLGQP 255
Cdd:cd06642   150 QLTDTQiKRNTFVGTPFWMAPEVI-KQSAYDFKADIWSLGITAIELAKGEP 199
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
60-268 3.40e-12

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: 66.28  E-value: 3.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGEL----VAIKKVLQDKRFKN-----RELQIMRKLDHCNIVRLRYFFYSSGEKKDEVYLNL 130
Cdd:cd05057    13 KVLGSGAFGTVYKGVWIPEGEKvkipVAIKVLREETGPKAneeilDEAYVMASVDHPHLVRLLGICLSSQVQLITQLMPL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 --VLDYVPETVYRVarhysRAKQTLPviyvklYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLV 208
Cdd:cd05057    93 gcLLDYVRNHRDNI-----GSQLLLN------WCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHV-KITDFGLAKLLD 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1231802383 209 RGEPNVSYICSRY---YRAPELIFgATDYTSSIDVWSAGCVLAELL-LGQPIFPGDSGVD--QLVE 268
Cdd:cd05057   161 VDEKEYHAEGGKVpikWMALESIQ-YRIYTHKSDVWSYGVTVWELMtFGAKPYEGIPAVEipDLLE 225
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
56-247 3.60e-12

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: 66.81  E-value: 3.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRfKNRELQIMR-------KLDHCNIVRLRYFFY---------SS 119
Cdd:cd13977     2 YSLIREVGRGSYGVVYEAVVRRTGARVAVKKIRCNAP-ENVELALREfwalssiQRQHPNVIQLEECVLqrdglaqrmSH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 120 GEKKDEVYLNLV-----------------LDYVPE-------TVYRVARHYSRAKQTLpviyvklYMYQLFRSLAYIHSF 175
Cdd:cd13977    81 GSSKSDLYLLLVetslkgercfdprsacyLWFVMEfcdggdmNEYLLSRRPDRQTNTS-------FMLQLSSALAFLHRN 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 176 GICHRDIKPQNLLLDP--DTAVLKLCDFGSAK----QLVRGEPNV-------SYIC-SRYYRAPELIFGatDYTSSIDVW 241
Cdd:cd13977   154 QIVHRDLKPDNILISHkrGEPILKVADFGLSKvcsgSGLNPEEPAnvnkhflSSACgSDFYMAPEVWEG--HYTAKADIF 231

                  ....*.
gi 1231802383 242 SAGCVL 247
Cdd:cd13977   232 ALGIII 237
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
60-253 3.66e-12

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: 66.22  E-value: 3.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLcdSGElVAIKKV-------LQDKRFKnRELQIMRKLDHCNIVrlryFFYssGEKKDEVYLNLVL 132
Cdd:cd14063     6 EVIGKGRFGRVHRGRW--HGD-VAIKLLnidylneEQLEAFK-EEVAAYKNTRHDNLV----LFM--GACMDPPHLAIVT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 DYVP-ETVYRVARHysrAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKlcDFG---SAKQLV 208
Cdd:cd14063    76 SLCKgRTLYSLIHE---RKEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLENGRVVIT--DFGlfsLSGLLQ 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1231802383 209 RGEPNVSYICSRY---YRAPELI---------FGATDYTSSIDVWSAGCVLAELLLG 253
Cdd:cd14063   151 PGRREDTLVIPNGwlcYLAPEIIralspdldfEESLPFTKASDVYAFGTVWYELLAG 207
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
56-257 3.84e-12

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: 66.99  E-value: 3.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNR-------ELQIMRKLDHCNIVRLRYFFyssgekKDEVYL 128
Cdd:cd05628     3 FESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEqvghiraERDILVEADSLWVVKMFYSF------QDKLNL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 129 NLVLDYVP--ETVYRVARhysraKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQ 206
Cdd:cd05628    77 YLIMEFLPggDMMTLLMK-----KDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHV-KLSDFGLCTG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 207 LV------------------------------------RGEPNVSYICSRYYRAPElIFGATDYTSSIDVWSAGCVLAEL 250
Cdd:cd05628   151 LKkahrtefyrnlnhslpsdftfqnmnskrkaetwkrnRRQLAFSTVGTPDYIAPE-VFMQTGYNKLCDWWSLGVIMYEM 229

                  ....*..
gi 1231802383 251 LLGQPIF 257
Cdd:cd05628   230 LIGYPPF 236
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
60-257 5.30e-12

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: 66.59  E-value: 5.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCN--------IVRLRYFFyssgekKDEVYLNLV 131
Cdd:cd05618    26 RVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEDIDWVQTEKHVFeqasnhpfLVGLHSCF------QTESRLFFV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 132 LDYVP--ETVYRVARhysraKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLVR 209
Cdd:cd05618   100 IEYVNggDLMFHMQR-----QRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHI-KLTDYGMCKEGLR 173
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1231802383 210 GEPNVSYIC-SRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIF 257
Cdd:cd05618   174 PGDTTSTFCgTPNYIAPEILRG-EDYGFSVDWWALGVLMFEMMAGRSPF 221
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
60-328 7.46e-12

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: 65.03  E-value: 7.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGElVAIKKVLQD--KRFKNR---ELQIMRKLDHCNIVRLryffYSSGEKKDEVYLnlVLDY 134
Cdd:cd05085     2 ELLGKGNFGEVYKGTLKDKTP-VAVKTCKEDlpQELKIKflsEARILKQYDHPNIVKL----IGVCTQRQPIYI--VMEL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 135 VPETVYrvARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQlvrgEPNV 214
Cdd:cd05085    75 VPGGDF--LSFLRKKKDELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVG-ENNALKISDFGMSRQ----EDDG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 215 SYICSRY------YRAPE-LIFGAtdYTSSIDVWSAGCVLAELL-LGQPIFPGdsgvdqlveiikvlgtPTREQIREMNP 286
Cdd:cd05085   148 VYSSSGLkqipikWTAPEaLNYGR--YSSESDVWSFGILLWETFsLGVCPYPG----------------MTNQQAREQVE 209
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1231802383 287 NYTEFKFPQikahpwtkvfrpRTPPEAIALCSRLLEYTPTAR 328
Cdd:cd05085   210 KGYRMSAPQ------------RCPEDIYKIMQRCWDYNPENR 239
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
62-270 8.43e-12

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: 65.08  E-value: 8.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLcdSGElVAIKKV-------LQDKRFKNrELQIMRKLDHCNIvrLRYFFYSSGEK---------KDE 125
Cdd:cd14151    16 IGSGSFGTVYKGKW--HGD-VAVKMLnvtaptpQQLQAFKN-EVGVLRKTRHVNI--LLFMGYSTKPQlaivtqwceGSS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 126 VYLNLvldYVPETVYRVARHYSRAKQTLpviyvklymyqlfRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSA- 204
Cdd:cd14151    90 LYHHL---HIIETKFEMIKLIDIARQTA-------------QGMDYLHAKSIIHRDLKSNNIFLHEDLTV-KIGDFGLAt 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 205 -KQLVRGEPNVSYIC-SRYYRAPELIF--GATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEII 270
Cdd:cd14151   153 vKSRWSGSHQFEQLSgSILWMAPEVIRmqDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMV 222
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
62-251 9.52e-12

Catalytic domain of the Dual-specificity protein kinase, Testicular protein 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. TESK proteins phosphorylate cofilin and induce actin cytoskeletal reorganization. In the Drosphila eye, TESK is required for epithelial cell organization. Mammals contain two TESK proteins, TESK1 and TESK2, which are highly expressed in testis and play roles in spermatogenesis. TESK1 is found in testicular germ cells while TESK2 is expressed mainly in nongerminal Sertoli cells. TESK1 is stimulated by integrin-mediated signaling pathways. It regulates cell spreading and focal adhesion formation. The TESK 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: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 64.42  E-value: 9.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIK--KVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEkkdevyLNLVLDYVP--- 136
Cdd:cd14155     1 IGSGFFSEVYKVRHRTSGQVMALKmnTLSSNRANMLREVQLMNRLSHPNILRFMGVCVHQGQ------LHALTEYINggn 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 137 -ETVYRVARHYSRAKQtlpviyVKLyMYQLFRSLAYIHSFGICHRDIKPQNLLLDPD----TAVLKlcDFGSAKQL---- 207
Cdd:cd14155    75 lEQLLDSNEPLSWTVR------VKL-ALDIARGLSYLHSKGIFHRDLTSKNCLIKRDengyTAVVG--DFGLAEKIpdys 145
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1231802383 208 VRGEPnVSYICSRYYRAPELIFGATdYTSSIDVWSAGCVLAELL 251
Cdd:cd14155   146 DGKEK-LAVVGSPYWMAPEVLRGEP-YNEKADVFSYGIILCEII 187
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
51-307 1.10e-11

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: 64.69  E-value: 1.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  51 PQEVsYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKV-LQDKRFK----NRELQIMRKLDHCNIVRLrYFFYSSGEKkde 125
Cdd:cd06640     2 PEEL-FTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIdLEEAEDEiediQQEITVLSQCDSPYVTKY-YGSYLKGTK--- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 126 vyLNLVLDYVPETVyrvARHYSRAKqTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAK 205
Cdd:cd06640    77 --LWIIMEYLGGGS---ALDLLRAG-PFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDV-KLADFGVAG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 206 QLVRGE-PNVSYICSRYYRAPELIfGATDYTSSIDVWSAGCVLAELLLGQpifPGDSGVDQLVEIIKVLGTPTREQIREM 284
Cdd:cd06640   150 QLTDTQiKRNTFVGTPFWMAPEVI-QQSAYDSKADIWSLGITAIELAKGE---PPNSDMHPMRVLFLIPKNNPPTLVGDF 225
                         250       260
                  ....*....|....*....|...
gi 1231802383 285 NPNYTEFKFPQIKAHPwtkVFRP 307
Cdd:cd06640   226 SKPFKEFIDACLNKDP---SFRP 245
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
60-340 1.16e-11

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: 65.44  E-value: 1.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSG----------ELVAIKKVLQDKRFKNRELQIMRkldHCNIVRLRYFFYSSGEkkdevyLN 129
Cdd:cd05594    31 KLLGKGTFGKVILVKEKATGryyamkilkkEVIVAKDEVAHTLTENRVLQNSR---HPFLTALKYSFQTHDR------LC 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 LVLDYVP--ETVYRVARHYSRAKQTlpviyVKLYMYQLFRSLAYIHS-FGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQ 206
Cdd:cd05594   102 FVMEYANggELFFHLSRERVFSEDR-----ARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHI-KITDFGLCKE 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 207 LVRGEPNVSYIC-SRYYRAPElIFGATDYTSSIDVWSAGCVLAELLLGQ-PIFPGDSgvDQLVEIIKVlgtptrEQIRem 284
Cdd:cd05594   176 GIKDGATMKTFCgTPEYLAPE-VLEDNDYGRAVDWWGLGVVMYEMMCGRlPFYNQDH--EKLFELILM------EEIR-- 244
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1231802383 285 npnytefkFPQIKAhpwtkvfrprtpPEAIALCSRLLEYTPTARL-----TPLEACAHSFF 340
Cdd:cd05594   245 --------FPRTLS------------PEAKSLLSGLLKKDPKQRLgggpdDAKEIMQHKFF 285
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
60-320 1.52e-11

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: 64.43  E-value: 1.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQA-----KLCDSGELVAIKKVLQDKRFKNR-----ELQIMRKL-DHCNIVRL---------------- 112
Cdd:cd05054    13 KPLGRGAFGKVIQAsafgiDKSATCRTVAVKMLKEGATASEHkalmtELKILIHIgHHLNVVNLlgactkpggplmvive 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 113 --RYFFYSS--GEKKDEVYLNLVLDyvPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLL 188
Cdd:cd05054    93 fcKFGNLSNylRSKREEFVPYRDKG--ARDVEEEEDDDELYKEPLTLEDLICYSFQVARGMEFLASRKCIHRDLAARNIL 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 189 LDpDTAVLKLCDFGSAKQLVRGEPNVSYICSRY---YRAPELIFGATdYTSSIDVWSAGCVLAELL-LGQPIFPGdsgvd 264
Cdd:cd05054   171 LS-ENNVVKICDFGLARDIYKDPDYVRKGDARLplkWMAPESIFDKV-YTTQSDVWSFGVLLWEIFsLGASPYPG----- 243
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1231802383 265 qlVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKvfRPRTPPEAIALCSRL 320
Cdd:cd05054   244 --VQMDEEFCRRLKEGTRMRAPEYTTPEIYQIMLDCWHG--EPKERPTFSELVEKL 295
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
60-251 1.87e-11

Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as ACVR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. Vertebrates contain two ACVR2 proteins, ACVR2a (or ActRIIA) and ACVR2b (or ActRIIB). The ACVR2 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: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 64.27  E-value: 1.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDsgELVAIKKV-LQDKRFKNRELQIMR--KLDHCNIVRlryfFYSS---GEKKDEVYLnLVLD 133
Cdd:cd14053     1 EIKARGRFGAVWKAQYLN--RLVAVKIFpLQEKQSWLTEREIYSlpGMKHENILQ----FIGAekhGESLEAEYW-LITE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 134 YVPE-TVYRVARHYSRAKQTLPVIyvklyMYQLFRSLAYIHS-----FG-----ICHRDIKPQNLLLDPD-TAVlkLCDF 201
Cdd:cd14053    74 FHERgSLCDYLKGNVISWNELCKI-----AESMARGLAYLHEdipatNGghkpsIAHRDFKSKNVLLKSDlTAC--IADF 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 202 GSAkqlVRGEPNVSY------ICSRYYRAPELIFGATDYTSS----IDVWSAGCVLAELL 251
Cdd:cd14053   147 GLA---LKFEPGKSCgdthgqVGTRRYMAPEVLEGAINFTRDaflrIDMYAMGLVLWELL 203
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
165-253 3.44e-11

Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called U2AF homology motif (UHM) kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KIS (or UHMK1) contains an N-terminal kinase domain and a C-terminal domain with a UHM motif, a protein interaction motif initially found in the pre-mRNA splicing factor U2AF. It phosphorylates the splicing factor SF1, which enhances binding to the splice site to promote spliceosome assembly. KIS was first identified as a kinase that interacts with stathmin, a phosphoprotein that plays a role in axon development and microtubule dynamics. It localizes in RNA granules in neurons and is important in neurite outgrowth. The KIS/UHMK1 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: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 63.42  E-value: 3.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 165 LFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFG-SAKQlvrGEPNVSYICSRYYRAPEL----------IFGATD 233
Cdd:cd14020   119 VLEALAFLHHEGYVHADLKPRNILWSAEDECFKLIDFGlSFKE---GNQDVKYIQTDGYRAPEAelqnclaqagLQSETE 195
                          90       100
                  ....*....|....*....|
gi 1231802383 234 YTSSIDVWSAGCVLAELLLG 253
Cdd:cd14020   196 CTSAVDLWSLGIVLLEMFSG 215
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
161-322 3.79e-11

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: 63.85  E-value: 3.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 161 YMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQLVRGEPNVSYICSRY---YRAPELIFGATdYTSS 237
Cdd:cd05102   177 YSFQVARGMEFLASRKCIHRDLAARNILLS-ENNVVKICDFGLARDIYKDPDYVRKGSARLplkWMAPESIFDKV-YTTQ 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 238 IDVWSAGCVLAELL-LGQPIFPGdsgvdqlVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKVFRPR-TPPEAIA 315
Cdd:cd05102   255 SDVWSFGVLLWEIFsLGASPYPG-------VQINEEFCQRLKDGTRMRAPEYATPEIYRIMLSCWHGDPKERpTFSDLVE 327

                  ....*..
gi 1231802383 316 LCSRLLE 322
Cdd:cd05102   328 ILGDLLQ 334
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
161-301 3.79e-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: 63.85  E-value: 3.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 161 YMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQLVRGEPNVSYICSRY---YRAPELIFGATdYTSS 237
Cdd:cd05103   184 YSFQVAKGMEFLASRKCIHRDLAARNILLS-ENNVVKICDFGLARDIYKDPDYVRKGDARLplkWMAPETIFDRV-YTIQ 261
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1231802383 238 IDVWSAGCVLAELL-LGQPIFPGdsgvdqlVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPW 301
Cdd:cd05103   262 SDVWSFGVLLWEIFsLGASPYPG-------VKIDEEFCRRLKEGTRMRAPDYTTPEMYQTMLDCW 319
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
56-279 4.29e-11

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 63.74  E-value: 4.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKkvLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGekkdevYLNLVLDYV 135
Cdd:PHA03209   68 YTVIKTLTPGSEGRVFVATKPGQPDPVVLK--IGQKGTTLIEAMLLQNVNHPSVIRMKDTLVSGA------ITCMVLPHY 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 136 PETVYRvarHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLkLCDFGSAKQLVRGEPNVS 215
Cdd:PHA03209  140 SSDLYT---YLTKRSRPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINDVDQVC-IGDLGAAQFPVVAPAFLG 215
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1231802383 216 YICSRYYRAPELIFGATdYTSSIDVWSAGCVLAELLL----------GQPIFPGDSGVDQLVEIIKVLGTPTRE 279
Cdd:PHA03209  216 LAGTVETNAPEVLARDK-YNSKADIWSAGIVLFEMLAypstifedppSTPEEYVKSCHSHLLKIISTLKVHPEE 288
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
56-249 5.11e-11

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: 62.82  E-value: 5.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELV-AIKKVLQDK-RFKNR-----ELQIMRKLD---HCNIVRLryffYSSGEKKDE 125
Cdd:cd14052     2 FANVELIGSGEFSQVYKVSERVPTGKVyAVKKLKPNYaGAKDRlrrleEVSILRELTldgHDNIVQL----IDSWEYHGH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 126 VYLnlVLDYVPE-TVYRVARHYSRAKQTLPVIYVKLyMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKLCDFGSA 204
Cdd:cd14052    78 LYI--QTELCENgSLDVFLSELGLLGRLDEFRVWKI-LVELSLGLRFIHDHHFVHLDLKPANVLITFE-GTLKIGDFGMA 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1231802383 205 KQL-----VRGEPNVSYICsryyraPELIFGATdYTSSIDVWSAGCVLAE 249
Cdd:cd14052   154 TVWplirgIEREGDREYIA------PEILSEHM-YDKPADIFSLGLILLE 196
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
60-352 5.94e-11

Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. There are two forms of STRAD, alpha and beta, that complex with LKB1 and MO25. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha stabilized through ATP and MO25 may be needed to activate LKB1. The STRAD 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: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 63.08  E-value: 5.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFG--VVYQAKLCDSGELVAIKKVLQDKRFKNR------ELQIMRKLDHCNIVRLRYFFYSsgekKDEVYLNLV 131
Cdd:cd08216     4 YEIGKCFKGggVVHLAKHKPTNTLVAVKKINLESDSKEDlkflqqEILTSRQLQHPNILPYVTSFVV----DNDLYVVTP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 132 L-DYVPETVYrVARHYSRAkqtLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLVRG 210
Cdd:cd08216    80 LmAYGSCRDL-LKTHFPEG---LPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKV-VLSGLRYAYSMVKH 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 211 --------EPNVSYICSRYYRAPEL----IFGatdYTSSIDVWSAGCVLAELLLG-QPIFpgDSGVDQLVeIIKVLGTP- 276
Cdd:cd08216   155 gkrqrvvhDFPKSSEKNLPWLSPEVlqqnLLG---YNEKSDIYSVGITACELANGvVPFS--DMPATQML-LEKVRGTTp 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 277 --------TREQIREMNPNYTEFKFPQIKA---HPWTKVFRPrtPPEAIA-LCsrlLEYTPTARLTPLEACAHSFFDELR 344
Cdd:cd08216   229 qlldcstyPLEEDSMSQSEDSSTEHPNNRDtrdIPYQRTFSE--AFHQFVeLC---LQRDPELRPSASQLLAHSFFKQCR 303

                  ....*...
gi 1231802383 345 DPNVKLPN 352
Cdd:cd08216   304 RSNTSLLD 311
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
51-250 6.26e-11

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: 62.27  E-value: 6.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  51 PQEVSYTDTkvIGNGSFGVVYQAKLCDSGElVAIKKV----LQDKRFKnRELQIMRKLDHCNIVRLryffYSSGEKKDEV 126
Cdd:cd05112     3 PSELTFVQE--IGSGQFGLVHLGYWLNKDK-VAIKTIregaMSEEDFI-EEAEVMMKLSHPKLVQL----YGVCLEQAPI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 127 YLnlVLDYVPE---TVYRVARHYSRAKQTLpviyvkLYM-YQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFG 202
Cdd:cd05112    75 CL--VFEFMEHgclSDYLRTQRGLFSAETL------LGMcLDVCEGMAYLEEASVIHRDLAARNCLVG-ENQVVKVSDFG 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1231802383 203 SAKqLVRGEPNVSYICSRY---YRAPElIFGATDYTSSIDVWSAGCVLAEL 250
Cdd:cd05112   146 MTR-FVLDDQYTSSTGTKFpvkWSSPE-VFSFSRYSSKSDVWSFGVLMWEV 194
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
169-261 7.22e-11

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: 62.70  E-value: 7.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 169 LAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLVRGEPNVSYIC-SRYYRAPElIFGATDYTSSIDVWSAGCVL 247
Cdd:cd05589   114 LQFLHEHKIVYRDLKLDNLLLDTEGYV-KIADFGLCKEGMGFGDRTSTFCgTPEFLAPE-VLTDTSYTRAVDWWGLGVLI 191
                          90
                  ....*....|....
gi 1231802383 248 AELLLGQPIFPGDS 261
Cdd:cd05589   192 YEMLVGESPFPGDD 205
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
60-257 8.45e-11

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: 62.44  E-value: 8.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKkVLQDKRFKNRE----LQIMRKL-----DHCNIVRLRYFFYSSGEkkdevyLNL 130
Cdd:cd05588     1 RVIGRGSYAKVLMVELKKTKRIYAMK-VIKKELVNDDEdidwVQTEKHVfetasNHPFLVGLHSCFQTESR------LFF 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 VLDYVP--ETVYRVARHysrakQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLV 208
Cdd:cd05588    74 VIEFVNggDLMFHMQRQ-----RRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHI-KLTDYGMCKEGL 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1231802383 209 RGEPNVSYIC-SRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIF 257
Cdd:cd05588   148 RPGDTTSTFCgTPNYIAPEILRG-EDYGFSVDWWALGVLMFEMLAGRSPF 196
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
60-271 8.88e-11

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: 61.81  E-value: 8.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLcdSGELVAIKKVLQDKRFKN--RELQIMRKLDHCNIVRLRYFFYSSGekkdevyLNLVLDYVPE 137
Cdd:cd05083    12 EIIGEGEFGAVLQGEY--MGQKVAVKNIKCDVTAQAflEETAVMTKLQHKNLVRLLGVILHNG-------LYIVMELMSK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 138 -TVYRVARhySRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKLCDFGSAKQLVRGEPNvsy 216
Cdd:cd05083    83 gNLVNFLR--SRGRALVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSED-GVAKISDFGLAKVGSMGVDN--- 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1231802383 217 icSRY---YRAPELIfGATDYTSSIDVWSAGCVLAELL-LGQPIFPGDSgVDQLVEIIK 271
Cdd:cd05083   157 --SRLpvkWTAPEAL-KNKKFSSKSDVWSYGVLLWEVFsYGRAPYPKMS-VKEVKEAVE 211
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
60-250 8.98e-11

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: 61.59  E-value: 8.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGEL---VAIKKVLQDKRFKN-------RELQIMRKLDHCNIVRLRYFFYSSGekkdevyLN 129
Cdd:cd05040     1 EKLGDGSFGVVRRGEWTTPSGKviqVAVKCLKSDVLSQPnamddflKEVNAMHSLDHPNLIRLYGVVLSSP-------LM 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 LVLDYVP-----ETVYRVARHYsrakqtlPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSA 204
Cdd:cd05040    74 MVTELAPlgsllDRLRKDQGHF-------LISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDKV-KIGDFGLM 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1231802383 205 KQLVRGEpnvsyicsRYYR------------APELIFGATdYTSSIDVWSAGCVLAEL 250
Cdd:cd05040   146 RALPQNE--------DHYVmqehrkvpfawcAPESLKTRK-FSHASDVWMFGVTLWEM 194
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
60-259 1.07e-10

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: 61.53  E-value: 1.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGElVAIKKVLQDKRFKN---RELQIMRKLDHCNIVRLryffYSSGEKKDEVYL-------- 128
Cdd:cd05034     1 KKLGAGQFGEVWMGVWNGTTK-VAVKTLKPGTMSPEaflQEAQIMKKLRHDKLVQL----YAVCSDEEPIYIvtelmskg 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 129 NLvLDYVpetvyrvaRHYSRAKQTLPVIyvkLYMY-QLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQL 207
Cdd:cd05034    76 SL-LDYL--------RTGEGRALRLPQL---IDMAaQIASGMAYLESRNYIHRDLAARNILVG-ENNVCKVADFGLARLI 142
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1231802383 208 VRGEpnvsYICSRYYR------APELIFGATdYTSSIDVWSAGCVLAELL-LGQPIFPG 259
Cdd:cd05034   143 EDDE----YTAREGAKfpikwtAPEAALYGR-FTIKSDVWSFGILLYEIVtYGRVPYPG 196
PTZ00284 PTZ00284
protein kinase; Provisional
61-274 1.09e-10

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 63.06  E-value: 1.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  61 VIGNGSFGVVYQAKLCDSGELVAIK---KVLQDKRFKNRELQIMRKL------DHCNIVRL-RYFFYSSGekkdevYLNL 130
Cdd:PTZ00284  136 LLGEGTFGKVVEAWDRKRKEYCAVKivrNVPKYTRDAKIEIQFMEKVrqadpaDRFPLMKIqRYFQNETG------HMCI 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 VL-DYVPETVYRVARHYSRAKQTLPVIyvklyMYQLFRSLAYIHS-FGICHRDIKPQNLLLD---------------PDT 193
Cdd:PTZ00284  210 VMpKYGPCLLDWIMKHGPFSHRHLAQI-----IFQTGVALDYFHTeLHLMHTDLKPENILMEtsdtvvdpvtnralpPDP 284
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 194 AVLKLCDFGSAKQlvRGEPNVSYICSRYYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVL 273
Cdd:PTZ00284  285 CRVRICDLGGCCD--ERHSRTAIVSTRHYRSPEVVLG-LGWMYSTDMWSMGCIIYELYTGKLLYDTHDNLEHLHLMEKTL 361

                  .
gi 1231802383 274 G 274
Cdd:PTZ00284  362 G 362
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
62-271 1.14e-10

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: 61.59  E-value: 1.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQ--AKLCDSGEL---VAIKKVLQDKRFKNR-----ELQIMRKLDHCNIVRLrYFFYSSGEKKdevylNLV 131
Cdd:cd05032    14 LGQGSFGMVYEglAKGVVKGEPetrVAIKTVNENASMRERieflnEASVMKEFNCHHVVRL-LGVVSTGQPT-----LVV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 132 LDYVPE----TVYRVARHYSRAKQTLPVIYVKLYMY---QLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSA 204
Cdd:cd05032    88 MELMAKgdlkSYLRSRRPEAENNPGLGPPTLQKFIQmaaEIADGMAYLAAKKFVHRDLAARNCMVAEDLTV-KIGDFGMT 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 205 KQLVRGEpnvsyicsrYYR------------APELIFGATdYTSSIDVWSAGCVLAELL-LGQPIFPGDSGvDQLVEIIK 271
Cdd:cd05032   167 RDIYETD---------YYRkggkgllpvrwmAPESLKDGV-FTTKSDVWSFGVVLWEMAtLAEQPYQGLSN-EEVLKFVI 235
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
61-253 1.23e-10

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: 61.12  E-value: 1.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  61 VIGNGSFGVVYQAKLcdSGELVAIKKVLQDKRFK--NRELQIMRKLDHCNIVRLryffYSSGEKKDEvylnLVLDYVPET 138
Cdd:cd14068     1 LLGDGGFGSVYRAVY--RGEDVAVKIFNKHTSFRllRQELVVLSHLHHPSLVAL----LAAGTAPRM----LVMELAPKG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 139 vyRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLL---LDPDTAVL-KLCDFGSAKQLVRGEPNV 214
Cdd:cd14068    71 --SLDALLQQDNASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLlftLYPNCAIIaKIADYGIAQYCCRMGIKT 148
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1231802383 215 SYiCSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLG 253
Cdd:cd14068   149 SE-GTPGFRAPEVARGNVIYNQQADVYSFGLLLYDILTC 186
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
62-250 1.32e-10

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: 61.21  E-value: 1.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLcdSGELVAIKKVLQDKRFKNR---ELQIMRKLDHCNIVRLryffyssgekkdevyLNLVLDYVPet 138
Cdd:cd05039    14 IGKGEFGDVMLGDY--RGQKVAVKCLKDDSTAAQAflaEASVMTTLRHPNLVQL---------------LGVVLEGNG-- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 139 VYRVARHY----------SRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTaVLKLCDFGSAKqlv 208
Cdd:cd05039    75 LYIVTEYMakgslvdylrSRGRAVITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDN-VAKVSDFGLAK--- 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1231802383 209 rgEPNVSYICSRY---YRAPELIfGATDYTSSIDVWSAGCVLAEL 250
Cdd:cd05039   151 --EASSNQDGGKLpikWTAPEAL-REKKFSTKSDVWSFGILLWEI 192
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
51-255 1.63e-10

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: 61.24  E-value: 1.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  51 PQEVsYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKV-LQDKRFK----NRELQIMRKLDHCNIVRlryfFYSSgekkde 125
Cdd:cd06641     2 PEEL-FTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIdLEEAEDEiediQQEITVLSQCDSPYVTK----YYGS------ 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 126 vylnlvldYVPETVYRVARHYSRAKQTLPVI--------YVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlK 197
Cdd:cd06641    71 --------YLKDTKLWIIMEYLGGGSALDLLepgpldetQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEV-K 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1231802383 198 LCDFGSAKQLVRGEPNVS-YICSRYYRAPELIfGATDYTSSIDVWSAGCVLAELLLGQP 255
Cdd:cd06641   142 LADFGVAGQLTDTQIKRN*FVGTPFWMAPEVI-KQSAYDSKADIWSLGITAIELARGEP 199
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
60-259 2.26e-10

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: 60.96  E-value: 2.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKL-----CDSGELVAIKKVLQDKRFKNR-----ELQIMRKL-DHCNIVRLryffYSSGEKKDEVYL 128
Cdd:cd05055    41 KTLGAGAFGKVVEATAyglskSDAVMKVAVKMLKPTAHSSERealmsELKIMSHLgNHENIVNL----LGACTIGGPILV 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 129 nlVLDYVpetVYRVARHYSRAKQTLPVIYVKL--YMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQ 206
Cdd:cd05055   117 --ITEYC---CYGDLLNFLRRKRESFLTLEDLlsFSYQVAKGMAFLASKNCIHRDLAARNVLLT-HGKIVKICDFGLARD 190
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1231802383 207 LVRGEPNVSYICSRY---YRAPELIFGATdYTSSIDVWSAGCVLAELL-LGQPIFPG 259
Cdd:cd05055   191 IMNDSNYVVKGNARLpvkWMAPESIFNCV-YTFESDVWSYGILLWEIFsLGSNPYPG 246
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
60-301 2.44e-10

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: 60.72  E-value: 2.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRK-----LDHCN--IVRLRYFFYSSGEkkdevyLNLVL 132
Cdd:cd14197    15 RELGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQDCRMEIIHEiavleLAQANpwVINLHEVYETASE------MILVL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 DYVP--ETVYR-VARHYSRAKQTlpviYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAV--LKLCDFGSAKQL 207
Cdd:cd14197    89 EYAAggEIFNQcVADREEAFKEK----DVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESPLgdIKIVDFGLSRIL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 208 VRGEPNVSYICSRYYRAPElIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPN 287
Cdd:cd14197   165 KNSEELREIMGTPEYVAPE-ILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQMNVSYSEEEFEHLSES 243
                         250       260
                  ....*....|....*....|....*..
gi 1231802383 288 YTEF------KFPQIKA-------HPW 301
Cdd:cd14197   244 AIDFiktlliKKPENRAtaedclkHPW 270
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
60-259 2.73e-10

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: 60.41  E-value: 2.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGEL--VAIK--KVLQDKRFKN----RELQIMRKLDHCNIVRLRYFFYSSGEKKDEVYLNLV 131
Cdd:cd05075     6 KTLGEGEFGSVMEGQLNQDDSVlkVAVKtmKIAICTRSEMedflSEAVCMKEFDHPNVMRLIGVCLQNTESEGYPSPVVI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 132 LDYVPETVYRVARHYSRAKQT---LPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLkLCDFGSAKQLV 208
Cdd:cd05075    86 LPFMKHGDLHSFLLYSRLGDCpvyLPTQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVC-VADFGLSKKIY 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1231802383 209 RGEpnvsyicsrYYRAPEL---------IFGATD--YTSSIDVWSAGCVLAELLL-GQPIFPG 259
Cdd:cd05075   165 NGD---------YYRQGRIskmpvkwiaIESLADrvYTTKSDVWSFGVTMWEIATrGQTPYPG 218
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
60-266 3.66e-10

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: 60.12  E-value: 3.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCD-----SGEL-VAIKKV-----LQDKRFKNRELQIMRKLDHCNIVRL---------RYFFYSS 119
Cdd:cd05044     1 KFLGSGAFGEVFEGTAKDilgdgSGETkVAVKTLrkgatDQEKAEFLKEAHLMSNFKHPNILKLlgvcldndpQYIILEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 120 GEKKDevylnlVLDYVpetvyRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLL---DPDTAVL 196
Cdd:cd05044    81 MEGGD------LLSYL-----RAARPTAFTPPLLTLKDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVsskDYRERVV 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 197 KLCDFGSAKQLVRgepnvsyicSRYYR------------APE-LIFGAtdYTSSIDVWSAGCVLAELL-LGQPIFPGDSG 262
Cdd:cd05044   150 KIGDFGLARDIYK---------NDYYRkegegllpvrwmAPEsLVDGV--FTTQSDVWAFGVLMWEILtLGQQPYPARNN 218

                  ....
gi 1231802383 263 VDQL 266
Cdd:cd05044   219 LEVL 222
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
62-340 3.90e-10

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: 60.02  E-value: 3.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVA-----IKKVLQDKRFK-NRELQIMRKLDHCNIVRlryfFYSSGEKKDEVYLNLVLDYV 135
Cdd:cd14033     9 IGRGSFKTVYRGLDTETTVEVAwcelqTRKLSKGERQRfSEEVEMLKGLQHPNIVR----FYDSWKSTVRGHKCIILVTE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 136 PETVYRVARHYSRAKQTLPVIyVKLYMYQLFRSLAYIHSFG--ICHRDIKPQNLLLDPDTAVLKLCDFGSAkQLVRGEPN 213
Cdd:cd14033    85 LMTSGTLKTYLKRFREMKLKL-LQRWSRQILKGLHFLHSRCppILHRDLKCDNIFITGPTGSVKIGDLGLA-TLKRASFA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 214 VSYICSRYYRAPELIfgATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVeiikvlgtptREQIREMNPN-YTEFK 292
Cdd:cd14033   163 KSVIGTPEFMAPEMY--EEKYDEAVDVYAFGMCILEMATSEYPYSECQNAAQIY----------RKVTSGIKPDsFYKVK 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1231802383 293 FPQIKahpwtkvfrprtppEAIALCSRLleyTPTARLTPLEACAHSFF 340
Cdd:cd14033   231 VPELK--------------EIIEGCIRT---DKDERFTIQDLLEHRFF 261
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
60-251 7.75e-10

Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2b (or ActRIIB) belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. The ACVR2b 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: 271042 [Multi-domain]  Cd Length: 291  Bit Score: 59.27  E-value: 7.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDsgELVAIKKV-LQDKRFKNRELQIMRK--LDHCNIVR----------------LRYFFYSSG 120
Cdd:cd14140     1 EIKARGRFGCVWKAQLMN--EYVAVKIFpIQDKQSWQSEREIFSTpgMKHENLLQfiaaekrgsnlemelwLITAFHDKG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 121 EKKDEVYLNLV----LDYVPETVyrvARHYSRAKQTLPviyvklymyqlfRSLAYIHSFGICHRDIKPQNLLLDPD-TAV 195
Cdd:cd14140    79 SLTDYLKGNIVswneLCHIAETM---ARGLSYLHEDVP------------RCKGEGHKPAIAHRDFKSKNVLLKNDlTAV 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1231802383 196 lkLCDFGSAKQLVRGEP---NVSYICSRYYRAPELIFGATDYTSS----IDVWSAGCVLAELL 251
Cdd:cd14140   144 --LADFGLAVRFEPGKPpgdTHGQVGTRRYMAPEVLEGAINFQRDsflrIDMYAMGLVLWELV 204
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
56-257 8.64e-10

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: 59.51  E-value: 8.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQ-DKRFKNRELQIMRKLDHCNIVRLRYF--FYSSGEKKDEVYLnlVL 132
Cdd:cd05610     6 FVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKaDMINKNMVHQVQAERDALALSKSPFIvhLYYSLQSANNVYL--VM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 DY-VPETVYRVARHYSRAKQTLPVIYVKlymyQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQLVRGE 211
Cdd:cd05610    84 EYlIGGDVKSLLHIYGYFDEEMAVKYIS----EVALALDYLHRHGIIHRDLKPDNMLIS-NEGHIKLTDFGLSKVTLNRE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 212 PNVSYICSR---------YYRAP---------------------------------ELIFGATDYT-----------SSI 238
Cdd:cd05610   159 LNMMDILTTpsmakpkndYSRTPgqvlslisslgfntptpyrtpksvrrgaarvegERILGTPDYLapelllgkphgPAV 238
                         250
                  ....*....|....*....
gi 1231802383 239 DVWSAGCVLAELLLGQPIF 257
Cdd:cd05610   239 DWWALGVCLFEFLTGIPPF 257
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
52-259 9.30e-10

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: 59.16  E-value: 9.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  52 QEVSYTDTKVIGNGSFGVVYQAKLC---DSGELVAIKkVLQDKRFKN-------RELQIMRKLDHCNIVRLRYFFYSSGE 121
Cdd:cd05074     7 QEQQFTLGRMLGKGEFGSVREAQLKsedGSFQKVAVK-MLKADIFSSsdieeflREAACMKEFDHPNVIKLIGVSLRSRA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 122 KKDEVYLNLVLDYVPETVYRVARHYSRAKQ---TLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLkL 198
Cdd:cd05074    86 KGRLPIPMVILPFMKHGDLHTFLLMSRIGEepfTLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNENMTVC-V 164
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1231802383 199 CDFGSAKQLVRGEpnvsyicsrYYR---APEL--------IFGATDYTSSIDVWSAGCVLAELL-LGQPIFPG 259
Cdd:cd05074   165 ADFGLSKKIYSGD---------YYRqgcASKLpvkwlaleSLADNVYTTHSDVWAFGVTMWEIMtRGQTPYAG 228
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
60-259 9.38e-10

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: 59.09  E-value: 9.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKL-CDSGEL--VAIKKVLQDKRFKN------RELQIMRKLDHCNIVRLRYFFYSSGEKKDEVYLNL 130
Cdd:cd05035     5 KILGEGEFGSVMEAQLkQDDGSQlkVAVKTMKVDIHTYSeieeflSEAACMKDFDHPNVMRLIGVCFTASDLNKPPSPMV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 VLDYVPETVYRVARHYSRAK---QTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLkLCDFGSAKQL 207
Cdd:cd05035    85 ILPFMKHGDLHSYLLYSRLGglpEKLPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVC-VADFGLSRKI 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1231802383 208 VRGEpnvsyicsrYYRAPEL---------IFGATD--YTSSIDVWSAGCVLAELL-LGQPIFPG 259
Cdd:cd05035   164 YSGD---------YYRQGRIskmpvkwiaLESLADnvYTSKSDVWSFGVTMWEIAtRGQTPYPG 218
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
49-259 1.12e-09

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: 58.60  E-value: 1.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  49 DRPQEvSYTDTKVIGNGSFGVVYQAKLCDSGElVAIKKVLQDKRFKNR----ELQIMRKLDHCNIVRLrYFFYSSGEKkd 124
Cdd:cd05148     2 ERPRE-EFTLERKLGSGYFGEVWEGLWKNRVR-VAIKILKSDDLLKQQdfqkEVQALKRLRHKHLISL-FAVCSVGEP-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 125 eVYLnlvldyVPETVYRVA-RHYSRAK--QTLPVIYVkLYM-YQLFRSLAYIHSFGICHRDIKPQNLLLDPDTaVLKLCD 200
Cdd:cd05148    77 -VYI------ITELMEKGSlLAFLRSPegQVLPVASL-IDMaCQVAEGMAYLEEQNSIHRDLAARNILVGEDL-VCKVAD 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1231802383 201 FGSAKQLvrGEPnvSYICSRY-----YRAPELIFGATdYTSSIDVWSAGCVLAELLL-GQPIFPG 259
Cdd:cd05148   148 FGLARLI--KED--VYLSSDKkipykWTAPEAASHGT-FSTKSDVWSFGILLYEMFTyGQVPYPG 207
STKc_SRPK3 cd14218
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs ...
151-274 1.18e-09

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK3 is highly expressed in the heart and skeletal muscles, and is controlled by a muscle-specific enhancer that is regulated by MEF2. It may play an important role in muscle development. 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. 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: 271120 [Multi-domain]  Cd Length: 365  Bit Score: 59.26  E-value: 1.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 151 QTLPVIYVKLYMYQLFRSLAYIHS-FGICHRDIKPQNLLLDPDTAVLK--------------------LCDFGSAKQLVR 209
Cdd:cd14218   114 QGLPLPCVKSILRQVLQGLDYLHTkCKIIHTDIKPENILMCVDEGYVRrlaaeatiwqqagapppsgsSVSFGASDFLVN 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 210 G-EP--------------NVSY--------ICSRYYRAPELIFGAtDYTSSIDVWSAGCVLAELLLGQPIFPGDSG---- 262
Cdd:cd14218   194 PlEPqnadkirvkiadlgNACWvhkhftedIQTRQYRALEVLIGA-EYGTPADIWSTACMAFELATGDYLFEPHSGedyt 272
                         170
                  ....*....|....
gi 1231802383 263 --VDQLVEIIKVLG 274
Cdd:cd14218   273 rdEDHIAHIVELLG 286
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
62-301 1.22e-09

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: 58.48  E-value: 1.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIK--KVLQDKRFKN--RELQIMRKLDHCNIVRLRYFFyssgEKKDEVYLNLVLDYVPE 137
Cdd:cd14191    10 LGSGKFGQVFRLVEKKTKKVWAGKffKAYSAKEKENirQEISIMNCLHHPKLVQCVDAF----EEKANIVMVLEMVSGGE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 138 TVYRVARHYSRAKQTlpviYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAV-LKLCDFGSAKQLVRGEPNVSY 216
Cdd:cd14191    86 LFERIIDEDFELTER----ECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTkIKLIDFGLARRLENAGSLKVL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 217 ICSRYYRAPELI-FGATDYTSsiDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTEF---- 291
Cdd:cd14191   162 FGTPEFVAPEVInYEPIGYAT--DMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFisnl 239
                         250
                  ....*....|....*....
gi 1231802383 292 ---------KFPQIKAHPW 301
Cdd:cd14191   240 lkkdmkarlTCTQCLQHPW 258
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
60-279 1.69e-09

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: 58.13  E-value: 1.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGElVAIKKV----LQDKRFKnRELQIMRKLDHCNIVRLryffYSSGEKKDEVYLnlVLDYV 135
Cdd:cd05072    13 KKLGAGQFGEVWMGYYNNSTK-VAVKTLkpgtMSVQAFL-EEANLMKTLQHDKLVRL----YAVVTKEEPIYI--ITEYM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 136 PE-TVYRVARHYSRAKQTLPviyvKL--YMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKqLVRGEP 212
Cdd:cd05072    85 AKgSLLDFLKSDEGGKVLLP----KLidFSAQIAEGMAYIERKNYIHRDLRAANVLVS-ESLMCKIADFGLAR-VIEDNE 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 213 NVSYICSRY---YRAPELI-FGAtdYTSSIDVWSAGCVLAELL-LGQPIFPGDSGVDQLVEIIKVLGTPTRE 279
Cdd:cd05072   159 YTAREGAKFpikWTAPEAInFGS--FTIKSDVWSFGILLYEIVtYGKIPYPGMSNSDVMSALQRGYRMPRME 228
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
59-251 1.89e-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: 57.77  E-value: 1.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  59 TKVIGNGSFGVVYQAKLCDSGE---LVAIKKV---LQDKRFKN--RELQIMRKLDHCNIVRLrYFFYSSGEKkdevyLNL 130
Cdd:cd05033     9 EKVIGGGEFGEVCSGSLKLPGKkeiDVAIKTLksgYSDKQRLDflTEASIMGQFDHPNVIRL-EGVVTKSRP-----VMI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 VLDYVPE-TVYRVARHYsraKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTaVLKLCDFGSAKQLvr 209
Cdd:cd05033    83 VTEYMENgSLDKFLREN---DGKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDL-VCKVSDFGLSRRL-- 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1231802383 210 GEPNVSY------ICSRYyRAPELI-FGAtdYTSSIDVWSAGCVLAELL 251
Cdd:cd05033   157 EDSEATYttkggkIPIRW-TAPEAIaYRK--FTSASDVWSFGIVMWEVM 202
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
58-301 1.91e-09

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: 58.01  E-value: 1.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  58 DTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN------RELQIMRKLDHC-NIVRLRYFFYSSGEkkdevyLNL 130
Cdd:cd14198    12 TSKELGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDcraeilHEIAVLELAKSNpRVVNLHEVYETTSE------IIL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 131 VLDY----------VPETVYRVARhysraKQTLPVIYvklymyQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAV--LKL 198
Cdd:cd14198    86 ILEYaaggeifnlcVPDLAEMVSE-----NDIIRLIR------QILEGVYYLHQNNIVHLDLKPQNILLSSIYPLgdIKI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 199 CDFGSAKQLVRGEPNVSYICSRYYRAPElIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTR 278
Cdd:cd14198   155 VDFGMSRKIGHACELREIMGTPEYLAPE-ILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQVNVDYSE 233
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1231802383 279 EQIREMNPNYTEF------KFPQIK-------AHPW 301
Cdd:cd14198   234 ETFSSVSQLATDFiqkllvKNPEKRptaeiclSHSW 269
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
164-249 1.95e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 59.14  E-value: 1.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 164 QLFRSLAYIHSFGICHRDIKPQNLLLD-PDTAVLKlcDFGSAkQLVRGepnvSYICSRYY--------RAPELIFGaTDY 234
Cdd:PHA03211  268 QLLSAIDYIHGEGIIHRDIKTENVLVNgPEDICLG--DFGAA-CFARG----SWSTPFHYgiagtvdtNAPEVLAG-DPY 339
                          90
                  ....*....|....*
gi 1231802383 235 TSSIDVWSAGCVLAE 249
Cdd:PHA03211  340 TPSVDIWSAGLVIFE 354
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
62-270 1.97e-09

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: 58.12  E-value: 1.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLcdSGEL-VAIKKVL-----QDKRFKNrELQIMRKLDHCNIVrlryffyssgekkdevylnLVLDYV 135
Cdd:cd14149    20 IGSGSFGTVYKGKW--HGDVaVKILKVVdptpeQFQAFRN-EVAVLRKTRHVNIL-------------------LFMGYM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 136 PETVYRVARHY---SRAKQTLPVIYVKLYMYQLF-------RSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAK 205
Cdd:cd14149    78 TKDNLAIVTQWcegSSLYKHLHVQETKFQMFQLIdiarqtaQGMDYLHAKNIIHRDMKSNNIFLHEGLTV-KIGDFGLAT 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 206 QLVR--GEPNVSYIC-SRYYRAPELIFGATD--YTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEII 270
Cdd:cd14149   157 VKSRwsGSQQVEQPTgSILWMAPEVIRMQDNnpFSFQSDVYSYGIVLYELMTGELPYSHINNRDQIIFMV 226
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
161-259 2.37e-09

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: 58.50  E-value: 2.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 161 YMYQLFRSLAYIHSFGICHRDIKPQNLLLdPDTAVLKLCDFGSAKQLVRGEPNV---SYICSRYYRAPELIFGATdYTSS 237
Cdd:cd05105   242 FTYQVARGMEFLASKNCVHRDLAARNVLL-AQGKIVKICDFGLARDIMHDSNYVskgSTFLPVKWMAPESIFDNL-YTTL 319
                          90       100
                  ....*....|....*....|...
gi 1231802383 238 IDVWSAGCVLAELL-LGQPIFPG 259
Cdd:cd05105   320 SDVWSYGILLWEIFsLGGTPYPG 342
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
60-267 2.90e-09

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: 57.40  E-value: 2.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKL----CDSGEL-VAIKKV-----LQDKRFKNRELQIMRKLDHCNIVRLryffysSGEKKDEVYLN 129
Cdd:cd05036    12 RALGQGAFGEVYEGTVsgmpGDPSPLqVAVKTLpelcsEQDEMDFLMEALIMSKFNHPNIVRC------IGVCFQRLPRF 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 LVLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLA----YIHSFGICHRDIKPQNLLLDPDTA--VLKLCDFGS 203
Cdd:cd05036    86 ILLELMAGGDLKSFLRENRPRPEQPSSLTMLDLLQLAQDVAkgcrYLEENHFIHRDIAARNCLLTCKGPgrVAKIGDFGM 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1231802383 204 AKQLVRgepnvsyicSRYYRA------------PElIFGATDYTSSIDVWSAGCVLAELL-LGQPIFPGDSG--VDQLV 267
Cdd:cd05036   166 ARDIYR---------ADYYRKggkamlpvkwmpPE-AFLDGIFTSKTDVWSFGVLLWEIFsLGYMPYPGKSNqeVMEFV 234
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
57-251 2.96e-09

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: 57.29  E-value: 2.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  57 TDTKVIGNGSFGVVYQAKLCDSGE---LVAIKKVLQDKRFKNR-----ELQIMRKLDHCNIVRLRYFF--YSSGEKKDEV 126
Cdd:cd05063     8 TKQKVIGAGEFGEVFRGILKMPGRkevAVAIKTLKPGYTEKQRqdflsEASIMGQFSHHNIIRLEGVVtkFKPAMIITEY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 127 YLNLVLDyvpetvyrvarHYSRAKQTLpviYVKLYMYQLFRSLA----YIHSFGICHRDIKPQNLLLDpDTAVLKLCDFG 202
Cdd:cd05063    88 MENGALD-----------KYLRDHDGE---FSSYQLVGMLRGIAagmkYLSDMNYVHRDLAARNILVN-SNLECKVSDFG 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1231802383 203 SAKQLvRGEPNVSYICSR-----YYRAPELIfGATDYTSSIDVWSAGCVLAELL 251
Cdd:cd05063   153 LSRVL-EDDPEGTYTTSGgkipiRWTAPEAI-AYRKFTSASDVWSFGIVMWEVM 204
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
54-250 3.15e-09

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: 57.07  E-value: 3.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  54 VSYTDTKVIGNGSFGVVYQAKLCDSGElVAIKK----VLQDKRFKNrELQIMRKLDHCNIVRLryffYSSGEKKDEVYln 129
Cdd:cd05059     4 SELTFLKELGSGQFGVVHLGKWRGKID-VAIKMikegSMSEDDFIE-EAKVMMKLSHPKLVQL----YGVCTKQRPIF-- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 LVLDYVPE----TVYRVARHYSRAKQTLPVIyvklymYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAK 205
Cdd:cd05059    76 IVTEYMANgcllNYLRERRGKFQTEQLLEMC------KDVCEAMEYLESNGFIHRDLAARNCLVG-EQNVVKVSDFGLAR 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1231802383 206 QLVRGEpnvsYICSRYYR-----APELIFGATDYTSSIDVWSAGCVLAEL 250
Cdd:cd05059   149 YVLDDE----YTSSVGTKfpvkwSPPEVFMYSKFSSKSDVWSFGVLMWEV 194
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
60-271 3.19e-09

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: 57.43  E-value: 3.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKL--CDSGE----LVAIKKVLQDKRFKN-----RELQIMRKL-DHCNIVRL---------RYF--- 115
Cdd:cd05053    18 KPLGEGAFGQVVKAEAvgLDNKPnevvTVAVKMLKDDATEKDlsdlvSEMEMMKMIgKHKNIINLlgactqdgpLYVvve 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 116 FYSSGEKKD--------EVYLNLVLDYVPEtvyrvarhysrakQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNL 187
Cdd:cd05053    98 YASKGNLREflrarrppGEEASPDDPRVPE-------------EQLTQKDLVSFAYQVARGMEYLASKKCIHRDLAARNV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 188 LLDPDTaVLKLCDFGSAKqlvrgepNVSYIcsRYYR------------APELIFGATdYTSSIDVWSAGCVLAELL-LGQ 254
Cdd:cd05053   165 LVTEDN-VMKIADFGLAR-------DIHHI--DYYRkttngrlpvkwmAPEALFDRV-YTHQSDVWSFGVLLWEIFtLGG 233
                         250
                  ....*....|....*..
gi 1231802383 255 PIFPGDSgVDQLVEIIK 271
Cdd:cd05053   234 SPYPGIP-VEELFKLLK 249
pknD PRK13184
serine/threonine-protein kinase PknD;
56-251 3.75e-09

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 58.63  E-value: 3.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  56 YTDTKVIGNGSFGVVYQA--KLCdsGELVAIKKVLQD--------KRFKnRELQIMRKLDHCNIVRLryffYSSGEKKDE 125
Cdd:PRK13184    4 YDIIRLIGKGGMGEVYLAydPVC--SRRVALKKIREDlsenpllkKRFL-REAKIAADLIHPGIVPV----YSICSDGDP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 126 VYLNL--VLDYVPETVYRVAR---------HYSRAKQTLPVIYVKLymyqlFRSLAYIHSFGICHRDIKPQNLLLDPDTA 194
Cdd:PRK13184   77 VYYTMpyIEGYTLKSLLKSVWqkeslskelAEKTSVGAFLSIFHKI-----CATIEYVHSKGVLHRDLKPDNILLGLFGE 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1231802383 195 VLKLcDFGSAK-------QLVRGEPNVSYICSRYYRAPELIFGATDY-----------TSSIDVWSAGCVLAELL 251
Cdd:PRK13184  152 VVIL-DWGAAIfkkleeeDLLDIDVDERNICYSSMTIPGKIVGTPDYmaperllgvpaSESTDIYALGVILYQML 225
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
62-249 3.92e-09

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: 56.86  E-value: 3.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKVLQD--KRFKNRELQ---IMRKLDHCNIVRLryffYSSGEKKDEVYLNLVL---- 132
Cdd:cd05084     4 IGRGNFGEVFSGRLRADNTPVAVKSCRETlpPDLKAKFLQearILKQYSHPNIVRL----IGVCTQKQPIYIVMELvqgg 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 DYVpeTVYRVARHYSRAKQTLPViyvklyMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQlvrgEP 212
Cdd:cd05084    80 DFL--TFLRTEGPRLKVKELIRM------VENAAAGMEYLESKHCIHRDLAARNCLVT-EKNVLKISDFGMSRE----EE 146
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1231802383 213 NVSYICSRYYR-------APE-LIFGAtdYTSSIDVWSAGCVLAE 249
Cdd:cd05084   147 DGVYAATGGMKqipvkwtAPEaLNYGR--YSSESDVWSFGILLWE 189
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
62-250 4.62e-09

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: 56.62  E-value: 4.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKV-------LQDKRFKnRELQIMRKLDHCNIVRLRYFFYSSGEKKDEVYLNLVLdy 134
Cdd:cd14032     9 LGRGSFKTVYKGLDTETWVEVAWCELqdrkltkVERQRFK-EEAEMLKGLQHPNIVRFYDFWESCAKGKRCIVLVTEL-- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 135 vpETVYRVARHYSRAKQTLPVIyVKLYMYQLFRSLAYIHSFG--ICHRDIKPQNLLLDPDTAVLKLCDFGSAkQLVRGEP 212
Cdd:cd14032    86 --MTSGTLKTYLKRFKVMKPKV-LRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITGPTGSVKIGDLGLA-TLKRASF 161
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1231802383 213 NVSYICSRYYRAPELIfgATDYTSSIDVWSAGCVLAEL 250
Cdd:cd14032   162 AKSVIGTPEFMAPEMY--EEHYDESVDVYAFGMCMLEM 197
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
52-251 5.81e-09

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: 56.95  E-value: 5.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  52 QEVSYTDTKVIGNGSFGVVYQAKLCDSGE----LVAIKKVLQDKRFK-NREL----QIMRKLDHCNIVRLRYFFYSSGEK 122
Cdd:cd05108     5 KETEFKKIKVLGSGAFGTVYKGLWIPEGEkvkiPVAIKELREATSPKaNKEIldeaYVMASVDNPHVCRLLGICLTSTVQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 123 --KDEVYLNLVLDYVPETVYRVARHysrakqtlpviYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCD 200
Cdd:cd05108    85 liTQLMPFGCLLDYVREHKDNIGSQ-----------YLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHV-KITD 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1231802383 201 FGSAKQLVRGEPNVSYICSRY---YRAPELIFGATdYTSSIDVWSAGCVLAELL 251
Cdd:cd05108   153 FGLAKLLGAEEKEYHAEGGKVpikWMALESILHRI-YTHQSDVWSYGVTVWELM 205
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
50-251 7.33e-09

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: 56.12  E-value: 7.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  50 RPQEVSytDTKVIGNGSFGVVYQAKLCDSGELVAIK---KVLQDKRFKNRELQI------MRKLDHCNIVRLRYFFYSSG 120
Cdd:cd05111     5 KETELR--KLKVLGSGVFGTVHKGIWIPEGDSIKIPvaiKVIQDRSGRQSFQAVtdhmlaIGSLDHAYIVRLLGICPGAS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 121 ekkdevyLNLVLDYVPETvyRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCD 200
Cdd:cd05111    83 -------LQLVTQLLPLG--SLLDHVRQHRGSLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQV-QVAD 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1231802383 201 FGSA-------KQLVRGEPNVSYicsRYYRAPELIFGAtdYTSSIDVWSAGCVLAELL 251
Cdd:cd05111   153 FGVAdllypddKKYFYSEAKTPI---KWMALESIHFGK--YTHQSDVWSYGVTVWEMM 205
STKc_IRAK2 cd14157
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; ...
62-255 8.16e-09

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; 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. IRAK2 plays a role in mediating NFkB activation by TLR3, TLR4, and TLR8. It is specifically targeted by the viral protein A52, which is important for virulence, to inhibit all IL-1/TLR pathways, indicating that IRAK2 has a predominant role in NFkB activation. It is redundant with IRAK1 in early signaling but is critical for late and sustained activation. The IRAK2 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: 271059 [Multi-domain]  Cd Length: 289  Bit Score: 56.38  E-value: 8.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKlcDSGELVAIKKVLQD--------KRFKNRELQIMRKLDHCNIVRLRYFFYSSgekkdeVYLNLVLD 133
Cdd:cd14157     1 ISEGTFADIYKGY--RHGKQYVIKRLKETecespkstERFFQTEVQICFRCCHPNILPLLGFCVES------DCHCLIYP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 134 YVPETVYRVARHYSRAKQTLP-VIYVKLYMyQLFRSLAYIHSFGICHRDIKPQNLLLDPDTA------VLKLCDFGSAKQ 206
Cdd:cd14157    73 YMPNGSLQDRLQQQGGSHPLPwEQRLSISL-GLLKAVQHLHNFGILHGNIKSSNVLLDGNLLpklghsGLRLCPVDKKSV 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1231802383 207 LVRGEPNVSYICSRYYraPELIFGATDYTSSIDVWSAGCVLAELLLGQP 255
Cdd:cd14157   152 YTMMKTKVLQISLAYL--PEDFVRHGQLTEKVDIFSCGVVLAEILTGIK 198
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
62-272 1.09e-08

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: 55.35  E-value: 1.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIK---KVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEkkdevyLNLVLDYVPET 138
Cdd:cd14115     1 IGRGRFSIVKKCLHKATRKDVAVKfvsKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTS------YILVLELMDDG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 139 vyRVArHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAV--LKLCDFGSAKQLvRGEPNVSY 216
Cdd:cd14115    75 --RLL-DYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVprVKLIDLEDAVQI-SGHRHVHH 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1231802383 217 ICSR-YYRAPELIFGaTDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKV 272
Cdd:cd14115   151 LLGNpEFAAPEVIQG-TPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRV 206
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
62-258 1.39e-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: 55.19  E-value: 1.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYqakLCDSGELV---AIKKVL--QDKRFKN--RELQIMRKL-DHCNIVRLRY----FFYSSGEKkdeVYLN 129
Cdd:cd13975     8 LGRGQYGVVY---ACDSWGGHfpcALKSVVppDDKHWNDlaLEFHYTRSLpKHERIVSLHGsvidYSYGGGSS---IAVL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 LVLDYVPETVYRVARhysrAKQTLPV-IYVKLYMYQLFRslaYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAK--Q 206
Cdd:cd13975    82 LIMERLHRDLYTGIK----AGLSLEErLQIALDVVEGIR---FLHSQGLVHRDIKLKNVLLDKKNRA-KITDLGFCKpeA 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 207 LVRGepnvSYICSRYYRAPELIFGatDYTSSIDVWSAGCVLAELLLGQPIFP 258
Cdd:cd13975   154 MMSG----SIVGTPIHMAPELFSG--KYDNSVDVYAFGILFWYLCAGHVKLP 199
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
60-251 1.54e-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: 55.26  E-value: 1.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGE---LVAIKKVLQDKRFKNR-----ELQIMRKLDHCNIVRLRyffyssGEKKDEVYLNLV 131
Cdd:cd05066    10 KVIGAGEFGEVCSGRLKLPGKreiPVAIKTLKAGYTEKQRrdflsEASIMGQFDHPNIIHLE------GVVTRSKPVMIV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 132 LDYVP----ETVYRvaRHYSRakqtLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTaVLKLCDFGSAKQL 207
Cdd:cd05066    84 TEYMEngslDAFLR--KHDGQ----FTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNL-VCKVSDFGLSRVL 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1231802383 208 vRGEPNVSYICSR-----YYRAPELIfGATDYTSSIDVWSAGCVLAELL 251
Cdd:cd05066   157 -EDDPEAAYTTRGgkipiRWTAPEAI-AYRKFTSASDVWSYGIVMWEVM 203
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
60-271 1.62e-08

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: 55.36  E-value: 1.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLC-------DSGELVAIKKVLQDKRFKN-----RELQIMRKLD-HCNIVRLRyffyssGEKKDEV 126
Cdd:cd05099    18 KPLGEGCFGQVVRAEAYgidksrpDQTVTVAVKMLKDNATDKDladliSEMELMKLIGkHKNIINLL------GVCTQEG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 127 YLNLVLDYVPETVYRvarHYSRAKQ--------------TLPVIYVKLY--MYQLFRSLAYIHSFGICHRDIKPQNLLLD 190
Cdd:cd05099    92 PLYVIVEYAAKGNLR---EFLRARRppgpdytfditkvpEEQLSFKDLVscAYQVARGMEYLESRRCIHRDLAARNVLVT 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 191 PDTaVLKLCDFGsakqLVRGEPNVSYICSRY-------YRAPELIFGATdYTSSIDVWSAGCVLAELL-LGQPIFPGDSg 262
Cdd:cd05099   169 EDN-VMKIADFG----LARGVHDIDYYKKTSngrlpvkWMAPEALFDRV-YTHQSDVWSFGILMWEIFtLGGSPYPGIP- 241

                  ....*....
gi 1231802383 263 VDQLVEIIK 271
Cdd:cd05099   242 VEELFKLLR 250
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
62-255 1.80e-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: 55.02  E-value: 1.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKVLQDKrFKNRELQIMRKLDHCNIVRLR---------YFFYSSGEKKDevylnlVL 132
Cdd:cd13995    12 IPRGAFGKVYLAQDTKTKKRMACKLIPVEQ-FKPSDVEIQACFRHENIAELYgallweetvHLFMEAGEGGS------VL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 DYVPETvyrvarhysRAKQTLPVIYVKlymYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlkLCDFGSAKQL----- 207
Cdd:cd13995    85 EKLESC---------GPMREFEIIWVT---KHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAV--LVDFGLSVQMtedvy 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 208 ----VRGepnvsyicSRYYRAPELIFgATDYTSSIDVWSAGCVLAELLLGQP 255
Cdd:cd13995   151 vpkdLRG--------TEIYMSPEVIL-CRGHNTKADIYSLGATIIHMQTGSP 193
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
60-250 2.28e-08

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: 54.78  E-value: 2.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKL----CDSGELVAIKKVLQDKRFKN------RELQIMRKLDHCNIVRLryffYSSGEKKDEVYln 129
Cdd:cd05046    11 TTLGRGEFGEVFLAKAkgieEEGGETLVLVKALQKTKDENlqsefrRELDMFRKLSHKNVVRL----LGLCREAEPHY-- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 LVLDYVP----ETVYRVARHYSRAKQTLPVIYV-KLYM-YQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLcdfgS 203
Cdd:cd05046    85 MILEYTDlgdlKQFLRATKSKDEKLKPPPLSTKqKVALcTQIALGMDHLSNARFVHRDLAARNCLVSSQREV-KV----S 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1231802383 204 AKQLVRGEPNvsyicSRYYR-----------APELIFgATDYTSSIDVWSAGCVLAEL 250
Cdd:cd05046   160 LLSLSKDVYN-----SEYYKlrnaliplrwlAPEAVQ-EDDFSTKSDVWSFGVLMWEV 211
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
161-317 2.46e-08

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: 55.40  E-value: 2.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 161 YMYQLFRSLAYIHSFGICHRDIKPQNLLLdPDTAVLKLCDFGSAKQLVRgepNVSYIC--SRY----YRAPELIFGATdY 234
Cdd:cd05107   244 FSYQVANGMEFLASKNCVHRDLAARNVLI-CEGKLVKICDFGLARDIMR---DSNYISkgSTFlplkWMAPESIFNNL-Y 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 235 TSSIDVWSAGCVLAELL-LGQPIFPGDSGVDQLVEIIKvlgtptrEQIREMNPNYTEFKFPQIKAHPWTKVFRPRTPPEA 313
Cdd:cd05107   319 TTLSDVWSFGILLWEIFtLGGTPYPELPMNEQFYNAIK-------RGYRMAKPAHASDEIYEIMQKCWEEKFEIRPDFSQ 391

                  ....
gi 1231802383 314 IALC 317
Cdd:cd05107   392 LVHL 395
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
62-261 2.47e-08

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: 54.83  E-value: 2.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSgeLVAIKKVLQDKRF-----KNR---ELQIMRKLDHCNIVRLryffysSGEKKDEVYLNLVLD 133
Cdd:cd14159     1 IGEGGFGCVYQAVMRNT--EYAVKRLKEDSELdwsvvKNSfltEVEKLSRFRHPNIVDL------AGYSAQQGNYCLIYV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 134 YVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSF--GICHRDIKPQNLLLDpDTAVLKLCDFGSAK------ 205
Cdd:cd14159    73 YLPNGSLEDRLHCQVSCPCLSWSQRLHVLLGTARAIQYLHSDspSLIHGDVKSSNILLD-AALNPKLGDFGLARfsrrpk 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1231802383 206 -----------QLVRGepNVSYICSRYYRAPELifgatdyTSSIDVWSAGCVLAELLLGQPIFPGDS 261
Cdd:cd14159   152 qpgmsstlartQTVRG--TLAYLPEEYVKTGTL-------SVEIDVYSFGVVLLELLTGRRAMEVDS 209
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
51-250 2.51e-08

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: 54.50  E-value: 2.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  51 PQEVSYTdtKVIGNGSFGVVYQAKLcdSGEL-VAIKKVLQDKRFKN---RELQIMRKLDHCNIVRLryffYSSGEKKDEV 126
Cdd:cd05113     3 PKDLTFL--KELGTGQFGVVKYGKW--RGQYdVAIKMIKEGSMSEDefiEEAKVMMNLSHEKLVQL----YGVCTKQRPI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 127 YLnlVLDYVPE----TVYRVARHYSRAKQTLPVIYvklymyQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFG 202
Cdd:cd05113    75 FI--ITEYMANgcllNYLREMRKRFQTQQLLEMCK------DVCEAMEYLESKQFLHRDLAARNCLVN-DQGVVKVSDFG 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1231802383 203 SAKQLVRGEpNVSYICSRY---YRAPElIFGATDYTSSIDVWSAGCVLAEL 250
Cdd:cd05113   146 LSRYVLDDE-YTSSVGSKFpvrWSPPE-VLMYSKFSSKSDVWAFGVLMWEV 194
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
61-329 2.97e-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: 54.68  E-value: 2.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  61 VIGNGSFGVVYQAKLCDSGELVAIK-----KVLQDKRFKN------RELQIMRKLDHCNIVRLRYFFyssgeKKDEVYLN 129
Cdd:cd14041    13 LLGRGGFSEVYKAFDLTEQRYVAVKihqlnKNWRDEKKENyhkhacREYRIHKELDHPRIVKLYDYF-----SLDTDSFC 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 LVLDYVP--ETVYRVARHYSRAKQTLPVIyvklyMYQLFRSLAYIHSFG--ICHRDIKPQNLLLDPDTAV--LKLCDFGS 203
Cdd:cd14041    88 TVLEYCEgnDLDFYLKQHKLMSEKEARSI-----IMQIVNALKYLNEIKppIIHYDLKPGNILLVNGTACgeIKITDFGL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 204 AKQL-------VRGEPNVSYICSRYYRAPELIF----GATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKV 272
Cdd:cd14041   163 SKIMdddsynsVDGMELTSQGAGTYWYLPPECFvvgkEPPKISNKVDVWSVGVIFYQCLYGRKPFGHNQSQQDILQENTI 242
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1231802383 273 LGTptreqiremnpnyTEFKFPQikahpwtkvfRPRTPPEAIALCSRLLEYTPTARL 329
Cdd:cd14041   243 LKA-------------TEVQFPP----------KPVVTPEAKAFIRRCLAYRKEDRI 276
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
60-259 3.29e-08

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: 54.56  E-value: 3.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCD---SGELVAIKKVLQDKrFKNRELQ-------IMRKLDHCNIVRLRYFFYSSGEK---KDEV 126
Cdd:cd14204    13 KVLGEGEFGSVMEGELQQpdgTNHKVAVKTMKLDN-FSQREIEeflseaaCMKDFNHPNVIRLLGVCLEVGSQripKPMV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 127 YLNLvLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLkLCDFGSAKQ 206
Cdd:cd14204    92 ILPF-MKYGDLHSFLLRSRLGSGPQHVPLQTLLKFMIDIALGMEYLSSRNFLHRDLAARNCMLRDDMTVC-VADFGLSKK 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1231802383 207 LVRGEpnvsyicsrYYRAPEL---------IFGATD--YTSSIDVWSAGCVLAELLL-GQPIFPG 259
Cdd:cd14204   170 IYSGD---------YYRQGRIakmpvkwiaVESLADrvYTVKSDVWAFGVTMWEIATrGMTPYPG 225
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
62-250 3.59e-08

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: 54.34  E-value: 3.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKvLQDK--------RFKnRELQIMRKLDHCNIVRlryfFYSSGEK--KDEVYLNLV 131
Cdd:cd14031    18 LGRGAFKTVYKGLDTETWVEVAWCE-LQDRkltkaeqqRFK-EEAEMLKGLQHPNIVR----FYDSWESvlKGKKCIVLV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 132 LDYVPETVYRVarHYSRAKQTLPVIyVKLYMYQLFRSLAYIHSFG--ICHRDIKPQNLLLDPDTAVLKLCDFGSAkQLVR 209
Cdd:cd14031    92 TELMTSGTLKT--YLKRFKVMKPKV-LRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGPTGSVKIGDLGLA-TLMR 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1231802383 210 GEPNVSYICSRYYRAPELIfgATDYTSSIDVWSAGCVLAEL 250
Cdd:cd14031   168 TSFAKSVIGTPEFMAPEMY--EEHYDESVDVYAFGMCMLEM 206
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
62-251 3.70e-08

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: 54.18  E-value: 3.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQA--KLCDSGELVAIKkVLQDKRFKN------RELQIMRKLDHCNIVRLryffysSGEKKDEVyLNLVLD 133
Cdd:cd05115    12 LGSGNFGCVKKGvyKMRKKQIDVAIK-VLKQGNEKAvrdemmREAQIMHQLDNPYIVRM------IGVCEAEA-LMLVME 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 134 YVPETvyRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLdPDTAVLKLCDFGSAKQLVRGEpn 213
Cdd:cd05115    84 MASGG--PLNKFLSGKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLL-VNQHYAKISDFGLSKALGADD-- 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1231802383 214 vSYICSRY-------YRAPELIfGATDYTSSIDVWSAGCVLAELL 251
Cdd:cd05115   159 -SYYKARSagkwplkWYAPECI-NFRKFSSRSDVWSYGVTMWEAF 201
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
62-259 4.07e-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: 53.96  E-value: 4.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKVLQD----KRFKnRELQIMRKLDHCNIVRLRYF------FYSSGEKKdeVYLNLv 131
Cdd:cd05052    14 LGGGQYGEVYEGVWKKYNLTVAVKTLKEDtmevEEFL-KEAAVMKEIKHPNLVQLLGVctreppFYIITEFM--PYGNL- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 132 LDYVPETvyrvarhysrAKQTLPVIyVKLYM-YQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKqLVRG 210
Cdd:cd05052    90 LDYLREC----------NREELNAV-VLLYMaTQIASAMEYLEKKNFIHRDLAARNCLVGENHLV-KVADFGLSR-LMTG 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1231802383 211 EPNVSYICSRY---YRAPElifGATDYTSSI--DVWSAGCVLAEL-LLGQPIFPG 259
Cdd:cd05052   157 DTYTAHAGAKFpikWTAPE---SLAYNKFSIksDVWAFGVLLWEIaTYGMSPYPG 208
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
60-251 4.16e-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: 54.11  E-value: 4.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGE---LVAIKKVLQDKRFKNR-----ELQIMRKLDHCNIVRLRYFFYSSGEKK--DEVYLN 129
Cdd:cd05065    10 EVIGAGEFGEVCRGRLKLPGKreiFVAIKTLKSGYTEKQRrdflsEASIMGQFDHPNIIHLEGVVTKSRPVMiiTEFMEN 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 LVLDyvpetvyrvarHYSRAKQ-TLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTaVLKLCDFGSAKQLV 208
Cdd:cd05065    90 GALD-----------SFLRQNDgQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNL-VCKVSDFGLSRFLE 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1231802383 209 RGEPNVSYICSR------YYRAPELIfGATDYTSSIDVWSAGCVLAELL 251
Cdd:cd05065   158 DDTSDPTYTSSLggkipiRWTAPEAI-AYRKFTSASDVWSYGIVMWEVM 205
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
62-257 4.34e-08

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: 53.69  E-value: 4.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKlCdSGELVAIKKVL-------QDKRFKNRELQIMRKLDHCNIVRlryFFYSSGEkkDEVYLNLVLDY 134
Cdd:cd14064     1 IGSGSFGKVYKGR-C-RNKIVAIKRYRantycskSDVDMFCREVSILCRLNHPCVIQ---FVGACLD--DPSQFAIVTQY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 135 VPETVYRVARHysRAKQTLPVIYVKLYMYQLFRSLAYIHSFG--ICHRDIKPQNLLLDPDTAVLkLCDFGSAKqlvrgep 212
Cdd:cd14064    74 VSGGSLFSLLH--EQKRVIDLQSKLIIAVDVAKGMEYLHNLTqpIIHRDLNSHNILLYEDGHAV-VADFGESR------- 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1231802383 213 nvsYICSRY------------YRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIF 257
Cdd:cd14064   144 ---FLQSLDednmtkqpgnlrWMAPEVFTQCTRYSIKADVFSYALCLWELLTGEIPF 197
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
60-271 4.52e-08

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: 54.25  E-value: 4.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLC-------DSGELVAIKKVLQDKRFKN-----RELQIMRKL-DHCNIVRLRyffyssGEKKDEV 126
Cdd:cd05101    30 KPLGEGCFGQVVMAEAVgidkdkpKEAVTVAVKMLKDDATEKDlsdlvSEMEMMKMIgKHKNIINLL------GACTQDG 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 127 YLNLVLDYVPETVYRvarHYSRAKQTL--------------PVIYVKLY--MYQLFRSLAYIHSFGICHRDIKPQNLLLD 190
Cdd:cd05101   104 PLYVIVEYASKGNLR---EYLRARRPPgmeysydinrvpeeQMTFKDLVscTYQLARGMEYLASQKCIHRDLAARNVLVT 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 191 pDTAVLKLCDFGsakqLVRGEPNVSYICSRY-------YRAPELIFGATdYTSSIDVWSAGCVLAELL-LGQPIFPGDSg 262
Cdd:cd05101   181 -ENNVMKIADFG----LARDINNIDYYKKTTngrlpvkWMAPEALFDRV-YTHQSDVWSFGVLMWEIFtLGGSPYPGIP- 253

                  ....*....
gi 1231802383 263 VDQLVEIIK 271
Cdd:cd05101   254 VEELFKLLK 262
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
60-246 4.85e-08

putative serine/threonine kinase; Provisional


Pssm-ID: 165211 [Multi-domain]  Cd Length: 294  Bit Score: 53.80  E-value: 4.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQ----AKLCDSGELVAIKKVLQDKRF------------KNRELQIMR--KLDHCNIVRlryfFYSSGE 121
Cdd:PHA02882   18 KLIGCGGFGCVYEtqcaSDHCINNQAVAKIENLENETIvmetlvynniydIDKIALWKNihNIDHLGIPK----YYGCGS 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 122 -KKDEVYLNLVLdyVPETVYRVARHYSRAKqTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLkLCD 200
Cdd:PHA02882   94 fKRCRMYYRFIL--LEKLVENTKEIFKRIK-CKNKKLIKNIMKDMLTTLEYIHEHGISHGDIKPENIMVDGNNRGY-IID 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1231802383 201 FGSAKQLVRGEPNVsyicsRYYRAPELIFGATDYTSSIDVWSAGCV 246
Cdd:PHA02882  170 YGIASHFIIHGKHI-----EYSKEQKDLHRGTLYYAGLDAHNGACV 210
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
161-301 4.87e-08

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: 54.52  E-value: 4.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 161 YMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQlVRGEPNvsYICSRYYR------APELIFGATdY 234
Cdd:cd05104   219 FSYQVAKGMEFLASKNCIHRDLAARNILLT-HGRITKICDFGLARD-IRNDSN--YVVKGNARlpvkwmAPESIFECV-Y 293
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1231802383 235 TSSIDVWSAGCVLAELL-LGQPIFPGDSGVDQLVEIIKvlgtptrEQIREMNPNYTEFKFPQIKAHPW 301
Cdd:cd05104   294 TFESDVWSYGILLWEIFsLGSSPYPGMPVDSKFYKMIK-------EGYRMDSPEFAPSEMYDIMRSCW 354
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
60-217 5.01e-08

Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 and BubR1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Bub1 (Budding uninhibited by benzimidazoles 1), BubR1, and similar proteins. They contain an N-terminal Bub1/Mad3 homology domain essential for Cdc20 binding and a C-terminal kinase domain. Bub1 and BubR1 are involved in SAC, a surveillance system that delays metaphase to anaphase transition by blocking the activity of APC/C (the anaphase promoting complex) until all chromosomes achieve proper attachments to the mitotic spindle, to avoid chromosome missegregation. Impaired SAC leads to genomic instabilities and tumor development. Bub1 and BubR1 facilitate the localization of SAC proteins to kinetochores and regulate kinetochore-microtubule (K-MT) attachments. Repression studies of Bub1 and BubR1 show that they exert an additive effect in misalignment phenotypes and may function cooperatively or in parallel pathways in regulating K-MT attachments. The Bub1/BubR1 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: 270883 [Multi-domain]  Cd Length: 298  Bit Score: 53.90  E-value: 5.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAK---LCDSGELVAIKKVLQDKRFknrELQIMRKL-DHCNIVRLRYFF--YSSGEK-KDEVYLnlVL 132
Cdd:cd13981     6 KELGEGGYASVYLAKdddEQSDGSLVALKVEKPPSIW---EFYICDQLhSRLKNSRLRESIsgAHSAHLfQDESIL--VM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 DYVPE-TVYRVA-RHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLL--------------DPDTAVL 196
Cdd:cd13981    81 DYSSQgTLLDVVnKMKNKTGGGMDEPLAMFFTIELLKVVEALHEVGIIHGDIKPDNFLLrleicadwpgegenGWLSKGL 160
                         170       180
                  ....*....|....*....|.
gi 1231802383 197 KLCDFGSAKQLVRGEPNVSYI 217
Cdd:cd13981   161 KLIDFGRSIDMSLFPKNQSFK 181
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
163-271 5.09e-08

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: 53.86  E-value: 5.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 163 YQLFRSLAYIHSFGICHRDIKPQNLLLDPDTaVLKLCDFGSA---------KQLVRGEPNVSYIcsryyrAPELIFGATd 233
Cdd:cd05098   142 YQVARGMEYLASKKCIHRDLAARNVLVTEDN-VMKIADFGLArdihhidyyKKTTNGRLPVKWM------APEALFDRI- 213
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1231802383 234 YTSSIDVWSAGCVLAELL-LGQPIFPGdSGVDQLVEIIK 271
Cdd:cd05098   214 YTHQSDVWSFGVLLWEIFtLGGSPYPG-VPVEELFKLLK 251
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
161-259 5.16e-08

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: 54.47  E-value: 5.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 161 YMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQLVRGEPNVSYICSRY---YRAPELIFGATdYTSS 237
Cdd:cd05106   217 FSSQVAQGMDFLASKNCIHRDVAARNVLLT-DGRVAKICDFGLARDIMNDSNYVVKGNARLpvkWMAPESIFDCV-YTVQ 294
                          90       100
                  ....*....|....*....|...
gi 1231802383 238 IDVWSAGCVLAELL-LGQPIFPG 259
Cdd:cd05106   295 SDVWSYGILLWEIFsLGKSPYPG 317
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
65-290 6.01e-08

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. 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 LRRK1 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: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 53.43  E-value: 6.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  65 GSFGVVYQAKLcdSGELVAIKKvLQDKRFKNR--------------------------ELQIMRKLDHCNIVRLRYFFYS 118
Cdd:cd14067     5 GSGTVIYRARY--QGQPVAVKR-FHIKKCKKRtdgsadtmlkhlraadamknfsefrqEASMLHSLQHPCIVYLIGISIH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 119 SgekkdevyLNLVLDYVP-ETVYRVARHYSRAKQTLPVIYVKLY--MYQLFRSLAYIHSFGICHRDIKPQNLL---LDPD 192
Cdd:cd14067    82 P--------LCFALELAPlGSLNTVLEENHKGSSFMPLGHMLTFkiAYQIAAGLAYLHKKNIIFCDLKSDNILvwsLDVQ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 193 TAV-LKLCDFGSAKQL-------VRGEPNvsyicsryYRAPELIFGATdYTSSIDVWSAGCVLAELLLGQ-PIFpgdsGV 263
Cdd:cd14067   154 EHInIKLSDYGISRQSfhegalgVEGTPG--------YQAPEIRPRIV-YDEKVDMFSYGMVLYELLSGQrPSL----GH 220
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1231802383 264 DQLvEIIK--------VLGTPTREQIREMNPNYTE 290
Cdd:cd14067   221 HQL-QIAKklskgirpVLGQPEEVQFFRLQALMME 254
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
60-258 6.22e-08

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: 53.25  E-value: 6.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGEL---VAIKKV-----LQDKRFKNRELQIMRKLDHCNIVRLryffysSGEKKDEVYLNLV 131
Cdd:cd05058     1 EVIGKGHFGCVYHGTLIDSDGQkihCAVKSLnritdIEEVEQFLKEGIIMKDFSHPNVLSL------LGICLPSEGSPLV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 132 LdyVPETVYRVARHYSRAKQTLPViyVKLYM---YQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQLV 208
Cdd:cd05058    75 V--LPYMKHGDLRNFIRSETHNPT--VKDLIgfgLQVAKGMEYLASKKFVHRDLAARNCMLD-ESFTVKVADFGLARDIY 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1231802383 209 RGEpnvsYICSRYYRAPEL--------IFGATDYTSSIDVWSAGCVLAELLL-GQPIFP 258
Cdd:cd05058   150 DKE----YYSVHNHTGAKLpvkwmaleSLQTQKFTTKSDVWSFGVLLWELMTrGAPPYP 204
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
60-268 6.83e-08

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: 53.18  E-value: 6.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAkLCDSGELVAIKKV----LQDKRFKnRELQIMRKLDHCNIVRLryffYSSGEKKDEVYLnlvldyv 135
Cdd:cd05068    14 RKLGSGQFGEVWEG-LWNNTTPVAVKTLkpgtMDPEDFL-REAQIMKKLRHPKLIQL----YAVCTLEEPIYI------- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 136 petVYRVARH-----YSRAKQTLPVIYVKLYMY-QLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQLVR 209
Cdd:cd05068    81 ---ITELMKHgslleYLQGKGRSLQLPQLIDMAaQVASGMAYLESQNYIHRDLAARNVLVG-ENNICKVADFGLARVIKV 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1231802383 210 GEPNVSYICSRY---YRAPElifgATDYTS-SI--DVWSAGCVLAELL-LGQPIFPGDSG--VDQLVE 268
Cdd:cd05068   157 EDEYEAREGAKFpikWTAPE----AANYNRfSIksDVWSFGILLTEIVtYGRIPYPGMTNaeVLQQVE 220
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
61-255 7.13e-08

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: 53.12  E-value: 7.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  61 VIGNGSFGVVYQAKLCDSGELV--AIKKVLQ-----DKRFKNRELQIMRKL-DHCNIVRLryffysSGEKKDEVYLNLVL 132
Cdd:cd05047     2 VIGEGNFGQVLKARIKKDGLRMdaAIKRMKEyaskdDHRDFAGELEVLCKLgHHPNIINL------LGACEHRGYLYLAI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 DYVPETVYRVARHYSRAKQTLPVIYVK------LYMYQLF-------RSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLC 199
Cdd:cd05047    76 EYAPHGNLLDFLRKSRVLETDPAFAIAnstastLSSQQLLhfaadvaRGMDYLSQKQFIHRDLAARNILVG-ENYVAKIA 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1231802383 200 DFG-SAKQLVRGEPNVSYICSRYYRAPELIFGAtdYTSSIDVWSAGCVLAEL--LLGQP 255
Cdd:cd05047   155 DFGlSRGQEVYVKKTMGRLPVRWMAIESLNYSV--YTTNSDVWSYGVLLWEIvsLGGTP 211
K-ycf53 COG5752
Signaling protein combining a Ser/Thr protein kinase domain and the GUN4/Ycf53 ...
169-257 7.77e-08

Signaling protein combining a Ser/Thr protein kinase domain and the GUN4/Ycf53 porphyrin-binding domain [Signal transduction mechanisms];


Pssm-ID: 444462 [Multi-domain]  Cd Length: 466  Bit Score: 53.85  E-value: 7.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 169 LAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSAKQL------VRGepnvSYICSRYYRAPELIFGATDYTSsiDVWS 242
Cdd:COG5752   151 LQFIHSRNVIHRDIKPANIIRRRSDGKLVLIDFGVAKLLtitallQTG----TIIGTPEYMAPEQLRGKVFPAS--DLYS 224
                          90
                  ....*....|....*
gi 1231802383 243 AGCVLAELLLGQPIF 257
Cdd:COG5752   225 LGVTCIYLLTGVSPF 239
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
163-271 9.61e-08

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: 53.10  E-value: 9.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 163 YQLFRSLAYIHSFGICHRDIKPQNLLLDPDTaVLKLCDFGsakqLVRGEPNVSYICSRY-------YRAPELIFGATdYT 235
Cdd:cd05100   141 YQVARGMEYLASQKCIHRDLAARNVLVTEDN-VMKIADFG----LARDVHNIDYYKKTTngrlpvkWMAPEALFDRV-YT 214
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1231802383 236 SSIDVWSAGCVLAELL-LGQPIFPGDSgVDQLVEIIK 271
Cdd:cd05100   215 HQSDVWSFGVLLWEIFtLGGSPYPGIP-VEELFKLLK 250
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
79-286 1.01e-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: 52.78  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  79 GELVAIKKVlQDKRFKNR----ELQIMRKLDHCNIVRlryffyssgekkdevYLNLVLDyvPETVYRVARHYSRAkqTLP 154
Cdd:cd13992    25 GRTVAIKHI-TFSRTEKRtilqELNQLKELVHDNLNK---------------FIGICIN--PPNIAVVTEYCTRG--SLQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 155 -VIYVK----------LYMYQLFRSLAYIH-SFGICHRDIKPQNLLLDpDTAVLKLCDFGSA----KQLVRGEPNVSYIC 218
Cdd:cd13992    85 dVLLNReikmdwmfksSFIKDIVKGMNYLHsSSIGYHGRLKSSNCLVD-SRWVVKLTDFGLRnlleEQTNHQLDEDAQHK 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1231802383 219 SRYYRAPELIFGATDY---TSSIDVWSAGCVLAELLLGQPIFPgDSGVDQLVEIIKVLGTPTR--EQIREMNP 286
Cdd:cd13992   164 KLLWTAPELLRGSLLEvrgTQKGDVYSFAIILYEILFRSDPFA-LEREVAIVEKVISGGNKPFrpELAVLLDE 235
STKc_CK1_delta_epsilon cd14125
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; ...
62-206 1.17e-07

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. The delta and epsilon isoforms of CK1 play important roles in circadian rhythm and cell growth. They phosphorylate PERIOD proteins (PER1-3), which are circadian clock proteins that fulfill negative regulatory functions. PER phosphorylation leads to its degradation. However, CRY proteins form a complex with PER and CK1delta/epsilon that protects PER from degradation and leads to nuclear accummulation of the complex, which inhibits BMAL1-CLOCK dependent transcription activation. CK1delta/epsilon also phosphorylate the tumor suppressor p53 and the cellular oncogene Mdm2, which are key regulators of cell growth, genome integrity, and the development of cancer. This subfamily also includes the CK1 fungal proteins Saccharomyces cerevisiae HRR25 and Schizosaccharomyces pombe HHP1. These fungal proteins are involved in DNA repair. The CK1 delta/epsilon 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: 271027 [Multi-domain]  Cd Length: 275  Bit Score: 52.76  E-value: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKkvLQDKRFKNRELQIMRKL-----DHCNIVRLRYFfyssGEKKDevYLNLVLDYVP 136
Cdd:cd14125     8 IGSGSFGDIYLGTNIQTGEEVAIK--LESVKTKHPQLLYESKLykilqGGVGIPNVRWY----GVEGD--YNVMVMDLLG 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 137 ETVYRVARHYSRaKQTLPViyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLL--LDPDTAVLKLCDFGSAKQ 206
Cdd:cd14125    80 PSLEDLFNFCSR-KFSLKT--VLMLADQMISRIEYVHSKNFIHRDIKPDNFLmgLGKKGNLVYIIDFGLAKK 148
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
60-259 1.22e-07

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: 52.66  E-value: 1.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKN----------RELQIMRKLDHCNIVRLRYFFYSSGEkkdevyLN 129
Cdd:cd05045     6 KTLGEGEFGKVVKATAFRLKGRAGYTTVAVKMLKENassselrdllSEFNLLKQVNHPHVIKLYGACSQDGP------LL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 LVLDYVPetvYRVARHYSRAKQTLPVIYVKL------------------------YMYQLFRSLAYIHSFGICHRDIKPQ 185
Cdd:cd05045    80 LIVEYAK---YGSLRSFLRESRKVGPSYLGSdgnrnssyldnpderaltmgdlisFAWQISRGMQYLAEMKLVHRDLAAR 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1231802383 186 NLLLdPDTAVLKLCDFGSAKQLVRGEPNVSYICSRY---YRAPELIFGATdYTSSIDVWSAGCVLAELL-LGQPIFPG 259
Cdd:cd05045   157 NVLV-AEGRKMKISDFGLSRDVYEEDSYVKRSKGRIpvkWMAIESLFDHI-YTTQSDVWSFGVLLWEIVtLGGNPYPG 232
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
62-202 1.25e-07

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 50.13  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIK----KVLQDKRFKNRELQIMRKLDhcNIVRLRYFFYSSGEKKDEvyLNLVLDYVPE 137
Cdd:cd13968     1 MGEGASAKVFWAEGECTTIGVAVKigddVNNEEGEDLESEMDILRRLK--GLELNIPKVLVTEDVDGP--NILLMELVKG 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1231802383 138 TVYRVARhysrAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDtAVLKLCDFG 202
Cdd:cd13968    77 GTLIAYT----QEEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSED-GNVKLIDFG 136
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
143-301 1.57e-07

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: 52.16  E-value: 1.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 143 ARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQLvrgEPNV-SYICSRY 221
Cdd:cd05576   100 ERLAAASRFYIPEECIQRWAAEMVVALDALHREGIVCRDLNPNNILLN-DRGHIQLTYFSRWSEV---EDSCdSDAIENM 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 222 YRAPElIFGATDYTSSIDVWSAGCVLAELLLGQPIF---PGDSGVDQLVEIIKVLGTPTR---EQIREMNP----NYTEF 291
Cdd:cd05576   176 YCAPE-VGGISEETEACDWWSLGALLFELLTGKALVechPAGINTHTTLNIPEWVSEEARsllQQLLQFNPterlGAGVA 254
                         170
                  ....*....|
gi 1231802383 292 KFPQIKAHPW 301
Cdd:cd05576   255 GVEDIKSHPF 264
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
162-273 2.00e-07

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 52.77  E-value: 2.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 162 MYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLkLCDFGSAKQL--VRGEPNVSYICSRYYRAPELIFGATdYTSSID 239
Cdd:PHA03210  273 MKQLLCAVEYIHDKKLIHRDIKLENIFLNCDGKIV-LGDFGTAMPFekEREAFDYGWVGTVATNSPEILAGDG-YCEITD 350
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1231802383 240 VWSAGCVLAELLLGQPIFPGDSGVD---QLVEIIKVL 273
Cdd:PHA03210  351 IWSCGLILLDMLSHDFCPIGDGGGKpgkQLLKIIDSL 387
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
60-259 2.31e-07

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: 51.46  E-value: 2.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGElVAIKKV----LQDKRFKNrELQIMRKLDHCNIVRLrYFFYSsgekKDEVYL------- 128
Cdd:cd14203     1 VKLGQGCFGEVWMGTWNGTTK-VAIKTLkpgtMSPEAFLE-EAQIMKKLRHDKLVQL-YAVVS----EEPIYIvtefmsk 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 129 NLVLDYVPETVYRVARhysrakqtLPVIyVKLYMyQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKqLV 208
Cdd:cd14203    74 GSLLDFLKDGEGKYLK--------LPQL-VDMAA-QIASGMAYIERMNYIHRDLRAANILVG-DNLVCKIADFGLAR-LI 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1231802383 209 RGEPNVSYICSRY---YRAPE-LIFGAtdYTSSIDVWSAGCVLAELLL-GQPIFPG 259
Cdd:cd14203   142 EDNEYTARQGAKFpikWTAPEaALYGR--FTIKSDVWSFGILLTELVTkGRVPYPG 195
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
62-250 2.38e-07

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 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: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 51.97  E-value: 2.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKvLQDKRFKNRELQ-------IMRKLDHCNIVRlryfFYSSGEK--KDEVYLNLVL 132
Cdd:cd14030    33 IGRGSFKTVYKGLDTETTVEVAWCE-LQDRKLSKSERQrfkeeagMLKGLQHPNIVR----FYDSWEStvKGKKCIVLVT 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 133 DYVPETVYRVarhYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFG--ICHRDIKPQNLLLDPDTAVLKLCDFGSAkQLVRG 210
Cdd:cd14030   108 ELMTSGTLKT---YLKRFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGPTGSVKIGDLGLA-TLKRA 183
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1231802383 211 EPNVSYICSRYYRAPELIfgATDYTSSIDVWSAGCVLAEL 250
Cdd:cd14030   184 SFAKSVIGTPEFMAPEMY--EEKYDESVDVYAFGMCMLEM 221
STKc_SRPK2 cd14217
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 2; STKs ...
151-279 2.94e-07

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK2 mediates neuronal cell cycle and cell death through regulation of nuclear cyclin D1. It has also been found to promote leukemia cell proliferation by regulating cyclin A1. SRPK2 also plays a role in regulating pre-mRNA splicing and is required for spliceosomal B complex formation. 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. 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: 271119 [Multi-domain]  Cd Length: 366  Bit Score: 51.96  E-value: 2.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 151 QTLPVIYVKLYMYQLFRSLAYIHS-FGICHRDIKPQNLL----------------------------------------- 188
Cdd:cd14217   116 QGLPIRCVKSIIRQVLQGLDYLHSkCKIIHTDIKPENILmcvddayvrrmaaeatewqkagapppsgsavstapdllvnp 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 189 LDP---DTAVLKLCDFGSA----KQLVRGepnvsyICSRYYRAPELIFGAtDYTSSIDVWSAGCVLAELLLGQPIFPGDS 261
Cdd:cd14217   196 LDPrnaDKIRVKIADLGNAcwvhKHFTED------IQTRQYRSIEVLIGA-GYSTPADIWSTACMAFELATGDYLFEPHS 268
                         170       180
                  ....*....|....*....|....
gi 1231802383 262 G------VDQLVEIIKVLGTPTRE 279
Cdd:cd14217   269 GedysrdEDHIAHIIELLGCIPRH 292
STKc_TTBK2 cd14129
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze ...
62-254 4.05e-07

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. Mutations in TTBK2 is associated with the development of spinocerebellar ataxia type 11, belonging to a group of neurodegenerative disorders characterized by progressive incoordination, dysarthria and impairment of eye movements. Brain tissues of SCA11 patients show the presence of neurofibrillary tangles and tau deposition in the brain, similar to Alzheimer's disease (AD) patients. The TTBK2 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: 271031 [Multi-domain]  Cd Length: 262  Bit Score: 50.82  E-value: 4.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIK--KVLQDKRFKNRELQIMRKL---DH-CNIVrlryffyssGEKKDEVYLNLVLDYV 135
Cdd:cd14129     8 IGGGGFGEIYDALDLLTRENVALKveSAQQPKQVLKMEVAVLKKLqgkDHvCRFI---------GCGRNDRFNYVVMQLQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 136 PETVYRVARHYSRAKQTLPVIyVKLyMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLC---DFGSAKQLVRGEP 212
Cdd:cd14129    79 GRNLADLRRSQSRGTFTISTT-LRL-GRQILESIESIHSVGFLHRDIKPSNFAMGRFPSTCRKCymlDFGLARQFTNSCG 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1231802383 213 NVsyicsRYYRAPELIFGATDYTS-----------SIDVWSAGCVLAELLLGQ 254
Cdd:cd14129   157 DV-----RPPRAVAGFRGTVRYASinahrnremgrHDDLWSLFYMLVEFVVGQ 204
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
60-286 4.25e-07

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: 50.79  E-value: 4.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLcDSGELVAIKKV----LQDKRFKNrELQIMRKLDHCNIVRLRYFFyssgeKKDEVYLnlVLDYV 135
Cdd:cd05073    17 KKLGAGQFGEVWMATY-NKHTKVAVKTMkpgsMSVEAFLA-EANVMKTLQHDKLVKLHAVV-----TKEPIYI--ITEFM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 136 PE-TVYRVARHYSRAKQTLPviyvKL--YMYQLFRSLAYIHSFGICHRDIKPQNLLLDPdTAVLKLCDFGSAKqLVRGEP 212
Cdd:cd05073    88 AKgSLLDFLKSDEGSKQPLP----KLidFSAQIAEGMAFIEQRNYIHRDLRAANILVSA-SLVCKIADFGLAR-VIEDNE 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1231802383 213 NVSYICSRY---YRAPELI-FGAtdYTSSIDVWSAGCVLAELL-LGQPIFPGDSGvdqlVEIIKVLGTPTREQIREMNP 286
Cdd:cd05073   162 YTAREGAKFpikWTAPEAInFGS--FTIKSDVWSFGILLMEIVtYGRIPYPGMSN----PEVIRALERGYRMPRPENCP 234
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
61-329 4.62e-07

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: 50.83  E-value: 4.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  61 VIGNGSFGVVYQAKLCDSGELVAIK-----KVLQDKRFKN------RELQIMRKLDHCNIVRLRYFFyssgeKKDEVYLN 129
Cdd:cd14040    13 LLGRGGFSEVYKAFDLYEQRYAAVKihqlnKSWRDEKKENyhkhacREYRIHKELDHPRIVKLYDYF-----SLDTDTFC 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 130 LVLDYVP--ETVYRVARHYSRAKQTLPVIyvklyMYQLFRSLAYIHSFG--ICHRDIKPQNLLLDPDTAV--LKLCDFGS 203
Cdd:cd14040    88 TVLEYCEgnDLDFYLKQHKLMSEKEARSI-----VMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACgeIKITDFGL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 204 AKQL------VRGEPNVSYICSRYYRAPELIF----GATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVL 273
Cdd:cd14040   163 SKIMdddsygVDGMDLTSQGAGTYWYLPPECFvvgkEPPKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENTIL 242
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1231802383 274 GTptreqiremnpnyTEFKFPqikahpwtkvFRPRTPPEAIALCSRLLEYTPTARL 329
Cdd:cd14040   243 KA-------------TEVQFP----------VKPVVSNEAKAFIRRCLAYRKEDRF 275
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
60-250 7.90e-07

Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2a (or ActRIIA) belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. The ACVR2a 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: 271043 [Multi-domain]  Cd Length: 290  Bit Score: 50.04  E-value: 7.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDsgELVAIKKV-LQDKRFKNRELQI--MRKLDHCNIVrlryfFYSSGEKKDEvylNLVLDYVP 136
Cdd:cd14141     1 EIKARGRFGCVWKAQLLN--EYVAVKIFpIQDKLSWQNEYEIysLPGMKHENIL-----QFIGAEKRGT---NLDVDLWL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 137 ETVYRVARHYSRAKQTLPVIYVKLYMY--QLFRSLAYIHSF----------GICHRDIKPQNLLLDPDTAVLkLCDFGSA 204
Cdd:cd14141    71 ITAFHEKGSLTDYLKANVVSWNELCHIaqTMARGLAYLHEDipglkdghkpAIAHRDIKSKNVLLKNNLTAC-IADFGLA 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1231802383 205 KQLVRGEP---NVSYICSRYYRAPELIFGATDYTSS----IDVWSAGCVLAEL 250
Cdd:cd14141   150 LKFEAGKSagdTHGQVGTRRYMAPEVLEGAINFQRDaflrIDMYAMGLVLWEL 202
STKc_CK1_alpha cd14128
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; STKs catalyze ...
62-216 8.42e-07

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. CK1alpha plays a role in cell cycle progression, spindle dynamics, and chromosome segregation. It is also involved in regulating apoptosis mediated by Fas or the retinoid X receptor (RXR), and is a positive regulator of Wnt signaling. CK1alpha phosphorylates the NS5A protein of flaviviruses such as the Hepatitis C virus (HCV) and yellow fever virus (YFV), and influences flaviviral replication. The CK1 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: 271030 [Multi-domain]  Cd Length: 266  Bit Score: 49.81  E-value: 8.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKkvLQDKRFKNRELQIMRKL-----DHCNIVRLRYFfyssGEKKDevYLNLVLDYVP 136
Cdd:cd14128     8 IGSGSFGDIYLGINITNGEEVAVK--LESQKARHPQLLYESKLykilqGGVGIPHIRWY----GQEKD--YNVLVMDLLG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 137 ETVYRVARHYSRaKQTLPViyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLK--LCDFGSAKQL--VRGEP 212
Cdd:cd14128    80 PSLEDLFNFCSR-RFTMKT--VLMLADQMIGRIEYVHNKNFIHRDIKPDNFLMGIGRHCNKlfLIDFGLAKKYrdSRTRQ 156

                  ....
gi 1231802383 213 NVSY 216
Cdd:cd14128   157 HIPY 160
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
62-250 1.03e-06

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: 49.83  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAK----LCDSGELVAIKKVLQD-------KRFKnRELQIMRKLDHCNIVRL------------RYFFYS 118
Cdd:cd05050    13 IGQGAFGRVFQARapglLPYEPFTMVAVKMLKEeasadmqADFQ-REAALMAEFDHPNIVKLlgvcavgkpmclLFEYMA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 119 SGEkkdevyLNLVL-DYVPETVYRVARHYSRAKQTLP-----VIYVKLYM-YQLFRSLAYIHSFGICHRDIKPQNLLLDP 191
Cdd:cd05050    92 YGD------LNEFLrHRSPRAQCSLSHSTSSARKCGLnplplSCTEQLCIaKQVAAGMAYLSERKFVHRDLATRNCLVGE 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1231802383 192 DTAVlKLCDFGSAKQLVRGEpnvsyicsrYYRA------------PELIFGATdYTSSIDVWSAGCVLAEL 250
Cdd:cd05050   166 NMVV-KIADFGLSRNIYSAD---------YYKAsendaipirwmpPESIFYNR-YTTESDVWAYGVVLWEI 225
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
151-254 1.19e-06

Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase (RTK) containing an extracellular region with two leucine-rich motifs, 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. The extracellular region of Ryk shows homology to the N-terminal domain of Wnt inhibitory factor-1 (WIF) and serves as the ligand (Wnt) binding domain of Ryk. Ryk is expressed in many different tissues both during development and in adults, suggesting a widespread function. It acts as a chemorepulsive axon guidance receptor of Wnt glycoproteins and is responsible for the establishment of axon tracts during the development of the central nervous system. In addition, studies in mice reveal that Ryk is essential in skeletal, craniofacial, and cardiac development. Thus, it appears Ryk is involved in signal transduction despite its lack of kinase activity. Ryk may function as an accessory protein that modulates the signals coming from catalytically active partner RTKs such as the Eph receptors. The Ryk 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: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 49.76  E-value: 1.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 151 QTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAKQLVRGEpnvsYIC-----SRYYR-- 223
Cdd:cd05043   111 QALSTQQLVHMALQIACGMSYLHRRGVIHKDIAARNCVID-DELQVKITDNALSRDLFPMD----YHClgdneNRPIKwm 185
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1231802383 224 APELIFGaTDYTSSIDVWSAGCVLAELL-LGQ 254
Cdd:cd05043   186 SLESLVN-KEYSSASDVWSFGVLLWELMtLGQ 216
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
60-251 1.38e-06

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: 49.58  E-value: 1.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLcdSGELVAIKKV-LQDKRFKNRELQI--MRKLDHCNIVRlryfFYSSgEKKDEVYLN---LVLD 133
Cdd:cd14056     1 KTIGKGRYGEVWLGKY--RGEKVAVKIFsSRDEDSWFRETEIyqTVMLRHENILG----FIAA-DIKSTGSWTqlwLITE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 134 YVPE-TVYrvarHYSRAKQTLPVIYVKLyMYQLFRSLAYIHS--FG------ICHRDIKPQNLLLDPDtAVLKLCDFGSA 204
Cdd:cd14056    74 YHEHgSLY----DYLQRNTLDTEEALRL-AYSAASGLAHLHTeiVGtqgkpaIAHRDLKSKNILVKRD-GTCCIADLGLA 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1231802383 205 --KQLVRGE--PNVSYIC-SRYYRAPELI---FGATDYTSSI--DVWSAGCVLAELL 251
Cdd:cd14056   148 vrYDSDTNTidIPPNPRVgTKRYMAPEVLddsINPKSFESFKmaDIYSFGLVLWEIA 204
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
97-286 1.43e-06

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: 49.42  E-value: 1.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  97 ELQIMRKLDHCNIVRLRYFFYSSGEkkdevyLNLVLDYVPE----TVYRvarhysraKQTLPVIYVKLYMYQLFRSLAYI 172
Cdd:cd14027    41 EGKMMNRLRHSRVVKLLGVILEEGK------YSLVMEYMEKgnlmHVLK--------KVSVPLSVKGRIILEIIEGMAYL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 173 HSFGICHRDIKPQNLLLDPDTAVlKLCDFGSA---------KQLVRGEPNVSYICSR-----YYRAPE-LIFGATDYTSS 237
Cdd:cd14027   107 HGKGVIHKDLKPENILVDNDFHI-KIADLGLAsfkmwskltKEEHNEQREVDGTAKKnagtlYYMAPEhLNDVNAKPTEK 185
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1231802383 238 IDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNP 286
Cdd:cd14027   186 SDVYSFAIVLWAIFANKEPYENAINEDQIIMCIKSGNRPDVDDITEYCP 234
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
51-251 1.57e-06

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: 49.09  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  51 PQEVSYTdtKVIGNGSFGVVYQAKLcDSGELVAIKKVLQDKRFKN---RELQIMRKLDHCNIVRLryffYSSGEKKDEVY 127
Cdd:cd05114     3 PSELTFM--KELGSGLFGVVRLGKW-RAQYKVAIKAIREGAMSEEdfiEEAKVMMKLTHPKLVQL----YGVCTQQKPIY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 128 LnlvldyVPETVYR-VARHYSRAKQTLPVIYVKLYMYQ-LFRSLAYIHSFGICHRDIKPQNLLLDpDTAVLKLCDFGSAK 205
Cdd:cd05114    76 I------VTEFMENgCLLNYLRQRRGKLSRDMLLSMCQdVCEGMEYLERNNFIHRDLAARNCLVN-DTGVVKVSDFGMTR 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1231802383 206 QLVRGEpNVSYICSRY---YRAPElIFGATDYTSSIDVWSAGCVLAELL 251
Cdd:cd05114   149 YVLDDQ-YTSSSGAKFpvkWSPPE-VFNYSKFSSKSDVWSFGVLMWEVF 195
PLN03224 PLN03224
probable serine/threonine protein kinase; Provisional
141-228 1.82e-06

probable serine/threonine protein kinase; Provisional


Pssm-ID: 178763 [Multi-domain]  Cd Length: 507  Bit Score: 49.68  E-value: 1.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 141 RVARHYSRAKQTLPVIyvKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDFGSAKQLVRG---EPNVSYI 217
Cdd:PLN03224  296 KIPDNMPQDKRDINVI--KGVMRQVLTGLRKLHRIGIVHRDIKPENLLVTVDGQV-KIIDFGAAVDMCTGinfNPLYGML 372
                          90
                  ....*....|.
gi 1231802383 218 CSRYYRAPELI 228
Cdd:PLN03224  373 DPRYSPPEELV 383
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
52-255 1.82e-06

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: 49.29  E-value: 1.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  52 QEVSYTDTKVIGNGSFGVVYQAKLCDSGELVAIK---KVLQDK-------RFKNRELqIMRKLDHCNIVRLRYFFYSSGe 121
Cdd:cd05110     5 KETELKRVKVLGSGAFGTVYKGIWVPEGETVKIPvaiKILNETtgpkanvEFMDEAL-IMASMDHPHLVRLLGVCLSPT- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 122 kkdevyLNLVLDYVPETVyrVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVlKLCDF 201
Cdd:cd05110    83 ------IQLVTQLMPHGC--LLDYVHEHKDNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHV-KITDF 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1231802383 202 GSAKQLVRGEPNVSYICSRY---YRAPELIFgATDYTSSIDVWSAGCVLAELLL--GQP 255
Cdd:cd05110   154 GLARLLEGDEKEYNADGGKMpikWMALECIH-YRKFTHQSDVWSYGVTIWELMTfgGKP 211
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
52-251 2.17e-06

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: 48.84  E-value: 2.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  52 QEVSYTDtkVIGNGSFGVVYQAKLCDSG-ELVAIKKVLQ------DKRFKNRELQIMRKL-DHCNIVRLRyffyssGEKK 123
Cdd:cd05089     2 EDIKFED--VIGEGNFGQVIKAMIKKDGlKMNAAIKMLKefasenDHRDFAGELEVLCKLgHHPNIINLL------GACE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 124 DEVYLNLVLDYVPETVYRVARHYSRAKQTLPVIYVK------LYMYQLFR-------SLAYIHSFGICHRDIKPQNLLLD 190
Cdd:cd05089    74 NRGYLYIAIEYAPYGNLLDFLRKSRVLETDPAFAKEhgtastLTSQQLLQfasdvakGMQYLSEKQFIHRDLAARNVLVG 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1231802383 191 pDTAVLKLCDFGsakqLVRGE-----PNVSYICSRYYRAPELIFGAtdYTSSIDVWSAGCVLAELL 251
Cdd:cd05089   154 -ENLVSKIADFG----LSRGEevyvkKTMGRLPVRWMAIESLNYSV--YTTKSDVWSFGVLLWEIV 212
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
62-195 3.76e-06

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: 48.10  E-value: 3.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  62 IGNGSFGVVYQAKLCDSGELVAIKKVLQ------DKRFKNRELQIMRKL-DHCNIVRlryfFYSSGEKKDEV-----YLN 129
Cdd:cd14138    13 IGSGEFGSVFKCVKRLDGCIYAIKRSKKplagsvDEQNALREVYAHAVLgQHSHVVR----YYSAWAEDDHMliqneYCN 88
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1231802383 130 --LVLDYVPETvYRVARHYSRAKqtlpviyVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLD----PDTAV 195
Cdd:cd14138    89 ggSLADAISEN-YRIMSYFTEPE-------LKDLLLQVARGLKYIHSMSLVHMDIKPSNIFISrtsiPNAAS 152
STKc_TTBK1 cd14130
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze ...
60-254 5.96e-06

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. Genetic variations in TTBK1 are linked to Alzheimer's disease (AD). Hyperphosphorylated tau is a major component of paired helical filaments that accumulate in the brain of AD patients. Studies in transgenic mice show that TTBK1 is involved in the phosphorylation-dependent pathogenic aggregation of tau. The TTBK1 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: 271032 [Multi-domain]  Cd Length: 262  Bit Score: 47.33  E-value: 5.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383  60 KVIGNGSFGVVYQAKLCDSGELVAIK--KVLQDKRFKNRELQIMRKLDHCNIVrLRYFfyssGEKKDEVYLNLVLDYVPE 137
Cdd:cd14130     6 KKIGGGGFGEIYEAMDLLTRENVALKveSAQQPKQVLKMEVAVLKKLQGKDHV-CRFI----GCGRNEKFNYVVMQLQGR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231802383 138 TVYRVARHYSRAKQTLPVIyVKLYMyQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLC---DFGSAKQLVRGEPNV 214
Cdd:cd14130    81 NLADLRRSQPRGTFTLSTT-LRLGK-QILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRKCymlDFGLARQYTNTTGEV 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1231802383 215 syicsryyRAPELI--FGATDYTSSI------------DVWSAGCVLAELLLGQ 254
Cdd:cd14130   159 --------RPPRNVagFRGTVRYASVnahknremgrhdDLWSLFYMLVEFAVGQ 204
 
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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