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Conserved domains on  [gi|341940659|sp|O09127|]
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RecName: Full=Ephrin type-A receptor 8; AltName: Full=EPH- and ELK-related kinase; AltName: Full=Tyrosine-protein kinase receptor EEK; Flags: Precursor

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
629-895 0e+00

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd05066:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 267  Bit Score: 555.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  629 IEASRIHIEKIIGSGESGEVCYGRLQVPGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLA 708
Cdd:cd05066     1 IDASCIKIEKVIGAGEFGEVCSGRLKLPGKREIPVAIKTLKAGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTRSKPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  709 MIVTEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDP 788
Cdd:cd05066    81 MIVTEYMENGSLDAFLRKHDGQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  789 EAAYTTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALHQ 868
Cdd:cd05066   161 EAAYTTRGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWEMSNQDVIKAIEEGYRLPAPMDCPAALHQ 240
                         250       260
                  ....*....|....*....|....*..
gi 341940659  869 LMLDCWHKDRAQRPRFAHVVSVLDALV 895
Cdd:cd05066   241 LMLDCWQKDRNERPKFEQIVSILDKLI 267
EphR_LBD_A8 cd10486
Ligand Binding Domain of Ephrin type-A Receptor 8; Ephrin receptors (EphRs) comprise the ...
30-202 2.79e-132

Ligand Binding Domain of Ephrin type-A Receptor 8; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (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. EphA8 has been implicated in various cancers. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine 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).


:

Pssm-ID: 198454  Cd Length: 173  Bit Score: 395.94  E-value: 2.79e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659   30 EVNLLDTSTIHGDWGWLTYPAHGWDSINEVDESFRPIHTYQVCNVMSPNQNNWLRTNWVPRDGARRVYAEIKFTLRDCNS 109
Cdd:cd10486     1 EVNLLDTSTISGDWGWLTYPSHGWDSINEMDEYFSPIHTYQVCNVMSPNQNNWLRTNWVQRDGARRVYAEIKFTLRDCNS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  110 IPGVLGTCKETFNLHYLESDRDLGASTQESQFLKIDTIAADESFTGADLGVRRLKLNTEVRGVGPLSKRGFYLAFQDIGA 189
Cdd:cd10486    81 MPGVLGTCKETFNLYYYESDRDLGTSTWESQFLKIDTIAADESFTNVDLGVRRLKLNTEVRGVGPLSKRGFYLAFQDIGA 160
                         170
                  ....*....|...
gi 341940659  190 CLAILSLRIYYKK 202
Cdd:cd10486   161 CIAIVSVRVYYKK 173
SAM_EPH-A8 cd09550
SAM domain of EPH-A8 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
932-994 1.47e-36

SAM domain of EPH-A8 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A8 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A8 receptors and appears to mediate cell-cell initiated signal transduction. EPH-A8 receptors are involved in ligand dependent (ephirin A2, A3, A5) regulation of cell adhesion and migration, and in ligand independent regulation of neurite outgrowth in neuronal cells. They perform signaling in kinase dependent and kinase independent manner. EPH-A8 receptors are known to interact with a number of different proteins including PI 3-kinase and AIDA1-like subfamily SAM repeat domain containing proteins. However other domains (not SAM) of EPH-A8 receptors are involved in these interactions.


:

Pssm-ID: 188949  Cd Length: 65  Bit Score: 131.91  E-value: 1.47e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341940659  932 LTVGDWLDSIRMGRYRDHFAAGGYSSLGMVLRMNAQDVRALGITLMGHQKKILGSIQTMRAQL 994
Cdd:cd09550     3 LSVDDWLDSIKMGRYKDHFAAGGYSSLGMVMRMNIEDIRRLGITLMGHQKKILTSIQVMRAQL 65
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
439-530 4.72e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 82.93  E-value: 4.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  439 PSQVVVIRQERAGQTSVSLLWQEPEQPNGIILEYEIKYYEKD-KEMQSYSTLKAVTTRATVSGLKPGTRYVFQVRARTSA 517
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGsGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80
                          90
                  ....*....|...
gi 341940659  518 GCGRFSQAMEVET 530
Cdd:cd00063    81 GESPPSESVTVTT 93
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
325-518 3.01e-15

Fibronectin type 3 domain [General function prediction only];


The actual alignment was detected with superfamily member COG3401:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 80.05  E-value: 3.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  325 TRPPSAPVNL-ISSVNGTSVTLEWAPPLDPGGRSditYNaVCRrcpwalshceACGSGTRFVpQQTSLAQASLLVANLLA 403
Cdd:COG3401   230 TTPPSAPTGLtATADTPGSVTLSWDPVTESDATG---YR-VYR----------SNSGDGPFT-KVATVTTTSYTDTGLTN 294
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  404 HMNYSFWIEAVNGVSNLSPeprSAAVVNITTNQAAPSQVVVIRQERAGQTSVSLLWQEPEQPNgiILEYEIkyYEKDKEM 483
Cdd:COG3401   295 GTTYYYRVTAVDAAGNESA---PSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSDAD--VTGYNV--YRSTSGG 367
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 341940659  484 QSYSTLKAV--TTRATVSGLKPGTRYVFQVRARTSAG 518
Cdd:COG3401   368 GTYTKIAETvtTTSYTDTGLTPGTTYYYKVTAVDAAG 404
EphA2_TM pfam14575
Ephrin type-A receptor 2 transmembrane domain; Epha2_TM represents the left-handed dimer ...
561-631 3.35e-11

Ephrin type-A receptor 2 transmembrane domain; Epha2_TM represents the left-handed dimer transmembrane domain of of EphA2 receptor. This domain oligomerises and is important for the active signalling process.


:

Pssm-ID: 464211  Cd Length: 72  Bit Score: 59.92  E-value: 3.35e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 341940659   561 ICKKRHCGYSKAFQDSDEEKMHYqngqapppvflplnhppgKFPETQFSAEPHTYEEPGRAGRSFTREIEA 631
Cdd:pfam14575   20 IRRRRCCGRKKSQDDDEEEFHQY------------------KPPGRKTYIDPHTYEDPNQAVLEFAKEIDA 72
 
Name Accession Description Interval E-value
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
629-895 0e+00

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: 555.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  629 IEASRIHIEKIIGSGESGEVCYGRLQVPGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLA 708
Cdd:cd05066     1 IDASCIKIEKVIGAGEFGEVCSGRLKLPGKREIPVAIKTLKAGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTRSKPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  709 MIVTEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDP 788
Cdd:cd05066    81 MIVTEYMENGSLDAFLRKHDGQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  789 EAAYTTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALHQ 868
Cdd:cd05066   161 EAAYTTRGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWEMSNQDVIKAIEEGYRLPAPMDCPAALHQ 240
                         250       260
                  ....*....|....*....|....*..
gi 341940659  869 LMLDCWHKDRAQRPRFAHVVSVLDALV 895
Cdd:cd05066   241 LMLDCWQKDRNERPKFEQIVSILDKLI 267
EphR_LBD_A8 cd10486
Ligand Binding Domain of Ephrin type-A Receptor 8; Ephrin receptors (EphRs) comprise the ...
30-202 2.79e-132

Ligand Binding Domain of Ephrin type-A Receptor 8; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (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. EphA8 has been implicated in various cancers. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine 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).


Pssm-ID: 198454  Cd Length: 173  Bit Score: 395.94  E-value: 2.79e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659   30 EVNLLDTSTIHGDWGWLTYPAHGWDSINEVDESFRPIHTYQVCNVMSPNQNNWLRTNWVPRDGARRVYAEIKFTLRDCNS 109
Cdd:cd10486     1 EVNLLDTSTISGDWGWLTYPSHGWDSINEMDEYFSPIHTYQVCNVMSPNQNNWLRTNWVQRDGARRVYAEIKFTLRDCNS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  110 IPGVLGTCKETFNLHYLESDRDLGASTQESQFLKIDTIAADESFTGADLGVRRLKLNTEVRGVGPLSKRGFYLAFQDIGA 189
Cdd:cd10486    81 MPGVLGTCKETFNLYYYESDRDLGTSTWESQFLKIDTIAADESFTNVDLGVRRLKLNTEVRGVGPLSKRGFYLAFQDIGA 160
                         170
                  ....*....|...
gi 341940659  190 CLAILSLRIYYKK 202
Cdd:cd10486   161 CIAIVSVRVYYKK 173
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
634-891 9.02e-132

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: 398.02  E-value: 9.02e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659   634 IHIEKIIGSGESGEVCYGRL-QVPGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVT 712
Cdd:pfam07714    1 LTLGEKLGEGAFGEVYKGTLkGEGENTKIKVAVKTLKEGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659   713 EYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEaAY 792
Cdd:pfam07714   81 EYMPGGDLLDFLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDIYDDDY-YR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659   793 TTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALHQLMLD 872
Cdd:pfam07714  160 KRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEFLEDGYRLPQPENCPDELYDLMKQ 239
                          250
                   ....*....|....*....
gi 341940659   873 CWHKDRAQRPRFAHVVSVL 891
Cdd:pfam07714  240 CWAYDPEDRPTFSELVEDL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
634-891 6.93e-123

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 374.56  E-value: 6.93e-123
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659    634 IHIEKIIGSGESGEVCYGRL-QVPGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVT 712
Cdd:smart00219    1 LTLGKKLGEGAFGEVYKGKLkGKGGKKKVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIVM 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659    713 EYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEaaY 792
Cdd:smart00219   81 EYMEGGDLLSYLRKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDY--Y 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659    793 TTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALHQLMLD 872
Cdd:smart00219  159 RKRGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEYLKNGYRLPQPPNCPPELYDLMLQ 238
                           250
                    ....*....|....*....
gi 341940659    873 CWHKDRAQRPRFAHVVSVL 891
Cdd:smart00219  239 CWAEDPEDRPTFSELVEIL 257
EPH_lbd smart00615
Ephrin receptor ligand binding domain;
30-202 5.46e-97

Ephrin receptor ligand binding domain;


Pssm-ID: 128877  Cd Length: 177  Bit Score: 303.44  E-value: 5.46e-97
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659     30 EVNLLDTSTIHGDWGWLTYPAHGWDSINEVDESFRPIHTYQVCNVMSPNQNNWLRTNWVPRDGARRVYAEIKFTLRDCNS 109
Cdd:smart00615    1 EVVLLDTKTETGELGWTTYPPEGWEEVSGMDENGTPIRTYQVCNVQEGNQNNWLRTNFIRRRGAQRIYVELKFTVRDCSS 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659    110 IPGVLGTCKETFNLHYLESDRDLGAST----QESQFLKIDTIAADESFTGADLGVRRLKLNTEVRGVGPLSKRGFYLAFQ 185
Cdd:smart00615   81 LPGVGGSCKETFNLYYYESDTDTATNTlpnwMENPYTKVDTIAADESFTGGDVGKRNVKLNTEVRSLGPLSKKGFYLAFQ 160
                           170
                    ....*....|....*..
gi 341940659    186 DIGACLAILSLRIYYKK 202
Cdd:smart00615  161 DQGACVALVSVRVFYKK 177
Ephrin_lbd pfam01404
Ephrin receptor ligand binding domain; The Eph receptors, which bind to ephrins pfam00812 are ...
31-203 2.58e-88

Ephrin receptor ligand binding domain; The Eph receptors, which bind to ephrins pfam00812 are a large family of receptor tyrosine kinases. This family represents the amino terminal domain which binds the ephrin ligand.


Pssm-ID: 460198  Cd Length: 177  Bit Score: 280.32  E-value: 2.58e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659    31 VNLLDTSTIHGDWGWLTYPA-HGWDSINEVDESFRPIHTYQVCNVMSPNQNNWLRTNWVPRDGARRVYAEIKFTLRDCNS 109
Cdd:pfam01404    1 EVLLDTTSATSDLGWTTYPYdGGWEEVSGLDENGRTIRTYQVCNVEEPNQNNWLRTPFIPRGGASRVYVELKFTVRDCSS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659   110 IPGVLGTCKETFNLHYLESDRDLGAST----QESQFLKIDTIAADESFTGADlGVRRLKLNTEVRGVGPLSKRGFYLAFQ 185
Cdd:pfam01404   81 IPGVSGTCKETFNLYYYESDADAATATppawRENPYKKIDTIAADESFTDTG-KGRVMKLNTETRSIGPLSKRGFYLAFQ 159
                          170
                   ....*....|....*...
gi 341940659   186 DIGACLAILSLRIYYKKC 203
Cdd:pfam01404  160 DQGACIALLSVRVFYKKC 177
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
636-918 1.04e-41

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 160.18  E-value: 1.04e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIIGSGESGEVCYGRLQVPGQrdvPVAIKALKAGYT--ERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTE 713
Cdd:COG0515    11 ILRLLGRGGMGVVYLARDLRLGR---PVALKVLRPELAadPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLVME 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  714 YMENGSLDAFLRTHdGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYT 793
Cdd:COG0515    88 YVEGESLADLLRRR-GPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATLTQTG 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  794 TAGGKIPirWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWNMTNQDVISSVEEGYRLPAP---MGCPRALHQLM 870
Cdd:COG0515   167 TVVGTPG--YMAPEQARGEPVDPRSDVYSLGVTLYELLT-GRPPFDGDSPAELLRAHLREPPPPPSelrPDLPPALDAIV 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 341940659  871 LDCWHKDRAQrpRFAHVVSVLDALVHSPESLRATATVSRCPPPAFARS 918
Cdd:COG0515   244 LRALAKDPEE--RYQSAAELAAALRAVLRSLAAAAAAAAAAAAAAAAA 289
SAM_EPH-A8 cd09550
SAM domain of EPH-A8 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
932-994 1.47e-36

SAM domain of EPH-A8 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A8 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A8 receptors and appears to mediate cell-cell initiated signal transduction. EPH-A8 receptors are involved in ligand dependent (ephirin A2, A3, A5) regulation of cell adhesion and migration, and in ligand independent regulation of neurite outgrowth in neuronal cells. They perform signaling in kinase dependent and kinase independent manner. EPH-A8 receptors are known to interact with a number of different proteins including PI 3-kinase and AIDA1-like subfamily SAM repeat domain containing proteins. However other domains (not SAM) of EPH-A8 receptors are involved in these interactions.


Pssm-ID: 188949  Cd Length: 65  Bit Score: 131.91  E-value: 1.47e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341940659  932 LTVGDWLDSIRMGRYRDHFAAGGYSSLGMVLRMNAQDVRALGITLMGHQKKILGSIQTMRAQL 994
Cdd:cd09550     3 LSVDDWLDSIKMGRYKDHFAAGGYSSLGMVMRMNIEDIRRLGITLMGHQKKILTSIQVMRAQL 65
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
927-991 3.59e-21

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 87.71  E-value: 3.59e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 341940659   927 SGNGDLTVGDWLDSIRMGRYRDHFAAGgYSSLGMVLRMNAQDVRALGITLMGHQKKILGSIQTMR 991
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSFRAG-YIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRLK 64
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
439-530 4.72e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 82.93  E-value: 4.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  439 PSQVVVIRQERAGQTSVSLLWQEPEQPNGIILEYEIKYYEKD-KEMQSYSTLKAVTTRATVSGLKPGTRYVFQVRARTSA 517
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGsGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80
                          90
                  ....*....|...
gi 341940659  518 GCGRFSQAMEVET 530
Cdd:cd00063    81 GESPPSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
438-523 5.86e-19

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 82.46  E-value: 5.86e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659   438 APSQVVVIRQeraGQTSVSLLWQEPEQPNGIILEYEIKYYEKDK-EMQSYSTLKAVTTRATVSGLKPGTRYVFQVRARTS 516
Cdd:pfam00041    2 APSNLTVTDV---TSTSLTVSWTPPPDGNGPITGYEVEYRPKNSgEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78

                   ....*..
gi 341940659   517 AGCGRFS 523
Cdd:pfam00041   79 GGEGPPS 85
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
636-833 1.80e-17

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 85.31  E-value: 1.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIIGSGESGEVCYGRlqVPGQRDvPVAIKALKAGYTerqrqdfLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYM 715
Cdd:PHA03209   70 VIKTLTPGSEGRVFVAT--KPGQPD-PVVLKIGQKGTT-------LIEAMLLQNVNHPSVIRMKDTLVSGAITCMVLPHY 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  716 eNGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDG-RLVCkVSDFGLSRALEDDPeAAYTT 794
Cdd:PHA03209  140 -SSDLYTYLTKRSRPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINDvDQVC-IGDLGAAQFPVVAP-AFLGL 216
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 341940659  795 AGgkiPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAY 833
Cdd:PHA03209  217 AG---TVETNAPEVLARDKYNSKADIWSAGIVLFEMLAY 252
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
933-993 2.00e-16

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 74.64  E-value: 2.00e-16
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 341940659    933 TVGDWLDSIRMGRYRDHFAAGGYSSLGMVLRMNAQDVRALGITLMGHQKKILGSIQTMRAQ 993
Cdd:smart00454    8 SVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLKEQ 68
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
439-520 8.46e-16

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 73.42  E-value: 8.46e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659    439 PSQVVVIRQERAGQTSVSLLWQEPEQPNGI--ILEYEIKYYEKDKEMQSYSTlKAVTTRATVSGLKPGTRYVFQVRARTS 516
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITgyIVGYRVEYREEGSEWKEVNV-TPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                    ....
gi 341940659    517 AGCG 520
Cdd:smart00060   80 AGEG 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
325-518 3.01e-15

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 80.05  E-value: 3.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  325 TRPPSAPVNL-ISSVNGTSVTLEWAPPLDPGGRSditYNaVCRrcpwalshceACGSGTRFVpQQTSLAQASLLVANLLA 403
Cdd:COG3401   230 TTPPSAPTGLtATADTPGSVTLSWDPVTESDATG---YR-VYR----------SNSGDGPFT-KVATVTTTSYTDTGLTN 294
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  404 HMNYSFWIEAVNGVSNLSPeprSAAVVNITTNQAAPSQVVVIRQERAGQTSVSLLWQEPEQPNgiILEYEIkyYEKDKEM 483
Cdd:COG3401   295 GTTYYYRVTAVDAAGNESA---PSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSDAD--VTGYNV--YRSTSGG 367
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 341940659  484 QSYSTLKAV--TTRATVSGLKPGTRYVFQVRARTSAG 518
Cdd:COG3401   368 GTYTKIAETvtTTSYTDTGLTPGTTYYYKVTAVDAAG 404
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
633-838 4.88e-12

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 69.82  E-value: 4.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  633 RIHIEKIIGSGESGEVCYG---RLQvpgqRDVpvAIKALKAGYTE----RQRqdFLSEAAIMGQFDHPNIIRLEGVVTRG 705
Cdd:NF033483    8 RYEIGERIGRGGMAEVYLAkdtRLD----RDV--AVKVLRPDLARdpefVAR--FRREAQSAASLSHPNIVSVYDVGEDG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  706 RLAMIVTEYMENGSLDAFLRTHdGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLV--DGRLvcKVSDFGLSRA 783
Cdd:NF033483   80 GIPYIVMEYVDGRTLKDYIREH-GPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILItkDGRV--KVTDFGIARA 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 341940659  784 LEddpEAAYT-------TA---------GGKIPIRwtapeaiafrtfssaSDVWSFGVVMWEVLAyGERPY 838
Cdd:NF033483  157 LS---STTMTqtnsvlgTVhylspeqarGGTVDAR---------------SDIYSLGIVLYEMLT-GRPPF 208
EphA2_TM pfam14575
Ephrin type-A receptor 2 transmembrane domain; Epha2_TM represents the left-handed dimer ...
561-631 3.35e-11

Ephrin type-A receptor 2 transmembrane domain; Epha2_TM represents the left-handed dimer transmembrane domain of of EphA2 receptor. This domain oligomerises and is important for the active signalling process.


Pssm-ID: 464211  Cd Length: 72  Bit Score: 59.92  E-value: 3.35e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 341940659   561 ICKKRHCGYSKAFQDSDEEKMHYqngqapppvflplnhppgKFPETQFSAEPHTYEEPGRAGRSFTREIEA 631
Cdd:pfam14575   20 IRRRRCCGRKKSQDDDEEEFHQY------------------KPPGRKTYIDPHTYEDPNQAVLEFAKEIDA 72
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
407-535 1.10e-10

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 65.41  E-value: 1.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  407 YSFWIEAVNGvSNLSPEPRSAAVVNITTNQAAPSQVVVIRQeraGQTSVSLLWQEPEQPNgiILEYEIkyYEKDKEMQSY 486
Cdd:COG3401   205 YYYRVAATDT-GGESAPSNEVSVTTPTTPPSAPTGLTATAD---TPGSVTLSWDPVTESD--ATGYRV--YRSNSGDGPF 276
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 341940659  487 STLKAVT-TRATVSGLKPGTRYVFQVRARTSAGC-GRFSQAMEVETGKPRP 535
Cdd:COG3401   277 TKVATVTtTSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSNVVSVTTDLTPP 327
fn3 pfam00041
Fibronectin type III domain;
329-422 2.53e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 54.73  E-value: 2.53e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659   329 SAPVNL-ISSVNGTSVTLEWAPPLDPGGrsDITYNAVcrrcpwalsHCEACGSGTRFVPQQTSLAQASLLVANLLAHMNY 407
Cdd:pfam00041    1 SAPSNLtVTDVTSTSLTVSWTPPPDGNG--PITGYEV---------EYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEY 69
                           90
                   ....*....|....*
gi 341940659   408 SFWIEAVNGVSNLSP 422
Cdd:pfam00041   70 EVRVQAVNGGGEGPP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
328-417 7.30e-09

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 53.39  E-value: 7.30e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659    328 PSAPVNL-ISSVNGTSVTLEWAPPLDPGGRSDITYNAVCRRcpwalshceacGSGTRFVPQQTSLAQASLLVANLLAHMN 406
Cdd:smart00060    1 PSPPSNLrVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYR-----------EEGSEWKEVNVTPSSTSYTLTGLKPGTE 69
                            90
                    ....*....|.
gi 341940659    407 YSFWIEAVNGV 417
Cdd:smart00060   70 YEFRVRAVNGA 80
 
Name Accession Description Interval E-value
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
629-895 0e+00

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: 555.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  629 IEASRIHIEKIIGSGESGEVCYGRLQVPGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLA 708
Cdd:cd05066     1 IDASCIKIEKVIGAGEFGEVCSGRLKLPGKREIPVAIKTLKAGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTRSKPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  709 MIVTEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDP 788
Cdd:cd05066    81 MIVTEYMENGSLDAFLRKHDGQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  789 EAAYTTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALHQ 868
Cdd:cd05066   161 EAAYTTRGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWEMSNQDVIKAIEEGYRLPAPMDCPAALHQ 240
                         250       260
                  ....*....|....*....|....*..
gi 341940659  869 LMLDCWHKDRAQRPRFAHVVSVLDALV 895
Cdd:cd05066   241 LMLDCWQKDRNERPKFEQIVSILDKLI 267
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
629-895 6.58e-175

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: 509.99  E-value: 6.58e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  629 IEASRIHIEKIIGSGESGEVCYGRLQVPGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLA 708
Cdd:cd05033     1 IDASYVTIEKVIGGGEFGEVCSGSLKLPGKKEIDVAIKTLKSGYSDKQRLDFLTEASIMGQFDHPNVIRLEGVVTKSRPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  709 MIVTEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEdDP 788
Cdd:cd05033    81 MIVTEYMENGSLDKFLRENDGKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLSRRLE-DS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  789 EAAYTTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALHQ 868
Cdd:cd05033   160 EATYTTKGGKIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSYGERPYWDMSNQDVIKAVEDGYRLPPPMDCPSALYQ 239
                         250       260
                  ....*....|....*....|....*..
gi 341940659  869 LMLDCWHKDRAQRPRFAHVVSVLDALV 895
Cdd:cd05033   240 LMLDCWQKDRNERPTFSQIVSTLDKMI 266
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
629-895 6.41e-163

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: 478.98  E-value: 6.41e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  629 IEASRIHIEKIIGSGESGEVCYGRLQVPGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLA 708
Cdd:cd05065     1 IDVSCVKIEEVIGAGEFGEVCRGRLKLPGKREIFVAIKTLKSGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTKSRPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  709 MIVTEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDP 788
Cdd:cd05065    81 MIITEFMENGALDSFLRQNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLEDDT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  789 -EAAYTTA-GGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRAL 866
Cdd:cd05065   161 sDPTYTSSlGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVINAIEQDYRLPPPMDCPTAL 240
                         250       260
                  ....*....|....*....|....*....
gi 341940659  867 HQLMLDCWHKDRAQRPRFAHVVSVLDALV 895
Cdd:cd05065   241 HQLMLDCWQKDRNLRPKFGQIVNTLDKMI 269
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
628-895 7.29e-159

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: 468.68  E-value: 7.29e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  628 EIEASRIHIEKIIGSGESGEVCYGRLQVPGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRL 707
Cdd:cd05063     1 EIHPSHITKQKVIGAGEFGEVFRGILKMPGRKEVAVAIKTLKPGYTEKQRQDFLSEASIMGQFSHHNIIRLEGVVTKFKP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  708 AMIVTEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDD 787
Cdd:cd05063    81 AMIITEYMENGALDKYLRDHDGEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRVLEDD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  788 PEAAYTTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALH 867
Cdd:cd05063   161 PEGTYTTSGGKIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSFGERPYWDMSNHEVMKAINDGFRLPAPMDCPSAVY 240
                         250       260
                  ....*....|....*....|....*...
gi 341940659  868 QLMLDCWHKDRAQRPRFAHVVSVLDALV 895
Cdd:cd05063   241 QLMLQCWQQDRARRPRFVDIVNLLDKLL 268
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
628-895 9.45e-135

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphA10, which contains an inactive tyr kinase domain, may function to attenuate signals of co-clustered active receptors. EphA10 is mainly expressed in the testis. Ephrin/EphR interaction 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. EphRs comprise the largest subfamily of receptor tyr kinases (RTKs). In general, 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). The EphA10 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: 133195 [Multi-domain]  Cd Length: 266  Bit Score: 406.23  E-value: 9.45e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  628 EIEASRIHIEKIIGSGESGEVCYGRLQVPGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRL 707
Cdd:cd05064     1 ELDNKSIKIERILGTGRFGELCRGCLKLPSKRELPVAIHTLRAGCSDKQRRGFLAEALTLGQFDHSNIVRLEGVITRGNT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  708 AMIVTEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGlsRALEDD 787
Cdd:cd05064    81 MMIVTEYMSNGALDSFLRKHEGQLVAGQLMGMLPGLASGMKYLSEMGYVHKGLAAHKVLVNSDLVCKISGFR--RLQEDK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  788 PEAAYTTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALH 867
Cdd:cd05064   159 SEAIYTTMSGKSPVLWAAPEAIQYHHFSSASDVWSFGIVMWEVMSYGERPYWDMSGQDVIKAVEDGFRLPAPRNCPNLLH 238
                         250       260
                  ....*....|....*....|....*...
gi 341940659  868 QLMLDCWHKDRAQRPRFAHVVSVLDALV 895
Cdd:cd05064   239 QLMLDCWQKERGERPRFSQIHSILSKMV 266
EphR_LBD_A8 cd10486
Ligand Binding Domain of Ephrin type-A Receptor 8; Ephrin receptors (EphRs) comprise the ...
30-202 2.79e-132

Ligand Binding Domain of Ephrin type-A Receptor 8; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (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. EphA8 has been implicated in various cancers. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine 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).


Pssm-ID: 198454  Cd Length: 173  Bit Score: 395.94  E-value: 2.79e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659   30 EVNLLDTSTIHGDWGWLTYPAHGWDSINEVDESFRPIHTYQVCNVMSPNQNNWLRTNWVPRDGARRVYAEIKFTLRDCNS 109
Cdd:cd10486     1 EVNLLDTSTISGDWGWLTYPSHGWDSINEMDEYFSPIHTYQVCNVMSPNQNNWLRTNWVQRDGARRVYAEIKFTLRDCNS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  110 IPGVLGTCKETFNLHYLESDRDLGASTQESQFLKIDTIAADESFTGADLGVRRLKLNTEVRGVGPLSKRGFYLAFQDIGA 189
Cdd:cd10486    81 MPGVLGTCKETFNLYYYESDRDLGTSTWESQFLKIDTIAADESFTNVDLGVRRLKLNTEVRGVGPLSKRGFYLAFQDIGA 160
                         170
                  ....*....|...
gi 341940659  190 CLAILSLRIYYKK 202
Cdd:cd10486   161 CIAIVSVRVYYKK 173
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
634-891 9.02e-132

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: 398.02  E-value: 9.02e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659   634 IHIEKIIGSGESGEVCYGRL-QVPGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVT 712
Cdd:pfam07714    1 LTLGEKLGEGAFGEVYKGTLkGEGENTKIKVAVKTLKEGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659   713 EYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEaAY 792
Cdd:pfam07714   81 EYMPGGDLLDFLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDIYDDDY-YR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659   793 TTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALHQLMLD 872
Cdd:pfam07714  160 KRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEFLEDGYRLPQPENCPDELYDLMKQ 239
                          250
                   ....*....|....*....
gi 341940659   873 CWHKDRAQRPRFAHVVSVL 891
Cdd:pfam07714  240 CWAYDPEDRPTFSELVEDL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
634-891 6.93e-123

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 374.56  E-value: 6.93e-123
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659    634 IHIEKIIGSGESGEVCYGRL-QVPGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVT 712
Cdd:smart00219    1 LTLGKKLGEGAFGEVYKGKLkGKGGKKKVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIVM 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659    713 EYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEaaY 792
Cdd:smart00219   81 EYMEGGDLLSYLRKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDY--Y 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659    793 TTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALHQLMLD 872
Cdd:smart00219  159 RKRGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEYLKNGYRLPQPPNCPPELYDLMLQ 238
                           250
                    ....*....|....*....
gi 341940659    873 CWHKDRAQRPRFAHVVSVL 891
Cdd:smart00219  239 CWAEDPEDRPTFSELVEIL 257
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
634-891 8.77e-123

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: 374.58  E-value: 8.77e-123
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659    634 IHIEKIIGSGESGEVCYGRL-QVPGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVT 712
Cdd:smart00221    1 LTLGKKLGEGAFGEVYKGTLkGKGDGKEVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIVM 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659    713 EYMENGSLDAFLRTHDGQF-TIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEaa 791
Cdd:smart00221   81 EYMPGGDLLDYLRKNRPKElSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDY-- 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659    792 YTTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALHQLML 871
Cdd:smart00221  159 YKVKGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEEPYPGMSNAEVLEYLKKGYRLPKPPNCPPELYKLML 238
                           250       260
                    ....*....|....*....|
gi 341940659    872 DCWHKDRAQRPRFAHVVSVL 891
Cdd:smart00221  239 QCWAEDPEDRPTFSELVEIL 258
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
638-892 6.57e-114

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: 351.46  E-value: 6.57e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVPGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMEN 717
Cdd:cd00192     1 KKLGEGAFGEVYKGKLKGGDGKTVDVAVKTLKEDASESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYMEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  718 GSLDAFLRTH--------DGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDpE 789
Cdd:cd00192    81 GDLLDFLRKSrpvfpspePSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRDIYDD-D 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  790 AAYTTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALHQL 869
Cdd:cd00192   160 YYRKKTGGKLPIRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTLGATPYPGLSNEEVLEYLRKGYRLPKPENCPDELYEL 239
                         250       260
                  ....*....|....*....|...
gi 341940659  870 MLDCWHKDRAQRPRFAHVVSVLD 892
Cdd:cd00192   240 MLSCWQLDPEDRPTFSELVERLE 262
EphR_LBD_A cd10473
Ligand Binding Domain of Ephrin type-A Receptors; Ephrin receptors (EphRs) comprise the ...
30-202 1.88e-112

Ligand Binding Domain of Ephrin type-A Receptors; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (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 a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine 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.


Pssm-ID: 198441  Cd Length: 173  Bit Score: 344.04  E-value: 1.88e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659   30 EVNLLDTSTIHGDWGWLTYPAHGWDSINEVDESFRPIHTYQVCNVMSPNQNNWLRTNWVPRDGARRVYAEIKFTLRDCNS 109
Cdd:cd10473     1 EVVLLDSKTAQGELGWITYPPNGWEEISEMDEDYTPIRTYQVCNVMEPNQNNWLRTNWIYRGEAQRIYIELKFTLRDCNS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  110 IPGVLGTCKETFNLHYLESDRDLGASTQESQFLKIDTIAADESFTGADLGVRRLKLNTEVRGVGPLSKRGFYLAFQDIGA 189
Cdd:cd10473    81 FPGVLGTCKETFNLYYMESDLDLGRNIRENQFTKIDTIAADESFTQGDLGDRIMKLNTEVREVGPLTKKGFYLAFQDVGA 160
                         170
                  ....*....|...
gi 341940659  190 CLAILSLRIYYKK 202
Cdd:cd10473   161 CVALVSVRVYYKK 173
EPH_lbd smart00615
Ephrin receptor ligand binding domain;
30-202 5.46e-97

Ephrin receptor ligand binding domain;


Pssm-ID: 128877  Cd Length: 177  Bit Score: 303.44  E-value: 5.46e-97
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659     30 EVNLLDTSTIHGDWGWLTYPAHGWDSINEVDESFRPIHTYQVCNVMSPNQNNWLRTNWVPRDGARRVYAEIKFTLRDCNS 109
Cdd:smart00615    1 EVVLLDTKTETGELGWTTYPPEGWEEVSGMDENGTPIRTYQVCNVQEGNQNNWLRTNFIRRRGAQRIYVELKFTVRDCSS 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659    110 IPGVLGTCKETFNLHYLESDRDLGAST----QESQFLKIDTIAADESFTGADLGVRRLKLNTEVRGVGPLSKRGFYLAFQ 185
Cdd:smart00615   81 LPGVGGSCKETFNLYYYESDTDTATNTlpnwMENPYTKVDTIAADESFTGGDVGKRNVKLNTEVRSLGPLSKKGFYLAFQ 160
                           170
                    ....*....|....*..
gi 341940659    186 DIGACLAILSLRIYYKK 202
Cdd:smart00615  161 DQGACVALVSVRVFYKK 177
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
638-892 3.33e-94

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: 298.81  E-value: 3.33e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQvpgqRDVPVAIKALKAGYTERQrqDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMEN 717
Cdd:cd05034     1 KKLGAGQFGEVWMGVWN----GTTKVAVKTLKPGTMSPE--AFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELMSK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  718 GSLDAFLRTHDGQ-FTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDpeaAYTT-A 795
Cdd:cd05034    75 GSLLDYLRTGEGRaLRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLARLIEDD---EYTArE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  796 GGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALHQLMLDCWH 875
Cdd:cd05034   152 GAKFPIKWTAPEAALYGRFTIKSDVWSFGILLYEIVTYGRVPYPGMTNREVLEQVERGYRMPKPPGCPDELYDIMLQCWK 231
                         250
                  ....*....|....*..
gi 341940659  876 KDRAQRPRFAHVVSVLD 892
Cdd:cd05034   232 KEPEERPTFEYLQSFLE 248
EphR_LBD_A6 cd10484
Ligand Binding Domain of Ephrin type-A Receptor 6; Ephrin receptors (EphRs) comprise the ...
30-202 6.13e-93

Ligand Binding Domain of Ephrin type-A Receptor 6; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (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. EphA6, like other Eph receptors and their ephrin ligands, seems to play a role in neural development, underlying learning and memory. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine 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).


Pssm-ID: 198452  Cd Length: 173  Bit Score: 292.31  E-value: 6.13e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659   30 EVNLLDTSTIHGDWGWLTYPAHGWDSINEVDESFRPIHTYQVCNVMSPNQNNWLRTNWVPRDGARRVYAEIKFTLRDCNS 109
Cdd:cd10484     1 QVVLLDTTMVLGELNWKTYPCNGWDAITEMDEYNRPIHTYQVCNVMEPNQNNWLRTNWISRDAAQKIYVEMKFTLRDCNS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  110 IPGVLGTCKETFNLHYLESDRDLGASTQESQFLKIDTIAADESFTGADLGVRRLKLNTEVRGVGPLSKRGFYLAFQDIGA 189
Cdd:cd10484    81 IPWVVGTCKETFNLHYMESDEAHAVKFKPNQYSKIDTIAADESFTQMDLGDRILKLNTEVREVGPITRKGFYLAFQDIGA 160
                         170
                  ....*....|...
gi 341940659  190 CLAILSLRIYYKK 202
Cdd:cd10484   161 CIALVSVRVYYKK 173
EphR_LBD_A3 cd10481
Ligand Binding Domain of Ephrin type-A Receptor 3; Ephrin receptors (EphRs) comprise the ...
30-202 9.63e-93

Ligand Binding Domain of Ephrin type-A Receptor 3; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (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. EphA3 has been implicated in leukemia, lung and other cancers. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine 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.


Pssm-ID: 198449  Cd Length: 173  Bit Score: 291.96  E-value: 9.63e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659   30 EVNLLDTSTIHGDWGWLTYPAHGWDSINEVDESFRPIHTYQVCNVMSPNQNNWLRTNWVPRDGARRVYAEIKFTLRDCNS 109
Cdd:cd10481     1 EVNLLDSKAIQGELGWISYPSHGWEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWIPRNSAQKIYVELKFTLRDCNS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  110 IPGVLGTCKETFNLHYLESDRDLGASTQESQFLKIDTIAADESFTGADLGVRRLKLNTEVRGVGPLSKRGFYLAFQDIGA 189
Cdd:cd10481    81 IPLVLGTCKETFNLYYMESDEDQGVKFREHQFTKIDTIAADESFTQMDLGDRILKLNTEVREVGPVSKKGFYLAFQDVGA 160
                         170
                  ....*....|...
gi 341940659  190 CLAILSLRIYYKK 202
Cdd:cd10481   161 CVALVSVRVYFKK 173
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
628-884 1.23e-88

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: 284.68  E-value: 1.23e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  628 EIEASRIHIEKIIGSGESGEVCYGRLQvpgqRDVPVAIKALKAGytERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRL 707
Cdd:cd05068     4 EIDRKSLKLLRKLGSGQFGEVWEGLWN----NTTPVAVKTLKPG--TMDPEDFLREAQIMKKLRHPKLIQLYAVCTLEEP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  708 AMIVTEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRAL--E 785
Cdd:cd05068    78 IYIITELMKHGSLLEYLQGKGRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGLARVIkvE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  786 DDPEAaytTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRA 865
Cdd:cd05068   158 DEYEA---REGAKFPIKWTAPEAANYNRFSIKSDVWSFGILLTEIVTYGRIPYPGMTNAEVLQQVERGYRMPCPPNCPPQ 234
                         250
                  ....*....|....*....
gi 341940659  866 LHQLMLDCWHKDRAQRPRF 884
Cdd:cd05068   235 LYDIMLECWKADPMERPTF 253
Ephrin_lbd pfam01404
Ephrin receptor ligand binding domain; The Eph receptors, which bind to ephrins pfam00812 are ...
31-203 2.58e-88

Ephrin receptor ligand binding domain; The Eph receptors, which bind to ephrins pfam00812 are a large family of receptor tyrosine kinases. This family represents the amino terminal domain which binds the ephrin ligand.


Pssm-ID: 460198  Cd Length: 177  Bit Score: 280.32  E-value: 2.58e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659    31 VNLLDTSTIHGDWGWLTYPA-HGWDSINEVDESFRPIHTYQVCNVMSPNQNNWLRTNWVPRDGARRVYAEIKFTLRDCNS 109
Cdd:pfam01404    1 EVLLDTTSATSDLGWTTYPYdGGWEEVSGLDENGRTIRTYQVCNVEEPNQNNWLRTPFIPRGGASRVYVELKFTVRDCSS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659   110 IPGVLGTCKETFNLHYLESDRDLGAST----QESQFLKIDTIAADESFTGADlGVRRLKLNTEVRGVGPLSKRGFYLAFQ 185
Cdd:pfam01404   81 IPGVSGTCKETFNLYYYESDADAATATppawRENPYKKIDTIAADESFTDTG-KGRVMKLNTETRSIGPLSKRGFYLAFQ 159
                          170
                   ....*....|....*...
gi 341940659   186 DIGACLAILSLRIYYKKC 203
Cdd:pfam01404  160 DQGACIALLSVRVFYKKC 177
EphR_LBD_A10 cd10487
Ligand Binding Domain of Ephrin type-A Receptor 10; Ephrin receptors (EphRs) comprise the ...
30-202 2.73e-88

Ligand Binding Domain of Ephrin type-A Receptor 10; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (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. EphA10, which contains an inactive tyr kinase domain, may function to attenuate signals of co-clustered active receptors. EphA10 is mainly expressed in the testis. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine 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 results in cell-cell repulsion or adhesion.


Pssm-ID: 198455  Cd Length: 173  Bit Score: 279.99  E-value: 2.73e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659   30 EVNLLDTSTIHGDWGWLTYPAHGWDSINEVDESFRPIHTYQVCNVMSPNQNNWLRTNWVPRDGARRVYAEIKFTLRDCNS 109
Cdd:cd10487     1 EVVLLDSKESQAELGWTSLPSNGWEEISGVDEHYKPIRTYQVCNVMEPNQNNWLQTGWISRGRGQRIFIELQFTLRDCNS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  110 IPGVLGTCKETFNLHYLESDRDLGASTQESQFLKIDTIAADESFTGADLGVRRLKLNTEVRGVGPLSKRGFYLAFQDIGA 189
Cdd:cd10487    81 IPGVAGTCKETFNLYYAESDADLGRRLRESRPRKIDTIAADESFTQGDLGERKMKLNTEVREIGHLSRRGFHLAFQDVGA 160
                         170
                  ....*....|...
gi 341940659  190 CLAILSLRIYYKK 202
Cdd:cd10487   161 CVALVSVRVYYKQ 173
EphR_LBD_A5 cd10483
Ligand Binding Domain of Ephrin type-A Receptor 5; Ephrin receptors (EphRs) comprise the ...
30-202 7.12e-88

Ligand Binding Domain of Ephrin type-A Receptor 5; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (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. EphA5 is almost exclusively expressed in the nervous system. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine 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).


Pssm-ID: 198451  Cd Length: 173  Bit Score: 278.84  E-value: 7.12e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659   30 EVNLLDTSTIHGDWGWLTYPAHGWDSINEVDESFRPIHTYQVCNVMSPNQNNWLRTNWVPRDGARRVYAEIKFTLRDCNS 109
Cdd:cd10483     1 EVNLLDSRSVMGDLGWIAYPKNGWEEIGEVDENYAPIHTYQVCKVMEQNQNNWLLTSWISNEGASRIFIELKFTLRDCNS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  110 IPGVLGTCKETFNLHYLESDRDLGASTQESQFLKIDTIAADESFTGADLGVRRLKLNTEVRGVGPLSKRGFYLAFQDIGA 189
Cdd:cd10483    81 LPGGLGTCKETFNVYYFESNDEDGRNIRENQYIKIDTIAADESFTELDLGDRVMKLNTEVRDVGPLTKKGFYLAFQDLGA 160
                         170
                  ....*....|...
gi 341940659  190 CLAILSLRIYYKK 202
Cdd:cd10483   161 CIALVSVRVYYKK 173
EphR_LBD_A7 cd10485
Ligand Binding Domain of Ephrin type-A Receptor 7; Ephrin receptors (EphRs) comprise the ...
30-203 1.12e-84

Ligand Binding Domain of Ephrin type-A Receptor 7; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (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. EphA7 has been implicated in various cancers, including prostate, gastic and colorectal cancers. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine 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).


Pssm-ID: 198453  Cd Length: 177  Bit Score: 270.37  E-value: 1.12e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659   30 EVNLLDTSTIHGDWGWLTYPAHGWDSINEVDESFRPIHTYQVCNVMSPNQNNWLRTNWVPRDGARRVYAEIKFTLRDCNS 109
Cdd:cd10485     3 EVILLDSKAQQTELEWISSPPSGWEEISGLDENYTPIRTYQVCQVMEPNQNNWLRTNWISKGNAQRIFVELKFTLRDCNS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  110 IPGVLGTCKETFNLHYLESDRDLGASTQESQFLKIDTIAADESFTGADLGVRRLKLNTEVRGVGPLSKRGFYLAFQDIGA 189
Cdd:cd10485    83 LPGVLGTCKETFNLYYYETDYDTGRNIRENQYVKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSKKGFYLAFQDVGA 162
                         170
                  ....*....|....
gi 341940659  190 CLAILSLRIYYKKC 203
Cdd:cd10485   163 CIALVSVKVYYKKC 176
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
640-891 1.74e-84

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: 273.07  E-value: 1.74e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVvTRGRLAMIVTEYMENGS 719
Cdd:cd05060     3 LGHGNFGSVRKGVYLMKSGKEVEVAVKTLKQEHEKAGKKEFLREASVMAQLDHPCIVRLIGV-CKGEPLMLVMELAPLGP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  720 LDAFLRTHdGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYTTAGGKI 799
Cdd:cd05060    82 LLKYLKKR-REIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSRALGAGSDYYRATTAGRW 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  800 PIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALHQLMLDCWHKDRA 879
Cdd:cd05060   161 PLKWYAPECINYGKFSSKSDVWSYGVTLWEAFSYGAKPYGEMKGPEVIAMLESGERLPRPEECPQEIYSIMLSCWKYRPE 240
                         250
                  ....*....|..
gi 341940659  880 QRPRFAHVVSVL 891
Cdd:cd05060   241 DRPTFSELESTF 252
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
640-892 8.42e-84

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: 270.85  E-value: 8.42e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGS 719
Cdd:cd05041     3 IGRGNFGDVYRGVLKPDNTE---VAVKTCRETLPPDLKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  720 LDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRAlEDDPEaaYTTAGG-- 797
Cdd:cd05041    80 LLTFLRKKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSRE-EEDGE--YTVSDGlk 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  798 KIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALHQLMLDCWHKD 877
Cdd:cd05041   157 QIPIKWTAPEALNYGRYTSESDVWSFGILLWEIFSLGATPYPGMSNQQTREQIESGYRMPAPELCPEAVYRLMLQCWAYD 236
                         250
                  ....*....|....*
gi 341940659  878 RAQRPRFAHVVSVLD 892
Cdd:cd05041   237 PENRPSFSEIYNELQ 251
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
628-894 2.31e-83

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: 269.99  E-value: 2.31e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  628 EIEASRIHIEKIIGSGESGEVCYGRLQvpGQRdvpVAIKALKAGYTERQRqdFLSEAAIMGQFDHPNIIRLEGVVTRGRL 707
Cdd:cd05039     2 AINKKDLKLGELIGKGEFGDVMLGDYR--GQK---VAVKCLKDDSTAAQA--FLAEASVMTTLRHPNLVQLLGVVLEGNG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  708 AMIVTEYMENGSLDAFLRTHdGQFTIV--QLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRale 785
Cdd:cd05039    75 LYIVTEYMAKGSLVDYLRSR-GRAVITrkDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAK--- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  786 ddpEAAYTTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRA 865
Cdd:cd05039   151 ---EASSNQDGGKLPIKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVVPHVEKGYRMEAPEGCPPE 227
                         250       260
                  ....*....|....*....|....*....
gi 341940659  866 LHQLMLDCWHKDRAQRPRFAHVVSVLDAL 894
Cdd:cd05039   228 VYKVMKNCWELDPAKRPTFKQLREKLEHI 256
EphR_LBD_A4 cd10482
Ligand Binding Domain of Ephrin type-A Receptor 4; Ephrin receptors (EphRs) comprise the ...
30-202 2.71e-82

Ligand Binding Domain of Ephrin type-A Receptor 4; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (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. A loss of EphA4, as well as EphB2, precedes memory decline in a murine model of Alzheimers disease. EphA4 has been shown to have a negative effect on axon regeneration and functional restoration in corticospinal lesions and is downregulated in some cervical cancers. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine 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).


Pssm-ID: 198450  Cd Length: 174  Bit Score: 263.83  E-value: 2.71e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659   30 EVNLLDTSTIHGDWGWLTYPAHG-WDSINEVDESFRPIHTYQVCNVMSPNQNNWLRTNWVPRDGARRVYAEIKFTLRDCN 108
Cdd:cd10482     1 EVTLLDSRSVQGELGWIASPLEGgWEEVSIMDEKNTPIRTYQVCNVMEPSQNNWLRTDWIPREGAQRVYIEIKFTLRDCN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  109 SIPGVLGTCKETFNLHYLESDRDLGASTQESQFLKIDTIAADESFTGADLGVRRLKLNTEVRGVGPLSKRGFYLAFQDIG 188
Cdd:cd10482    81 SLPGVMGTCKETFNLYYYESNNDKERFIRENQFVKIDTIAADESFTQVDIGDRIMKLNTEVRDVGPLSKKGFYLAFQDVG 160
                         170
                  ....*....|....
gi 341940659  189 ACLAILSLRIYYKK 202
Cdd:cd10482   161 ACIALVSVRVFYKK 174
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
629-891 1.10e-80

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: 262.77  E-value: 1.10e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  629 IEASRIHIEKIIGSGESGEVCYGRLQvpGQRDVpvAIKALKAGytERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLA 708
Cdd:cd05059     1 IDPSELTFLKELGSGQFGVVHLGKWR--GKIDV--AIKMIKEG--SMSEDDFIEEAKVMMKLSHPKLVQLYGVCTKQRPI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  709 MIVTEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDp 788
Cdd:cd05059    75 FIVTEYMANGCLLNYLRERRGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARYVLDD- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  789 eaAYTTAGG-KIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALH 867
Cdd:cd05059   154 --EYTSSVGtKFPVKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSEGKMPYERFSNSEVVEHISQGYRLYRPHLAPTEVY 231
                         250       260
                  ....*....|....*....|....
gi 341940659  868 QLMLDCWHKDRAQRPRFAHVVSVL 891
Cdd:cd05059   232 TIMYSCWHEKPEERPTFKILLSQL 255
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
636-893 1.74e-80

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: 262.37  E-value: 1.74e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIIGSGESGEVCYGRLQvpgqRDVPVAIKALKAGYTERQrQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYM 715
Cdd:cd05148    10 LERKLGSGYFGEVWEGLWK----NRVRVAIKILKSDDLLKQ-QDFQKEVQALKRLRHKHLISLFAVCSVGEPVYIITELM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  716 ENGSLDAFLRTHDGQ-FTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDpeaAYTT 794
Cdd:cd05148    85 EKGSLLAFLRSPEGQvLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLARLIKED---VYLS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  795 AGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALHQLMLDCW 874
Cdd:cd05148   162 SDKKIPYKWTAPEAASHGTFSTKSDVWSFGILLYEMFTYGQVPYPGMNNHEVYDQITAGYRMPCPAKCPQEIYKIMLECW 241
                         250
                  ....*....|....*....
gi 341940659  875 HKDRAQRPRFAHVVSVLDA 893
Cdd:cd05148   242 AAEPEDRPSFKALREELDN 260
EphR_LBD_B cd10472
Ligand Binding Domain of Ephrin type-B receptors; Ephrin receptors (EphRs) comprise the ...
33-202 5.12e-77

Ligand Binding Domain of Ephrin type-B receptors; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphB receptors bind to transmembrane ephrin-B ligands. They play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphB receptors are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. There are six vertebrate EhpB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine 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.


Pssm-ID: 198440  Cd Length: 176  Bit Score: 249.79  E-value: 5.12e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659   33 LLDTSTIHGDWGWLTYPAHGWDSINEVDESFRPIHTYQVCNVMSPNQNNWLRTNWVPRDGARRVYAEIKFTLRDCNSIPG 112
Cdd:cd10472     3 LMDTRTATAELGWTAHPPSGWEEVSGYDENMNTIRTYQVCNVFESNQNNWLRTKFIRRRGAHRVYVEMKFTVRDCSSIPN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  113 VLGTCKETFNLHYLESDRDLGAST----QESQFLKIDTIAADESFTGADLGVRRLKLNTEVRGVGPLSKRGFYLAFQDIG 188
Cdd:cd10472    83 VPGSCKETFNLYYYESDSDIATKTspfwMENPYVKVDTIAADESFSQVDLGGRVMKVNTEVRSFGPLSRNGFYLAFQDYG 162
                         170
                  ....*....|....
gi 341940659  189 ACLAILSLRIYYKK 202
Cdd:cd10472   163 ACMSLISVRVFYKK 176
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
628-891 1.17e-76

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: 252.34  E-value: 1.17e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  628 EIEASRIHIEKIIGSGESGEVCYGRLQVPGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRL 707
Cdd:cd05056     2 EIQREDITLGRCIGEGQFGDVYQGVYMSPENEKIAVAVKTCKNCTSPSVREKFLQEAYIMRQFDHPHIVKLIGVITENPV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  708 aMIVTEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDd 787
Cdd:cd05056    82 -WIVMELAPLGELRSYLQVNKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRYMED- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  788 pEAAYTTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALH 867
Cdd:cd05056   160 -ESYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMLGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLY 238
                         250       260
                  ....*....|....*....|....
gi 341940659  868 QLMLDCWHKDRAQRPRFAHVVSVL 891
Cdd:cd05056   239 SLMTKCWAYDPSKRPRFTELKAQL 262
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
628-892 6.42e-75

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


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 247.49  E-value: 6.42e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  628 EIEASRIHIEKIIGSGESGEVCYGRLQvpgqRDVPVAIKALKAGYTERQRqdFLSEAAIMGQFDHPNIIRLEGVVTRGRL 707
Cdd:cd05067     3 EVPRETLKLVERLGAGQFGEVWMGYYN----GHTKVAIKSLKQGSMSPDA--FLAEANLMKQLQHQRLVRLYAVVTQEPI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  708 aMIVTEYMENGSLDAFLRTHDG-QFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALED 786
Cdd:cd05067    77 -YIITEYMENGSLVDFLKTPSGiKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLIED 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  787 DPEAAytTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRAL 866
Cdd:cd05067   156 NEYTA--REGAKFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVTHGRIPYPGMTNPEVIQNLERGYRMPRPDNCPEEL 233
                         250       260
                  ....*....|....*....|....*.
gi 341940659  867 HQLMLDCWHKDRAQRPRFAHVVSVLD 892
Cdd:cd05067   234 YQLMRLCWKERPEDRPTFEYLRSVLE 259
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
640-891 1.03e-74

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: 245.91  E-value: 1.03e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLqvpgqRDVPVAIKALKAGY-TERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENG 718
Cdd:cd13999     1 IGSGSFGEVYKGKW-----RGTDVAIKKLKVEDdNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  719 SLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYTTAGGk 798
Cdd:cd13999    76 SLYDLLHKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKMTGVVGT- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  799 ipIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWNMTN-QDVISSVEEGYRLPAPMGCPRALHQLMLDCWHKD 877
Cdd:cd13999   155 --PRWMAPEVLRGEPYTEKADVYSFGIVLWELLT-GEVPFKELSPiQIAAAVVQKGLRPPIPPDCPPELSKLIKRCWNED 231
                         250
                  ....*....|....
gi 341940659  878 RAQRPRFAHVVSVL 891
Cdd:cd13999   232 PEKRPSFSEIVKRL 245
EphR_LBD cd10319
Ligand Binding Domain of Ephrin Receptors; Ephrin receptors (EphRs) comprise the largest ...
31-202 1.23e-74

Ligand Binding Domain of Ephrin Receptors; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). They are subdivided into 2 groups, A and B type receptors, depending on their ligand ephrin-A or ephrin-B, respectively. In general, 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. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EhpB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine 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.


Pssm-ID: 198439  Cd Length: 177  Bit Score: 243.08  E-value: 1.23e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659   31 VNLLDTSTIHGDWGWLTYP--AHGWDSINEVDESFRPIHTYQVCNVMSPNQNNWLRTNWVPRDGARRVYAEIKFTLRDCN 108
Cdd:cd10319     1 VVLLDTTLATSDLGWLTYPygHGGWDEESGLDPDGANIRTYVVCNVAMPNQDNWLRTPFIERRGAQRIYVELKFTVRDCE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  109 SIPGVLGTCKETFNLHYLESDRDLGAST----QESQFLKIDTIAADESFTgADLGVRRLKLNTEVRGVGPLSKRGFYLAF 184
Cdd:cd10319    81 SFPGNARSCKETFNLYYYESDHDTATKEfppwNEDPYTKIDTIAADESFK-SSNEDTTEKLNTETRSIGPLTKRGFYLAF 159
                         170
                  ....*....|....*...
gi 341940659  185 QDIGACLAILSLRIYYKK 202
Cdd:cd10319   160 QDQGACMSLLSVKVYYKK 177
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
628-893 1.54e-72

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: 241.48  E-value: 1.54e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  628 EIEASRIHIEKIIGSGESGEVCYGRLQ--VPGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRG 705
Cdd:cd05032     2 ELPREKITLIRELGQGSFGMVYEGLAKgvVKGEPETRVAIKTVNENASMRERIEFLNEASVMKEFNCHHVVRLLGVVSTG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  706 RLAMIVTEYMENGSLDAFLRTH--DGQF-------TIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVS 776
Cdd:cd05032    82 QPTLVVMELMAKGDLKSYLRSRrpEAENnpglgppTLQKFIQMAAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVKIG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  777 DFGLSRaleDDPEAAYTTAGGK--IPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGY 854
Cdd:cd05032   162 DFGMTR---DIYETDYYRKGGKglLPVRWMAPESLKDGVFTTKSDVWSFGVVLWEMATLAEQPYQGLSNEEVLKFVIDGG 238
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 341940659  855 RLPAPMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVLDA 893
Cdd:cd05032   239 HLDLPENCPDKLLELMRMCWQYNPKMRPTFLEIVSSLKD 277
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
627-898 1.49e-71

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: 238.85  E-value: 1.49e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  627 REIEASRIHIEKIIGSGESGEVCYGRLQVPGQR-DVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRG 705
Cdd:cd05057     2 RIVKETELEKGKVLGSGAFGTVYKGVWIPEGEKvKIPVAIKVLREETGPKANEEILDEAYVMASVDHPHLVRLLGICLSS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  706 RLaMIVTEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALE 785
Cdd:cd05057    82 QV-QLITQLMPLGCLLDYVRNHRDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGLAKLLD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  786 DDpEAAYTTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRA 865
Cdd:cd05057   161 VD-EKEYHAEGGKVPIKWMALESIQYRIYTHKSDVWSYGVTVWELMTFGAKPYEGIPAVEIPDLLEKGERLPQPPICTID 239
                         250       260       270
                  ....*....|....*....|....*....|...
gi 341940659  866 LHQLMLDCWHKDRAQRPRFAHVVSVLDALVHSP 898
Cdd:cd05057   240 VYMVLVKCWMIDAESRPTFKELANEFSKMARDP 272
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
640-891 1.56e-71

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: 237.52  E-value: 1.56e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPgqrDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGS 719
Cdd:cd05084     4 IGRGNFGEVFSGRLRAD---NTPVAVKSCRETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  720 LDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDdpeAAYTTAGG-- 797
Cdd:cd05084    81 FLTFLRTEGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSREEED---GVYAATGGmk 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  798 KIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALHQLMLDCWHKD 877
Cdd:cd05084   158 QIPVKWTAPEALNYGRYSSESDVWSFGILLWETFSLGAVPYANLSNQQTREAVEQGVRLPCPENCPDEVYRLMEQCWEYD 237
                         250
                  ....*....|....
gi 341940659  878 RAQRPRFAHVVSVL 891
Cdd:cd05084   238 PRKRPSFSTVHQDL 251
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
628-887 1.81e-71

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: 237.70  E-value: 1.81e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  628 EIEASRIHIEKIIGSGESGEVCYGrlqVPGQRDVPVAIKALKAGYTERQrqDFLSEAAIMGQFDHPNIIRLEGVVTRGRL 707
Cdd:cd05052     2 EIERTDITMKHKLGGGQYGEVYEG---VWKKYNLTVAVKTLKEDTMEVE--EFLKEAAVMKEIKHPNLVQLLGVCTREPP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  708 AMIVTEYMENGSLDAFLRTHDGQ-FTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALED 786
Cdd:cd05052    77 FYIITEFMPYGNLLDYLRECNREeLNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  787 DpeaAYTT-AGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRA 865
Cdd:cd05052   157 D---TYTAhAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKGYRMERPEGCPPK 233
                         250       260
                  ....*....|....*....|..
gi 341940659  866 LHQLMLDCWHKDRAQRPRFAHV 887
Cdd:cd05052   234 VYELMRACWQWNPSDRPSFAEI 255
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
628-893 3.65e-71

Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Trk subfamily consists of TrkA, TrkB, TrkC, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, the nerve growth factor (NGF) family of neutrotrophins, leads to Trk receptor oligomerization and activation of the catalytic domain. Trk receptors are mainly expressed in the peripheral and central nervous systems. They play important roles in cell fate determination, neuronal survival and differentiation, as well as in the regulation of synaptic plasticity. Altered expression of Trk receptors is associated with many human diseases. The Trk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 237.75  E-value: 3.65e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  628 EIEASRIHIEKIIGSGESGEVCYGRLQ--VPGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRG 705
Cdd:cd05049     1 HIKRDTIVLKRELGEGAFGKVFLGECYnlEPEQDKMLVAVKTLKDASSPDARKDFEREAELLTNLQHENIVKFYGVCTEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  706 RLAMIVTEYMENGSLDAFLRTHD-------------GQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLV 772
Cdd:cd05049    81 DPLLMVFEYMEHGDLNKFLRSHGpdaaflasedsapGELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLVGTNLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  773 CKVSDFGLSRaleDDPEAAYTTAGGK--IPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSV 850
Cdd:cd05049   161 VKIGDFGMSR---DIYSTDYYRVGGHtmLPIRWMPPESILYRKFTTESDVWSFGVVLWEIFTYGKQPWFQLSNTEVIECI 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 341940659  851 EEGYRLPAPMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVLDA 893
Cdd:cd05049   238 TQGRLLQRPRTCPSEVYAVMLGCWKREPQQRLNIKDIHKRLQE 280
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
628-900 3.74e-71

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: 237.25  E-value: 3.74e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  628 EIEASRIHIEKIIGSGESGEVCYGRLQvpgqRDVPVAIKALKAGYTERQRqdFLSEAAIMGQFDHPNIIRLEGVVTRGRL 707
Cdd:cd05072     3 EIPRESIKLVKKLGAGQFGEVWMGYYN----NSTKVAVKTLKPGTMSVQA--FLEEANLMKTLQHDKLVRLYAVVTKEEP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  708 AMIVTEYMENGSLDAFLRTHDG-QFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALED 786
Cdd:cd05072    77 IYIITEYMAKGSLLDFLKSDEGgKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIED 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  787 DPEAAytTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRAL 866
Cdd:cd05072   157 NEYTA--REGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLYEIVTYGKIPYPGMSNSDVMSALQRGYRMPRMENCPDEL 234
                         250       260       270
                  ....*....|....*....|....*....|....
gi 341940659  867 HQLMLDCWHKDRAQRPRFAHVVSVLDALVHSPES 900
Cdd:cd05072   235 YDIMKTCWKEKAEERPTFDYLQSVLDDFYTATEG 268
EphR_LBD_A2 cd10480
Ligand Binding Domain of Ephrin type-A Receptor 2; EphRs comprise the largest subfamily of ...
30-203 4.24e-71

Ligand Binding Domain of Ephrin type-A Receptor 2; EphRs comprise the largest subfamily of receptor tyr kinases (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. EphA2 negatively regulates cell differentiation and has been shown to be 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 contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine 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.


Pssm-ID: 198448  Cd Length: 174  Bit Score: 233.58  E-value: 4.24e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659   30 EVNLLDTSTIHGDWGWLTYP-AHGWDSI-NEVDESfrPIHTYQVCNVMSPNQNNWLRTNWVPRDGARRVYAEIKFTLRDC 107
Cdd:cd10480     1 EVVLLDFAAAGGELGWLTHPyGKGWDLMqNVMNDS--PIYMYSVCNVMSGEQDNWLRTNWIYRSEAERIFIELKFTVRDC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  108 NSIPGVLGTCKETFNLHYLESDRDLGASTQESQFLKIDTIAADESFTGADLGVRRLKLNTEVRGVGPLSKRGFYLAFQDI 187
Cdd:cd10480    79 NSFPGGAGSCKETFNLYYAESDVDYGTNFQKRQFRKIDTIAPDEITVSSDFETRNVKLNVEERSVGPLTRKGFYLAFQDI 158
                         170
                  ....*....|....*.
gi 341940659  188 GACLAILSLRIYYKKC 203
Cdd:cd10480   159 GACVALLSVRVYYKKC 174
EphR_LBD_B1 cd10476
Ligand Binding Domain of Ephrin type-B Receptor 1; Ephrin receptors (EphRs) comprise the ...
33-202 1.19e-70

Ligand Binding Domain of Ephrin type-B Receptor 1; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EhpB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. Using EphB1 knockout-mice, EphB1 has been shown to be essential to the development of long-term potentiation (LTP), a cellular model of synaptic plasticity, learning and memory formation. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine 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).


Pssm-ID: 198444  Cd Length: 176  Bit Score: 232.25  E-value: 1.19e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659   33 LLDTSTIHGDWGWLTYPAHGWDSINEVDESFRPIHTYQVCNVMSPNQNNWLRTNWVPRDGARRVYAEIKFTLRDCNSIPG 112
Cdd:cd10476     3 LMDTRTATAELGWTANPASGWEEVSGYDENLNTIRTYQVCNVFEPNQNNWLLTTFINRRGAHRIYTEMRFTVRDCSSLPN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  113 VLGTCKETFNLHYLESDRDLGASTQ----ESQFLKIDTIAADESFTGADLGVRRLKLNTEVRGVGPLSKRGFYLAFQDIG 188
Cdd:cd10476    83 VPGSCKETFNLYYYETDSVIATKKSafwtEAPYLKVDTIAADESFSQVDFGGRLMKVNTEVRSFGPLTRNGFYLAFQDYG 162
                         170
                  ....*....|....
gi 341940659  189 ACLAILSLRIYYKK 202
Cdd:cd10476   163 ACMSLLSVRVFFKK 176
EphR_LBD_B3 cd10478
Ligand Binding Domain of Ephrin type-B Receptor 3; Ephrin receptors (EphRs) comprise the ...
30-202 2.01e-70

Ligand Binding Domain of Ephrin type-B Receptor 3; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EhpB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. EphB3 plays a role in cell positioning in the gastrointestinal tract by being preferentially expressed in Paneth cells. It also has been implicated in early colorectal cancer and early stage squamous cell lung cancer. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine 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).


Pssm-ID: 198446  Cd Length: 173  Bit Score: 231.44  E-value: 2.01e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659   30 EVNLLDTSTIHGDWGWLTYPAHGWDSINEVDESFRPIHTYQVCNVMSPNQNNWLRTNWVPRDGARRVYAEIKFTLRDCNS 109
Cdd:cd10478     1 EETLMDTKWVTSELAWTTHPESGWEEVSGYDEAMNPIRTYQVCNVRESNQNNWLRTGFIPRRDVQRVYVELKFTVRDCNS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  110 IPGVLGTCKETFNLHYLESDRDLGAST----QESQFLKIDTIAADESFTGADLGvrrlKLNTEVRGVGPLSKRGFYLAFQ 185
Cdd:cd10478    81 IPNIPGSCKETFNLFYYESDSDSASASspfwMENPYVKVDTIAPDESFSRLDSG----RVNTKVRSFGPLSKAGFYLAFQ 156
                         170
                  ....*....|....*..
gi 341940659  186 DIGACLAILSLRIYYKK 202
Cdd:cd10478   157 DLGACMSLISVRAFFKK 173
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
638-891 2.26e-70

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: 234.54  E-value: 2.26e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVPGQRDVPVAIKALKagyTERQRQ-----DFLSEAAIMGQFDHPNIIRLEGVVTRGRLaMIVT 712
Cdd:cd05040     1 EKLGDGSFGVVRRGEWTTPSGKVIQVAVKCLK---SDVLSQpnamdDFLKEVNAMHSLDHPNLIRLYGVVLSSPL-MMVT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  713 EYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAY 792
Cdd:cd05040    77 ELAPLGSLLDRLRKDQGHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLMRALPQNEDHYV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  793 TTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVE-EGYRLPAPMGCPRALHQLML 871
Cdd:cd05040   157 MQEHRKVPFAWCAPESLKTRKFSHASDVWMFGVTLWEMFTYGEEPWLGLNGSQILEKIDkEGERLERPDDCPQDIYNVML 236
                         250       260
                  ....*....|....*....|
gi 341940659  872 DCWHKDRAQRPRFAHVVSVL 891
Cdd:cd05040   237 QCWAHKPADRPTFVALRDFL 256
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
628-884 7.67e-70

Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Ror subfamily consists of Ror1, Ror2, and similar proteins. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. Ror kinases are expressed in many tissues during development. They play important roles in bone and heart formation. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Drosophila Ror is expressed only in the developing nervous system during neurite outgrowth and neuronal differentiation, suggesting a role for Drosophila Ror in neural development. More recently, mouse Ror1 and Ror2 have also been found to play an important role in regulating neurite growth in central neurons. Ror1 and Ror2 are believed to have some overlapping and redundant functions. The Ror subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 234.19  E-value: 7.67e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  628 EIEASRIHIEKIIGSGESGEVCYGRLQVPGQRD--VPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRG 705
Cdd:cd05048     1 EIPLSAVRFLEELGEGAFGKVYKGELLGPSSEEsaISVAIKTLKENASPKTQQDFRREAELMSDLQHPNIVCLLGVCTKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  706 RLAMIVTEYMENGSLDAFLRTH------------DGQFTIVQLVGMLR---GVGAGMRYLSDLGYIHRDLAARNVLVDGR 770
Cdd:cd05048    81 QPQCMLFEYMAHGDLHEFLVRHsphsdvgvssddDGTASSLDQSDFLHiaiQIAAGMEYLSSHHYVHRDLAARNCLVGDG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  771 LVCKVSDFGLSRaleDDPEAAYTTAGGK--IPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVIS 848
Cdd:cd05048   161 LTVKISDFGLSR---DIYSSDYYRVQSKslLPVRWMPPEAILYGKFTTESDVWSFGVVLWEIFSYGLQPYYGYSNQEVIE 237
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 341940659  849 SVEEGYRLPAPMGCPRALHQLMLDCWHKDRAQRPRF 884
Cdd:cd05048   238 MIRSRQLLPCPEDCPARVYSLMVECWHEIPSRRPRF 273
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
628-884 7.75e-70

Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The DDR subfamily consists of homologs of mammalian DDR1, DDR2, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 234.54  E-value: 7.75e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  628 EIEASRIHIEKIIGSGESGEV--C---------YGRLQVPGQRDVP--VAIKALKAGYTERQRQDFLSEAAIMGQFDHPN 694
Cdd:cd05051     1 EFPREKLEFVEKLGEGQFGEVhlCeanglsdltSDDFIGNDNKDEPvlVAVKMLRPDASKNAREDFLKEVKIMSQLKDPN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  695 IIRLEGVVTRGRLAMIVTEYMENGSLDAFLRTHDGQFTIVQ-----------LVGMLRGVGAGMRYLSDLGYIHRDLAAR 763
Cdd:cd05051    81 IVRLLGVCTRDEPLCMIVEYMENGDLNQFLQKHEAETQGASatnsktlsygtLLYMATQIASGMKYLESLNFVHRDLATR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  764 NVLVDGRLVCKVSDFGLSRALEddpEAAYTTAGGK--IPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYG-ERPYWN 840
Cdd:cd05051   161 NCLVGPNYTIKIADFGMSRNLY---SGDYYRIEGRavLPIRWMAWESILLGKFTTKSDVWAFGVTLWEILTLCkEQPYEH 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 341940659  841 MTNQDVISSVEEGYR-------LPAPMGCPRALHQLMLDCWHKDRAQRPRF 884
Cdd:cd05051   238 LTDEQVIENAGEFFRddgmevyLSRPPNCPKEIYELMLECWRRDEEDRPTF 288
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
638-892 3.51e-69

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: 230.96  E-value: 3.51e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQvpgqRDVPVAIKALKAGYTERQRqdFLSEAAIMGQFDHPNIIRLEGVVTRGRLaMIVTEYMEN 717
Cdd:cd14203     1 VKLGQGCFGEVWMGTWN----GTTKVAIKTLKPGTMSPEA--FLEEAQIMKKLRHDKLVQLYAVVSEEPI-YIVTEFMSK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  718 GSLDAFLRTHDGQF-TIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAytTAG 796
Cdd:cd14203    74 GSLLDFLKDGEGKYlKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTA--RQG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  797 GKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALHQLMLDCWHK 876
Cdd:cd14203   152 AKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPPGCPESLHELMCQCWRK 231
                         250
                  ....*....|....*.
gi 341940659  877 DRAQRPRFAHVVSVLD 892
Cdd:cd14203   232 DPEERPTFEYLQSFLE 247
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
638-891 3.99e-69

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: 231.54  E-value: 3.99e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGR---LQVPGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEY 714
Cdd:cd05044     1 KFLGSGAFGEVFEGTakdILGDGSGETKVAVKTLRKGATDQEKAEFLKEAHLMSNFKHPNILKLLGVCLDNDPQYIILEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  715 MENGSLDAFLR------THDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLV---DGR-LVCKVSDFGLSRAL 784
Cdd:cd05044    81 MEGGDLLSYLRaarptaFTPPLLTLKDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVsskDYReRVVKIGDFGLARDI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  785 -EDDpeaAYTTAG-GKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGC 862
Cdd:cd05044   161 yKND---YYRKEGeGLLPVRWMAPESLVDGVFTTQSDVWAFGVLMWEILTLGQQPYPARNNLEVLHFVRAGGRLDQPDNC 237
                         250       260
                  ....*....|....*....|....*....
gi 341940659  863 PRALHQLMLDCWHKDRAQRPRFAHVVSVL 891
Cdd:cd05044   238 PDDLYELMLRCWSTDPEERPSFARILEQL 266
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
628-892 1.46e-68

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: 230.87  E-value: 1.46e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  628 EIEASRIHIEKIIGSGESGEVCYGRLQ--VPGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRG 705
Cdd:cd05050     1 EYPRNNIEYVRDIGQGAFGRVFQARAPglLPYEPFTMVAVKMLKEEASADMQADFQREAALMAEFDHPNIVKLLGVCAVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  706 RLAMIVTEYMENGSLDAFLR----------THDG-----------QFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARN 764
Cdd:cd05050    81 KPMCLLFEYMAYGDLNEFLRhrspraqcslSHSTssarkcglnplPLSCTEQLCIAKQVAAGMAYLSERKFVHRDLATRN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  765 VLVDGRLVCKVSDFGLSRALEddpEAAYTTAGGK--IPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMT 842
Cdd:cd05050   161 CLVGENMVVKIADFGLSRNIY---SADYYKASENdaIPIRWMPPESIFYNRYTTESDVWAYGVVLWEIFSYGMQPYYGMA 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 341940659  843 NQDVISSVEEGYRLPAPMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVLD 892
Cdd:cd05050   238 HEEVIYYVRDGNVLSCPDNCPLELYNLMRLCWSKLPSDRPSFASINRILQ 287
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
638-889 3.94e-68

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: 228.61  E-value: 3.94e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQvpGQRDVpvAIKALKAGytERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMEN 717
Cdd:cd05113    10 KELGTGQFGVVKYGKWR--GQYDV--AIKMIKEG--SMSEDEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMAN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  718 GSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDpeaAYTTA-G 796
Cdd:cd05113    84 GCLLNYLREMRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVLDD---EYTSSvG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  797 GKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALHQLMLDCWHK 876
Cdd:cd05113   161 SKFPVRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSLGKMPYERFTNSETVEHVSQGLRLYRPHLASEKVYTIMYSCWHE 240
                         250
                  ....*....|...
gi 341940659  877 DRAQRPRFAHVVS 889
Cdd:cd05113   241 KADERPTFKILLS 253
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
635-895 1.26e-67

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: 228.03  E-value: 1.26e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  635 HIEKI--IGSGESGEVCYGRLQVPG--QRDVpVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVT-RGRLAM 709
Cdd:cd05038     5 HLKFIkqLGEGHFGSVELCRYDPLGdnTGEQ-VAVKSLQPSGEEQHMSDFKREIEILRTLDHEYIVKYKGVCEsPGRRSL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  710 -IVTEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDP 788
Cdd:cd05038    84 rLIMEYLPSGSLRDYLQRHRDQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAKVLPEDK 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  789 EAAYTTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPY--------------WNMTNQDVISSVEEGY 854
Cdd:cd05038   164 EYYYVKEPGESPIFWYAPECLRESRFSSASDVWSFGVTLYELFTYGDPSQsppalflrmigiaqGQMIVTRLLELLKSGE 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 341940659  855 RLPAPMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVLDALV 895
Cdd:cd05038   244 RLPRPPSCPDEVYDLMKECWEYEPQDRPSFSDLILIIDRLR 284
EphR_LBD_B2 cd10477
Ligand Binding Domain of Ephrin type-B Receptor 2; Ephrin receptors (EphRs) comprise the ...
30-202 1.47e-67

Ligand Binding Domain of Ephrin type-B Receptor 2; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EhpB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. EphB2 plays a role in cell positioning in the gastrointestinal tract by being expressed in proliferating progenitor cells. It also has been implicated in colorectal cancer. A loss of EphB2, as well as EphA4, also precedes memory decline in a murine model of Alzheimers disease. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine 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).


Pssm-ID: 198445  Cd Length: 178  Bit Score: 223.78  E-value: 1.47e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659   30 EVNLLDTSTIHGDWGWLTYPAHGWDSINEVDESFRPIHTYQVCNVMSPNQNNWLRTNWVPRDGARRVYAEIKFTLRDCNS 109
Cdd:cd10477     2 EETLMDSTTATAELGWMVHPPSGWEEVSGYDENMNTIRTYQVCNVFESSQNNWLRTKYIRRRGAHRIHVEMKFSVRDCSS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  110 IPGVLGTCKETFNLHYLESDRDLGAST----QESQFLKIDTIAADESFTGADLGVRRLKLNTEVRGVGPLSKRGFYLAFQ 185
Cdd:cd10477    82 IPSVPGSCKETFNLYYYESDFDSATKTfpnwMENPWVKVDTIAADESFSQVDLGGRVMKINTEVRSFGPVSRNGFYLAFQ 161
                         170
                  ....*....|....*..
gi 341940659  186 DIGACLAILSLRIYYKK 202
Cdd:cd10477   162 DYGGCMSLIAVRVFYRK 178
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
640-887 3.69e-67

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: 226.37  E-value: 3.69e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPgQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLaMIVTEYMENGS 719
Cdd:cd05115    12 LGSGNFGCVKKGVYKMR-KKQIDVAIKVLKQGNEKAVRDEMMREAQIMHQLDNPYIVRMIGVCEAEAL-MLVMEMASGGP 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  720 LDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYTTAGGKI 799
Cdd:cd05115    90 LNKFLSGKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSKALGADDSYYKARSAGKW 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  800 PIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALHQLMLDCWHKDRA 879
Cdd:cd05115   170 PLKWYAPECINFRKFSSRSDVWSYGVTMWEAFSYGQKPYKKMKGPEVMSFIEQGKRMDCPAECPPEMYALMSDCWIYKWE 249

                  ....*...
gi 341940659  880 QRPRFAHV 887
Cdd:cd05115   250 DRPNFLTV 257
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
629-885 5.72e-67

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: 225.21  E-value: 5.72e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  629 IEASRIHIEKIIGSGESGEVCYGRLQvpgqRDVPVAIKALKAGYTerQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLA 708
Cdd:cd05112     1 IDPSELTFVQEIGSGQFGLVHLGYWL----NKDKVAIKTIREGAM--SEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  709 MIVTEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDp 788
Cdd:cd05112    75 CLVFEFMEHGCLSDYLRTQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTRFVLDD- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  789 eaAYTTA-GGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALH 867
Cdd:cd05112   154 --QYTSStGTKFPVKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSEGKIPYENRSNSEVVEDINAGFRLYKPRLASTHVY 231
                         250
                  ....*....|....*...
gi 341940659  868 QLMLDCWHKDRAQRPRFA 885
Cdd:cd05112   232 EIMNHCWKERPEDRPSFS 249
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
627-893 1.84e-65

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: 221.88  E-value: 1.84e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  627 REIEASRIHIEKIIGSGESGEVCYGRLQ-VPGQ-RDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTR 704
Cdd:cd05036     1 KEVPRKNLTLIRALGQGAFGEVYEGTVSgMPGDpSPLQVAVKTLPELCSEQDEMDFLMEALIMSKFNHPNIVRCIGVCFQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  705 GRLAMIVTEYMENGSLDAFLR------THDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVD----GRlVCK 774
Cdd:cd05036    81 RLPRFILLELMAGGDLKSFLRenrprpEQPSSLTMLDLLQLAQDVAKGCRYLEENHFIHRDIAARNCLLTckgpGR-VAK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  775 VSDFGLSRaleDDPEAAYTTAGGK--IPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEE 852
Cdd:cd05036   160 IGDFGMAR---DIYRADYYRKGGKamLPVKWMPPEAFLDGIFTSKTDVWSFGVLLWEIFSLGYMPYPGKSNQEVMEFVTS 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 341940659  853 GYRLPAPMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVLDA 893
Cdd:cd05036   237 GGRMDPPKNCPGPVYRIMTQCWQHIPEDRPNFSTILERLNY 277
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
638-887 1.60e-64

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: 218.34  E-value: 1.60e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQvpgqRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMEN 717
Cdd:cd05085     2 ELLGKGNFGEVYKGTLK----DKTPVAVKTCKEDLPQELKIKFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVPG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  718 GSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRAlEDDpeAAYTTAGG 797
Cdd:cd05085    78 GDFLSFLRKKKDELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQ-EDD--GVYSSSGL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  798 K-IPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALHQLMLDCWHK 876
Cdd:cd05085   155 KqIPIKWTAPEALNYGRYSSESDVWSFGILLWETFSLGVCPYPGMTNQQAREQVEKGYRMSAPQRCPEDIYKIMQRCWDY 234
                         250
                  ....*....|.
gi 341940659  877 DRAQRPRFAHV 887
Cdd:cd05085   235 NPENRPKFSEL 245
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
629-895 1.79e-64

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: 218.58  E-value: 1.79e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  629 IEASRIHIEKIIGSGESGEVCYGRLQVpgqrDVPVAIKALKAGytERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLA 708
Cdd:cd05114     1 INPSELTFMKELGSGLFGVVRLGKWRA----QYKVAIKAIREG--AMSEEDFIEEAKVMMKLTHPKLVQLYGVCTQQKPI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  709 MIVTEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDp 788
Cdd:cd05114    75 YIVTEFMENGCLLNYLRQRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRYVLDD- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  789 eaAYTTA-GGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALH 867
Cdd:cd05114   154 --QYTSSsGAKFPVKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTEGKMPFESKSNYEVVEMVSRGHRLYRPKLASKSVY 231
                         250       260
                  ....*....|....*....|....*...
gi 341940659  868 QLMLDCWHKDRAQRPRFAHVVSVLDALV 895
Cdd:cd05114   232 EVMYSCWHEKPEGRPTFADLLRTITEIA 259
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
628-892 2.37e-64

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: 218.36  E-value: 2.37e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  628 EIEASRIHIEKIIGSGESGEVCYGRLQvpgqRDVPVAIKALKAGytERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRL 707
Cdd:cd05073     7 EIPRESLKLEKKLGAGQFGEVWMATYN----KHTKVAVKTMKPG--SMSVEAFLAEANVMKTLQHDKLVKLHAVVTKEPI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  708 aMIVTEYMENGSLDAFLRTHDG-QFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALED 786
Cdd:cd05073    81 -YIITEFMAKGSLLDFLKSDEGsKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVIED 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  787 DPEAAytTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRAL 866
Cdd:cd05073   160 NEYTA--REGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTYGRIPYPGMSNPEVIRALERGYRMPRPENCPEEL 237
                         250       260
                  ....*....|....*....|....*.
gi 341940659  867 HQLMLDCWHKDRAQRPRFAHVVSVLD 892
Cdd:cd05073   238 YNIMMRCWKNRPEERPTFEYIQSVLD 263
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
628-892 3.98e-64

Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fyn and Yrk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Fyn/Yrk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase.


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 218.01  E-value: 3.98e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  628 EIEASRIHIEKIIGSGESGEVCYGRLQvpgqRDVPVAIKALKAGytERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRgRL 707
Cdd:cd05070     5 EIPRESLQLIKRLGNGQFGEVWMGTWN----GNTKVAIKTLKPG--TMSPESFLEEAQIMKKLKHDKLVQLYAVVSE-EP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  708 AMIVTEYMENGSLDAFLRTHDGQ-FTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALED 786
Cdd:cd05070    78 IYIVTEYMSKGSLLDFLKDGEGRaLKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIED 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  787 DPEAAytTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRAL 866
Cdd:cd05070   158 NEYTA--RQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPQDCPISL 235
                         250       260
                  ....*....|....*....|....*.
gi 341940659  867 HQLMLDCWHKDRAQRPRFAHVVSVLD 892
Cdd:cd05070   236 HELMIHCWKKDPEERPTFEYLQGFLE 261
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
638-884 1.26e-63

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: 215.89  E-value: 1.26e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGrlQVPGQrdvPVAIKALKAGYTErqrQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLaMIVTEYMEN 717
Cdd:cd05083    12 EIIGEGEFGAVLQG--EYMGQ---KVAVKNIKCDVTA---QAFLEETAVMTKLQHKNLVRLLGVILHNGL-YIVMELMSK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  718 GSLDAFLRTHdGQFTI--VQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRAledDPEAAYTTa 795
Cdd:cd05083    83 GNLVNFLRSR-GRALVpvIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAKV---GSMGVDNS- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  796 ggKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALHQLMLDCWH 875
Cdd:cd05083   158 --RLPVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFSYGRAPYPKMSVKEVKEAVEKGYRMEPPEGCPPDVYSIMTSCWE 235

                  ....*....
gi 341940659  876 KDRAQRPRF 884
Cdd:cd05083   236 AEPGKRPSF 244
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
635-893 1.75e-63

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkA is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkA to its ligand, nerve growth factor (NGF), results in receptor oligomerization and activation of the catalytic domain. TrkA is expressed mainly in neural-crest-derived sensory and sympathetic neurons of the peripheral nervous system, and in basal forebrain cholinergic neurons of the central nervous system. It is critical for neuronal growth, differentiation and survival. Alternative TrkA splicing has been implicated as a pivotal regulator of neuroblastoma (NB) behavior. Normal TrkA expression is associated with better NB prognosis, while the hypoxia-regulated TrkAIII splice variant promotes NB pathogenesis and progression. Aberrant TrkA expression has also been demonstrated in non-neural tumors including prostate, breast, lung, and pancreatic cancers. The TrkA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 216.37  E-value: 1.75e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  635 HIEK--IIGSGESGEVCYGRLQV-------PGQRDVPVAIKALKAGyTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRG 705
Cdd:cd05092     1 HIKRrdIVLKWELGEGAFGKVFLaechnllPEQDKMLVAVKALKEA-TESARQDFQREAELLTVLQHQHIVRFYGVCTEG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  706 RLAMIVTEYMENGSLDAFLRTHD--------------GQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRL 771
Cdd:cd05092    80 EPLIMVFEYMRHGDLNRFLRSHGpdakildggegqapGQLTLGQMLQIASQIASGMVYLASLHFVHRDLATRNCLVGQGL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  772 VCKVSDFGLSRaleDDPEAAYTTAGGK--IPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISS 849
Cdd:cd05092   160 VVKIGDFGMSR---DIYSTDYYRVGGRtmLPIRWMPPESILYRKFTTESDIWSFGVVLWEIFTYGKQPWYQLSNTEAIEC 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 341940659  850 VEEGYRLPAPMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVLDA 893
Cdd:cd05092   237 ITQGRELERPRTCPPEVYAIMQGCWQREPQQRHSIKDIHSRLQA 280
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
634-884 3.20e-62

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


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 212.15  E-value: 3.20e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  634 IHIEKIIGSGESGEVCYGRlqvpgQRDVPVAIKALKAGYTErqrQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAM-IVT 712
Cdd:cd05082     8 LKLLQTIGKGEFGDVMLGD-----YRGNKVAVKCIKNDATA---QAFLAEASVMTQLRHSNLVQLLGVIVEEKGGLyIVT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  713 EYMENGSLDAFLRTH-----DGQftivQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRaledd 787
Cdd:cd05082    80 EYMAKGSLVDYLRSRgrsvlGGD----CLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTK----- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  788 pEAAYTTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALH 867
Cdd:cd05082   151 -EASSTQDTGKLPVKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVVPRVEKGYKMDAPDGCPPAVY 229
                         250
                  ....*....|....*..
gi 341940659  868 QLMLDCWHKDRAQRPRF 884
Cdd:cd05082   230 DVMKNCWHLDAAMRPSF 246
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
628-892 6.62e-62

Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Yes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 211.85  E-value: 6.62e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  628 EIEASRIHIEKIIGSGESGEVCYGRLQvpgqRDVPVAIKALKAGytERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRL 707
Cdd:cd05069     8 EIPRESLRLDVKLGQGCFGEVWMGTWN----GTTKVAIKTLKPG--TMMPEAFLQEAQIMKKLRHDKLVPLYAVVSEEPI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  708 aMIVTEYMENGSLDAFLRTHDGQF-TIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALED 786
Cdd:cd05069    82 -YIVTEFMGKGSLLDFLKEGDGKYlKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIED 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  787 DPEAAytTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRAL 866
Cdd:cd05069   161 NEYTA--RQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMVNREVLEQVERGYRMPCPQGCPESL 238
                         250       260
                  ....*....|....*....|....*.
gi 341940659  867 HQLMLDCWHKDRAQRPRFAHVVSVLD 892
Cdd:cd05069   239 HELMKLCWKKDPDERPTFEYIQSFLE 264
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
628-895 8.57e-62

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: 212.28  E-value: 8.57e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  628 EIEASRIHIEKIIGSGESGEVCYGRL-QVPGQRD--VPVAIKALKAGYTERQRQDFLSEAAIM---GQfdHPNIIRLEGV 701
Cdd:cd05053     8 ELPRDRLTLGKPLGEGAFGQVVKAEAvGLDNKPNevVTVAVKMLKDDATEKDLSDLVSEMEMMkmiGK--HKNIINLLGA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  702 VTRGRLAMIVTEYMENGSLDAFLR---------------THDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVL 766
Cdd:cd05053    86 CTQDGPLYVVVEYASKGNLREFLRarrppgeeaspddprVPEEQLTQKDLVSFAYQVARGMEYLASKKCIHRDLAARNVL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  767 VDGRLVCKVSDFGLSRALEDDPEAAYTTaGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDV 846
Cdd:cd05053   166 VTEDNVMKIADFGLARDIHHIDYYRKTT-NGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEEL 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 341940659  847 ISSVEEGYRLPAPMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVLDALV 895
Cdd:cd05053   245 FKLLKEGHRMEKPQNCTQELYMLMRDCWHEVPSQRPTFKQLVEDLDRIL 293
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
628-899 7.50e-60

Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK, containing an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region with a conserved tyr. It is activated by autophosphorylation at the tyr kinase domain, and is negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). c-Src is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. The Src subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 206.08  E-value: 7.50e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  628 EIEASRIHIEKIIGSGESGEVCYGRLQVPGQrdvpVAIKALKAGYTERQRqdFLSEAAIMGQFDHPNIIRLEGVVTRGRL 707
Cdd:cd05071     5 EIPRESLRLEVKLGQGCFGEVWMGTWNGTTR----VAIKTLKPGTMSPEA--FLQEAQVMKKLRHEKLVQLYAVVSEEPI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  708 aMIVTEYMENGSLDAFLRTHDGQF-TIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALED 786
Cdd:cd05071    79 -YIVTEYMSKGSLLDFLKGEMGKYlRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIED 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  787 DPEAAytTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRAL 866
Cdd:cd05071   158 NEYTA--RQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPCPPECPESL 235
                         250       260       270
                  ....*....|....*....|....*....|...
gi 341940659  867 HQLMLDCWHKDRAQRPRFAHVVSVLDALVHSPE 899
Cdd:cd05071   236 HDLMCQCWRKEPEERPTFEYLQAFLEDYFTSTE 268
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
640-887 9.68e-60

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 205.20  E-value: 9.68e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPgQRDVPVAIKALKAGYTERQRQD-FLSEAAIMGQFDHPNIIRLEGVVtRGRLAMIVTEYMENG 718
Cdd:cd05116     3 LGSGNFGTVKKGYYQMK-KVVKTVAVKILKNEANDPALKDeLLREANVMQQLDNPYIVRMIGIC-EAESWMLVMEMAELG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  719 SLDAFLRtHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYTTAGGK 798
Cdd:cd05116    81 PLNKFLQ-KNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKALRADENYYKAQTHGK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  799 IPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALHQLMLDCWHKDR 878
Cdd:cd05116   160 WPVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSYGQKPYKGMKGNEVTQMIEKGERMECPAGCPPEMYDLMKLCWTYDV 239

                  ....*....
gi 341940659  879 AQRPRFAHV 887
Cdd:cd05116   240 DERPGFAAV 248
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
638-897 6.77e-59

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: 202.70  E-value: 6.77e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVPGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGR-LAMIVTEYME 716
Cdd:cd05058     1 EVIGKGHFGCVYHGTLIDSDGQKIHCAVKSLNRITDIEEVEQFLKEGIIMKDFSHPNVLSLLGICLPSEgSPLVVLPYMK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  717 NGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALED-DPEAAYTTA 795
Cdd:cd05058    81 HGDLRNFIRSETHNPTVKDLIGFGLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLARDIYDkEYYSVHNHT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  796 GGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALHQLMLDCWH 875
Cdd:cd05058   161 GAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPDVDSFDITVYLLQGRRLLQPEYCPDPLYEVMLSCWH 240
                         250       260
                  ....*....|....*....|..
gi 341940659  876 KDRAQRPRFAHVVSVLDALVHS 897
Cdd:cd05058   241 PKPEMRPTFSELVSRISQIFST 262
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
638-895 2.26e-58

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: 201.99  E-value: 2.26e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVPGQRDVPVAIKALKA-GYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGR------LAMI 710
Cdd:cd05035     5 KILGEGEFGSVMEAQLKQDDGSQLKVAVKTMKVdIHTYSEIEEFLSEAACMKDFDHPNVMRLIGVCFTASdlnkppSPMV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  711 VTEYMENGSLDAFL---RTHDG--QFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALE 785
Cdd:cd05035    85 ILPFMKHGDLHSYLlysRLGGLpeKLPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVADFGLSRKIY 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  786 DdpeAAYTTAG--GKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCP 863
Cdd:cd05035   165 S---GDYYRQGriSKMPVKWIALESLADNVYTSKSDVWSFGVTMWEIATRGQTPYPGVENHEIYDYLRNGNRLKQPEDCL 241
                         250       260       270
                  ....*....|....*....|....*....|..
gi 341940659  864 RALHQLMLDCWHKDRAQRPRFAHVVSVLDALV 895
Cdd:cd05035   242 DEVYFLMYFCWTVDPKDRPTFTKLREVLENIL 273
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
640-891 2.43e-56

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR2 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR2 results in a slow but sustained receptor activation. DDR2 binds mostly to fibrillar collagens as well as collagen X. DDR2 is widely expressed in many tissues with the highest levels found in skeletal muscle, skin, kidney and lung. It is important in cell proliferation and development. Mice, with a deletion of DDR2, suffer from dwarfism and delayed healing of epidermal wounds. DDR2 also contributes to collagen (type I) regulation by inhibiting fibrillogenesis and altering the morphology of collagen fibers. It is also expressed in immature dendritic cells (DCs), where it plays a role in DC activation and function. The DDR2 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 (PI3K).


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 197.14  E-value: 2.43e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEV--CYGR-----------LQVPGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGV-VTRG 705
Cdd:cd05095    13 LGEGQFGEVhlCEAEgmekfmdkdfaLEVSENQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIRLLAVcITDD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  706 RLAMIvTEYMENGSLDAFLRTH--DGQFTIV---------QLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCK 774
Cdd:cd05095    93 PLCMI-TEYMENGDLNQFLSRQqpEGQLALPsnaltvsysDLRFMAAQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIK 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  775 VSDFGLSRALEddpEAAYTTAGGK--IPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAY-GERPYWNMTNQDVISSVE 851
Cdd:cd05095   172 IADFGMSRNLY---SGDYYRIQGRavLPIRWMSWESILLGKFTTASDVWAFGVTLWETLTFcREQPYSQLSDEQVIENTG 248
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 341940659  852 EGYR-------LPAPMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVL 891
Cdd:cd05095   249 EFFRdqgrqtyLPQPALCPDSVYKLMLSCWRRDTKDRPSFQEIHTLL 295
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
627-899 3.11e-56

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: 197.17  E-value: 3.11e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  627 REIEASRIhieKIIGSGESGEVcYGRLQVP-GQR-DVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTR 704
Cdd:cd05108     5 KETEFKKI---KVLGSGAFGTV-YKGLWIPeGEKvKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  705 GRLAMIvTEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRAL 784
Cdd:cd05108    81 STVQLI-TQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  785 EDDpEAAYTTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPR 864
Cdd:cd05108   160 GAE-EKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTI 238
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 341940659  865 ALHQLMLDCWHKDRAQRPRFAHVVSVLDALVHSPE 899
Cdd:cd05108   239 DVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQ 273
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
628-884 3.21e-56

Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR-like proteins are members of the DDR subfamily, which are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 196.74  E-value: 3.21e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  628 EIEASRIHIEKIIGSGESGEV--CYGR-----LQVPG----QRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNII 696
Cdd:cd05097     1 EFPRQQLRLKEKLGEGQFGEVhlCEAEglaefLGEGApefdGQPVLVAVKMLRADVTKTARNDFLKEIKIMSRLKNPNII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  697 RLEGVVTRGRLAMIVTEYMENGSLDAFL--RTHDGQFTIVQ---------LVGMLRGVGAGMRYLSDLGYIHRDLAARNV 765
Cdd:cd05097    81 RLLGVCVSDDPLCMITEYMENGDLNQFLsqREIESTFTHANnipsvsianLLYMAVQIASGMKYLASLNFVHRDLATRNC 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  766 LVDGRLVCKVSDFGLSRALEddpEAAYTTAGGK--IPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAY-GERPYWNMT 842
Cdd:cd05097   161 LVGNHYTIKIADFGMSRNLY---SGDYYRIQGRavLPIRWMAWESILLGKFTTASDVWAFGVTLWEMFTLcKEQPYSLLS 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 341940659  843 NQDVISSVEEGYR-------LPAPMGCPRALHQLMLDCWHKDRAQRPRF 884
Cdd:cd05097   238 DEQVIENTGEFFRnqgrqiyLSQTPLCPSPVFKLMMRCWSRDIKDRPTF 286
EphR_LBD_A1 cd10479
Ligand Binding Domain of Ephrin type-A Receptor 1; Ephrin receptors (EphRs) comprise the ...
30-202 4.48e-56

Ligand Binding Domain of Ephrin type-A Receptor 1; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (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. EphA1 is downregulated in some advanced colorectal and myeloid cancers and upregulated in neuroblasoma and glioblastoma. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine 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.


Pssm-ID: 198447  Cd Length: 177  Bit Score: 191.78  E-value: 4.48e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659   30 EVNLLDTSTIHGDWGWLTYPAH-GWDSINEVDESfRPIHTYQVCNVMSP-NQNNWLRTNWVPR-DGARRVYAEIKFTLRD 106
Cdd:cd10479     1 EVTLMDTSTAQGELGWLLDPPEvGWSEVQQMLNG-TPLYMYQDCPVQSEgDTDHWLRSNWIYRgEEASRIYVELQFTVRD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  107 CNSIPGVLG--TCKETFNLHYLESDRDLGASTQESQFLKIDTIAADESFTGADLGVRRLKLNTEVRGVGPLSKRGFYLAF 184
Cdd:cd10479    80 CKSFPGGAGplGCKETFNLYYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLASGSVKLNVERCSLGKLTRRGLYLAF 159
                         170
                  ....*....|....*...
gi 341940659  185 QDIGACLAILSLRIYYKK 202
Cdd:cd10479   160 HNPGACVALVSVRVFYQR 177
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
638-891 4.76e-56

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: 195.38  E-value: 4.76e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVP--GQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYM 715
Cdd:cd05046    11 TTLGRGEFGEVFLAKAKGIeeEGGETLVLVKALQKTKDENLQSEFRRELDMFRKLSHKNVVRLLGLCREAEPHYMILEYT 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  716 ENGSLDAFLRTHDGQ--------FTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDD 787
Cdd:cd05046    91 DLGDLKQFLRATKSKdeklkpppLSTKQKVALCTQIALGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLSLSKDVYNS 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  788 PEAAYTTAggKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEG-YRLPAPMGCPRAL 866
Cdd:cd05046   171 EYYKLRNA--LIPLRWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTQGELPFYGLSDEEVLNRLQAGkLELPVPEGCPSRL 248
                         250       260
                  ....*....|....*....|....*
gi 341940659  867 HQLMLDCWHKDRAQRPRFAHVVSVL 891
Cdd:cd05046   249 YKLMTRCWAVNPKDRPSFSELVSAL 273
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
628-896 9.37e-56

Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. InsR is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the insulin ligand to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR signaling plays an important role in many cellular processes including glucose homeostasis, glycogen synthesis, lipid and protein metabolism, ion and amino acid transport, cell cycle and proliferation, cell differentiation, gene transcription, and nitric oxide synthesis. Insulin resistance, caused by abnormalities in InsR signaling, has been described in diabetes, hypertension, cardiovascular disease, metabolic syndrome, heart failure, and female infertility. The InsR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 195.19  E-value: 9.37e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  628 EIEASRIHIEKIIGSGESGEVCYGRLQ--VPGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRG 705
Cdd:cd05061     2 EVSREKITLLRELGQGSFGMVYEGNARdiIKGEAETRVAVKTVNESASLRERIEFLNEASVMKGFTCHHVVRLLGVVSKG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  706 RLAMIVTEYMENGSLDAFLRT-------HDGQF--TIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVS 776
Cdd:cd05061    82 QPTLVVMELMAHGDLKSYLRSlrpeaenNPGRPppTLQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  777 DFGLSRaleDDPEAAYTTAGGK--IPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGY 854
Cdd:cd05061   162 DFGMTR---DIYETDYYRKGGKglLPVRWMAPESLKDGVFTTSSDMWSFGVVLWEITSLAEQPYQGLSNEQVLKFVMDGG 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 341940659  855 RLPAPMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVLDALVH 896
Cdd:cd05061   239 YLDQPDNCPERVTDLMRMCWQFNPKMRPTFLEIVNLLKDDLH 280
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
628-891 1.27e-55

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR1 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR1 results in a slow but sustained receptor activation. DDR1 binds to all collagens tested to date (types I-IV). It is widely expressed in many tissues. It is abundant in the brain and is also found in keratinocytes, colonic mucosa epithelium, lung epithelium, thyroid follicles, and the islets of Langerhans. During embryonic development, it is found in the developing neuroectoderm. DDR1 is a key regulator of cell morphogenesis, differentiation and proliferation. It is important in the development of the mammary gland, the vasculator and the kidney. DDR1 is also found in human leukocytes, where it facilitates cell adhesion, migration, maturation, and cytokine production. The DDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 195.15  E-value: 1.27e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  628 EIEASRIHIEKIIGSGESGEVCYGRLQVPGQ-------------RDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPN 694
Cdd:cd05096     1 KFPRGHLLFKEKLGEGQFGEVHLCEVVNPQDlptlqfpfnvrkgRPLLVAVKILRPDANKNARNDFLKEVKILSRLKDPN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  695 IIRLEGVVTRGRLAMIVTEYMENGSLDAFLRTH---------------DGQFTIVQ---LVGMLRGVGAGMRYLSDLGYI 756
Cdd:cd05096    81 IIRLLGVCVDEDPLCMITEYMENGDLNQFLSSHhlddkeengndavppAHCLPAISyssLLHVALQIASGMKYLSSLNFV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  757 HRDLAARNVLVDGRLVCKVSDFGLSRALEddpEAAYTTAGGK--IPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAY- 833
Cdd:cd05096   161 HRDLATRNCLVGENLTIKIADFGMSRNLY---AGDYYRIQGRavLPIRWMAWECILMGKFTTASDVWAFGVTLWEILMLc 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 341940659  834 GERPYWNMTNQDVISSVEEGYR-------LPAPMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVL 891
Cdd:cd05096   238 KEQPYGELTDEQVIENAGEFFRdqgrqvyLFRPPPCPQGLYELMLQCWSRDCRERPSFSDIHAFL 302
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
625-895 1.36e-55

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: 195.57  E-value: 1.36e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  625 FTREieasRIHIEKIIGSGESGEVC----YGRLQVPGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFD-HPNIIRLE 699
Cdd:cd05099     9 FPRD----RLVLGKPLGEGCFGQVVraeaYGIDKSRPDQTVTVAVKMLKDNATDKDLADLISEMELMKLIGkHKNIINLL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  700 GVVTRGRLAMIVTEYMENGSLDAFLR---------------THDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARN 764
Cdd:cd05099    85 GVCTQEGPLYVIVEYAAKGNLREFLRarrppgpdytfditkVPEEQLSFKDLVSCAYQVARGMEYLESRRCIHRDLAARN 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  765 VLVDGRLVCKVSDFGLSRALEDdPEAAYTTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQ 844
Cdd:cd05099   165 VLVTEDNVMKIADFGLARGVHD-IDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILMWEIFTLGGSPYPGIPVE 243
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 341940659  845 DVISSVEEGYRLPAPMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVLDALV 895
Cdd:cd05099   244 ELFKLLREGHRMDKPSNCTHELYMLMRECWHAVPTQRPTFKQLVEALDKVL 294
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
628-887 2.83e-55

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 193.30  E-value: 2.83e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  628 EIEASRIHIEKIIGSGESGEVCYGRLQVPGQRDVP-VAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGR 706
Cdd:cd05090     1 ELPLSAVRFMEELGECAFGKIYKGHLYLPGMDHAQlVAIKTLKDYNNPQQWNEFQQEASLMTELHHPNIVCLLGVVTQEQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  707 LAMIVTEYMENGSLDAFL------------RTHDGQFTIV----QLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGR 770
Cdd:cd05090    81 PVCMLFEFMNQGDLHEFLimrsphsdvgcsSDEDGTVKSSldhgDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILVGEQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  771 LVCKVSDFGLSRALEddpEAAYTTAGGK--IPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVIS 848
Cdd:cd05090   161 LHVKISDLGLSREIY---SSDYYRVQNKslLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIE 237
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 341940659  849 SVEEGYRLPAPMGCPRALHQLMLDCWHKDRAQRPRFAHV 887
Cdd:cd05090   238 MVRKRQLLPCSEDCPPRMYSLMTECWQEIPSRRPRFKDI 276
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
629-894 3.53e-55

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: 193.21  E-value: 3.53e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  629 IEASRIHIEKIIGSGESGEVCYGRLQVPGQRDVPVAIKALKAG-YTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGR- 706
Cdd:cd05074     6 IQEQQFTLGRMLGKGEFGSVREAQLKSEDGSFQKVAVKMLKADiFSSSDIEEFLREAACMKEFDHPNVIKLIGVSLRSRa 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  707 -----LAMIVTEYMENGSLDAFL---RTHDGQFTIVQ--LVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVS 776
Cdd:cd05074    86 kgrlpIPMVILPFMKHGDLHTFLlmsRIGEEPFTLPLqtLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNENMTVCVA 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  777 DFGLSRALEddpEAAYTTAG--GKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGY 854
Cdd:cd05074   166 DFGLSKKIY---SGDYYRQGcaSKLPVKWLALESLADNVYTTHSDVWAFGVTMWEIMTRGQTPYAGVENSEIYNYLIKGN 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 341940659  855 RLPAPMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVLDAL 894
Cdd:cd05074   243 RLKQPPDCLEDVYELMCQCWSPEPKCRPSFQHLRDQLELI 282
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
629-897 4.12e-55

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: 192.84  E-value: 4.12e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  629 IEASRIHIEKIIGSGESGEVCYGRLQVPGQRDVPVAIKALKA-GYTERQRQDFLSEAAIMGQFDHPNIIRLEGV---VTR 704
Cdd:cd14204     4 IDRNLLSLGKVLGEGEFGSVMEGELQQPDGTNHKVAVKTMKLdNFSQREIEEFLSEAACMKDFNHPNVIRLLGVcleVGS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  705 GRLA--MIVTEYMENGSLDAFL---RTHDG-QFTIVQ-LVGMLRGVGAGMRYLSDLGYIHRDLAARN-VLVDGRLVCkVS 776
Cdd:cd14204    84 QRIPkpMVILPFMKYGDLHSFLlrsRLGSGpQHVPLQtLLKFMIDIALGMEYLSSRNFLHRDLAARNcMLRDDMTVC-VA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  777 DFGLSRALEddpEAAYTTAG--GKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGY 854
Cdd:cd14204   163 DFGLSKKIY---SGDYYRQGriAKMPVKWIAVESLADRVYTVKSDVWAFGVTMWEIATRGMTPYPGVQNHEIYDYLLHGH 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 341940659  855 RLPAPMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVLDALVHS 897
Cdd:cd14204   240 RLKQPEDCLDELYDIMYSCWRSDPTDRPTFTQLRENLEKLLES 282
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
627-899 3.22e-54

Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER2 (ErbB2, HER2/neu) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER2 does not bind to any known EGFR subfamily ligands, but contributes to the kinase activity of all possible heterodimers. It acts as the preferred partner of other ligand-bound EGFR proteins and functions as a signal amplifier, with the HER2-HER3 heterodimer being the most potent pair in mitogenic signaling. HER2 plays an important role in cell development, proliferation, survival and motility. Overexpression of HER2 results in its activation and downstream signaling, even in the absence of ligand. HER2 overexpression, mainly due to gene amplification, has been shown in a variety of human cancers. Its role in breast cancer is especially well-documented. HER2 is up-regulated in about 25% of breast tumors and is associated with increases in tumor aggressiveness, recurrence and mortality. HER2 is a target for monoclonal antibodies and small molecule inhibitors, which are being developed as treatments for cancer. The first humanized antibody approved for clinical use is Trastuzumab (Herceptin), which is being used in combination with other therapies to improve the survival rates of patients with HER2-overexpressing breast cancer. The HER2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 190.24  E-value: 3.22e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  627 REIEASRIhieKIIGSGESGEVcYGRLQVPGQRDV--PVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTR 704
Cdd:cd05109     5 KETELKKV---KVLGSGAFGTV-YKGIWIPDGENVkiPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVCRLLGICLT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  705 GRLAMiVTEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRAL 784
Cdd:cd05109    81 STVQL-VTQLMPYGCLLDYVRENKDRIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLARLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  785 EDDpEAAYTTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPR 864
Cdd:cd05109   160 DID-ETEYHADGGKVPIKWMALESILHRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTI 238
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 341940659  865 ALHQLMLDCWHKDRAQRPRFAHVVSVLDALVHSPE 899
Cdd:cd05109   239 DVYMIMVKCWMIDSECRPRFRELVDEFSRMARDPS 273
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
627-891 3.36e-54

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror2 plays important roles in skeletal and heart formation. Ror2-deficient mice show widespread bone abnormalities, ventricular defects in the heart, and respiratory dysfunction. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Ror2 is also implicated in neural development. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 190.61  E-value: 3.36e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  627 REIEASRIHIEKIIGSGESGEVCYGRL--QVPGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTR 704
Cdd:cd05091     1 KEINLSAVRFMEELGEDRFGKVYKGHLfgTAPGEQTQAVAIKTLKDKAEGPLREEFRHEAMLRSRLQHPNIVCLLGVVTK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  705 GRLAMIVTEYMENGSLDAFL---------------RTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDG 769
Cdd:cd05091    81 EQPMSMIFSYCSHGDLHEFLvmrsphsdvgstdddKTVKSTLEPADFLHIVTQIAAGMEYLSSHHVVHKDLATRNVLVFD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  770 RLVCKVSDFGLSRALEddpEAAYTTAGGK--IPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVI 847
Cdd:cd05091   161 KLNVKISDLGLFREVY---AADYYKLMGNslLPIRWMSPEAIMYGKFSIDSDIWSYGVVLWEVFSYGLQPYCGYSNQDVI 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 341940659  848 SSVEEGYRLPAPMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVL 891
Cdd:cd05091   238 EMIRNRQVLPCPDDCPAWVYTLMLECWNEFPSRRPRFKDIHSRL 281
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
633-895 4.24e-54

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: 190.56  E-value: 4.24e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  633 RIHIEKIIGSGESGEVCYG-RLQVPGQRDVP-VAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMI 710
Cdd:cd05045     1 NLVLGKTLGEGEFGKVVKAtAFRLKGRAGYTtVAVKMLKENASSSELRDLLSEFNLLKQVNHPHVIKLYGACSQDGPLLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  711 VTEYMENGSLDAFLRT---------------------HDGQ--FTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLV 767
Cdd:cd05045    81 IVEYAKYGSLRSFLREsrkvgpsylgsdgnrnssyldNPDEraLTMGDLISFAWQISRGMQYLAEMKLVHRDLAARNVLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  768 -DGRlVCKVSDFGLSRALEDDpEAAYTTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDV 846
Cdd:cd05045   161 aEGR-KMKISDFGLSRDVYEE-DSYVKRSKGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIAPERL 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 341940659  847 ISSVEEGYRLPAPMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVLDALV 895
Cdd:cd05045   239 FNLLKTGYRMERPENCSEEMYNLMLTCWKQEPDKRPTFADISKELEKMM 287
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
627-899 3.50e-53

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: 188.35  E-value: 3.50e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  627 REIEASRIhieKIIGSGESGEVcYGRLQVPGQRDV--PVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTR 704
Cdd:cd05110     5 KETELKRV---KVLGSGAFGTV-YKGIWVPEGETVkiPVAIKILNETTGPKANVEFMDEALIMASMDHPHLVRLLGVCLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  705 GRLAMiVTEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRAL 784
Cdd:cd05110    81 PTIQL-VTQLMPHGCLLDYVHEHKDNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLARLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  785 EDDpEAAYTTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPR 864
Cdd:cd05110   160 EGD-EKEYNADGGKMPIKWMALECIHYRKFTHQSDVWSYGVTIWELMTFGGKPYDGIPTREIPDLLEKGERLPQPPICTI 238
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 341940659  865 ALHQLMLDCWHKDRAQRPRFAHVVSVLDALVHSPE 899
Cdd:cd05110   239 DVYMVMVKCWMIDADSRPKFKELAAEFSRMARDPQ 273
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
629-897 5.36e-53

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 187.17  E-value: 5.36e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  629 IEASRIHIEKIIGSGESGEV----CYGrlQVPGQRDVPVAIKALKAGyTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTR 704
Cdd:cd05093     2 IKRHNIVLKRELGEGAFGKVflaeCYN--LCPEQDKILVAVKTLKDA-SDNARKDFHREAELLTNLQHEHIVKFYGVCVE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  705 GRLAMIVTEYMENGSLDAFLRTH--------DGQ----FTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLV 772
Cdd:cd05093    79 GDPLIMVFEYMKHGDLNKFLRAHgpdavlmaEGNrpaeLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  773 CKVSDFGLSRaleDDPEAAYTTAGGK--IPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSV 850
Cdd:cd05093   159 VKIGDFGMSR---DVYSTDYYRVGGHtmLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECI 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 341940659  851 EEGYRLPAPMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVLDALVHS 897
Cdd:cd05093   236 TQGRVLQRPRTCPKEVYDLMLGCWQREPHMRLNIKEIHSLLQNLAKA 282
EphR_LBD_B4 cd10474
Ligand Binding Domain of Ephrin type-B Receptor 4; Ephrin receptors (EphRs) comprise the ...
30-202 2.30e-52

Ligand Binding Domain of Ephrin type-B Receptor 4; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EhpB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. EphB4 plays a role in osteoblast differentiation and has been linked to multiple myeloma. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine 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).


Pssm-ID: 198442  Cd Length: 180  Bit Score: 181.31  E-value: 2.30e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659   30 EVNLLDTSTIHGDWGWLTYP-AHG-WDSINEVDESFRPIHTYQVCNVMSP-NQNNWLRTNWVPRDGARRVYAEIKFTLRD 106
Cdd:cd10474     1 EETLLNTKLETADLKWVTYPqVDGqWEELSGLDEEQHSVRTYEVCDAQRAgGQAHWLRTGWVPRRGAVHVYATLRFTMLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  107 CNSIPGVLGTCKETFNLHYLESDRDLGAST----QESQFLKIDTIAADESFTGADLGVRRLKLNTEVRGVGPLSKRGFYL 182
Cdd:cd10474    81 CLSLPRAGRSCKETFTVFYYESDADTATAHtpawMENPYIKVDTVAAEHLTRKRPGAEATGKVNVKTLRLGPLSKAGFYL 160
                         170       180
                  ....*....|....*....|
gi 341940659  183 AFQDIGACLAILSLRIYYKK 202
Cdd:cd10474   161 AFQDQGACMALLSLHLFYKK 180
EphR_LBD_B6 cd10475
Ligand Binding Domain of Ephrin type-B Receptor 6; Ephrin receptors (EphRs) comprise the ...
33-202 4.90e-52

Ligand Binding Domain of Ephrin type-B Receptor 6; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EhpB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. EphB6, a kinase-defective member of this family, is downregulated in MDA-MB-231-breast cancer cells and myeloid cancers and upregulated in neuroblasoma and glioblastoma. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine 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).


Pssm-ID: 198443  Cd Length: 180  Bit Score: 180.51  E-value: 4.90e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659   33 LLDTSTIHGDWGWLTYPAHGWDSINEVDESFRPIHTYQVCNV--MSPNQNNWLRTNWVPRDGARRVYAEIKFTLRDCNSI 110
Cdd:cd10475     4 LLDTTGETSEIGWLTYPPGGWDEVSVLDDQRRLTRTFEVCNVaaQGPGQDNWLRTHFIERRGAHRVHVRLHFSVRDCASL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  111 PGVLGTCKETFNLHYLESDRDLGAST----QESQFLKIDTIAADESFTGADL-GVRRLKLNTEVRGVGPLSKRGFYLAFQ 185
Cdd:cd10475    84 GVPGGTCRETFTLYYRQADEPDEPADksewHEGPWTKVDTIAADESFPASLGkGGQGLQMNVKERSFGPLTQRGFYLAFQ 163
                         170
                  ....*....|....*..
gi 341940659  186 DIGACLAILSLRIYYKK 202
Cdd:cd10475   164 DSGACLSLVAVKVFFYK 180
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
635-896 7.75e-52

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 182.73  E-value: 7.75e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659    635 HIEKIIGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGV-VTRGRLAMiVTE 713
Cdd:smart00220    2 EILEKLGEGSFGKVYLARDKKTGKL---VAIKVIKKKKIKKDRERILREIKILKKLKHPNIVRLYDVfEDEDKLYL-VME 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659    714 YMENGSLDAFLRTHdGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALeDDPEAAYT 793
Cdd:smart00220   78 YCEGGDLFDLLKKR-GRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQL-DPGEKLTT 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659    794 TAGgkiPIRWTAPEAIAFRTFSSASDVWSFGVVMWEvLAYGERPYWNMTNQDVISSV--EEGYRLPAPM-GCPRALHQLM 870
Cdd:smart00220  156 FVG---TPEYMAPEVLLGKGYGKAVDIWSLGVILYE-LLTGKPPFPGDDQLLELFKKigKPKPPFPPPEwDISPEAKDLI 231
                           250       260
                    ....*....|....*....|....*.
gi 341940659    871 LDCWHKDRAQRPrfahvvSVLDALVH 896
Cdd:smart00220  232 RKLLVKDPEKRL------TAEEALQH 251
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
633-884 8.96e-52

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: 183.29  E-value: 8.96e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  633 RIHIEKIIGSGESGEVCYGRLQvpgQRD--VPVAIKALK-AGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLA- 708
Cdd:cd05075     1 KLALGKTLGEGEFGSVMEGQLN---QDDsvLKVAVKTMKiAICTRSEMEDFLSEAVCMKEFDHPNVMRLIGVCLQNTESe 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  709 -----MIVTEYMENGSLDAFL---RTHDGQFTI--VQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDF 778
Cdd:cd05075    78 gypspVVILPFMKHGDLHSFLlysRLGDCPVYLptQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  779 GLSRALEDdpeAAYTTAG--GKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRL 856
Cdd:cd05075   158 GLSKKIYN---GDYYRQGriSKMPVKWIAIESLADRVYTTKSDVWSFGVTMWEIATRGQTPYPGVENSEIYDYLRQGNRL 234
                         250       260
                  ....*....|....*....|....*...
gi 341940659  857 PAPMGCPRALHQLMLDCWHKDRAQRPRF 884
Cdd:cd05075   235 KQPPDCLDGLYELMSSCWLLNPKDRPSF 262
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
615-895 9.92e-52

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: 184.45  E-value: 9.92e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  615 YEEPGRAGRSFTREieasRIHIEKIIGSGESGEVCYGR-LQVPGQR---DVPVAIKALKAGYTERQRQDFLSEAAIMGQF 690
Cdd:cd05101    11 YELPEDPKWEFPRD----KLTLGKPLGEGCFGQVVMAEaVGIDKDKpkeAVTVAVKMLKDDATEKDLSDLVSEMEMMKMI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  691 -DHPNIIRLEGVVTRGRLAMIVTEYMENGSLDAFLRTH---------------DGQFTIVQLVGMLRGVGAGMRYLSDLG 754
Cdd:cd05101    87 gKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARrppgmeysydinrvpEEQMTFKDLVSCTYQLARGMEYLASQK 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  755 YIHRDLAARNVLVDGRLVCKVSDFGLSRALeDDPEAAYTTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYG 834
Cdd:cd05101   167 CIHRDLAARNVLVTENNVMKIADFGLARDI-NNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLG 245
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 341940659  835 ERPYWNMTNQDVISSVEEGYRLPAPMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVLDALV 895
Cdd:cd05101   246 GSPYPGIPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIL 306
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
629-894 2.05e-51

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkC is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkC to its ligand, neurotrophin 3 (NT3), results in receptor oligomerization and activation of the catalytic domain. TrkC is broadly expressed in the nervous system and in some non-neural tissues including the developing heart. NT3/TrkC signaling plays an important role in the innervation of the cardiac conducting system and the development of smooth muscle cells. Mice deficient with NT3 and TrkC have multiple heart defects. NT3/TrkC signaling is also critical for the development and maintenance of enteric neurons that are important for the control of gut peristalsis. The TrkC subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 182.52  E-value: 2.05e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  629 IEASRIHIEKIIGSGESGEV----CYGrlQVPGQRDVPVAIKALKAGyTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTR 704
Cdd:cd05094     2 IKRRDIVLKRELGEGAFGKVflaeCYN--LSPTKDKMLVAVKTLKDP-TLAARKDFQREAELLTNLQHDHIVKFYGVCGD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  705 GRLAMIVTEYMENGSLDAFLRTH---------------DGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDG 769
Cdd:cd05094    79 GDPLIMVFEYMKHGDLNKFLRAHgpdamilvdgqprqaKGELGLSQMLHIATQIASGMVYLASQHFVHRDLATRNCLVGA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  770 RLVCKVSDFGLSRaleDDPEAAYTTAGGK--IPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVI 847
Cdd:cd05094   159 NLLVKIGDFGMSR---DVYSTDYYRVGGHtmLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEVI 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 341940659  848 SSVEEGYRLPAPMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVLDAL 894
Cdd:cd05094   236 ECITQGRVLERPRVCPKEVYDIMLGCWQREPQQRLNIKEIYKILHAL 282
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
625-891 2.37e-50

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: 179.99  E-value: 2.37e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  625 FTREieasRIHIEKIIGSGESGEV----CYGRLQVPGQRDVpvAIKALKAGYTERQRQDFLSEAAIMGQF-DHPNIIRLE 699
Cdd:cd05054     4 FPRD----RLKLGKPLGRGAFGKViqasAFGIDKSATCRTV--AVKMLKEGATASEHKALMTELKILIHIgHHLNVVNLL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  700 GVVTR-GRLAMIVTEYMENGSLDAFLRT-------------------------HDGQFTIVQLVGMLRGVGAGMRYLSDL 753
Cdd:cd05054    78 GACTKpGGPLMVIVEFCKFGNLSNYLRSkreefvpyrdkgardveeeedddelYKEPLTLEDLICYSFQVARGMEFLASR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  754 GYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEaaYTTAG-GKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLA 832
Cdd:cd05054   158 KCIHRDLAARNILLSENNVVKICDFGLARDIYKDPD--YVRKGdARLPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFS 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  833 YGERPYWNMT-NQDVISSVEEGYRLPAPMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVL 891
Cdd:cd05054   236 LGASPYPGVQmDEEFCRRLKEGTRMRAPEYTTPEIYQIMLDCWHGEPKERPTFSELVEKL 295
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
639-894 3.24e-50

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: 178.70  E-value: 3.24e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  639 IIGSGESGEVCYGRLQVPGQRdVPVAIKALKAGYTERQRQDFLSEAAIMGQF-DHPNIIRLEGVVTRGRLAMIVTEYMEN 717
Cdd:cd05047     2 VIGEGNFGQVLKARIKKDGLR-MDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  718 GSLDAFLRTH-----DGQFTIV----------QLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSR 782
Cdd:cd05047    81 GNLLDFLRKSrvletDPAFAIAnstastlssqQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  783 AleddPEAAYTTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGC 862
Cdd:cd05047   161 G----QEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPLNC 236
                         250       260       270
                  ....*....|....*....|....*....|..
gi 341940659  863 PRALHQLMLDCWHKDRAQRPRFAHVVSVLDAL 894
Cdd:cd05047   237 DDEVYDLMRQCWREKPYERPSFAQILVSLNRM 268
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
628-895 5.29e-50

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: 179.05  E-value: 5.29e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  628 EIEASRIHIEKIIGSGESGEV----CYGRLQVPGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQF-DHPNIIRLEGVV 702
Cdd:cd05098     9 ELPRDRLVLGKPLGEGCFGQVvlaeAIGLDKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIgKHKNIINLLGAC 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  703 TRGRLAMIVTEYMENGSLDAFLRTH---------------DGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLV 767
Cdd:cd05098    89 TQDGPLYVIVEYASKGNLREYLQARrppgmeycynpshnpEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLV 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  768 DGRLVCKVSDFGLSRALEDDPEAAYTTaGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVI 847
Cdd:cd05098   169 TEDNVMKIADFGLARDIHHIDYYKKTT-NGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPGVPVEELF 247
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 341940659  848 SSVEEGYRLPAPMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVLDALV 895
Cdd:cd05098   248 KLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIV 295
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
628-889 2.82e-49

Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. IGF-1R is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the ligand (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, which stimulates downstream kinase activities and biological function. IGF-1R signaling is important in the differentiation, growth, and survival of normal cells. In cancer cells, where it is frequently overexpressed, IGF-1R is implicated in proliferation, the suppression of apoptosis, invasion, and metastasis. IGF-1R is being developed as a therapeutic target in cancer treatment. The IGF-1R 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: 133193 [Multi-domain]  Cd Length: 277  Bit Score: 175.99  E-value: 2.82e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  628 EIEASRIHIEKIIGSGESGEVCYGRLQ--VPGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRG 705
Cdd:cd05062     2 EVAREKITMSRELGQGSFGMVYEGIAKgvVKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  706 RLAMIVTEYMENGSLDAFLRTHDGQF---------TIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVS 776
Cdd:cd05062    82 QPTLVIMELMTRGDLKSYLRSLRPEMennpvqappSLKKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVKIG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  777 DFGLSRaleDDPEAAYTTAGGK--IPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGY 854
Cdd:cd05062   162 DFGMTR---DIYETDYYRKGGKglLPVRWMSPESLKDGVFTTYSDVWSFGVVLWEIATLAEQPYQGMSNEQVLRFVMEGG 238
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 341940659  855 RLPAPMGCPRALHQLMLDCWHKDRAQRPRFAHVVS 889
Cdd:cd05062   239 LLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEIIS 273
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
630-884 7.26e-49

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: 175.20  E-value: 7.26e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  630 EASRIHIEKIIGSGESGEVCYGRLQvPGQRDVP--VAIKALKAGyTERQRQDFLSEAAIMGQFDHPNIIRLEGVV-TRGR 706
Cdd:cd14205     2 EERHLKFLQQLGKGNFGSVEMCRYD-PLQDNTGevVAVKKLQHS-TEEHLRDFEREIEILKSLQHDNIVKYKGVCySAGR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  707 LAM-IVTEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALE 785
Cdd:cd14205    80 RNLrLIMEYLPYGSLRDYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  786 DDPEAAYTTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERP------YWNMTNQD---------VISSV 850
Cdd:cd14205   160 QDKEYYKVKEPGESPIFWYAPESLTESKFSVASDVWSFGVVLYELFTYIEKSksppaeFMRMIGNDkqgqmivfhLIELL 239
                         250       260       270
                  ....*....|....*....|....*....|....
gi 341940659  851 EEGYRLPAPMGCPRALHQLMLDCWHKDRAQRPRF 884
Cdd:cd14205   240 KNNGRLPRPDGCPDEIYMIMTECWNNNVNQRPSF 273
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
634-887 1.04e-48

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: 175.19  E-value: 1.04e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  634 IHIEKIIGSGESGEVCYGRLQVPGQRdVPVAIKALKAGYTERQRQDFLSEAAIMGQF-DHPNIIRLEGVV-TRGRLaMIV 711
Cdd:cd05089     4 IKFEDVIGEGNFGQVIKAMIKKDGLK-MNAAIKMLKEFASENDHRDFAGELEVLCKLgHHPNIINLLGACeNRGYL-YIA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  712 TEYMENGSLDAFLRT-------------HDGQFTIV--QLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVS 776
Cdd:cd05089    82 IEYAPYGNLLDFLRKsrvletdpafakeHGTASTLTsqQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSKIA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  777 DFGLSRAleddPEAAYTTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRL 856
Cdd:cd05089   162 DFGLSRG----EEVYVKKTMGRLPVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRM 237
                         250       260       270
                  ....*....|....*....|....*....|.
gi 341940659  857 PAPMGCPRALHQLMLDCWHKDRAQRPRFAHV 887
Cdd:cd05089   238 EKPRNCDDEVYELMRQCWRDRPYERPPFSQI 268
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
628-895 2.03e-48

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: 175.59  E-value: 2.03e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  628 EIEASRIHIEKIIGSGESGEVCYGRlQVPGQRDVP-----VAIKALKAGYTERQRQDFLSEAAIMGQF-DHPNIIRLEGV 701
Cdd:cd05100     8 ELSRTRLTLGKPLGEGCFGQVVMAE-AIGIDKDKPnkpvtVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  702 VTRGRLAMIVTEYMENGSLDAFLRTH---------------DGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVL 766
Cdd:cd05100    87 CTQDGPLYVLVEYASKGNLREYLRARrppgmdysfdtcklpEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  767 VDGRLVCKVSDFGLSRALEDDPEAAYTTaGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDV 846
Cdd:cd05100   167 VTEDNVMKIADFGLARDVHNIDYYKKTT-NGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEEL 245
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 341940659  847 ISSVEEGYRLPAPMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVLDALV 895
Cdd:cd05100   246 FKLLKEGHRMDKPANCTHELYMIMRECWHAVPSQRPTFKQLVEDLDRVL 294
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
633-891 3.02e-47

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: 170.32  E-value: 3.02e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  633 RIHIEKIIGSGESGEVCYGRLQVPGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLA-MIV 711
Cdd:cd05043     7 RVTLSDLLQEGTFGRIFHGILRDEKGKEEEVLVKTVKDHASEIQVTMLLQESSLLYGLSHQNLLPILHVCIEDGEKpMVL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  712 TEYMENGSLDAFLR-------THDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRAL 784
Cdd:cd05043    87 YPYMNWGNLKLFLQqcrlseaNNPQALSTQQLVHMALQIACGMSYLHRRGVIHKDIAARNCVIDDELQVKITDNALSRDL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  785 -EDDpeaaYTTAGGK--IPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMG 861
Cdd:cd05043   167 fPMD----YHCLGDNenRPIKWMSLESLVNKEYSSASDVWSFGVLLWELMTLGQTPYVEIDPFEMAAYLKDGYRLAQPIN 242
                         250       260       270
                  ....*....|....*....|....*....|
gi 341940659  862 CPRALHQLMLDCWHKDRAQRPRFAHVVSVL 891
Cdd:cd05043   243 CPDELFAVMACCWALDPEERPSFQQLVQCL 272
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
627-898 3.59e-47

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: 170.14  E-value: 3.59e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  627 REIEASRIhieKIIGSGESGEVCYGRLQVPGQR-DVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRG 705
Cdd:cd05111     5 KETELRKL---KVLGSGVFGTVHKGIWIPEGDSiKIPVAIKVIQDRSGRQSFQAVTDHMLAIGSLDHAYIVRLLGICPGA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  706 RLAMiVTEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRAL- 784
Cdd:cd05111    82 SLQL-VTQLLPLGSLLDHVRQHRGSLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQVQVADFGVADLLy 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  785 EDDPEAAYTTAggKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPR 864
Cdd:cd05111   161 PDDKKYFYSEA--KTPIKWMALESIHFGKYTHQSDVWSYGVTVWEMMTFGAEPYAGMRLAEVPDLLEKGERLAQPQICTI 238
                         250       260       270
                  ....*....|....*....|....*....|....
gi 341940659  865 ALHQLMLDCWHKDRAQRPRFAHVVSVLDALVHSP 898
Cdd:cd05111   239 DVYMVMVKCWMIDENIRPTFKELANEFTRMARDP 272
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
640-889 4.12e-46

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: 164.75  E-value: 4.12e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQrdvPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGS 719
Cdd:cd00180     1 LGKGSFGKVYKARDKETGK---KVAVKVIPKEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  720 LDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALeDDPEAAYTTAGGKI 799
Cdd:cd00180    78 LKDLLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDL-DSDDSLLKTTGGTT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  800 PIRWTAPEAIAFRTFSSASDVWSFGVVMWEVlaygerpywnmtnqdvissveegyrlpapmgcpRALHQLMLDCWHKDRA 879
Cdd:cd00180   157 PPYYAPPELLGGRYYGPKVDIWSLGVILYEL---------------------------------EELKDLIRRMLQYDPK 203
                         250
                  ....*....|
gi 341940659  880 QRPRFAHVVS 889
Cdd:cd00180   204 KRPSAKELLE 213
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
640-895 1.18e-44

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: 163.18  E-value: 1.18e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQRDVP-VAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTR--GRLAMIVTEYME 716
Cdd:cd05079    12 LGEGHFGKVELCRYDPEGDNTGEqVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEdgGNGIKLIMEFLP 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  717 NGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYTTAG 796
Cdd:cd05079    92 SGSLKEYLPRNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTVKDD 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  797 GKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPY--------------WNMTNQDVISSVEEGYRLPAPMGC 862
Cdd:cd05079   172 LDSPVFWYAPECLIQSKFYIASDVWSFGVTLYELLTYCDSESspmtlflkmigpthGQMTVTRLVRVLEEGKRLPRPPNC 251
                         250       260       270
                  ....*....|....*....|....*....|...
gi 341940659  863 PRALHQLMLDCWHKDRAQRPRFAHVVSVLDALV 895
Cdd:cd05079   252 PEEVYQLMRKCWEFQPSKRTTFQNLIEGFEAIL 284
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
628-891 1.47e-44

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: 163.43  E-value: 1.47e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  628 EIEASRIHIEKIIGSGESGEVCYGRLQVPGQRDV--PVAIKALKAGYTERQRQDFLSEAAIMGQF-DHPNIIRLEGVVTR 704
Cdd:cd05055    31 EFPRNNLSFGKTLGAGAFGKVVEATAYGLSKSDAvmKVAVKMLKPTAHSSEREALMSELKIMSHLgNHENIVNLLGACTI 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  705 GRLAMIVTEYMENGSLDAFLRTHDGQF-TIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRA 783
Cdd:cd05055   111 GGPILVITEYCCYGDLLNFLRRKRESFlTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTHGKIVKICDFGLARD 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  784 LEDDpeAAYTTAG-GKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNM-TNQDVISSVEEGYRLPAPMG 861
Cdd:cd05055   191 IMND--SNYVVKGnARLPVKWMAPESIFNCVYTFESDVWSYGILLWEIFSLGSNPYPGMpVDSKFYKLIKEGYRMAQPEH 268
                         250       260       270
                  ....*....|....*....|....*....|
gi 341940659  862 CPRALHQLMLDCWHKDRAQRPRFAHVVSVL 891
Cdd:cd05055   269 APAEIYDIMKTCWDADPLKRPTFKQIVQLI 298
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
629-895 3.23e-44

Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie2 is a receptor PTK (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie2 is expressed mainly in endothelial cells and hematopoietic stem cells. It is also found in a subset of tumor-associated monocytes and eosinophils. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. Tie2 signaling plays key regulatory roles in vascular integrity and quiescence, and in inflammation. The Tie2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 162.47  E-value: 3.23e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  629 IEASRIHIEKIIGSGESGEVCYGRLQVPGQRdVPVAIKALKAGYTERQRQDFLSEAAIMGQF-DHPNIIRLEGVVTRGRL 707
Cdd:cd05088     4 LEWNDIKFQDVIGEGNFGQVLKARIKKDGLR-MDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  708 AMIVTEYMENGSLDAFLRTH-----DGQFTIV----------QLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLV 772
Cdd:cd05088    83 LYLAIEYAPHGNLLDFLRKSrvletDPAFAIAnstastlssqQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  773 CKVSDFGLSRAleddPEAAYTTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEE 852
Cdd:cd05088   163 AKIADFGLSRG----QEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQ 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 341940659  853 GYRLPAPMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVLDALV 895
Cdd:cd05088   239 GYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRML 281
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
663-894 3.65e-44

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: 161.60  E-value: 3.65e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  663 VAIKALKAgYTERQRQDFLSEAAIMGQFDHPNIIRLEGVV-TRGRLAM-IVTEYMENGSLDAFLRTHDGQFTIVQLVGML 740
Cdd:cd05081    36 VAVKQLQH-SGPDQQRDFQREIQILKALHSDFIVKYRGVSyGPGRRSLrLVMEYLPSGCLRDFLQRHRARLDASRLLLYS 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  741 RGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYTTAGGKIPIRWTAPEAIAFRTFSSASDV 820
Cdd:cd05081   115 SQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLLPLDKDYYVVREPGQSPIFWYAPESLSDNIFSRQSDV 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  821 WSFGVVMWEVLAYGERP------YWNMTN-----QDVISSVE---EGYRLPAPMGCPRALHQLMLDCWHKDRAQRPRFAH 886
Cdd:cd05081   195 WSFGVVLYELFTYCDKScspsaeFLRMMGcerdvPALCRLLElleEGQRLPAPPACPAEVHELMKLCWAPSPQDRPSFSA 274

                  ....*...
gi 341940659  887 VVSVLDAL 894
Cdd:cd05081   275 LGPQLDML 282
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
628-897 4.92e-44

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: 163.23  E-value: 4.92e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  628 EIEASRIHIEKIIGSGESGEV----CYGRLQVPGQRDVpvAIKALKAGYTERQRQDFLSEAAIMGQFDHP-NIIRLEGVV 702
Cdd:cd05103     3 EFPRDRLKLGKPLGRGAFGQVieadAFGIDKTATCRTV--AVKMLKEGATHSEHRALMSELKILIHIGHHlNVVNLLGAC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  703 T-RGRLAMIVTEYMENGSLDAFLRTHDGQF-------------------------------------------------- 731
Cdd:cd05103    81 TkPGGPLMVIVEFCKFGNLSAYLRSKRSEFvpyktkgarfrqgkdyvgdisvdlkrrldsitssqssassgfveekslsd 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  732 ----------------TIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEaaYTTA 795
Cdd:cd05103   161 veeeeagqedlykdflTLEDLICYSFQVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDPD--YVRK 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  796 G-GKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNM-TNQDVISSVEEGYRLPAPMGCPRALHQLMLDC 873
Cdd:cd05103   239 GdARLPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFSLGASPYPGVkIDEEFCRRLKEGTRMRAPDYTTPEMYQTMLDC 318
                         330       340
                  ....*....|....*....|....
gi 341940659  874 WHKDRAQRPRFAHVVSVLDALVHS 897
Cdd:cd05103   319 WHGEPSQRPTFSELVEHLGNLLQA 342
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
633-883 7.79e-44

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: 159.67  E-value: 7.79e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  633 RIHIEKIIGSGESGEVCYGRLQVPGQrdvPVAIKALKAGYT--ERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMI 710
Cdd:cd14014     1 RYRLVRLLGRGGMGEVYRARDTLLGR---PVAIKVLRPELAedEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  711 VTEYMENGSLDAFLRTHdGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEA 790
Cdd:cd14014    78 VMEYVEGGSLADLLRER-GPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  791 AYTTAGGKIPirWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWNMTNQDVISSVEEGYRLPAP---MGCPRALH 867
Cdd:cd14014   157 QTGSVLGTPA--YMAPEQARGGPVDPRSDIYSLGVVLYELLT-GRPPFDGDSPAAVLAKHLQEAPPPPSplnPDVPPALD 233
                         250
                  ....*....|....*.
gi 341940659  868 QLMLDCWHKDRAQRPR 883
Cdd:cd14014   234 AIILRALAKDPEERPQ 249
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
628-894 1.29e-43

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: 162.09  E-value: 1.29e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  628 EIEASRIHIEKIIGSGESGEV----CYGRLQVPGQRdvPVAIKALKAGYTERQRQDFLSEAAIMGQFDHP-NIIRLEGVV 702
Cdd:cd14207     3 EFARERLKLGKSLGRGAFGKVvqasAFGIKKSPTCR--VVAVKMLKEGATASEYKALMTELKILIHIGHHlNVVNLLGAC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  703 TR-GRLAMIVTEYMENGSLDAFLRTHDGQF-------------------------------------------------- 731
Cdd:cd14207    81 TKsGGPLMVIVEYCKYGNLSNYLKSKRDFFvtnkdtslqeelikekkeaeptggkkkrlesvtssesfassgfqedksls 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  732 -----------------TIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEaaYTT 794
Cdd:cd14207   161 dveeeeedsgdfykrplTMEDLISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARDIYKNPD--YVR 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  795 AG-GKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMT-NQDVISSVEEGYRLPAPMGCPRALHQLMLD 872
Cdd:cd14207   239 KGdARLPLKWMAPESIFDKIYSTKSDVWSYGVLLWEIFSLGASPYPGVQiDEDFCSKLKEGIRMRAPEFATSEIYQIMLD 318
                         330       340
                  ....*....|....*....|..
gi 341940659  873 CWHKDRAQRPRFAHVVSVLDAL 894
Cdd:cd14207   319 CWQGDPNERPRFSELVERLGDL 340
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
638-896 1.44e-43

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: 160.07  E-value: 1.44e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEV---CYGrlqvPGQRDVP--VAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRG--RLAMI 710
Cdd:cd05080    10 RDLGEGHFGKVslyCYD----PTNDGTGemVAVKALKADCGPQHRSGWKQEIDILKTLYHENIVKYKGCCSEQggKSLQL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  711 VTEYMENGSLDAFLRTHdgQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEA 790
Cdd:cd05080    86 IMEYVPLGSLRDYLPKH--SIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAKAVPEGHEY 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  791 AYTTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGErPYWN---------------MTNQDVISSVEEGYR 855
Cdd:cd05080   164 YRVREDGDSPVFWYAPECLKEYKFYYASDVWSFGVTLYELLTHCD-SSQSpptkflemigiaqgqMTVVRLIELLERGER 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 341940659  856 LPAPMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVLDALVH 896
Cdd:cd05080   243 LPCPDKCPQEVYHLMKNCWETEASFRPTFENLIPILKTVHE 283
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
636-918 1.04e-41

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 160.18  E-value: 1.04e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIIGSGESGEVCYGRLQVPGQrdvPVAIKALKAGYT--ERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTE 713
Cdd:COG0515    11 ILRLLGRGGMGVVYLARDLRLGR---PVALKVLRPELAadPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLVME 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  714 YMENGSLDAFLRTHdGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYT 793
Cdd:COG0515    88 YVEGESLADLLRRR-GPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATLTQTG 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  794 TAGGKIPirWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWNMTNQDVISSVEEGYRLPAP---MGCPRALHQLM 870
Cdd:COG0515   167 TVVGTPG--YMAPEQARGEPVDPRSDVYSLGVTLYELLT-GRPPFDGDSPAELLRAHLREPPPPPSelrPDLPPALDAIV 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 341940659  871 LDCWHKDRAQrpRFAHVVSVLDALVHSPESLRATATVSRCPPPAFARS 918
Cdd:COG0515   244 LRALAKDPEE--RYQSAAELAAALRAVLRSLAAAAAAAAAAAAAAAAA 289
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
628-896 1.96e-40

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: 152.44  E-value: 1.96e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  628 EIEASRIHIEKIIGSGESGEV----CYGRLQvpGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQF-DHPNIIRLEGVV 702
Cdd:cd05102     3 EFPRDRLRLGKVLGHGAFGKVveasAFGIDK--SSSCETVAVKMLKEGATASEHKALMSELKILIHIgNHLNVVNLLGAC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  703 TR--GRLaMIVTEYMENGSLDAFLRTHDGQF------------------------------------------------- 731
Cdd:cd05102    81 TKpnGPL-MVIVEFCKYGNLSNFLRAKREGFspyrersprtrsqvrsmveavradrrsrqgsdrvasftestsstnqprq 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  732 ----------TIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEaaYTTAG-GKIP 800
Cdd:cd05102   160 evddlwqsplTMEDLICYSFQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDPD--YVRKGsARLP 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  801 IRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMT-NQDVISSVEEGYRLPAPMGCPRALHQLMLDCWHKDRA 879
Cdd:cd05102   238 LKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSLGASPYPGVQiNEEFCQRLKDGTRMRAPEYATPEIYRIMLSCWHGDPK 317
                         330
                  ....*....|....*..
gi 341940659  880 QRPRFAHVVSVLDALVH 896
Cdd:cd05102   318 ERPTFSDLVEILGDLLQ 334
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
640-892 2.71e-40

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: 148.80  E-value: 2.71e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLqvpgqRDVPVAIKALKAgyterqrqdfLSEAAI--MGQFDHPNIIRLEGVVTRGRLAMIVTEYMEN 717
Cdd:cd14059     1 LGSGAQGAVFLGKF-----RGEEVAVKKVRD----------EKETDIkhLRKLNHPNIIKFKGVCTQAPCYCILMEYCPY 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  718 GSLDAFLRthDGQ-FTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDpEAAYTTAG 796
Cdd:cd14059    66 GQLYEVLR--AGReITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKELSEK-STKMSFAG 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  797 gkiPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWNMTNQDVISSV-EEGYRLPAPMGCPRALHQLMLDCWH 875
Cdd:cd14059   143 ---TVAWMAPEVIRNEPCSEKVDIWSFGVVLWELLT-GEIPYKDVDSSAIIWGVgSNSLQLPVPSTCPDGFKLLMKQCWN 218
                         250
                  ....*....|....*..
gi 341940659  876 KDRAQRPRFAHVVSVLD 892
Cdd:cd14059   219 SKPRNRPSFRQILMHLD 235
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
639-894 2.84e-38

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: 143.69  E-value: 2.84e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  639 IIGSGESGEVCYGRLqvpgqRDVPVAIKALKAGYTE---RQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYM 715
Cdd:cd14061     1 VIGVGGFGKVYRGIW-----RGEEVAVKAARQDPDEdisVTLENVRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEYA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  716 ENGSLDAFLrthdGQFTI--VQLVGMLRGVGAGMRYLSDLG---YIHRDLAARNVLVDGRL--------VCKVSDFGLSR 782
Cdd:cd14061    76 RGGALNRVL----AGRKIppHVLVDWAIQIARGMNYLHNEApvpIIHRDLKSSNILILEAIenedlenkTLKITDFGLAR 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  783 aleddpEAAYTT---AGGKIPirWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWNMTNQDVISSVE-EGYRLPA 858
Cdd:cd14061   152 ------EWHKTTrmsAAGTYA--WMAPEVIKSSTFSKASDVWSYGVLLWELLT-GEVPYKGIDGLAVAYGVAvNKLTLPI 222
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 341940659  859 PMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVLDAL 894
Cdd:cd14061   223 PSTCPEPFAQLMKDCWQPDPHDRPSFADILKQLENI 258
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
624-897 7.89e-38

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: 143.25  E-value: 7.89e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  624 SFTREIEASRIHIEKIIGSGESGEVCYGRLQVPgqrdvpVAIKALK-AGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVV 702
Cdd:cd14149     4 SYYWEIEASEVMLSTRIGSGSFGTVYKGKWHGD------VAVKILKvVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  703 TRGRLAmIVTEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLS- 781
Cdd:cd14149    78 TKDNLA-IVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAt 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  782 -RALEDDPEAAYTTAGGkipIRWTAPEAIAFRT---FSSASDVWSFGVVMWEVLAyGERPYWNMTNQD-VISSVEEGYRL 856
Cdd:cd14149   157 vKSRWSGSQQVEQPTGS---ILWMAPEVIRMQDnnpFSFQSDVYSYGIVLYELMT-GELPYSHINNRDqIIFMVGRGYAS 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 341940659  857 P----APMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVLDALVHS 897
Cdd:cd14149   233 PdlskLYKNCPKAMKRLVADCIKKVKEERPLFPQILSSIELLQHS 277
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
640-892 2.56e-37

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: 140.99  E-value: 2.56e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQvpGqrdvPVAIKALK-AGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAmIVTEYMENG 718
Cdd:cd14062     1 IGSGSFGTVYKGRWH--G----DVAVKKLNvTDPTPSQLQAFKNEVAVLRKTRHVNILLFMGYMTKPQLA-IVTQWCEGS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  719 SLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRAleddpeAAYTTAGGK 798
Cdd:cd14062    74 SLYKHLHVLETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLATV------KTRWSGSQQ 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  799 IP-----IRWTAPEAIAFRT---FSSASDVWSFGVVMWEVLAyGERPYWNMTNQD-VISSVEEGYRLP----APMGCPRA 865
Cdd:cd14062   148 FEqptgsILWMAPEVIRMQDenpYSFQSDVYAFGIVLYELLT-GQLPYSHINNRDqILFMVGRGYLRPdlskVRSDTPKA 226
                         250       260
                  ....*....|....*....|....*..
gi 341940659  866 LHQLMLDCWHKDRAQRPRFAHVVSVLD 892
Cdd:cd14062   227 LRRLMEDCIKFQRDERPLFPQILASLE 253
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
640-894 7.86e-37

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: 140.10  E-value: 7.86e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQvpgqRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGS 719
Cdd:cd14066     1 IGSGGFGTVYKGVLE----NGTVVAVKRLNEMNCAASKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  720 LDAFLRTHDGQ--FTIVQLVGMLRGVGAGMRYL---SDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDpEAAYTT 794
Cdd:cd14066    77 LEDRLHCHKGSppLPWPQRLKIAKGIARGLEYLheeCPPPIIHGDIKSSNILLDEDFEPKLTDFGLARLIPPS-ESVSKT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  795 AGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPY----WNMTNQDVISSVEEGY----------RLPAPM 860
Cdd:cd14066   156 SAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLT-GKPAVdenrENASRKDLVEWVESKGkeeledildkRLVDDD 234
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 341940659  861 GCPR----ALHQLMLDCWHKDRAQRPRFAHVVSVLDAL 894
Cdd:cd14066   235 GVEEeeveALLRLALLCTRSDPSLRPSMKEVVQMLEKL 272
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
640-897 9.26e-37

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: 139.11  E-value: 9.26e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLqvpgqRDVPVAIKALKAgytERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGS 719
Cdd:cd14058     1 VGRGSFGVVCKARW-----RNQIVAVKIIES---ESEKKAFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGS 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  720 LDAFLRTHDGQ--FTIVQLVGMLRGVGAGMRYLSDL---GYIHRDLAARNVL-VDGRLVCKVSDFGLSRaledDPEAAYT 793
Cdd:cd14058    73 LYNVLHGKEPKpiYTAAHAMSWALQCAKGVAYLHSMkpkALIHRDLKPPNLLlTNGGTVLKICDFGTAC----DISTHMT 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  794 TAGGKIPirWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYgERPYWNMTNQD--VISSVEEGYRLPAPMGCPRALHQLML 871
Cdd:cd14058   149 NNKGSAA--WMAPEVFEGSKYSEKCDVFSWGIILWEVITR-RKPFDHIGGPAfrIMWAVHNGERPPLIKNCPKPIESLMT 225
                         250       260
                  ....*....|....*....|....*.
gi 341940659  872 DCWHKDRAQRPRFAHVVSVLDALVHS 897
Cdd:cd14058   226 RCWSKDPEKRPSMKEIVKIMSHLMQF 251
SAM_EPH-A8 cd09550
SAM domain of EPH-A8 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
932-994 1.47e-36

SAM domain of EPH-A8 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A8 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A8 receptors and appears to mediate cell-cell initiated signal transduction. EPH-A8 receptors are involved in ligand dependent (ephirin A2, A3, A5) regulation of cell adhesion and migration, and in ligand independent regulation of neurite outgrowth in neuronal cells. They perform signaling in kinase dependent and kinase independent manner. EPH-A8 receptors are known to interact with a number of different proteins including PI 3-kinase and AIDA1-like subfamily SAM repeat domain containing proteins. However other domains (not SAM) of EPH-A8 receptors are involved in these interactions.


Pssm-ID: 188949  Cd Length: 65  Bit Score: 131.91  E-value: 1.47e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341940659  932 LTVGDWLDSIRMGRYRDHFAAGGYSSLGMVLRMNAQDVRALGITLMGHQKKILGSIQTMRAQL 994
Cdd:cd09550     3 LSVDDWLDSIKMGRYKDHFAAGGYSSLGMVMRMNIEDIRRLGITLMGHQKKILTSIQVMRAQL 65
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
640-891 3.02e-36

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: 137.97  E-value: 3.02e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGqrdVPVAIKALKAGYT-ERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENG 718
Cdd:cd13978     1 LGSGGFGTVSKARHVSWF---GMVAIKCLHSSPNcIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  719 SLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDL--GYIHRDLAARNVLVDGRLVCKVSDFGLSR----ALEDDPEAAY 792
Cdd:cd13978    78 SLKSLLEREIQDVPWSLRFRIIHEIALGMNFLHNMdpPLLHHDLKPENILLDNHFHVKISDFGLSKlgmkSISANRRRGT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  793 TTAGGKipIRWTAPEAI--AFRTFSSASDVWSFGVVMWEVLAyGERPYWNMTNQDVI-SSVEEGYR-------LPAPMGC 862
Cdd:cd13978   158 ENLGGT--PIYMAPEAFddFNKKPTSKSDVYSFAIVIWAVLT-RKEPFENAINPLLImQIVSKGDRpslddigRLKQIEN 234
                         250       260
                  ....*....|....*....|....*....
gi 341940659  863 PRALHQLMLDCWHKDRAQRPRFAHVVSVL 891
Cdd:cd13978   235 VQELISLMIRCWDGNPDARPTFLECLDRL 263
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
638-895 7.24e-35

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: 137.28  E-value: 7.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVPGQRD--VPVAIKALKAGYTERQRQDFLSEAAIMGQF-DHPNIIRLEGVVTRGRLAMIVTEY 714
Cdd:cd05106    44 KTLGAGAFGKVVEATAFGLGKEDnvLRVAVKMLKASAHTDEREALMSELKILSHLgQHKNIVNLLGACTHGGPVLVITEY 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  715 MENGSLDAFLRTHDGQFTI------------------------------------------------------------- 733
Cdd:cd05106   124 CCYGDLLNFLRKKAETFLNfvmalpeisetssdyknitlekkyirsdsgfssqgsdtyvemrpvsssssqssdskdeedt 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  734 -----VQLVGMLR---GVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDpeAAYTTAG-GKIPIRWT 804
Cdd:cd05106   204 edswpLDLDDLLRfssQVAQGMDFLASKNCIHRDVAARNVLLTDGRVAKICDFGLARDIMND--SNYVVKGnARLPVKWM 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  805 APEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNM-TNQDVISSVEEGYRLPAPMGCPRALHQLMLDCWHKDRAQRPR 883
Cdd:cd05106   282 APESIFDCVYTVQSDVWSYGILLWEIFSLGKSPYPGIlVNSKFYKMVKRGYQMSRPDFAPPEIYSIMKMCWNLEPTERPT 361
                         330
                  ....*....|..
gi 341940659  884 FAHVVSVLDALV 895
Cdd:cd05106   362 FSQISQLIQRQL 373
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
634-894 1.99e-34

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: 132.83  E-value: 1.99e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  634 IHIEKIIGSGESGEVCYGRLQvpGQrdvpVAIKALKAGY-TERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAmIVT 712
Cdd:cd14150     2 VSMLKRIGTGSFGTVFRGKWH--GD----VAVKILKVTEpTPEQLQAFKNEMQVLRKTRHVNILLFMGFMTRPNFA-IIT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  713 EYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSrALEDDPEAAY 792
Cdd:cd14150    75 QWCEGSSLYRHLHVTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLA-TVKTRWSGSQ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  793 TTAGGKIPIRWTAPEAIAFRT---FSSASDVWSFGVVMWEVLAyGERPYWNMTNQD-VISSVEEGYRLP----APMGCPR 864
Cdd:cd14150   154 QVEQPSGSILWMAPEVIRMQDtnpYSFQSDVYAYGVVLYELMS-GTLPYSNINNRDqIIFMVGRGYLSPdlskLSSNCPK 232
                         250       260       270
                  ....*....|....*....|....*....|
gi 341940659  865 ALHQLMLDCWHKDRAQRPRFAHVVSVLDAL 894
Cdd:cd14150   233 AMKRLLIDCLKFKREERPLFPQILVSIELL 262
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
641-894 2.75e-34

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: 131.62  E-value: 2.75e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  641 GSGESGEVcYGRLQVPgqRDVPVAIKALkagyterqrQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSL 720
Cdd:cd14060     2 GGGSFGSV-YRAIWVS--QDKEVAVKKL---------LKIEKEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  721 DAFLRTHDGQ-FTIVQLVGMLRGVGAGMRYL---SDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEddpEAAYTTAG 796
Cdd:cd14060    70 FDYLNSNESEeMDMDQIMTWATDIAKGMHYLhmeAPVKVIHRDLKSRNVVIAADGVLKICDFGASRFHS---HTTHMSLV 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  797 GKIPirWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYgERPYWNMTNQDVI-SSVEEGYRLPAPMGCPRALHQLMLDCWH 875
Cdd:cd14060   147 GTFP--WMAPEVIQSLPVSETCDTYSYGVVLWEMLTR-EVPFKGLEGLQVAwLVVEKNERPTIPSSCPRSFAELMRRCWE 223
                         250
                  ....*....|....*....
gi 341940659  876 KDRAQRPRFAHVVSVLDAL 894
Cdd:cd14060   224 ADVKERPSFKQIIGILESM 242
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
639-894 7.14e-34

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: 131.31  E-value: 7.14e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  639 IIGSGESGEVCYGRLQvpGQRdvpVAIKALK-------AGYTERQRQdflsEAAIMGQFDHPNIIRLEGVVTRGRLAMIV 711
Cdd:cd14146     1 IIGVGGFGKVYRATWK--GQE---VAVKAARqdpdediKATAESVRQ----EAKLFSMLRHPNIIKLEGVCLEEPNLCLV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  712 TEYMENGSLDAFLRTHDGQFTIVQ--------LVGMLRGVGAGMRYLSDLGY---IHRDLAARNVLV--------DGRLV 772
Cdd:cd14146    72 MEFARGGTLNRALAAANAAPGPRRarripphiLVNWAVQIARGMLYLHEEAVvpiLHRDLKSSNILLlekiehddICNKT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  773 CKVSDFGLSRalEDDPEAAYTTAGgkiPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWNMTNQDVISSVE- 851
Cdd:cd14146   152 LKITDFGLAR--EWHRTTKMSAAG---TYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLT-GEVPYRGIDGLAVAYGVAv 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 341940659  852 EGYRLPAPMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVLDAL 894
Cdd:cd14146   226 NKLTLPIPSTCPEPFAKLMKECWEQDPHIRPSFALILEQLTAI 268
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
628-897 8.99e-34

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: 131.34  E-value: 8.99e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  628 EIEASRIHIEKIIGSGESGEVCYGRLQvpgqRDVPVAIKALKAGyTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRL 707
Cdd:cd14151     4 EIPDGQITVGQRIGSGSFGTVYKGKWH----GDVAVKMLNVTAP-TPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  708 AmIVTEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSrALEDD 787
Cdd:cd14151    79 A-IVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLA-TVKSR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  788 PEAAYTTAGGKIPIRWTAPEAIAFRT---FSSASDVWSFGVVMWEVLAyGERPYWNMTNQD-VISSVEEGYRLP----AP 859
Cdd:cd14151   157 WSGSHQFEQLSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDqIIFMVGRGYLSPdlskVR 235
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 341940659  860 MGCPRALHQLMLDCWHKDRAQRPRFAHVVSVLDALVHS 897
Cdd:cd14151   236 SNCPKAMKRLMAECLKKKRDERPLFPQILASIELLARS 273
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
628-892 1.57e-33

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: 133.49  E-value: 1.57e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  628 EIEASRIHIEKIIGSGESGEV----CYGRLQVPGQrdVPVAIKALKAGYTERQRQDFLSEAAIMGQF-DHPNIIRLEGVV 702
Cdd:cd05104    31 EFPRDRLRFGKTLGAGAFGKVveatAYGLAKADSA--MTVAVKMLKPSAHSTEREALMSELKVLSYLgNHINIVNLLGAC 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  703 TRGRLAMIVTEYMENGSLDAFLR--------------------------------------------------------- 725
Cdd:cd05104   109 TVGGPTLVITEYCCYGDLLNFLRrkrdsficpkfedlaeaalyrnllhqremacdslneymdmkpsvsyvvptkadkrrg 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  726 THDGQFT-----------------IVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDp 788
Cdd:cd05104   189 VRSGSYVdqdvtseileedelaldTEDLLSFSYQVAKGMEFLASKNCIHRDLAARNILLTHGRITKICDFGLARDIRND- 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  789 eAAYTTAG-GKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNM-TNQDVISSVEEGYRLPAPMGCPRAL 866
Cdd:cd05104   268 -SNYVVKGnARLPVKWMAPESIFECVYTFESDVWSYGILLWEIFSLGSSPYPGMpVDSKFYKMIKEGYRMDSPEFAPSEM 346
                         330       340
                  ....*....|....*....|....*.
gi 341940659  867 HQLMLDCWHKDRAQRPRFAHVVSVLD 892
Cdd:cd05104   347 YDIMRSCWDADPLKRPTFKQIVQLIE 372
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
628-894 1.72e-33

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: 130.55  E-value: 1.72e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  628 EIEASRIHIEKIIGSGESGEVCygRLQVPGQRdvpVAIKALKAGYTERQRQDFLS---EAAIMGQFDHPNIIRLEGVVTR 704
Cdd:cd14145     2 EIDFSELVLEEIIGIGGFGKVY--RAIWIGDE---VAVKAARHDPDEDISQTIENvrqEAKLFAMLKHPNIIALRGVCLK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  705 GRLAMIVTEYMENGSLDAFLRTHDGQFTIvqLVGMLRGVGAGMRYLSD---LGYIHRDLAARNVLVDGRL--------VC 773
Cdd:cd14145    77 EPNLCLVMEFARGGPLNRVLSGKRIPPDI--LVNWAVQIARGMNYLHCeaiVPVIHRDLKSSNILILEKVengdlsnkIL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  774 KVSDFGLSRALEDDPE--AAYTTAggkipirWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWNMTNQDVISSVE 851
Cdd:cd14145   155 KITDFGLAREWHRTTKmsAAGTYA-------WMAPEVIRSSMFSKGSDVWSYGVLLWELLT-GEVPFRGIDGLAVAYGVA 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 341940659  852 -EGYRLPAPMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVLDAL 894
Cdd:cd14145   227 mNKLSLPIPSTCPEPFARLMEDCWNPDPHSRPPFTNILDQLTAI 270
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
636-882 2.43e-33

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: 129.25  E-value: 2.43e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIIGSGESGEVCYGRLQVPGQRdvpVAIKALKAGyTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYM 715
Cdd:cd05122     4 ILEKIGKGGFGVVYKARHKKTGQI---VAIKKINLE-SKEKKESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEFC 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  716 ENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLV--DGRLvcKVSDFGLSRALEDDPeAAYT 793
Cdd:cd05122    80 SGGSLKDLLKNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLtsDGEV--KLIDFGLSAQLSDGK-TRNT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  794 TAGGKIpirWTAPEAIAFRTFSSASDVWSFGVVMWEvLAYGERPYWNMTNQ---DVISSVEEgYRLPAPMGCPRALHQLM 870
Cdd:cd05122   157 FVGTPY---WMAPEVIQGKPYGFKADIWSLGITAIE-MAEGKPPYSELPPMkalFLIATNGP-PGLRNPKKWSKEFKDFL 231
                         250
                  ....*....|..
gi 341940659  871 LDCWHKDRAQRP 882
Cdd:cd05122   232 KKCLQKDPEKRP 243
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
613-895 3.13e-33

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: 133.21  E-value: 3.13e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  613 HTYEEPGRAGRSFTREIEASRIHIEKIIGSGESGEVCYGRLQ--VPGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQF 690
Cdd:cd05107    18 YIYVDPMQLPYDSAWEMPRDNLVLGRTLGSGAFGRVVEATAHglSHSQSTMKVAVKMLKSTARSSEKQALMSELKIMSHL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  691 D-HPNIIRLEGVVTRGRLAMIVTEYMENGSL--------DAFLRTH-------------------------------DGQ 730
Cdd:cd05107    98 GpHLNIVNLLGACTKGGPIYIITEYCRYGDLvdylhrnkHTFLQYYldknrddgslisggstplsqrkshvslgsesDGG 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  731 F----------------------------------------------------------TIVQLVGMLRGVGAGMRYLSD 752
Cdd:cd05107   178 YmdmskdesadyvpmqdmkgtvkyadiessnyespydqylpsapertrrdtlinespalSYMDLVGFSYQVANGMEFLAS 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  753 LGYIHRDLAARNVLV-DGRLVcKVSDFGLSRALEDDpeAAYTTAGGK-IPIRWTAPEAIAFRTFSSASDVWSFGVVMWEV 830
Cdd:cd05107   258 KNCVHRDLAARNVLIcEGKLV-KICDFGLARDIMRD--SNYISKGSTfLPLKWMAPESIFNNLYTTLSDVWSFGILLWEI 334
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 341940659  831 LAYGERPYWNM-TNQDVISSVEEGYRLPAPMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVLDALV 895
Cdd:cd05107   335 FTLGGTPYPELpMNEQFYNAIKRGYRMAKPAHASDEIYEIMQKCWEEKFEIRPDFSQLVHLVGDLL 400
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
639-894 6.73e-33

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: 128.18  E-value: 6.73e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  639 IIGSGESGEVCYGRLqvpgqRDVPVAIKALK-------AGYTERQRQdflsEAAIMGQFDHPNIIRLEGVVTRGRLAMIV 711
Cdd:cd14148     1 IIGVGGFGKVYKGLW-----RGEEVAVKAARqdpdediAVTAENVRQ----EARLFWMLQHPNIIALRGVCLNPPHLCLV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  712 TEYMENGSLDaflRTHDGQFTIVQ-LVGMLRGVGAGMRYLSDLGY---IHRDLAARNVLVDGRL--------VCKVSDFG 779
Cdd:cd14148    72 MEYARGGALN---RALAGKKVPPHvLVNWAVQIARGMNYLHNEAIvpiIHRDLKSSNILILEPIenddlsgkTLKITDFG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  780 LSRALEDDPE--AAYTTAggkipirWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWNMTNQDVISSVE-EGYRL 856
Cdd:cd14148   149 LAREWHKTTKmsAAGTYA-------WMAPEVIRLSLFSKSSDVWSFGVLLWELLT-GEVPYREIDALAVAYGVAmNKLTL 220
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 341940659  857 PAPMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVLDAL 894
Cdd:cd14148   221 PIPSTCPEPFARLLEECWDPDPHGRPDFGSILKRLEDI 258
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
628-895 1.44e-32

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: 131.30  E-value: 1.44e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  628 EIEASRIHIEKIIGSGESGEV----CYGRLQvpGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFD-HPNIIRLEGVV 702
Cdd:cd05105    33 EFPRDGLVLGRILGSGAFGKVvegtAYGLSR--SQPVMKVAVKMLKPTARSSEKQALMSELKIMTHLGpHLNIVNLLGAC 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  703 TRGRLAMIVTEYMENGSL--------DAFLRTH----------------------------------------------- 727
Cdd:cd05105   111 TKSGPIYIITEYCFYGDLvnylhknrDNFLSRHpekpkkdldifginpadestrsyvilsfenkgdymdmkqadttqyvp 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  728 --------------------------------------DGQ--FTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLV 767
Cdd:cd05105   191 mleikeaskysdiqrsnydrpasykgsndsevknllsdDGSegLTTLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLL 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  768 DGRLVCKVSDFGLSRALEDDpeAAYTTAGGK-IPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNM-TNQD 845
Cdd:cd05105   271 AQGKIVKICDFGLARDIMHD--SNYVSKGSTfLPVKWMAPESIFDNLYTTLSDVWSYGILLWEIFSLGGTPYPGMiVDST 348
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 341940659  846 VISSVEEGYRLPAPMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVLDALV 895
Cdd:cd05105   349 FYNKIKSGYRMAKPDHATQEVYDIMVKCWNSEPEKRPSFLHLSDIVESLL 398
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
634-894 2.87e-32

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: 126.68  E-value: 2.87e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  634 IHIEKIIGSGESGEVCYGRLqvpgqRDVPVAIKALKAGYTER---QRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMI 710
Cdd:cd14147     5 LRLEEVIGIGGFGKVYRGSW-----RGELVAVKAARQDPDEDisvTAESVRQEARLFAMLAHPNIIALKAVCLEEPNLCL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  711 VTEYMENGSLDAFLRTHDGQFTIvqLVGMLRGVGAGMRYL---SDLGYIHRDLAARNVL----VDGR----LVCKVSDFG 779
Cdd:cd14147    80 VMEYAAGGPLSRALAGRRVPPHV--LVNWAVQIARGMHYLhceALVPVIHRDLKSNNILllqpIENDdmehKTLKITDFG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  780 LSRalEDDPEAAYTTAGgkiPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWNMTNQDVISSVE-EGYRLPA 858
Cdd:cd14147   158 LAR--EWHKTTQMSAAG---TYAWMAPEVIKASTFSKGSDVWSFGVLLWELLT-GEVPYRGIDCLAVAYGVAvNKLTLPI 231
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 341940659  859 PMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVLDAL 894
Cdd:cd14147   232 PSTCPEPFAQLMADCWAQDPHRRPDFASILQQLEAL 267
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
672-894 6.74e-32

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: 125.70  E-value: 6.74e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  672 YTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLS 751
Cdd:cd14154    29 FDEEAQRNFLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGGTLKDVLKDMARPLPWAQRVRFAKDIASGMAYLH 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  752 DLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAA--------------------YTTAGGKIpirWTAPEAIAF 811
Cdd:cd14154   109 SMNIIHRDLNSHNCLVREDKTVVVADFGLARLIVEERLPSgnmspsetlrhlkspdrkkrYTVVGNPY---WMAPEMLNG 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  812 RTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVL 891
Cdd:cd14154   186 RSYDEKVDIFSFGIVLCEIIGRVEADPDYLPRTKDFGLNVDSFREKFCAGCPPPFFKLAFLCCDLDPEKRPPFETLEEWL 265

                  ...
gi 341940659  892 DAL 894
Cdd:cd14154   266 EAL 268
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
633-882 8.23e-32

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: 125.03  E-value: 8.23e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  633 RIHIEKIIGSGESGEVCYGRLQVPGQRdvpVAIKALK-AGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIV 711
Cdd:cd06627     1 NYQLGDLIGRGAFGSVYKGLNLNTGEF---VAIKQISlEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYII 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  712 TEYMENGSLDAFLRTHdGQF----TIVQLVGMLRGVGagmrYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDD 787
Cdd:cd06627    78 LEYVENGSLASIIKKF-GKFpeslVAVYIYQVLEGLA----YLHEQGVIHRDIKGANILTTKDGLVKLADFGVATKLNEV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  788 PEAAYTTAGGkiPiRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWNMTnqdvisSVEEGYRL------PAPMG 861
Cdd:cd06627   153 EKDENSVVGT--P-YWMAPEVIEMSGVTTASDIWSVGCTVIELLT-GNPPYYDLQ------PMAALFRIvqddhpPLPEN 222
                         250       260
                  ....*....|....*....|.
gi 341940659  862 CPRALHQLMLDCWHKDRAQRP 882
Cdd:cd06627   223 ISPELRDFLLQCFQKDPTLRP 243
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
640-897 2.40e-31

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: 124.20  E-value: 2.40e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYTERQR-------------QDFLSEAAIMGQFDHPNIIRLEGVV---T 703
Cdd:cd14008     1 LGRGSFGKVKLALDTETGQL---YAIKIFNKSRLRKRRegkndrgkiknalDDVRREIAIMKKLDHPNIVRLYEVIddpE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  704 RGRLAMiVTEYMENGSLDAFLRTHDGQ-FTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSR 782
Cdd:cd14008    78 SDKLYL-VLEYCEGGPVMELDSGDRVPpLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGVSE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  783 ALEDDPEAAYTTAGgkipirwT----APEAIAF--RTFSS-ASDVWSFGVVMWeVLAYGERPYWNMTNQDVISSV-EEGY 854
Cdd:cd14008   157 MFEDGNDTLQKTAG-------TpaflAPELCDGdsKTYSGkAADIWALGVTLY-CLVFGRLPFNGDNILELYEAIqNQND 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 341940659  855 RLPAPMGCPRALHQLMLDCWHKDRAQRprfahvVSVLDALVHS 897
Cdd:cd14008   229 EFPIPPELSPELKDLLRRMLEKDPEKR------ITLKEIKEHP 265
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
638-844 2.52e-31

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: 123.78  E-value: 2.52e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYTERQRQDFL-SEAAIMGQFDHPNIIRLEGV-VTRGRLAmIVTEYM 715
Cdd:cd06606     6 ELLGKGSFGSVYLALNLDTGEL---MAVKEVELSGDSEEELEALeREIRILSSLKHPNIVRYLGTeRTENTLN-IFLEYV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  716 ENGSLDAFLRThDGQFTIvQLVGML-RGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDdpeaAYTT 794
Cdd:cd06606    82 PGGSLASLLKK-FGKLPE-PVVRKYtRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRLAE----IATG 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 341940659  795 AGGKIPI---RWTAPEAIAFRTFSSASDVWSFGVVMWEvLAYGERPYWNMTNQ 844
Cdd:cd06606   156 EGTKSLRgtpYWMAPEVIRGEGYGRAADIWSLGCTVIE-MATGKPPWSELGNP 207
SAM_EPH-R cd09488
SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH ...
933-990 7.48e-31

SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH (erythropoietin-producing hepatocyte) family of receptor tyrosine kinases is a C-terminal signal transduction module located in the cytoplasmic region of these receptors. SAM appears to mediate cell-cell initiated signal transduction via binding proteins to a conserved tyrosine that is phosphorylated. In some cases the SAM domain mediates homodimerization/oligomerization and plays a role in the clustering process necessary for signaling. EPH kinases are the largest family of receptor tyrosine kinases. They are classified into two groups based on their abilities to bind ephrin-A and ephrin-B ligands. The EPH receptors are involved in regulation of cell movement, shape, and attachment during embryonic development; they control cell-cell interactions in the vascular, nervous, epithelial, and immune systems, and in many tumors. They are potential molecular markers for cancer diagnostics and potential targets for cancer therapy.


Pssm-ID: 188887  Cd Length: 61  Bit Score: 115.41  E-value: 7.48e-31
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 341940659  933 TVGDWLDSIRMGRYRDHFAAGGYSSLGMVLRMNAQDVRALGITLMGHQKKILGSIQTM 990
Cdd:cd09488     4 SVGEWLESIKMGRYKENFTAAGYTSLDAVAQMTAEDLTRLGVTLVGHQKKILNSIQAL 61
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
636-882 8.07e-30

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: 119.49  E-value: 8.07e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIIGSGESGEVCYGRLQVPGQrdvPVAIKALK-AGYTERQRQDFLSEAAIMGQFDHPNIIR-LEGVVTRGRLaMIVTE 713
Cdd:cd08215     4 KIRVIGKGSFGSAYLVRRKSDGK---LYVLKEIDlSNMSEKEREEALNEVKLLSKLKHPNIVKyYESFEENGKL-CIVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  714 YMENGSLDAFL--RTHDGQ-FTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEA 790
Cdd:cd08215    80 YADGGDLAQKIkkQKKKGQpFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKVLESTTDL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  791 AYTTAGgkipirwT----APEAIAFRTFSSASDVWSFGVVMWEVLAyGERPY--WNMtnQDVISSVEEGYRLPAPMGCPR 864
Cdd:cd08215   160 AKTVVG-------TpyylSPELCENKPYNYKSDIWALGCVLYELCT-LKHPFeaNNL--PALVYKIVKGQYPPIPSQYSS 229
                         250
                  ....*....|....*...
gi 341940659  865 ALHQLMLDCWHKDRAQRP 882
Cdd:cd08215   230 ELRDLVNSMLQKDPEKRP 247
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
640-894 4.10e-29

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: 117.25  E-value: 4.10e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLqvpgqRDVPVAIKALKA-GYTERQRQD-FLSEAAIMGQFDHPNIIRLEGVVTR--GRLAmIVTEYM 715
Cdd:cd14064     1 IGSGSFGKVYKGRC-----RNKIVAIKRYRAnTYCSKSDVDmFCREVSILCRLNHPCVIQFVGACLDdpSQFA-IVTQYV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  716 ENGSLdaFLRTHdGQFTIVQLVGMLR---GVGAGMRYLSDLGY--IHRDLAARNVLV--DGRLVckVSDFGLSRALEDDP 788
Cdd:cd14064    75 SGGSL--FSLLH-EQKRVIDLQSKLIiavDVAKGMEYLHNLTQpiIHRDLNSHNILLyeDGHAV--VADFGESRFLQSLD 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  789 EAAYTTAGGKipIRWTAPEAIAFRT-FSSASDVWSFGVVMWEVLAyGERPYWNMtnQDVISSVEEGY---RLPAPMGCPR 864
Cdd:cd14064   150 EDNMTKQPGN--LRWMAPEVFTQCTrYSIKADVFSYALCLWELLT-GEIPFAHL--KPAAAAADMAYhhiRPPIGYSIPK 224
                         250       260       270
                  ....*....|....*....|....*....|
gi 341940659  865 ALHQLMLDCWHKDRAQRPRFAHVVSVLDAL 894
Cdd:cd14064   225 PISSLLMRGWNAEPESRPSFVEIVALLEPC 254
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
674-894 1.14e-28

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: 116.58  E-value: 1.14e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  674 ERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLDAFLRTHDgQFTIVQLVGMLRGVGAGMRYLSDL 753
Cdd:cd14222    31 EETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTLKDFLRADD-PFPWQQKVSFAKGIASGMAYLHSM 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  754 GYIHRDLAARNVLV--DGRLVckVSDFGLSRALEDD-----PEAA---------------YTTAGGKIpirWTAPEAIAF 811
Cdd:cd14222   110 SIIHRDLNSHNCLIklDKTVV--VADFGLSRLIVEEkkkppPDKPttkkrtlrkndrkkrYTVVGNPY---WMAPEMLNG 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  812 RTFSSASDVWSFGVVMWEVLA--YGErPYWNMTNQDVISSVEEGYRLPAPMGCPRALHQLMLDCWHKDRAQRPRFAHVVS 889
Cdd:cd14222   185 KSYDEKVDIFSFGIVLCEIIGqvYAD-PDCLPRTLDFGLNVRLFWEKFVPKDCPPAFFPLAAICCRLEPDSRPAFSKLED 263

                  ....*
gi 341940659  890 VLDAL 894
Cdd:cd14222   264 SFEAL 268
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
646-894 1.98e-28

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: 115.44  E-value: 1.98e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  646 GEVCYGR-LQVPGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLDAFL 724
Cdd:cd14221     2 GKGCFGQaIKVTHRETGEVMVMKELIRFDEETQRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLRGII 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  725 RTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLV--DGRLVckVSDFGLSRALEDDPEAAYTTAGGKIPIR 802
Cdd:cd14221    82 KSMDSHYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVreNKSVV--VADFGLARLMVDEKTQPEGLRSLKKPDR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  803 -----------WTAPEAIAFRTFSSASDVWSFGVVMWEVLA-YGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALHQLM 870
Cdd:cd14221   160 kkrytvvgnpyWMAPEMINGRSYDEKVDVFSFGIVLCEIIGrVNADPDYLPRTMDFGLNVRGFLDRYCPPNCPPSFFPIA 239
                         250       260
                  ....*....|....*....|....
gi 341940659  871 LDCWHKDRAQRPRFAHVVSVLDAL 894
Cdd:cd14221   240 VLCCDLDPEKRPSFSKLEHWLETL 263
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
640-882 2.04e-28

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Aatyk subfamily is also referred to as the lemur tyrosine kinase (Lmtk) subfamily. It consists of Aatyk1 (Lmtk1), Aatyk2 (Lmtk2, Brek), Aatyk3 (Lmtk3), and similar proteins. Aatyk proteins are mostly receptor PTKs (RTKs) containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk1 does not contain a transmembrane segment and is a cytoplasmic (or nonreceptor) kinase. Aatyk proteins are classified as PTKs based on overall sequence similarity and the phylogenetic tree. However, analysis of catalytic residues suggests that Aatyk proteins may be multispecific kinases, functioning also as serine/threonine kinases. They are involved in neural differentiation, nerve growth factor (NGF) signaling, apoptosis, and spermatogenesis. The Aatyk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270638 [Multi-domain]  Cd Length: 269  Bit Score: 115.76  E-value: 2.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQvPGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGS 719
Cdd:cd05042     3 IGNGWFGKVLLGEIY-SGTSVAQVVVKELKASANPKEQDTFLKEGQPYRILQHPNILQCLGQCVEAIPYLLVMEFCDLGD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  720 LDAFLRTH------DGQFTIVQLVGMlrGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGL--SRALEDdpeaA 791
Cdd:cd05042    82 LKAYLRSErehergDSDTRTLQRMAC--EVAAGLAHLHKLNFVHSDLALRNCLLTSDLTVKIGDYGLahSRYKED----Y 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  792 YTTAGGK-IPIRWTAPEAIA-----FRTF--SSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSV--EEGYRLPAP-M 860
Cdd:cd05042   156 IETDDKLwFPLRWTAPELVTefhdrLLVVdqTKYSNIWSLGVTLWELFENGAQPYSNLSDLDVLAQVvrEQDTKLPKPqL 235
                         250       260
                  ....*....|....*....|....
gi 341940659  861 GCPRA--LHQLMLDCWhKDRAQRP 882
Cdd:cd05042   236 ELPYSdrWYEVLQFCW-LSPEQRP 258
Pkinase pfam00069
Protein kinase domain;
635-889 6.58e-28

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 112.34  E-value: 6.58e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659   635 HIEKIIGSGESGEVCYGRLQVPGQrdvPVAIKAL-KAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTE 713
Cdd:pfam00069    2 EVLRKLGSGSFGTVYKAKHRDTGK---IVAIKKIkKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659   714 YMENGSLDAFLRTHdGQFTivqlvgmlrgvgagMRYLSDLgyihrdlaARNVLvdgrlvckvsdfglsRALEDDPEaaYT 793
Cdd:pfam00069   79 YVEGGSLFDLLSEK-GAFS--------------EREAKFI--------MKQIL---------------EGLESGSS--LT 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659   794 TAGGKipIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWNMTNQDVISSV--EEGYRLPAPMGCPRALHQLML 871
Cdd:pfam00069  119 TFVGT--PWYMAPEVLGGNPYGPKVDVWSLGCILYELLT-GKPPFPGINGNEIYELIidQPYAFPELPSNLSEEAKDLLK 195
                          250
                   ....*....|....*...
gi 341940659   872 DCWHKDRAQRPRFAHVVS 889
Cdd:pfam00069  196 KLLKKDPSKRLTATQALQ 213
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
666-891 1.85e-27

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: 112.87  E-value: 1.85e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  666 KALKAGYTER--QRQDfLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLDAFLRTHDGQFTIVQLVGMLRGV 743
Cdd:cd13992    28 VAIKHITFSRteKRTI-LQELNQLKELVHDNLNKFIGICINPPNIAVVTEYCTRGSLQDVLLNREIKMDWMFKSSFIKDI 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  744 GAGMRYL--SDLGYiHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYTTAGGKIPIRWTAPEAIAFRTF----SSA 817
Cdd:cd13992   107 VKGMNYLhsSSIGY-HGRLKSSNCLVDSRWVVKLTDFGLRNLLEEQTNHQLDEDAQHKKLLWTAPELLRGSLLevrgTQK 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  818 SDVWSFGVVMWEVLAYgERPYWNMTN-QDVISSVEEGYRLPAP------MGCPRALHQLMLDCWHKDRAQRPRFAHVVSV 890
Cdd:cd13992   186 GDVYSFAIILYEILFR-SDPFALEREvAIVEKVISGGNKPFRPelavllDEFPPRLVLLVKQCWAENPEKRPSFKQIKKT 264

                  .
gi 341940659  891 L 891
Cdd:cd13992   265 L 265
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
641-891 2.52e-27

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They 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. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. In the case of Jak2, the presumed pseudokinase (repeat 1) domain exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. 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 serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270633 [Multi-domain]  Cd Length: 259  Bit Score: 112.19  E-value: 2.52e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  641 GSGESGEVCYGRLQVPGQ---RDVPVAIKALKAGYTERQrQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMiVTEYMEN 717
Cdd:cd05037     8 GQGTFTNIYDGILREVGDgrvQEVEVLLKVLDSDHRDIS-ESFFETASLMSQISHKHLVKLYGVCVADENIM-VQEYVRY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  718 GSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLV------DGRLVCKVSDFGLSRALEDDPEAA 791
Cdd:cd05037    86 GPLDKYLRRMGNNVPLSWKLQVAKQLASALHYLEDKKLIHGNVRGRNILLaregldGYPPFIKLSDPGVPITVLSREERV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  792 yttaggkIPIRWTAPEAI--AFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPraLHQL 869
Cdd:cd05037   166 -------DRIPWIAPECLrnLQANLTIAADKWSFGTTLWEICSGGEEPLSALSSQEKLQFYEDQHQLPAPDCAE--LAEL 236
                         250       260
                  ....*....|....*....|..
gi 341940659  870 MLDCWHKDRAQRPRFAHVVSVL 891
Cdd:cd05037   237 IMQCWTYEPTKRPSFRAILRDL 258
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
636-882 4.56e-27

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: 111.07  E-value: 4.56e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIIGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYTERQRQDFL-SEAAIMGQFDHPNIIRLEGVV-TRGRLAMiVTE 713
Cdd:cd14003     4 LGKTLGEGSFGKVKLARHKLTGEK---VAIKIIDKSKLKEEIEEKIkREIEIMKLLNHPNIIKLYEVIeTENKIYL-VME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  714 YMENGSLDAFLRTHDG------QFTIVQLVgmlrgvgAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDD 787
Cdd:cd14003    80 YASGGELFDYIVNNGRlsedeaRRFFQQLI-------SAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEFRGG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  788 pEAAYTTAGGkipIRWTAPEAIAFRTF-SSASDVWSFGVVMWeVLAYGERPyWNMTNQDVISS--VEEGYRLPA--PMGC 862
Cdd:cd14003   153 -SLLKTFCGT---PAYAAPEVLLGRKYdGPKADVWSLGVILY-AMLTGYLP-FDDDNDSKLFRkiLKGKYPIPShlSPDA 226
                         250       260
                  ....*....|....*....|
gi 341940659  863 PRALHQLMldcwHKDRAQRP 882
Cdd:cd14003   227 RDLIRRML----VVDPSKRI 242
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
637-831 6.24e-27

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: 111.89  E-value: 6.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  637 EKI--IGSGESGEVCYGRLQVPGQRdvpVAIKALKagyTERQRQDF----LSEAAIMGQFDHPNIIRLEGVVT------- 703
Cdd:cd07840     2 EKIaqIGEGTYGQVYKARNKKTGEL---VALKKIR---MENEKEGFpitaIREIKLLQKLDHPNVVRLKEIVTskgsaky 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  704 RGRLAMiVTEYMENgSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRA 783
Cdd:cd07840    76 KGSIYM-VFEYMDH-DLTGLLDNPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLARP 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 341940659  784 LEDDPEAAYTTaggKIPIRW-TAPEAIAFRT-FSSASDVWSFGVVMWEVL 831
Cdd:cd07840   154 YTKENNADYTN---RVITLWyRPPELLLGATrYGPEVDMWSVGCILAELF 200
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
640-887 6.65e-27

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk3, also called lemur tyrosine kinase 3 (Lmtk3) is a receptor kinase containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. The function of Aatyk3 is still unknown. The Aatyk3 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: 271108 [Multi-domain]  Cd Length: 276  Bit Score: 111.58  E-value: 6.65e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRL---QVPGQrdvpVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYME 716
Cdd:cd14206     5 IGNGWFGKVILGEIfsdYTPAQ----VVVKELRVSAGPLEQRKFISEAQPYRSLQHPNILQCLGLCTETIPFLLIMEFCQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  717 NGSLDAFLRTH---DGQF------TIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRalEDD 787
Cdd:cd14206    81 LGDLKRYLRAQrkaDGMTpdlptrDLRTLQRMAYEITLGLLHLHKNNYIHSDLALRNCLLTSDLTVRIGDYGLSH--NNY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  788 PEAAYTTAGGK-IPIRWTAPE-------AIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSV--EEGYRLP 857
Cdd:cd14206   159 KEDYYLTPDRLwIPLRWVAPElldelhgNLIVVDQSKESNVWSLGVTIWELFEFGAQPYRHLSDEEVLTFVvrEQQMKLA 238
                         250       260       270
                  ....*....|....*....|....*....|...
gi 341940659  858 AP-MGCPRA--LHQLMLDCWhKDRAQRPRFAHV 887
Cdd:cd14206   239 KPrLKLPYAdyWYEIMQSCW-LPPSQRPSVEEL 270
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
635-853 2.58e-26

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: 109.10  E-value: 2.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  635 HIEKIIGSGESGEVCYGRLQVPGQRdvpVAIKAL-KAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGV-VTRGRLAmIVT 712
Cdd:cd05117     3 ELGKVLGRGSFGVVRLAVHKKTGEE---YAVKIIdKKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVfEDDKNLY-LVM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  713 EYMENGSLdaFLRTHD-GQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGR---LVCKVSDFGLSRALEDDp 788
Cdd:cd05117    79 ELCTGGEL--FDRIVKkGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKdpdSPIKIIDFGLAKIFEEG- 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 341940659  789 EAAYTTAGgkipirwT----APEAIAFRTFSSASDVWSFGVVMWeVLAYGERPYWNMTNQDVISSVEEG 853
Cdd:cd05117   156 EKLKTVCG-------TpyyvAPEVLKGKGYGKKCDIWSLGVILY-ILLCGYPPFYGETEQELFEKILKG 216
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
640-876 2.71e-26

Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk2 is a member of the Aatyk subfamily of proteins, which are receptor kinases containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk2 is also called lemur tyrosine kinase 2 (Lmtk2) or brain-enriched kinase (Brek). It is expressed at high levels in early postnatal brain, and has been shown to play a role in nerve growth factor (NGF) signaling. Studies with knockout mice reveal that Aatyk2 is essential for late stage spermatogenesis. Although it is classified as a PTK based on sequence similarity and the phylogenetic tree, Aatyk2 has been functionally characterized as a serine/threonine kinase. The Aatyk2 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: 270669 [Multi-domain]  Cd Length: 271  Bit Score: 109.57  E-value: 2.71e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVpGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGS 719
Cdd:cd05086     5 IGNGWFGKVLLGEIYT-GTSVARVVVKELKASANPKEQDDFLQQGEPYYILQHPNILQCVGQCVEAIPYLLVFEFCDLGD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  720 LDAFLRTHD----GQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGL--SRALEDDPEaayT 793
Cdd:cd05086    84 LKTYLANQQeklrGDSQIMLLQRMACEIAAGLAHMHKHNFLHSDLALRNCYLTSDLTVKVGDYGIgfSRYKEDYIE---T 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  794 TAGGKIPIRWTAPEAIAFR-------TFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSV--EEGYRLPAPMgcpr 864
Cdd:cd05086   161 DDKKYAPLRWTAPELVTSFqdgllaaEQTKYSNIWSLGVTLWELFENAAQPYSDLSDREVLNHVikERQVKLFKPH---- 236
                         250
                  ....*....|..
gi 341940659  865 aLHQLMLDCWHK 876
Cdd:cd05086   237 -LEQPYSDRWYE 247
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
676-891 2.85e-26

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: 108.73  E-value: 2.85e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  676 QRQDFLSEAAIMGQFDHPNIIRLEGV-VTRGRLAMIvTEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLG 754
Cdd:cd14065    31 EQRSFLKEVKLMRRLSHPNILRFIGVcVKDNKLNFI-TEYVNGGTLEELLKSMDEQLPWSQRVSLAKDIASGMAYLHSKN 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  755 YIHRDLAARNVLV---DGRLVCKVSDFGLSRALEDDPEA------AYTTAGGKIpirWTAPEAIAFRTFSSASDVWSFGV 825
Cdd:cd14065   110 IIHRDLNSKNCLVreaNRGRNAVVADFGLAREMPDEKTKkpdrkkRLTVVGSPY---WMAPEMLRGESYDEKVDVFSFGI 186
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 341940659  826 VMWEVLAY-----GERPYWNMTNQDVissveEGYRLPAPMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVL 891
Cdd:cd14065   187 VLCEIIGRvpadpDYLPRTMDFGLDV-----RAFRTLYVPDCPPSFLPLAIRCCQLDPEKRPSFVELEHHL 252
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
639-877 1.54e-25

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: 108.22  E-value: 1.54e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  639 IIGSGESGEVCYGRLQvpgqrDVPVAIKAlkagYTERQRQDFLSEAAIMGQF--DHPNIIRL----EGVVTRGRLA-MIV 711
Cdd:cd14054     2 LIGQGRYGTVWKGSLD-----ERPVAVKV----FPARHRQNFQNEKDIYELPlmEHSNILRFigadERPTADGRMEyLLV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  712 TEYMENGSLDAFLRTHDGQFTivQLVGMLRGVGAGMRYL-SDL--------GYIHRDLAARNVLVDGRLVCKVSDFGLSR 782
Cdd:cd14054    73 LEYAPKGSLCSYLRENTLDWM--SSCRMALSLTRGLAYLhTDLrrgdqykpAIAHRDLNSRNVLVKADGSCVICDFGLAM 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  783 AL----------EDDPEAAYTTAGgkiPIRWTAPE----AIAFRTFSSA---SDVWSFGVVMWEV--------------- 830
Cdd:cd14054   151 VLrgsslvrgrpGAAENASISEVG---TLRYMAPEvlegAVNLRDCESAlkqVDVYALGLVLWEIamrcsdlypgesvpp 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 341940659  831 --LAYGERPYWNMTNQDVISSVEEGYR---LPAPMGC----PRALHQLMLDCWHKD 877
Cdd:cd14054   228 yqMPYEAELGNHPTFEDMQLLVSREKArpkFPDAWKEnslaVRSLKETIEDCWDQD 283
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
640-838 1.72e-25

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: 106.54  E-value: 1.72e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQrdvPVAIKAL-KAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENG 718
Cdd:cd14009     1 IGRGSFATVWKGRHKQTGE---VVAIKEIsRKKLNKKLQENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  719 SLDAFLRTHDGQFTIVQLVgMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGR---LVCKVSDFGLSRALEDDPEAAyTTA 795
Cdd:cd14009    78 DLSQYIRKRGRLPEAVARH-FMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSgddPVLKIADFGFARSLQPASMAE-TLC 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 341940659  796 GGkiPIrWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPY 838
Cdd:cd14009   156 GS--PL-YMAPEILQFQKYDAKADLWSVGAILFEMLV-GKPPF 194
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
638-882 3.21e-25

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk1 (or simply Aatyk) is also called lemur tyrosine kinase 1 (Lmtk1). It is a cytoplasmic (or nonreceptor) kinase containing a long C-terminal region. The expression of Aatyk1 is upregulated during growth arrest and apoptosis in myeloid cells. Aatyk1 has been implicated in neural differentiation, and is a regulator of the Na-K-2Cl cotransporter, a membrane protein involved in cell proliferation and survival, epithelial transport, and blood pressure control. The Aatyk1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 106.23  E-value: 3.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVpGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMEN 717
Cdd:cd05087     3 KEIGHGWFGKVFLGEVNS-GLSSTQVVVKELKASASVQDQMQFLEEAQPYRALQHTNLLQCLAQCAEVTPYLLVMEFCPL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  718 GSLDAFLRTHDGQFTI----VQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRA-LEDDpeaAY 792
Cdd:cd05087    82 GDLKGYLRSCRAAESMapdpLTLQRMACEVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGLSHCkYKED---YF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  793 TTAGGK-IPIRWTAPEAI-------AFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSV--EEGYRLPAP--- 859
Cdd:cd05087   159 VTADQLwVPLRWIAPELVdevhgnlLVVDQTKQSNVWSLGVTIWELFELGNQPYRHYSDRQVLTYTvrEQQLKLPKPqlk 238
                         250       260
                  ....*....|....*....|...
gi 341940659  860 MGCPRALHQLMLDCWHKDRaQRP 882
Cdd:cd05087   239 LSLAERWYEVMQFCWLQPE-QRP 260
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
640-894 4.07e-25

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: 105.64  E-value: 4.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQrdvpvaIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGV-VTRGRLAMIvTEYMENG 718
Cdd:cd14155     1 IGSGFFSEVYKVRHRTSGQ------VMALKMNTLSSNRANMLREVQLMNRLSHPNILRFMGVcVHQGQLHAL-TEYINGG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  719 SLDAFLRThDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLV---DGRLVCKVSDFGLSRALEDdpeaaYTTA 795
Cdd:cd14155    74 NLEQLLDS-NEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIkrdENGYTAVVGDFGLAEKIPD-----YSDG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  796 GGKIPI----RWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGErpywnmTNQDVISSVEE-GYRLPAPMG----CPRAL 866
Cdd:cd14155   148 KEKLAVvgspYWMAPEVLRGEPYNEKADVFSYGIILCEIIARIQ------ADPDYLPRTEDfGLDYDAFQHmvgdCPPDF 221
                         250       260
                  ....*....|....*....|....*...
gi 341940659  867 HQLMLDCWHKDRAQRPRFAHVVSVLDAL 894
Cdd:cd14155   222 LQLAFNCCNMDPKSRPSFHDIVKTLEEI 249
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
638-838 4.24e-24

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: 103.06  E-value: 4.24e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVPGQrdvPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMEN 717
Cdd:cd06623     7 KVLGQGSSGVVYKVRHKPTGK---IYALKKIHVDGDEEFRKQLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLEYMDG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  718 GSLDAFLRTHdGQFTIVQLVGMLRGVGAGMRYL-SDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYTTAG 796
Cdd:cd06623    84 GSLADLLKKV-GKIPEPVLAYIARQILKGLDYLhTKRHIIHRDIKPSNLLINSKGEVKIADFGISKVLENTLDQCNTFVG 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 341940659  797 gkipirwTA----PEAIAFRTFSSASDVWSFGVVMWEvLAYGERPY 838
Cdd:cd06623   163 -------TVtymsPERIQGESYSYAADIWSLGLTLLE-CALGKFPF 200
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
638-842 9.06e-24

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: 102.07  E-value: 9.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVPGQrdvPVAIKALKAGYTERQRQDFL---------SEAAIMGQFDHPNIIRLEGVVTRGRLA 708
Cdd:cd06629     7 ELIGKGTYGRVYLAMNATTGE---MLAVKQVELPKTSSDRADSRqktvvdalkSEIDTLKDLDHPNIVQYLGFEETEDYF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  709 MIVTEYMENGSLDAFLRTHdGQFTiVQLV-GMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDd 787
Cdd:cd06629    84 SIFLEYVPGGSIGSCLRKY-GKFE-EDLVrFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISKKSDD- 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 341940659  788 peaAY-----TTAGGKIPirWTAPEAIAF--RTFSSASDVWSFGVVMWEVLAyGERPYWNMT 842
Cdd:cd06629   161 ---IYgnngaTSMQGSVF--WMAPEVIHSqgQGYSAKVDIWSLGCVVLEMLA-GRRPWSDDE 216
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
640-882 1.02e-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: 102.05  E-value: 1.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVcYGRLQVPGQRDVpvAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGS 719
Cdd:cd06610     9 IGSGATAVV-YAAYCLPKKEKV--AIKRIDLEKCQTSMDELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMPLLSGGS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  720 LDAFLRTH--DGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDD----PEAAYT 793
Cdd:cd06610    86 LLDIMKSSypRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSASLATGgdrtRKVRKT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  794 TAGgkIPIrWTAPEAIA-FRTFSSASDVWSFGVVMWEvLAYGERPYWN--------MTNQDVISSVEEGYRLPApmgCPR 864
Cdd:cd06610   166 FVG--TPC-WMAPEVMEqVRGYDFKADIWSFGITAIE-LATGAAPYSKyppmkvlmLTLQNDPPSLETGADYKK---YSK 238
                         250
                  ....*....|....*...
gi 341940659  865 ALHQLMLDCWHKDRAQRP 882
Cdd:cd06610   239 SFRKMISLCLQKDPSKRP 256
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
640-842 1.33e-23

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: 101.13  E-value: 1.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQRdvpVAIKALKagYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGS 719
Cdd:cd06614     8 IGEGASGEVYKATDRATGKE---VAIKKMR--LRKQNKELIINEILIMKECKHPNIVDYYDSYLVGDELWVVMEYMDGGS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  720 LDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSraleddpeAAYTTAGGKi 799
Cdd:cd06614    83 LTDIITQNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFA--------AQLTKEKSK- 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 341940659  800 piR--------WTAPEAIAFRTFSSASDVWSFGVVMWEvLAYGERPYWNMT 842
Cdd:cd06614   154 --RnsvvgtpyWMAPEVIKRKDYGPKVDIWSLGIMCIE-MAEGEPPYLEEP 201
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
640-882 1.58e-23

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: 101.31  E-value: 1.58e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLqvpgqRDVPVAIKALKA-GYTERQRQDFLSEAAIMgQFDHPNIIRL---EGVVTRGRLAMIVTEYM 715
Cdd:cd13979    11 LGSGGFGSVYKATY-----KGETVAVKIVRRrRKNRASRQSFWAELNAA-RLRHENIVRVlaaETGTDFASLGLIIMEYC 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  716 ENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYTTA 795
Cdd:cd13979    85 GNGTLQQLIYEGSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSVKLGEGNEVGTPRS 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  796 GGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWNMtNQDVISSVeEGYRLPAPMGCP------RALHQL 869
Cdd:cd13979   165 HIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLT-RELPYAGL-RQHVLYAV-VAKDLRPDLSGLedsefgQRLRSL 241
                         250
                  ....*....|...
gi 341940659  870 MLDCWHKDRAQRP 882
Cdd:cd13979   242 ISRCWSAQPAERP 254
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
640-882 2.20e-23

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: 101.28  E-value: 2.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGrlqVPGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGS 719
Cdd:cd06640    12 IGKGSFGEVFKG---IDNRTQQVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEYLGGGS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  720 LDAFLRThdGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYTTAGGKI 799
Cdd:cd06640    89 ALDLLRA--GPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNTFVGTPF 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  800 pirWTAPEAIAFRTFSSASDVWSFGVVMWEvLAYGERPYWNMTNQDVISSVEegyRLPAPM---GCPRALHQLMLDCWHK 876
Cdd:cd06640   167 ---WMAPEVIQQSAYDSKADIWSLGITAIE-LAKGEPPNSDMHPMRVLFLIP---KNNPPTlvgDFSKPFKEFIDACLNK 239

                  ....*.
gi 341940659  877 DRAQRP 882
Cdd:cd06640   240 DPSFRP 245
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
640-831 3.62e-23

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: 100.65  E-value: 3.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQvpgqrDVPVAIKALKA---GYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYME 716
Cdd:cd14158    23 LGEGGFGVVFKGYIN-----DKNVAVKKLAAmvdISTEDLTKQFEQEIQVMAKCQHENLVELLGYSCDGPQLCLVYTYMP 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  717 NGSLDAFLRTHDGQ--FTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYT- 793
Cdd:cd14158    98 NGSLLDRLACLNDTppLSWHMRCKIAQGTANGINYLHENNHIHRDIKSANILLDETFVPKISDFGLARASEKFSQTIMTe 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 341940659  794 ----TAGgkipirWTAPEAIAfRTFSSASDVWSFGVVMWEVL 831
Cdd:cd14158   178 rivgTTA------YMAPEALR-GEITPKSDIFSFGVVLLEII 212
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
636-882 7.07e-23

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: 99.02  E-value: 7.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIIGSGESGEVCYGRLQVPGQrdvPVAIKALK-AGYTERQRQDFLSEAAIMGQFDHPNIIR-LEGVVTRGRLAmIVTE 713
Cdd:cd08529     4 ILNKLGKGSFGVVYKVVRKVDGR---VYALKQIDiSRMSRKMREEAIDEARVLSKLNSPYVIKyYDSFVDKGKLN-IVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  714 YMENGSLDAFLRTHDGQ---------FTIVQLVgmlrgvgaGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRAL 784
Cdd:cd08529    80 YAENGDLHSLIKSQRGRplpedqiwkFFIQTLL--------GLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKIL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  785 EDDPEAAYTTAGgkIPIrWTAPEAIAFRTFSSASDVWSFGVVMWEvLAYGERPYwNMTNQD-VISSVEEGYRLPAPMGCP 863
Cdd:cd08529   152 SDTTNFAQTIVG--TPY-YLSPELCEDKPYNEKSDVWALGCVLYE-LCTGKHPF-EAQNQGaLILKIVRGKYPPISASYS 226
                         250
                  ....*....|....*....
gi 341940659  864 RALHQLMLDCWHKDRAQRP 882
Cdd:cd08529   227 QDLSQLIDSCLTKDYRQRP 245
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
642-884 7.43e-23

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: 99.50  E-value: 7.43e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  642 SGESGEV--CYGRLQvpGQrdvpVAIKALKAGYTERQRQD-FLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENG 718
Cdd:cd14027     3 SGGFGKVslCFHRTQ--GL----VVLKTVYTGPNCIEHNEaLLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  719 SLDAFLR------THDGQFtIVQLVgmlrgvgAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLS----------- 781
Cdd:cd14027    77 NLMHVLKkvsvplSVKGRI-ILEII-------EGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwskltke 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  782 -RALEDDPEAAYTTAGGKipIRWTAPE---AIAFRTfSSASDVWSFGVVMWEVLAyGERPYWNMTNQDVIS-SVEEGYRl 856
Cdd:cd14027   149 eHNEQREVDGTAKKNAGT--LYYMAPEhlnDVNAKP-TEKSDVYSFAIVLWAIFA-NKEPYENAINEDQIImCIKSGNR- 223
                         250       260       270
                  ....*....|....*....|....*....|..
gi 341940659  857 PA----PMGCPRALHQLMLDCWHKDRAQRPRF 884
Cdd:cd14027   224 PDvddiTEYCPREIIDLMKLCWEANPEARPTF 255
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
634-899 8.54e-23

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: 99.35  E-value: 8.54e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  634 IHIEKIIGSGESGEVCYGRLQvpGQrdvpVAIKALKAGY-TERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVT 712
Cdd:cd14063     2 LEIKEVIGKGRFGRVHRGRWH--GD----VAIKLLNIDYlNEEQLEAFKEEVAAYKNTRHDNLVLFMGACMDPPHLAIVT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  713 EYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVD-GRLVckVSDFGLSR--ALEDDPE 789
Cdd:cd14063    76 SLCKGRTLYSLIHERKEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLEnGRVV--ITDFGLFSlsGLLQPGR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  790 AAYTTAggkIPIRWT---APEAIAFRT----------FSSASDVWSFGVVMWEVLAyGERPYWNMTNQDVISSVEEGYRL 856
Cdd:cd14063   154 REDTLV---IPNGWLcylAPEIIRALSpdldfeeslpFTKASDVYAFGTVWYELLA-GRWPFKEQPAESIIWQVGCGKKQ 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 341940659  857 P-APMGCPRALHQLMLDCWHKDRAQRPRFAhvvSVLDALVHSPE 899
Cdd:cd14063   230 SlSQLDIGREVKDILMQCWAYDPEKRPTFS---DLLRMLERLPK 270
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
661-886 1.08e-22

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP2, also called RICK or CARDIAK, harbors a C-terminal Caspase Activation and Recruitment domain (CARD) belonging to the Death domain (DD) superfamily. It functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR) family, Nod1 and Nod2, which recognizes bacterial peptidoglycans released upon infection. RIP2 may also be involved in regulating wound healing and keratinocyte proliferation. RIP kinases serve as essential sensors of cellular stress. The RIP2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 99.22  E-value: 1.08e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  661 VPVAIKALK--AGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLDAFLRTHDGQFTIVQLV- 737
Cdd:cd14026    23 VTVAIKCLKldSPVGDSERNCLLKEAEILHKARFSYILPILGICNEPEFLGIVTEYMTNGSLNELLHEKDIYPDVAWPLr 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  738 -GMLRGVGAGMRYLSDLG--YIHRDLAARNVLVDGRLVCKVSDFGLS--RALEDDPEAAYTTAGGKIPIRWTAPEAIAFR 812
Cdd:cd14026   103 lRILYEIALGVNYLHNMSppLLHHDLKTQNILLDGEFHVKIADFGLSkwRQLSISQSRSSKSAPEGGTIIYMPPEEYEPS 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  813 TFSSAS---DVWSFGVVMWEVLAYgERPYWNMTNQ-DVISSVEEGYRL-----PAPMGCP-RA-LHQLMLDCWHKDRAQR 881
Cdd:cd14026   183 QKRRASvkhDIYSYAIIMWEVLSR-KIPFEEVTNPlQIMYSVSQGHRPdtgedSLPVDIPhRAtLINLIESGWAQNPDER 261

                  ....*
gi 341940659  882 PRFAH 886
Cdd:cd14026   262 PSFLK 266
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
640-892 1.17e-22

Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. ILK contains N-terminal ankyrin repeats, a Pleckstrin Homology (PH) domain, and a C-terminal pseudokinase domain. It is a component of the IPP (ILK/PINCH/Parvin) complex that couples beta integrins to the actin cytoskeleton, and plays important roles in cell adhesion, spreading, invasion, and migration. ILK was initially thought to be an active kinase despite the lack of key conserved residues because of in vitro studies showing that it can phosphorylate certain protein substrates. However, in vivo experiments in Caenorhabditis elegans, Drosophila melanogaster, and mice (ILK-null and knock-in) proved that ILK is not an active kinase. In addition to actin cytoskeleton regulation, ILK also influences the microtubule network and mitotic spindle orientation. The pseudokinase domain of ILK binds several adaptor proteins including the parvins and paxillin. The ILK subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270959 [Multi-domain]  Cd Length: 251  Bit Score: 98.33  E-value: 1.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQvpgQRDVpvAIKALKAG-YTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENG 718
Cdd:cd14057     3 INETHSGELWKGRWQ---GNDI--VAKILKVRdVTTRISRDFNEEYPRLRIFSHPNVLPVLGACNSPPNLVVISQYMPYG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  719 SLDAFLrtHDGQFTIV---QLVGMLRGVGAGMRYLSDLGYI--HRDLAARNVLVDGRLVCKVSdFGLSRALEDDPEAAYT 793
Cdd:cd14057    78 SLYNVL--HEGTGVVVdqsQAVKFALDIARGMAFLHTLEPLipRHHLNSKHVMIDEDMTARIN-MADVKFSFQEPGKMYN 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  794 TAggkipirWTAPEAIAFR---TFSSASDVWSFGVVMWEvLAYGERPYWNMTNQDV-ISSVEEGYRLPAPMGCPRALHQL 869
Cdd:cd14057   155 PA-------WMAPEALQKKpedINRRSADMWSFAILLWE-LVTREVPFADLSNMEIgMKIALEGLRVTIPPGISPHMCKL 226
                         250       260
                  ....*....|....*....|...
gi 341940659  870 MLDCWHKDRAQRPRFAHVVSVLD 892
Cdd:cd14057   227 MKICMNEDPGKRPKFDMIVPILE 249
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
640-882 1.93e-22

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: 98.19  E-value: 1.93e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGS 719
Cdd:cd06605     9 LGEGNGGVVSKVRHRPSGQI---MAVKVIRLEIDEALQKQILRELDVLHKCNSPYIVGFYGAFYSEGDISICMEYMDGGS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  720 LDAFLRtHDGQFTIVQLVGMLRGVGAGMRYL-SDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDpeAAYTTAGGK 798
Cdd:cd06605    86 LDKILK-EVGRIPERILGKIAVAVVKGLIYLhEKHKIIHRDVKPSNILVNSRGQVKLCDFGVSGQLVDS--LAKTFVGTR 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  799 ipiRWTAPEAIAFRTFSSASDVWSFGVVMWEvLAYGERPY--WN----MTNQDVISSV--EEGYRLPAPMGCPRALHqLM 870
Cdd:cd06605   163 ---SYMAPERISGGKYTVKSDIWSLGLSLVE-LATGRFPYppPNakpsMMIFELLSYIvdEPPPLLPSGKFSPDFQD-FV 237
                         250
                  ....*....|..
gi 341940659  871 LDCWHKDRAQRP 882
Cdd:cd06605   238 SQCLQKDPTERP 249
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
640-899 2.22e-22

Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-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: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 97.95  E-value: 2.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQvpgQRDVPVAIKALKAGYT-ERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGrlAMIVTEYMENG 718
Cdd:cd14025     4 VGSGGFGQVYKVRHK---HWKTWLAIKCPPSLHVdDSERMELLEEAKKMEMAKFRHILPVYGICSEP--VGLVMEYMETG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  719 SLDAFLRTH----DGQFTIVQLVGMlrgvgaGMRYLSDLG--YIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAY 792
Cdd:cd14025    79 SLEKLLASEplpwELRFRIIHETAV------GMNFLHCMKppLLHLDLKPANILLDAHYHVKISDFGLAKWNGLSHSHDL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  793 TTAGGKIPIRWTAPEAI--AFRTFSSASDVWSFGVVMWEVLAYgERPY--W-NMTNqdVISSVEEGYR---LPAPMGCPR 864
Cdd:cd14025   153 SRDGLRGTIAYLPPERFkeKNRCPDTKHDVYSFAIVIWGILTQ-KKPFagEnNILH--IMVKVVKGHRpslSPIPRQRPS 229
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 341940659  865 ALHQ---LMLDCWHKDRAQRPRFAHVVSVLDALVHSPE 899
Cdd:cd14025   230 ECQQmicLMKRCWDQDPRKRPTFQDITSETENLLSLLE 267
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
640-892 2.90e-22

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: 97.57  E-value: 2.90e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQvpgqRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGS 719
Cdd:cd14664     1 IGRGGAGTVYKGVMP----NGTLVAVKRLKGEGTQGGDHGFQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPNGS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  720 LDAFLRTHDGQFTIVQLVGMLR-GVGA--GMRYL---SDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYT 793
Cdd:cd14664    77 LGELLHSRPESQPPLDWETRQRiALGSarGLAYLhhdCSPLIIHRDVKSNNILLDEEFEAHVADFGLAKLMDDKDSHVMS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  794 TAGGKIPirWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPY-------WNMTNQDVISSVEEGYRL----PAPMGC 862
Cdd:cd14664   157 SVAGSYG--YIAPEYAYTGKVSEKSDVYSYGVVLLELIT-GKRPFdeaflddGVDIVDWVRGLLEEKKVEalvdPDLQGV 233
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 341940659  863 PR-----ALHQLMLDCWHKDRAQRPRFAHVVSVLD 892
Cdd:cd14664   234 YKleeveQVFQVALLCTQSSPMERPTMREVVRMLE 268
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
633-882 5.71e-22

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: 96.57  E-value: 5.71e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  633 RIHIEKIIGSGESGEVCYGRLQVPGQRDVPVAIKALKAGYTERQRQDflSEAAIMGQFDHPNIIRL-EGVVTRGRLaMIV 711
Cdd:cd08225     1 RYEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEKEASK--KEVILLAKMKHPNIVTFfASFQENGRL-FIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  712 TEYMENGSL-DAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNV-LVDGRLVCKVSDFGLSRALEDDPE 789
Cdd:cd08225    78 MEYCDGGDLmKRINRQRGVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIfLSKNGMVAKLGDFGIARQLNDSME 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  790 AAYTTAGGKIpirWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYgERPYWNMTNQDVISSVEEGYRLPAPMGCPRALHQL 869
Cdd:cd08225   158 LAYTCVGTPY---YLSPEICQNRPYNNKTDIWSLGCVLYELCTL-KHPFEGNNLHQLVLKICQGYFAPISPNFSRDLRSL 233
                         250
                  ....*....|...
gi 341940659  870 MLDCWHKDRAQRP 882
Cdd:cd08225   234 ISQLFKVSPRDRP 246
SAM_EPH-A5 cd09546
SAM domain of EPH-A5 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
933-994 6.37e-22

SAM domain of EPH-A5 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A5 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A5 receptors and appears to mediate cell-cell initiated signal transduction. Eph-A5 gene is almost exclusively expressed in the nervous system. Murine EPH-A5 receptors participate in axon guidance during embryogenesis and play a role in the adult synaptic plasticity, particularly in neuron-target interactions in multiple neural circuits. Additionally EPH-A5 receptors and its ligand ephrin A5 regulate dopaminergic axon outgrowth and influence the formation of the midbrain dopaminergic pathways. EphA5 gene expression was found decreased in a few different breast cancer cell lines, thus it might be a potential molecular marker for breast cancer carcinogenesis and progression.


Pssm-ID: 188945  Cd Length: 66  Bit Score: 89.99  E-value: 6.37e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 341940659  933 TVGDWLDSIRMGRYRDHFAAGGYSSLGMVLRMNAQDVRALGITLMGHQKKILGSIQTMRAQL 994
Cdd:cd09546     5 SVGEWLEAIKMGRYTEIFMENGYSSMDAVAQVTLEDLRRLGVTLVGHQKKIMNSIQEMRVQL 66
SAM_EPH-A7 cd09548
SAM domain of EPH-A7 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
933-994 8.25e-22

SAM domain of EPH-A7 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A7 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A7 receptors and appears to mediate cell-cell initiated signal transduction. EphA7 was found expressed in human embryonic stem (ES) cells, neural tissues, kidney vasculature. EphA7 knockout mice show decrease in cortical progenitor cell death at mid-neurogenesis and significant increase in cortical size. EphA7 may be involved in the pathogenesis and development of different cancers; in particular, EphA7 was found upregulated in glioblastoma and downregulated in colorectal cancer and gastric cancer. Thus, it is a potential molecular marker and/or therapy target for these types of cancers.


Pssm-ID: 188947  Cd Length: 70  Bit Score: 90.09  E-value: 8.25e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 341940659  933 TVGDWLDSIRMGRYRDHFAAGGYSSLGMVLRMNAQDVRALGITLMGHQKKILGSIQTMRAQL 994
Cdd:cd09548     9 SVGEWLEAIKMERYKDNFTAAGYNSLESVARMTIEDVMSLGITLVGHQKKIMSSIQTMRAQM 70
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
640-882 9.69e-22

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: 96.74  E-value: 9.69e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGrLQVPGQRdvPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGV-VTRGRLAMIVTEYMENG 718
Cdd:cd06620    13 LGAGNGGSVSKV-LHIPTGT--IMAKKVIHIDAKSSVRKQILRELQILHECHSPYIVSFYGAfLNENNNIIICMEYMDCG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  719 SLDAFLRTHdGQFTiVQLVGMLR-GVGAGMRYLSDLGYI-HRDLAARNVLVDGRLVCKVSDFGLSRALEDdpEAAYTTAG 796
Cdd:cd06620    90 SLDKILKKK-GPFP-EEVLGKIAvAVLEGLTYLYNVHRIiHRDIKPSNILVNSKGQIKLCDFGVSGELIN--SIADTFVG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  797 GKIpirWTAPEAIAFRTFSSASDVWSFGVVMWEvLAYGERPYWnMTNQDVISSV--------------EEGYRLPAPMGC 862
Cdd:cd06620   166 TST---YMSPERIQGGKYSVKSDVWSLGLSIIE-LALGEFPFA-GSNDDDDGYNgpmgildllqrivnEPPPRLPKDRIF 240
                         250       260
                  ....*....|....*....|
gi 341940659  863 PRALHQLMLDCWHKDRAQRP 882
Cdd:cd06620   241 PKDLRDFVDRCLLKDPRERP 260
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
640-840 1.13e-21

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: 95.59  E-value: 1.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQRdvpVAIKalKAGYTERQRQDFL-SEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENG 718
Cdd:cd06648    15 IGEGSTGIVCIATDKSTGRQ---VAVK--KMDLRKQQRRELLfNEVVIMRDYQHPNIVEMYSSYLVGDELWVVMEFLEGG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  719 SLDAFLrTHdGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLV--DGRLvcKVSDFGLSRALEDDpeaayttag 796
Cdd:cd06648    90 ALTDIV-TH-TRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLtsDGRV--KLSDFGFCAQVSKE--------- 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 341940659  797 gkIPIR--------WTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWN 840
Cdd:cd06648   157 --VPRRkslvgtpyWMAPEVISRLPYGTEVDIWSLGIMVIEMVD-GEPPYFN 205
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
636-841 1.38e-21

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: 95.41  E-value: 1.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIIGSGESGEVCYGRLQVPGQrdvPVAIKALKagyTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYM 715
Cdd:cd06612     7 ILEKLGEGSYGSVYKAIHKETGQ---VVAIKVVP---VEEDLQEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVMEYC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  716 ENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYTTA 795
Cdd:cd06612    81 GAGSVSDIMKITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLTDTMAKRNTVI 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 341940659  796 GgkIPIrWTAPEAIAFRTFSSASDVWSFGVVMWEvLAYGERPYWNM 841
Cdd:cd06612   161 G--TPF-WMAPEVIQEIGYNNKADIWSLGITAIE-MAEGKPPYSDI 202
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
638-883 2.05e-21

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: 94.92  E-value: 2.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVPGQRdvpVAIKALKAG-YTERQRQDFLSEAAIMGQFDHPNIIR-LEGVVTRGRLAM-IVTEY 714
Cdd:cd08217     6 ETIGKGSFGTVRKVRRKSDGKI---LVWKEIDYGkMSEKEKQQLVSEVNILRELKHPNIVRyYDRIVDRANTTLyIVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  715 MENGSLDAFLRTH--DGQF--------TIVQLVGML----RGVGAGMRYLsdlgyiHRDLAARNVLVDGRLVCKVSDFGL 780
Cdd:cd08217    83 CEGGDLAQLIKKCkkENQYipeefiwkIFTQLLLALyechNRSVGGGKIL------HRDLKPANIFLDSDNNVKLGDFGL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  781 SRALEDDPEAAYTTAGgkIPIRWtAPEAIAFRTFSSASDVWSFGVVMWEvLAYGERPYwNMTNQDVISS-VEEGYRLPAP 859
Cdd:cd08217   157 ARVLSHDSSFAKTYVG--TPYYM-SPELLNEQSYDEKSDIWSLGCLIYE-LCALHPPF-QAANQLELAKkIKEGKFPRIP 231
                         250       260
                  ....*....|....*....|....
gi 341940659  860 MGCPRALHQLMLDCWHKDRAQRPR 883
Cdd:cd08217   232 SRYSSELNEVIKSMLNVDPDKRPS 255
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
635-838 2.18e-21

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: 94.94  E-value: 2.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  635 HIEKIIGSGESGEVCYGRLQVPGQRDVpVAIKALKagyTERQRQDFLS-----EAAIMGQFDHPNIIRLEGVVTRGRLAM 709
Cdd:cd14080     3 RLGKTIGEGSYSKVKLAEYTKSGLKEK-VACKIID---KKKAPKDFLEkflprELEILRKLRHPNIIQVYSIFERGSKVF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  710 IVTEYMENGSLDAFLRTHdGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPE 789
Cdd:cd14080    79 IFMEYAEHGDLLEYIQKR-GALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFARLCPDDDG 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  790 ----------AAYttaggkipirwTAPEAIAFRTFSS-ASDVWSFGVVMWeVLAYGERPY 838
Cdd:cd14080   158 dvlsktfcgsAAY-----------AAPEILQGIPYDPkKYDIWSLGVILY-IMLCGSMPF 205
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
927-991 3.59e-21

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 87.71  E-value: 3.59e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 341940659   927 SGNGDLTVGDWLDSIRMGRYRDHFAAGgYSSLGMVLRMNAQDVRALGITLMGHQKKILGSIQTMR 991
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSFRAG-YIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRLK 64
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
636-831 3.96e-21

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: 94.47  E-value: 3.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIiGSGESGEVCYGRLQVPGQrdvPVAIKALKAGYTE--------RqrqdflsEAAIMGQFDHPNIIRLEGVVTRGRL 707
Cdd:cd07829     4 LEKL-GEGTYGVVYKAKDKKTGE---IVALKKIRLDNEEegipstalR-------EISLLKELKHPNIVKLLDVIHTENK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  708 AMIVTEYMENgSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEdD 787
Cdd:cd07829    73 LYLVFEYCDQ-DLKKYLDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLARAFG-I 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 341940659  788 PEAAYTTaggKIPIRW-TAPEaIAF--RTFSSASDVWSFGVVMWEVL 831
Cdd:cd07829   151 PLRTYTH---EVVTLWyRAPE-ILLgsKHYSTAVDIWSVGCIFAELI 193
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
643-882 4.69e-21

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: 94.42  E-value: 4.69e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  643 GESGEVCYGRLQVPGQR--DVPVAIKALKAGyTERQRQDFLSEAAIMGQFDHPNIIRL-EGVVTRGRLAMIVtEYMENGS 719
Cdd:cd06611    11 GELGDGAFGKVYKAQHKetGLFAAAKIIQIE-SEEELEDFMVEIDILSECKHPNIVGLyEAYFYENKLWILI-EFCDGGA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  720 LDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLV--DGRLvcKVSDFGLSRALEDDPEAAYTTAGG 797
Cdd:cd06611    89 LDSIMLELERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLtlDGDV--KLADFGVSAKNKSTLQKRDTFIGT 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  798 KipiRWTAPEAIAFRTFSSA-----SDVWSFGVVMWEvLAYGERPYWNMTNQDVISSVEEGY--RLPAPMGCPRALHQLM 870
Cdd:cd06611   167 P---YWMAPEVVACETFKDNpydykADIWSLGITLIE-LAQMEPPHHELNPMRVLLKILKSEppTLDQPSKWSSSFNDFL 242
                         250
                  ....*....|..
gi 341940659  871 LDCWHKDRAQRP 882
Cdd:cd06611   243 KSCLVKDPDDRP 254
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
663-887 5.53e-21

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-2D is allso called Retinal Guanylyl Cyclase 1 (RETGC-1) or Rod Outer Segment membrane Guanylate Cyclase (ROS-GC). It is found in the photoreceptors of the retina where it anchors the reciprocal feedback loop between calcium and cGMP, which regulates the dark, light, and recovery phases in phototransduction. It is also found in other sensory neurons and may be a universal transduction component that plays a role in the perception of all senses. 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 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-2D 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: 270945 [Multi-domain]  Cd Length: 267  Bit Score: 94.01  E-value: 5.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  663 VAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGV-VTRGRLAmIVTEYMENGSLDAFLRTHDGQ----FTIVQLV 737
Cdd:cd14043    26 VWLKKFPGGSHTELRPSTKNVFSKLRELRHENVNLFLGLfVDCGILA-IVSEHCSRGSLEDLLRNDDMKldwmFKSSLLL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  738 GMLRGvgagMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALE--------DDPEAAYttaggkipirWTAPE-- 807
Cdd:cd14043   105 DLIKG----MRYLHHRGIVHGRLKSRNCVVDGRFVLKITDYGYNEILEaqnlplpePAPEELL----------WTAPEll 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  808 --AIAFRTFSSASDVWSFGVVMWEVLAYGErPY--WNMTNQDVISSVeegyRLPAPMgC---------PRALHQLMLDCW 874
Cdd:cd14043   171 rdPRLERRGTFPGDVFSFAIIMQEVIVRGA-PYcmLGLSPEEIIEKV----RSPPPL-CrpsvsmdqaPLECIQLMKQCW 244
                         250
                  ....*....|...
gi 341940659  875 HKDRAQRPRFAHV 887
Cdd:cd14043   245 SEAPERRPTFDQI 257
SAM_EPH-A6 cd09547
SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
932-991 5.78e-21

SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A6 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A6 receptors and appears to mediate cell-cell initiated signal transduction. Eph-A6 gene is preferentially expressed in the nervous system. EPH-A6 receptors are involved in primate retina vascular and axon guidance, and in neural circuits responsible for learning and memory. EphA6 gene was significantly down regulated in colorectal cancer and in malignant melanomas. It is a potential molecular marker for these cancers.


Pssm-ID: 188946  Cd Length: 64  Bit Score: 87.25  E-value: 5.78e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  932 LTVGDWLDSIRMGRYRDHFAAGGYSSLGMVLRMNAQDVRALGITLMGHQKKILGSIQTMR 991
Cdd:cd09547     4 VTVSDWLDSIKMGQYKNNFMAAGFTTLDMVSRMTIDDIRRIGVTLIGHQRRIVSSIQTLR 63
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
633-882 7.04e-21

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: 93.22  E-value: 7.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  633 RIHIEKIIGSGESGEVCYGRLQVPGQRdvpVAIK-ALKAGYTERQRQDFLSE---AAIMGQfdHPNIIRLEGVVTRGRLA 708
Cdd:cd13997     1 HFHELEQIGSGSFSEVFKVRSKVDGCL---YAVKkSKKPFRGPKERARALREveaHAALGQ--HPNIVRYYSSWEEGGHL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  709 MIVTEYMENGSLDAFLRTHdGQFTIV---QLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALE 785
Cdd:cd13997    76 YIQMELCENGSLQDALEEL-SPISKLseaEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRLE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  786 DDPEAAYTTAggkipiRWTAPEAIA-FRTFSSASDVWSFGVVMWEVLAYGERPywnmTNQDVISSVEEGYrLPAPMGCPR 864
Cdd:cd13997   155 TSGDVEEGDS------RYLAPELLNeNYTHLPKADIFSLGVTVYEAATGEPLP----RNGQQWQQLRQGK-LPLPPGLVL 223
                         250       260
                  ....*....|....*....|
gi 341940659  865 A--LHQLMLDCWHKDRAQRP 882
Cdd:cd13997   224 SqeLTRLLKVMLDPDPTRRP 243
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
663-887 7.85e-21

Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-A binds and is activated by the atrial and B-type natriuretic peptides, ANP and BNP, which are important in blood pressure regulation and cardiac pathophysiology. GC-B binds the C-type natriuretic peptide, CNP, which is a potent vasorelaxant and functions in vascular remodeling and bone growth regulation. 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 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-A/B 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: 270944 [Multi-domain]  Cd Length: 279  Bit Score: 93.81  E-value: 7.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  663 VAIKALkagytERQRQD----FLSEAAIMGQFDHPNIIRLEGV-VTRGRLAmIVTEYMENGSLDAFLRTHDgqftiVQLV 737
Cdd:cd14042    33 VAIKKV-----NKKRIDltreVLKELKHMRDLQHDNLTRFIGAcVDPPNIC-ILTEYCPKGSLQDILENED-----IKLD 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  738 GMLRG-----VGAGMRYL--SDLGYiHRDLAARNVLVDGRLVCKVSDFGLS--RALEDDPEAAYTTAGGKIpirWTAPEA 808
Cdd:cd14042   102 WMFRYslihdIVKGMHYLhdSEIKS-HGNLKSSNCVVDSRFVLKITDFGLHsfRSGQEPPDDSHAYYAKLL---WTAPEL 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  809 IafRTFSSAS------DVWSFGVVMWEVlAYGERPYWN-----MTNQDVISSVEEGYRLP-----APMGCPRALHQLMLD 872
Cdd:cd14042   178 L--RDPNPPPpgtqkgDVYSFGIILQEI-ATRQGPFYEegpdlSPKEIIKKKVRNGEKPPfrpslDELECPDEVLSLMQR 254
                         250
                  ....*....|....*
gi 341940659  873 CWHKDRAQRPRFAHV 887
Cdd:cd14042   255 CWAEDPEERPDFSTL 269
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
640-838 7.95e-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: 93.46  E-value: 7.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQrdvPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGS 719
Cdd:cd06609     9 IGKGSFGEVYKGIDKRTNQ---VVAIKVIDLEEAEDEIEDIQQEIQFLSQCDSPYITKYYGSFLKGSKLWIIMEYCGGGS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  720 LDAFLRThdGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLV--DGRLvcKVSDFGLSRALEDDPEAAYTTAGg 797
Cdd:cd06609    86 VLDLLKP--GPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLseEGDV--KLADFGVSGQLTSTMSKRNTFVG- 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 341940659  798 kIPIrWTAPEAIAFRTFSSASDVWSFGVVMWEvLAYGERPY 838
Cdd:cd06609   161 -TPF-WMAPEVIKQSGYDEKADIWSLGITAIE-LAKGEPPL 198
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
638-882 8.43e-21

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: 93.75  E-value: 8.43e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYTErqrqdfLSEA-------AIMGQFDHPNIIRL-EGVVTRGRLaM 709
Cdd:cd07830     5 KQLGDGTFGSVYLARNKETGEL---VAIKKMKKKFYS------WEECmnlrevkSLRKLNEHPNIVKLkEVFRENDEL-Y 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  710 IVTEYMEnGSLDAFLRTHDGQ-FTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDP 788
Cdd:cd07830    75 FVFEYME-GNLYQLMKDRKGKpFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLAREIRSRP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  789 eaAYTTAggkIPIRW-TAPEAIAFRTF-SSASDVWSFGVVMWEVlaYGERPYWNMTNQ----DVISSV---------EEG 853
Cdd:cd07830   154 --PYTDY---VSTRWyRAPEILLRSTSySSPVDIWALGCIMAEL--YTLRPLFPGSSEidqlYKICSVlgtptkqdwPEG 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 341940659  854 YRLPAPMG-----------------CPRALHQLMLDCWHKDRAQRP 882
Cdd:cd07830   227 YKLASKLGfrfpqfaptslhqlipnASPEAIDLIKDMLRWDPKKRP 272
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
638-831 8.88e-21

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: 93.93  E-value: 8.88e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQvpgqrDVPVAIKALKagytERQRQDFLSEAAIMG--QFDHPNIIRLEGVVTRGRLAM----IV 711
Cdd:cd14053     1 EIKARGRFGAVWKAQYL-----NRLVAVKIFP----LQEKQSWLTEREIYSlpGMKHENILQFIGAEKHGESLEaeywLI 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  712 TEYMENGSLDAFLRTHDgqFTIVQLVGMLRGVGAGMRYL-SDLGY---------IHRDLAARNVLVDGRLVCKVSDFGLS 781
Cdd:cd14053    72 TEFHERGSLCDYLKGNV--ISWNELCKIAESMARGLAYLhEDIPAtngghkpsiAHRDFKSKNVLLKSDLTACIADFGLA 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 341940659  782 RALEDD--PEAAYTTAGGKipiRWTAPE----AIAFRTFS-SASDVWSFGVVMWEVL 831
Cdd:cd14053   150 LKFEPGksCGDTHGQVGTR---RYMAPEvlegAINFTRDAfLRIDMYAMGLVLWELL 203
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
635-827 9.71e-21

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: 93.23  E-value: 9.71e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  635 HIEKIIGSGESGEVcygRLQVPGQRDVPVAIKAL-KAGYTERQRQDF------LSEAAIMGQFDHPNIIRLEGVVTRGRL 707
Cdd:cd14084     9 IMSRTLGSGACGEV---KLAYDKSTCKKVAIKIInKRKFTIGSRREInkprniETEIEILKKLSHPCIIKIEDFFDAEDD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  708 AMIVTEYMENGSL------DAFLRTHDGQFTIVQlvgMLRGVgagmRYLSDLGYIHRDLAARNVLV---DGRLVCKVSDF 778
Cdd:cd14084    86 YYIVLELMEGGELfdrvvsNKRLKEAICKLYFYQ---MLLAV----KYLHSNGIIHRDLKPENVLLssqEEECLIKITDF 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 341940659  779 GLSRALEDDpEAAYTTAGgkIPIrWTAPEAIAF---RTFSSASDVWSFGVVM 827
Cdd:cd14084   159 GLSKILGET-SLMKTLCG--TPT-YLAPEVLRSfgtEGYTRAVDCWSLGVIL 206
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
639-881 1.05e-20

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: 93.66  E-value: 1.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  639 IIGSGESGEVCYGRLQvpgqrDVPVAIKAlkagYTERQRQDFLSEAAIMG--QFDHPNIIRL---EGVVTRGRLAM-IVT 712
Cdd:cd13998     2 VIGKGRFGEVWKASLK-----NEPVAVKI----FSSRDKQSWFREKEIYRtpMLKHENILQFiaaDERDTALRTELwLVT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  713 EYMENGSLDAFLRTHdgqftIVQLVGMLRGVGAGMRYLSDL------------GYIHRDLAARNVLVDGRLVCKVSDFGL 780
Cdd:cd13998    73 AFHPNGSL*DYLSLH-----TIDWVSLCRLALSVARGLAHLhseipgctqgkpAIAHRDLKSKNILVKNDGTCCIADFGL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  781 S----RALEDDPEAAYTTAGGKipiRWTAPE----AIAFRTFSS--ASDVWSFGVVMWEVL-----AYGERPYWNMTNQD 845
Cdd:cd13998   148 AvrlsPSTGEEDNANNGQVGTK---RYMAPEvlegAINLRDFESfkRVDIYAMGLVLWEMAsrctdLFGIVEEYKPPFYS 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 341940659  846 VIS---SVEEGYRL-----------PAPMGCP--RALHQLMLDCWHKDRAQR 881
Cdd:cd13998   225 EVPnhpSFEDMQEVvvrdkqrpnipNRWLSHPglQSLAETIEECWDHDAEAR 276
SAM_EPH-B2 cd09552
SAM domain of EPH-B2 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
933-995 3.01e-20

SAM domain of EPH-B2 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B2 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B2 receptors and appears to mediate cell-cell initiated signal transduction. SAM domains of this subfamily form homodimers/oligomers (in head-to-head/tail-to-tail orientation); apparently such clustering is necessary for signaling. EPH-B2 receptor is involved in regulation of synaptic function; it is needed for normal vestibular function, proper formation of anterior commissure, control of cell positioning, and ordered migration in the intestinal epithelium. EPH-B2 plays a tumor suppressor role in colorectal cancer. It was found to be downregulated in gastric cancer and thus may be a negative biomarker for it.


Pssm-ID: 188951  Cd Length: 71  Bit Score: 85.44  E-value: 3.01e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341940659  933 TVGDWLDSIRMGRYRDHFAAGGYSSLGMVLRMNAQDVRALGITLMGHQKKILGSIQTMRAQLS 995
Cdd:cd09552     8 TVDEWLDAIKMGQYKESFANAGFTSFDVVSQMTMEDILRVGVTLAGHQKKILNSIQVMRAQMN 70
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
639-882 3.76e-20

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: 91.44  E-value: 3.76e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  639 IIGSGESGEVCYGRLQVPGQRDV--PVAIKALKAGYTERQRQ--DFLS-EAAIMGQFDHPNIIRLEGVVTRGRLAMIVTE 713
Cdd:cd06628     7 LIGSGSFGSVYLGMNASSGELMAvkQVELPSVSAENKDRKKSmlDALQrEIALLRELQHENIVQYLGSSSDANHLNIFLE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  714 YMENGSLDAFLRTHdGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDpeAAYT 793
Cdd:cd06628    87 YVPGGSVATLLNNY-GAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKKLEAN--SLST 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  794 TAGGKIP-----IRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALHQ 868
Cdd:cd06628   164 KNNGARPslqgsVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLT-GTHPFPDCTQMQAIFKIGENASPTIPSNISSEARD 242
                         250
                  ....*....|....
gi 341940659  869 LMLDCWHKDRAQRP 882
Cdd:cd06628   243 FLEKTFEIDHNKRP 256
PTK_Jak2_rpt1 cd05078
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely ...
678-892 4.41e-20

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely expressed in many tissues. It 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 cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Despite this, the presumed pseudokinase (repeat 1) domain of Jak2 exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Inactivation of the repeat 1 domain increased Jak2 basal activity, suggesting that it modulates the kinase activity of the C-terminal catalytic (repeat 2) domain. The Jak2 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: 270663 [Multi-domain]  Cd Length: 262  Bit Score: 91.16  E-value: 4.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  678 QDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIH 757
Cdd:cd05078    48 ESFFEAASMMSQLSHKHLVLNYGVCVCGDENILVQEYVKFGSLDTYLKKNKNCINILWKLEVAKQLAWAMHFLEEKTLVH 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  758 RDLAARNVLV-------DGRL-VCKVSDFGLSRALEddPEAAYTTaggKIPirWTAPEAIAF-RTFSSASDVWSFGVVMW 828
Cdd:cd05078   128 GNVCAKNILLireedrkTGNPpFIKLSDPGISITVL--PKDILLE---RIP--WVPPECIENpKNLSLATDKWSFGTTLW 200
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 341940659  829 EVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCprALHQLMLDCWHKDRAQRPRFAHVVSVLD 892
Cdd:cd05078   201 EICSGGDKPLSALDSQRKLQFYEDRHQLPAPKWT--ELANLINNCMDYEPDHRPSFRAIIRDLN 262
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
663-889 5.54e-20

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: 90.69  E-value: 5.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  663 VAIK--ALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLDAFLRTHDG------QFTIV 734
Cdd:cd14099    29 YAGKvvPKSSLTKPKQREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILLELCSNGSLMELLKRRKAltepevRYFMR 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  735 QLVGmlrgvgaGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYTTAGgkipirwT----APEAIA 810
Cdd:cd14099   109 QILS-------GVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARLEYDGERKKTLCG-------TpnyiAPEVLE 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  811 -FRTFSSASDVWSFGVVMWeVLAYGERPYWNMTNQDVISSVEEG-YRLPAPMGCPRALHQLMLDCWHKDRAQRPRFAHVV 888
Cdd:cd14099   175 kKKGHSFEVDIWSLGVILY-TLLVGKPPFETSDVKETYKRIKKNeYSFPSHLSISDEAKDLIRSMLQPDPTKRPSLDEIL 253

                  .
gi 341940659  889 S 889
Cdd:cd14099   254 S 254
SAM_EPH-B3 cd09553
SAM domain of EPH-B3 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
933-994 5.74e-20

SAM domain of EPH-B3 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B3 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B3 receptors and appears to mediate cell-cell initiated signal transduction. EPH-B3 receptor protein kinase performs kinase-dependent and kinase-independent functions. It is known to be involved in thymus morphogenesis, in regulation of cell adhesion and migration. Also EphB3 controls cell positioning and ordered migration in the intestinal epithelium and plays a role in the regulation of adult retinal ganglion cell axon plasticity after optic nerve injury. In some experimental models overexpression of EphB3 enhances cell/cell contacts and suppresses colon tumor growth.


Pssm-ID: 188952  Cd Length: 69  Bit Score: 84.70  E-value: 5.74e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 341940659  933 TVGDWLDSIRMGRYRDHFAAGGYSSLGMVLRMNAQDVRALGITLMGHQKKILGSIQTMRAQL 994
Cdd:cd09553     8 TVGDWLDAIKMGRYKENFVSAGFASFDLVAQMTAEDLLRIGVTLAGHQKKILSSIQDMRLQM 69
PTK_Jak3_rpt1 cd14208
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is ...
659-892 6.88e-20

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; 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 cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. Jaks 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 Jak3 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: 271110 [Multi-domain]  Cd Length: 260  Bit Score: 90.35  E-value: 6.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  659 RDVPVAIKALKAGYTERQrQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMiVTEYMENGSLDAFLRT--HDGQFTIVQL 736
Cdd:cd14208    29 CETEVLLKVMDPTHGNCQ-ESFLEAASIMSQISHKHLVLLHGVCVGKDSIM-VQEFVCHGALDLYLKKqqQKGPVAISWK 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  737 VGMLRGVGAGMRYLSDLGYIHRDLAARNVLV-----DGRL-VCKVSDFGLSRALEDDPEAAyttagGKIPirWTAPEAIA 810
Cdd:cd14208   107 LQVVKQLAYALNYLEDKQLVHGNVSAKKVLLsregdKGSPpFIKLSDPGVSIKVLDEELLA-----ERIP--WVAPECLS 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  811 -FRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALhqLMLDCWHKDRAQRPRFAHVVS 889
Cdd:cd14208   180 dPQNLALEADKWGFGATLWEIFSGGHMPLSALDPSKKLQFYNDRKQLPAPHWIELAS--LIQQCMSYNPLLRPSFRAIIR 257

                  ...
gi 341940659  890 VLD 892
Cdd:cd14208   258 DLN 260
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
635-838 7.97e-20

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: 90.47  E-value: 7.97e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  635 HIEKIIGSGESGEVcygRLQVPGQRDVPVAIKAL-KAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTE 713
Cdd:cd14069     4 DLVQTLGEGAFGEV---FLAVNRNTEEAVAVKFVdMKRAPGDCPENIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  714 YMENGSL------DAFLRTHDGQFTIVQLVgmlrgvgAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGL-SRALED 786
Cdd:cd14069    81 YASGGELfdkiepDVGMPEDVAQFYFQQLM-------AGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLaTVFRYK 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 341940659  787 DPEAAYTTAGGKIPirWTAPEAIAFRTF-SSASDVWSFGVVMWEVLAyGERPY 838
Cdd:cd14069   154 GKERLLNKMCGTLP--YVAPELLAKKKYrAEPVDVWSCGIVLFAMLA-GELPW 203
SAM_EPH-B4 cd09554
SAM domain of EPH-B4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
933-993 8.84e-20

SAM domain of EPH-B4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B4 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B4 receptors and appears to mediate cell-cell initiated signal transduction. EPH-B4 protein kinase performs kinase-dependent and kinase-independent functions. These receptors play a role in the regular vascular system development during embryogenesis. They were found overexpressed in a variety of cancers, including carcinoma of the head and neck, ovarian cancer, bladder cancer, and downregulated in bone myeloma. Thus, EphB4 is a potential biomarker and a target for drug design.


Pssm-ID: 188953  Cd Length: 67  Bit Score: 84.15  E-value: 8.84e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 341940659  933 TVGDWLDSIRMGRYRDHFAAGGYSSLGMVLRMNAQDVRALGITLMGHQKKILGSIQTMRAQ 993
Cdd:cd09554     5 SVGEWLRAIKMERYEDSFLQAGFTTFQLVSQISTEDLLRMGVTLAGHQKKILSSIQAMGIQ 65
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
633-882 1.08e-19

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: 89.79  E-value: 1.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  633 RIHIEKIIGSGESGEVCYGR-LQVPGQRDVPVaIKALKAG-YTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMI 710
Cdd:cd08222     1 RYRVVRKLGSGNFGTVYLVSdLKATADEELKV-LKEISVGeLQPDETVDANREAKLLSKLDHPAIVKFHDSFVEKESFCI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  711 VTEYMENGSLDAFL---RTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVcKVSDFGLSRALEDD 787
Cdd:cd08222    80 VTEYCEGGDLDDKIseyKKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKNNVI-KVGDFGISRILMGT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  788 PEAAYTTAGgkIPIrWTAPEAIAFRTFSSASDVWSFGVVMWEvLAYGERPYWNMTNQDVISSVEEGyRLPA-PMGCPRAL 866
Cdd:cd08222   159 SDLATTFTG--TPY-YMSPEVLKHEGYNSKSDIWSLGCILYE-MCCLKHAFDGQNLLSVMYKIVEG-ETPSlPDKYSKEL 233
                         250
                  ....*....|....*.
gi 341940659  867 HQLMLDCWHKDRAQRP 882
Cdd:cd08222   234 NAIYSRMLNKDPALRP 249
SAM_EPH-B1 cd09551
SAM domain of EPH-B1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
933-993 1.18e-19

SAM domain of EPH-B1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B1 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH- B1 receptors. In human vascular endothelial cells it appears to mediate cell-cell initiated signal transduction via the binding of the adaptor protein GRB10 (growth factor) through its SH2 domain to a conserved tyrosine that is phosphorylated. EPH-B1 receptors play a role in neurogenesis, in particular in regulation of proliferation and migration of neural progenitors in the hippocampus and in corneal neovascularization; they are involved in converting the crossed retinal projection to ipsilateral retinal projection. They may be potential targets in angiogenesis-related disorders.


Pssm-ID: 188950  Cd Length: 68  Bit Score: 83.93  E-value: 1.18e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 341940659  933 TVGDWLDSIRMGRYRDHFAAGGYSSLGMVLRMNAQDVRALGITLMGHQKKILGSIQTMRAQ 993
Cdd:cd09551     8 SVEDWLSAIKMSQYRDNFLSSGFTSLQLVAQMTSEDLLRIGVTLAGHQKKILNSIQSMRVQ 68
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
636-832 1.19e-19

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: 91.43  E-value: 1.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIIGSGESGEVCygrLQVPGQRDVPVAIKalKAGYTERQRQD---FLSEAAIMGQFDHPNIIRLEGVVT-RGRLAM-- 709
Cdd:cd07834     4 LLKPIGSGAYGVVC---SAYDKRTGRKVAIK--KISNVFDDLIDakrILREIKILRHLKHENIIGLLDILRpPSPEEFnd 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  710 --IVTEYMENgSLDAFLR-----THD-GQFTIVQlvgMLRGvgagMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLS 781
Cdd:cd07834    79 vyIVTELMET-DLHKVIKspqplTDDhIQYFLYQ---ILRG----LKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGLA 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 341940659  782 RALEDDPEAAYTTagGKIPIRW-TAPEAI-AFRTFSSASDVWSFGVVMWEVLA 832
Cdd:cd07834   151 RGVDPDEDKGFLT--EYVVTRWyRAPELLlSSKKYTKAIDIWSVGCIFAELLT 201
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
638-860 1.57e-19

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: 89.12  E-value: 1.57e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRlQVPGQRDVpvAIKAL-KAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYME 716
Cdd:cd14072     6 KTIGKGNFAKVKLAR-HVLTGREV--AIKIIdKTQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEYAS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  717 NGSLDAFLRTHdGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRalEDDPEAAYTTAG 796
Cdd:cd14072    83 GGEVFDYLVAH-GRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSN--EFTPGNKLDTFC 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 341940659  797 GKIPirWTAPEAIAFRTFSSAS-DVWSFGVVMWeVLAYGERPYWNMTNQDVISSVEEG-YRLPAPM 860
Cdd:cd14072   160 GSPP--YAAPELFQGKKYDGPEvDVWSLGVILY-TLVSGSLPFDGQNLKELRERVLRGkYRIPFYM 222
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
664-882 1.58e-19

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: 89.37  E-value: 1.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  664 AIKALKAG-YTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLDAFLRTHDGQFTIVQ------- 735
Cdd:cd08530    29 ALKEVNLGsLSQKEREDSVNEIRLLASVNHPNIIRYKEAFLDGNRLCIVMEYAPFGDLSKLISKRKKKRRLFPeddiwri 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  736 LVGMLRGVGAgmryLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDpeAAYTTAGgkIPIrWTAPEAIAFRTFS 815
Cdd:cd08530   109 FIQMLRGLKA----LHDQKILHRDLKSANILLSAGDLVKIGDLGISKVLKKN--LAKTQIG--TPL-YAAPEVWKGRPYD 179
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 341940659  816 SASDVWSFGVVMWEvLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALHQLMLDCWHKDRAQRP 882
Cdd:cd08530   180 YKSDIWSLGCLLYE-MATFRPPFEARTMQELRYKVCRGKFPPIPPVYSQDLQQIIRSLLQVNPKKRP 245
PTK_Tyk2_rpt1 cd05076
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Tyk2 is ...
640-891 1.58e-19

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; 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 domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Tyk2 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: 270661 [Multi-domain]  Cd Length: 273  Bit Score: 89.58  E-value: 1.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQRDvPVAIKALKAGYTERQ------------RQD----FLSEAAIMGQFDHPNIIRLEGVVT 703
Cdd:cd05076     7 LGQGTRTNIYEGRLLVEGSGE-PEEDKELVPGRDRGQelrvvlkvldpsHHDialaFFETASLMSQVSHTHLVFVHGVCV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  704 RGRLAMIVTEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLV-------CKVS 776
Cdd:cd05076    86 RGSENIMVEEFVEHGPLDVWLRKEKGHVPMAWKFVVARQLASALSYLENKNLVHGNVCAKNILLARLGLeegtspfIKLS 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  777 DFG-----LSRalEDDPEaayttaggKIPirWTAPEAI-AFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSV 850
Cdd:cd05076   166 DPGvglgvLSR--EERVE--------RIP--WIAPECVpGGNSLSTAADKWGFGATLLEICFNGEAPLQSRTPSEKERFY 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 341940659  851 EEGYRLPAPmGCPRaLHQLMLDCWHKDRAQRPRFAHVVSVL 891
Cdd:cd05076   234 QRQHRLPEP-SCPE-LATLISQCLTYEPTQRPSFRTILRDL 272
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
637-889 1.60e-19

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: 89.41  E-value: 1.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  637 EKIIGSGESGEVCYGRLQVPGQ----RDVPVAikalkaGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVT 712
Cdd:cd08220     5 IRVVGRGAYGTVYLCRRKDDNKlviiKQIPVE------QMTKEERQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  713 EYMENGSLDAFLRTHDGQF----TIVQL-VGMLrgvgAGMRYLSDLGYIHRDLAARNVLVDG-RLVCKVSDFGLSRALED 786
Cdd:cd08220    79 EYAPGGTLFEYIQQRKGSLlseeEILHFfVQIL----LALHHVHSKQILHRDLKTQNILLNKkRTVVKIGDFGISKILSS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  787 DPEaAYTTAGGKIPIrwtAPEAIAFRTFSSASDVWSFGVVMWEvLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRAL 866
Cdd:cd08220   155 KSK-AYTVVGTPCYI---SPELCEGKPYNQKSDIWALGCVLYE-LASLKRAFEAANLPALVLKIMRGTFAPISDRYSEEL 229
                         250       260
                  ....*....|....*....|...
gi 341940659  867 HQLMLDCWHKDRAQRPRFAHVVS 889
Cdd:cd08220   230 RHLILSMLHLDPNKRPTLSEIMA 252
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
638-875 1.79e-19

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: 90.02  E-value: 1.79e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQvpGQRdvpVAIKAlkagYTERQRQDFLSEAAI----MGQfdHPNIIRL-------EGVVTRGR 706
Cdd:cd14056     1 KTIGKGRYGEVWLGKYR--GEK---VAVKI----FSSRDEDSWFRETEIyqtvMLR--HENILGFiaadiksTGSWTQLW 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  707 LamiVTEYMENGSLDAFLRTHdgQFTIVQLVGMLRGVGAGMRYL--------SDLGYIHRDLAARNVLVDGRLVCKVSDF 778
Cdd:cd14056    70 L---ITEYHEHGSLYDYLQRN--TLDTEEALRLAYSAASGLAHLhteivgtqGKPAIAHRDLKSKNILVKRDGTCCIADL 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  779 GL----SRALEDDPEAAYTTAGGKipiRWTAPE----AIAFRTFSS--ASDVWSFGVVMWEVLAYGER---------PYW 839
Cdd:cd14056   145 GLavryDSDTNTIDIPPNPRVGTK---RYMAPEvlddSINPKSFESfkMADIYSFGLVLWEIARRCEIggiaeeyqlPYF 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 341940659  840 NMTNQD--------VIssVEEGYRLPAP---MGCP--RALHQLMLDCWH 875
Cdd:cd14056   222 GMVPSDpsfeemrkVV--CVEKLRPPIPnrwKSDPvlRSMVKLMQECWS 268
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
636-860 1.94e-19

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: 88.99  E-value: 1.94e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIIGSGESGEVCYGRLQVPGQRdvpVAIKAL-KAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEY 714
Cdd:cd14071     4 IERTIGKGNFAVVKLARHRITKTE---VAIKIIdKSQLDEENLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  715 MENGSLDAFLRTHdGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEddPEAAYTT 794
Cdd:cd14071    81 ASNGEIFDYLAQH-GRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSNFFK--PGELLKT 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 341940659  795 AGGKIPirWTAPEAIAFRTFSSAS-DVWSFGVVMWeVLAYGERPYWNMTNQDVISSVEEG-YRLPAPM 860
Cdd:cd14071   158 WCGSPP--YAAPEVFEGKEYEGPQlDIWSLGVVLY-VLVCGALPFDGSTLQTLRDRVLSGrFRIPFFM 222
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
640-881 4.16e-19

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: 87.96  E-value: 4.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQRdvpVAIKALKAG--YTERQRQDFLSEAAIMGQFDHPNIIRLEGVV-TRGRLAMiVTEYME 716
Cdd:cd05123     1 LGKGSFGKVLLVRKKDTGKL---YAMKVLRKKeiIKRKEVEHTLNERNILERVNHPFIVKLHYAFqTEEKLYL-VLDYVP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  717 NGSLDAFLRTH------DGQFTIVQLVgmlrgvgAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEA 790
Cdd:cd05123    77 GGELFSHLSKEgrfpeeRARFYAAEIV-------LALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSDGDR 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  791 AYTTAGgkipirwT----APEAIAFRTFSSASDVWSFGVVMWEVLaYGERPYW---NMTNQDVISSVEEGYrlpaPMGCP 863
Cdd:cd05123   150 TYTFCG-------TpeylAPEVLLGKGYGKAVDWWSLGVLLYEML-TGKPPFYaenRKEIYEKILKSPLKF----PEYVS 217
                         250
                  ....*....|....*...
gi 341940659  864 RALHQLMLDCWHKDRAQR 881
Cdd:cd05123   218 PEAKSLISGLLQKDPTKR 235
SAM_EPH-A4 cd09545
SAM domain of EPH-A4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
933-999 4.29e-19

SAM domain of EPH-A4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A4 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A4 receptors and appears to mediate cell-cell initiated signal transduction. SAM domains of EPH-A4 receptors can form homodimers. EPH-A4 receptors bind ligands such as erphirin A1, A4, A5. They are known to interact with a number of different proteins, including meltrin beta metalloprotease, Cdk5, and EFS2alpha, however SAM domain doesn't participate in these interactions. EPH-A4 receptors are involved in regulation of corticospinal tract formation, in pathway controlling voluntary movements, in formation of motor neurons, and in axon guidance (SAM domain is not required for axon guidance or for EPH-A4 kinase signaling). In Xenopus embryos EPH-A4 induces loss of cell adhesion, ventro-lateral protrusions, and severely expanded posterior structures. Mutations in SAM domain conserved tyrosine (Y928F) enhance the ability of EPH-A4 to induce these phenotypes, thus supporting the idea that the SAM domain may negatively regulate some aspects of EPH-A4 activity. EphA4 gene was found overexpressed in a number of different cancers including human gastric cancer, colorectal cancer, and pancreatic ductal adenocarcinoma. It is likely to be a promising molecular target for the cancer therapy.


Pssm-ID: 188944  Cd Length: 71  Bit Score: 82.31  E-value: 4.29e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 341940659  933 TVGDWLDSIRMGRYRDHFAAGGYSSLGMVLRMNAQDVRALGITLMGHQKKILGSIQTMRAQLSSTQG 999
Cdd:cd09545     5 SVDDWLQAIKMERYKDNFTAAGYTTLEAVVHMNQDDLARIGISAIAHQNKILSSVQGMRSQMQQMQG 71
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
634-882 4.36e-19

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: 88.78  E-value: 4.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  634 IHIEKIIGSGESGEVcYGRLQVPGQRDVPVAIKALKAGyTERQRQdFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTE 713
Cdd:cd06619     3 IQYQEILGHGNGGTV-YKAYHLLTRRILAVKVIPLDIT-VELQKQ-IMSELEILYKCDSPYIIGFYGAFFVENRISICTE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  714 YMENGSLDAFLRTHDgqftivQLVGMLR-GVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAY 792
Cdd:cd06619    80 FMDGGSLDVYRKIPE------HVLGRIAvAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLVNSIAKTY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  793 TTAGGkipirWTAPEAIAFRTFSSASDVWSFGVVMWEvLAYGERPYWNM-TNQDVISSV--------EEGYRLPAPMGCP 863
Cdd:cd06619   154 VGTNA-----YMAPERISGEQYGIHSDVWSLGISFME-LALGRFPYPQIqKNQGSLMPLqllqcivdEDPPVLPVGQFSE 227
                         250
                  ....*....|....*....
gi 341940659  864 RALHqLMLDCWHKDRAQRP 882
Cdd:cd06619   228 KFVH-FITQCMRKQPKERP 245
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
439-530 4.72e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 82.93  E-value: 4.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  439 PSQVVVIRQERAGQTSVSLLWQEPEQPNGIILEYEIKYYEKD-KEMQSYSTLKAVTTRATVSGLKPGTRYVFQVRARTSA 517
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGsGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80
                          90
                  ....*....|...
gi 341940659  518 GCGRFSQAMEVET 530
Cdd:cd00063    81 GESPPSESVTVTT 93
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
640-882 5.32e-19

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: 88.19  E-value: 5.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGrlqVPGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGS 719
Cdd:cd06642    12 IGKGSFGEVYKG---IDNRTKEVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIMEYLGGGS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  720 LDAFLRThdGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYTTAGGKI 799
Cdd:cd06642    89 ALDLLKP--GPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNTFVGTPF 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  800 pirWTAPEAIAFRTFSSASDVWSFGVVMWEvLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALHQLMLDCWHKDRA 879
Cdd:cd06642   167 ---WMAPEVIKQSAYDFKADIWSLGITAIE-LAKGEPPNSDLHPMRVLFLIPKNSPPTLEGQHSKPFKEFVEACLNKDPR 242

                  ...
gi 341940659  880 QRP 882
Cdd:cd06642   243 FRP 245
SAM_EPH-A10 cd09549
SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
933-994 5.83e-19

SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A10 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A10 receptors and appears to mediate cell-cell initiated signal transduction. It was found preferentially expressed in the testis. EphA10 may be involved in the pathogenesis and development of prostate carcinoma and lymphocytic leukemia. It is a potential molecular marker and/or therapy target for these types of cancers.


Pssm-ID: 188948  Cd Length: 70  Bit Score: 81.83  E-value: 5.83e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 341940659  933 TVGDWLDSIRMGRYRDHFAAGGYSSLGMVLRMNAQDVRALGITLMGHQKKILGSIQTMRAQL 994
Cdd:cd09549     9 SVGEWLEALDLCRYKDNFAAAGYGSLEAVARMTAQDVLSLGITSLEHQELLLAGIQALRAQV 70
fn3 pfam00041
Fibronectin type III domain;
438-523 5.86e-19

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 82.46  E-value: 5.86e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659   438 APSQVVVIRQeraGQTSVSLLWQEPEQPNGIILEYEIKYYEKDK-EMQSYSTLKAVTTRATVSGLKPGTRYVFQVRARTS 516
Cdd:pfam00041    2 APSNLTVTDV---TSTSLTVSWTPPPDGNGPITGYEVEYRPKNSgEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78

                   ....*..
gi 341940659   517 AGCGRFS 523
Cdd:pfam00041   79 GGEGPPS 85
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
636-890 9.71e-19

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: 87.33  E-value: 9.71e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIIGSGESGEVCYGRLQVPGQrdvPVAIKALKAG--YTERQRQDFLSEAAIMGQFDHPNIIR-LEGVVTRGRLaMIVT 712
Cdd:cd08224     4 IEKKIGKGQFSVVYRARCLLDGR---LVALKKVQIFemMDAKARQDCLKEIDLLQQLNHPNIIKyLASFIENNEL-NIVL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  713 EYMENGSLDAFLRTHDGQFT----------IVQLVGMLrgvgagmRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSR 782
Cdd:cd08224    80 ELADAGDLSRLIKHFKKQKRlipertiwkyFVQLCSAL-------EHMHSKRIMHRDIKPANVFITANGVVKLGDLGLGR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  783 ALEDDPEAAYTTAGgkIPIrWTAPEAIAFRTFSSASDVWSFGVVMWEVLA-----YGErpywNMTNQDVISSVEEGYRLP 857
Cdd:cd08224   153 FFSSKTTAAHSLVG--TPY-YMSPERIREQGYDFKSDIWSLGCLLYEMAAlqspfYGE----KMNLYSLCKKIEKCEYPP 225
                         250       260       270
                  ....*....|....*....|....*....|....
gi 341940659  858 APMGC-PRALHQLMLDCWHKDRAQRPRFAHVVSV 890
Cdd:cd08224   226 LPADLySQELRDLVAACIQPDPEKRPDISYVLDV 259
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
640-831 1.12e-18

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: 86.52  E-value: 1.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQRdvpVAIKALKAgYTERQRQDfLSEAAIMGQF----DHPNIIRLEGVVTR---GRLAMiVT 712
Cdd:cd05118     7 IGEGAFGTVWLARDKVTGEK---VAIKKIKN-DFRHPKAA-LREIKLLKHLndveGHPNIVKLLDVFEHrggNHLCL-VF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  713 EYMENgSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRL-VCKVSDFGLSRALEDDPeaa 791
Cdd:cd05118    81 ELMGM-NLYELIKDYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELgQLKLADFGLARSFTSPP--- 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 341940659  792 YTtagGKIPIRW-TAPEAI-AFRTFSSASDVWSFGVVMWEVL 831
Cdd:cd05118   157 YT---PYVATRWyRAPEVLlGAKPYGSSIDIWSLGCILAELL 195
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
636-838 1.34e-18

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: 86.54  E-value: 1.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIIGSGESGEVCYGRLQVPGQRdvpVAIKALKAG--YTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTE 713
Cdd:cd14081     5 LGKTLGKGQTGLVKLAKHCVTGQK---VAIKIVNKEklSKESVLMKVEREIAIMKLIEHPNVLKLYDVYENKKYLYLVLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  714 YMENGSLDAFLRTHdGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSrALEDDPEAAYT 793
Cdd:cd14081    82 YVSGGELFDYLVKK-GRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMA-SLQPEGSLLET 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 341940659  794 TAGGkiPiRWTAPEAIAFRTF-SSASDVWSFGVVMWeVLAYGERPY 838
Cdd:cd14081   160 SCGS--P-HYACPEVIKGEKYdGRKADIWSCGVILY-ALLVGALPF 201
PTK_Jak1_rpt1 cd05077
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely ...
656-888 1.38e-18

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; 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 cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Jak1 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: 270662 [Multi-domain]  Cd Length: 266  Bit Score: 86.91  E-value: 1.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  656 PGQRDVPVAikalkagyterqrqdFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLDAFLRTHDGQFTIVQ 735
Cdd:cd05077    46 PSHRDISLA---------------FFETASMMRQVSHKHIVLLYGVCVRDVENIMVEEFVEFGPLDLFMHRKSDVLTTPW 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  736 LVGMLRGVGAGMRYLSDLGYIHRDLAARNVLV-------DGRLVCKVSDFGLSRALEDDPEAAyttagGKIPirWTAPEA 808
Cdd:cd05077   111 KFKVAKQLASALSYLEDKDLVHGNVCTKNILLaregidgECGPFIKLSDPGIPITVLSRQECV-----ERIP--WIAPEC 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  809 IA-FRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPmGCpRALHQLMLDCWHKDRAQRPRFAHV 887
Cdd:cd05077   184 VEdSKNLSIAADKWSFGTTLWEICYNGEIPLKDKTLAEKERFYEGQCMLVTP-SC-KELADLMTHCMNYDPNQRPFFRAI 261

                  .
gi 341940659  888 V 888
Cdd:cd05077   262 M 262
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
636-882 1.45e-18

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


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 87.05  E-value: 1.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIiGSGESGEVCYGrlqVPGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYM 715
Cdd:cd06641     9 LEKI-GKGSFGEVFKG---IDNRTQKVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  716 ENGSLDAFLRThdGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYTTA 795
Cdd:cd06641    85 GGGSALDLLEP--GPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKRN*FV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  796 GGKIpirWTAPEAIAFRTFSSASDVWSFGVVMWEvLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALHQLMLDCWH 875
Cdd:cd06641   163 GTPF---WMAPEVIKQSAYDSKADIWSLGITAIE-LARGEPPHSELHPMKVLFLIPKNNPPTLEGNYSKPLKEFVEACLN 238

                  ....*..
gi 341940659  876 KDRAQRP 882
Cdd:cd06641   239 KEPSFRP 245
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
638-832 1.97e-18

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: 86.30  E-value: 1.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVPGQrdvPVAIK------ALKAGYTERQRQdflsEAAIMGQFDHPNIIRLEGVVTRGRLAMIV 711
Cdd:cd14663     6 RTLGEGTFAKVKFARNTKTGE---SVAIKiidkeqVAREGMVEQIKR----EIAIMKLLRHPNIVELHEVMATKTKIFFV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  712 TEYMENGSL------DAFLRTHDGQFTIVQLVgmlrgvgAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALE 785
Cdd:cd14663    79 MELVTGGELfskiakNGRLKEDKARKYFQQLI-------DAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSALSE 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 341940659  786 --DDPEAAYTTAGgkIPiRWTAPEAIAFRTFSSA-SDVWSFGVVMWEVLA 832
Cdd:cd14663   152 qfRQDGLLHTTCG--TP-NYVAPEVLARRGYDGAkADIWSCGVILFVLLA 198
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
635-843 2.09e-18

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: 85.77  E-value: 2.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  635 HIEKIIGSGESGEVCYGRLQVPGQRdvpVAIK-ALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTE 713
Cdd:cd14002     4 HVLELIGEGSFGKVYKGRRKYTGQV---VALKfIPKRGKSEKELRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  714 YMEnGSL------DAFLRTHDGQFTIVQLVGMLRgvgagmrYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDD 787
Cdd:cd14002    81 YAQ-GELfqiledDGTLPEEEVRSIAKQLVSALH-------YLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARAMSCN 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 341940659  788 PEAAYTTAGgkIPIrWTAPEAIAFRTFSSASDVWSFGVVMWEvLAYGERPYWnmTN 843
Cdd:cd14002   153 TLVLTSIKG--TPL-YMAPELVQEQPYDHTADLWSLGCILYE-LFVGQPPFY--TN 202
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
691-832 2.77e-18

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: 86.23  E-value: 2.77e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  691 DHPNIIRLEGVVTRGRLAMIVTEYMEnGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGR 770
Cdd:cd07832    58 GHPYVVKLRDVFPHGTGFVLVFEYML-SSLSEVLRDEERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISST 136
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 341940659  771 LVCKVSDFGLSRALEDDPEAAYTTaggKIPIRW-TAPEAI-AFRTFSSASDVWSFGVVMWEVLA 832
Cdd:cd07832   137 GVLKIADFGLARLFSEEDPRLYSH---QVATRWyRAPELLyGSRKYDEGVDLWAVGCIFAELLN 197
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
639-898 3.22e-18

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: 85.83  E-value: 3.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  639 IIGSGESGEVCYGRLQvpGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENG 718
Cdd:cd14202     9 LIGHGAFAVVFKGRHK--EKHDLEVAVKCINKKNLAKSQTLLGKEIKILKELKHENIVALYDFQEIANSVYLVMEYCNGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  719 SLDAFLRTHdGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVD---GR------LVCKVSDFGLSRALEDDPE 789
Cdd:cd14202    87 DLADYLHTM-RTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSysgGRksnpnnIRIKIADFGFARYLQNNMM 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  790 AAyTTAGGKIpirWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWNMTNQDVISSVEEGYRL----PAPMGCPra 865
Cdd:cd14202   166 AA-TLCGSPM---YMAPEVIMSQHYDAKADLWSIGTIIYQCLT-GKAPFQASSPQDLRLFYEKNKSLspniPRETSSH-- 238
                         250       260       270
                  ....*....|....*....|....*....|...
gi 341940659  866 LHQLMLDCWHKDRAQRPRFahvvsvlDALVHSP 898
Cdd:cd14202   239 LRQLLLGLLQRNQKDRMDF-------DEFFHHP 264
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
638-896 3.74e-18

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: 85.56  E-value: 3.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGeSGEVCYGrlqvpgQRDVP----VAIKALK-----AGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLA 708
Cdd:cd06630     6 PLLGTG-AFSSCYQ------ARDVKtgtlMAVKQVSfcrnsSSEQEEVVEAIREEIRMMARLNHPNIVRMLGATQHKSHF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  709 MIVTEYMENGSLDAFLRTHdGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVD--GRLVcKVSDFGLSRALed 786
Cdd:cd06630    79 NIFVEWMAGGSVASLLSKY-GAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDstGQRL-RIADFGAAARL-- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  787 dpeAAYTTAGGKI------PIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAygERPYWNMTNQD-------VISSVEEG 853
Cdd:cd06630   155 ---ASKGTGAGEFqgqllgTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMAT--AKPPWNAEKISnhlalifKIASATTP 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 341940659  854 yrLPAPMGCPRALHQLMLDCWHKDRAQRPrfahvvSVLDALVH 896
Cdd:cd06630   230 --PPIPEHLSPGLRDVTLRCLELQPEDRP------PARELLKH 264
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
636-831 4.54e-18

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


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 85.42  E-value: 4.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIIGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRL------EGVVtrgrlaM 709
Cdd:cd13996    10 EIELLGSGGFGSVYKVRNKVDGVT---YAIKKIRLTEKSSASEKVLREVKALAKLNHPNIVRYytawveEPPL------Y 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  710 IVTEYMENGSLDAFL--RTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGR-LVCKVSDFGLSRALED 786
Cdd:cd13996    81 IQMELCEGGTLRDWIdrRNSSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDdLQVKIGDFGLATSIGN 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 341940659  787 DPE-------------AAYTTAGGKipIRWTAPEAIAFRTFSSASDVWSFGVVMWEVL 831
Cdd:cd13996   161 QKRelnnlnnnnngntSNNSVGIGT--PLYASPEQLDGENYNEKADIYSLGIILFEML 216
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
638-859 5.72e-18

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: 85.08  E-value: 5.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQvpgQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMEN 717
Cdd:cd14167     9 EVLGTGAFSEVVLAEEK---RTQKLVAIKCIAKKALEGKETSIENEIAVLHKIKHPNIVALDDIYESGGHLYLIMQLVSG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  718 GSLdaFLR-THDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVL---VDGRLVCKVSDFGLSRAleDDPEAAYT 793
Cdd:cd14167    86 GEL--FDRiVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGLSKI--EGSGSVMS 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 341940659  794 TAGGKiPiRWTAPEAIAFRTFSSASDVWSFGVVMWeVLAYGERPYWNMTNQDVISSVEEG-YRLPAP 859
Cdd:cd14167   162 TACGT-P-GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDAKLFEQILKAeYEFDSP 225
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
663-831 6.75e-18

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: 85.35  E-value: 6.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  663 VAIKALKagyTERQRQDF----LSEAAIMGQFDHPNIIRLEGVVTRGRLAMI--VTEYMENgSLDAFLRTHDGQFTIVQL 736
Cdd:cd07843    33 VALKKLK---MEKEKEGFpitsLREINILLKLQHPNIVTVKEVVVGSNLDKIymVMEYVEH-DLKSLMETMKQPFLQSEV 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  737 VGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEdDPEAAYTTaggKIPIRW-TAPEAI-AFRTF 814
Cdd:cd07843   109 KCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLAREYG-SPLKPYTQ---LVVTLWyRAPELLlGAKEY 184
                         170
                  ....*....|....*..
gi 341940659  815 SSASDVWSFGVVMWEVL 831
Cdd:cd07843   185 STAIDMWSVGCIFAELL 201
SAM_EPH-A2 cd09543
SAM domain of EPH-A2 family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of ...
933-996 7.13e-18

SAM domain of EPH-A2 family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A2 subfamily of receptor tyrosine kinases is a C-terminal protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A2 receptors and appears to mediate cell-cell initiated signal transduction. For example, SAM domain of EPH-A2 receptors interacts with SAM domain of Ship2 proteins (SH2 containing phosphoinositide 5-phosphotase-2) forming heterodimers; such recruitment of Ship2 by EPH-A2 attenuates the positive signal for receptor endocytosis. Eph-A2 is found overexpressed in many types of human cancer, including breast, prostate, lung and colon cancer. High level of expression could induce cancer progression by a variety of mechanisms and could be used as a novel tag for cancer immunotherapy. EPH-A2 receptors are attractive targets for drag design.


Pssm-ID: 188942  Cd Length: 70  Bit Score: 78.72  E-value: 7.13e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 341940659  933 TVGDWLDSIRMGRYRDHFAAGGYSSLGMVLRMNAQDVRALGITLMGHQKKILGSIQTMRAQLSS 996
Cdd:cd09543     7 TVAEWLESIKMQQYTEHFMAAGYNSIDKVLQMTQEDIKHIGVRLPGHQKRIAYSILGLKEQVST 70
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
663-838 9.68e-18

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: 84.27  E-value: 9.68e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  663 VAIKALKAGyterQRQDFLSEAAIMGQFDHPNIIRL-EGVVTRGRLAMIVtEYMENGSLDAFLRtHDGQFT--IVQLVGm 739
Cdd:cd14010    28 VAIKCVDKS----KRPEVLNEVRLTHELKHPNVLKFyEWYETSNHLWLVV-EYCTGGDLETLLR-QDGNLPesSVRKFG- 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  740 lRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYTTAGG---------KIPIR----WTAP 806
Cdd:cd14010   101 -RDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLARREGEILKELFGQFSDegnvnkvskKQAKRgtpyYMAP 179
                         170       180       190
                  ....*....|....*....|....*....|..
gi 341940659  807 EAIAFRTFSSASDVWSFGVVMWEvLAYGERPY 838
Cdd:cd14010   180 ELFQGGVHSFASDLWALGCVLYE-MFTGKPPF 210
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
640-894 1.24e-17

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: 84.49  E-value: 1.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLqvpgqRDVPVAIKALKAGYT---ERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYME 716
Cdd:cd14159     1 IGEGGFGCVYQAVM-----RNTEYAVKRLKEDSEldwSVVKNSFLTEVEKLSRFRHPNIVDLAGYSAQQGNYCLIYVYLP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  717 NGSLDAFLRTHDG--QFTIVQLVGMLRGVGAGMRYLSDL--GYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAY 792
Cdd:cd14159    76 NGSLEDRLHCQVScpCLSWSQRLHVLLGTARAIQYLHSDspSLIHGDVKSSNILLDAALNPKLGDFGLARFSRRPKQPGM 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  793 T-----TAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERP-------------------------YWNMT 842
Cdd:cd14159   156 SstlarTQTVRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLT-GRRAmevdscsptkylkdlvkeeeeaqhtPTTMT 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 341940659  843 NQDVISSVEEGYRL------PAPMGCPR----ALHQLMLDCWHKDRAQRPRFAHVVSVLDAL 894
Cdd:cd14159   235 HSAEAQAAQLATSIcqkhldPQAGPCPPelgiEISQLACRCLHRRAKKRPPMTEVFQELERL 296
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
637-832 1.25e-17

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


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 84.73  E-value: 1.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  637 EKI--IGSGESGEVCYGRLQVPGQrdvpvaIKALKAGYTERQRQDF----LSEAAIMGQFDHPNIIRLEGVVTRGRLAMI 710
Cdd:cd07845    10 EKLnrIGEGTYGIVYRARDTTSGE------IVALKKVRMDNERDGIpissLREITLLLNLRHPNIVELKEVVVGKHLDSI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  711 --VTEYMENgSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEdDP 788
Cdd:cd07845    84 flVMEYCEQ-DLASLLDNMPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLARTYG-LP 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 341940659  789 EAAYTTaggKIPIRW-TAPEAI-AFRTFSSASDVWSFGVVMWEVLA 832
Cdd:cd07845   162 AKPMTP---KVVTLWyRAPELLlGCTTYTTAIDMWAVGCILAELLA 204
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
636-833 1.80e-17

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 85.31  E-value: 1.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIIGSGESGEVCYGRlqVPGQRDvPVAIKALKAGYTerqrqdfLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYM 715
Cdd:PHA03209   70 VIKTLTPGSEGRVFVAT--KPGQPD-PVVLKIGQKGTT-------LIEAMLLQNVNHPSVIRMKDTLVSGAITCMVLPHY 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  716 eNGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDG-RLVCkVSDFGLSRALEDDPeAAYTT 794
Cdd:PHA03209  140 -SSDLYTYLTKRSRPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINDvDQVC-IGDLGAAQFPVVAP-AFLGL 216
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 341940659  795 AGgkiPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAY 833
Cdd:PHA03209  217 AG---TVETNAPEVLARDKYNSKADIWSAGIVLFEMLAY 252
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
652-891 2.23e-17

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-C binds and is activated by the intestinal hormones, guanylin (GN) and uroguanylin (UGN), which are secreted after salty meals to inhibit sodium absorption and induce the secretion of chloride, bicarbonate, and water. GN and UGN are also present in the kidney, where they induce increased salt and water secretion. This prevents the development of hypernatremia and hypervolemia after ingestion of high amounts of salt. 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 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-C 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: 270946 [Multi-domain]  Cd Length: 271  Bit Score: 83.40  E-value: 2.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  652 RLQVPGQRDVPVAIKALK---AGYTERQRQdflsEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLDAFLRTH- 727
Cdd:cd14044    23 RLRQGKYDKKVVILKDLKnneGNFTEKQKI----ELNKLLQIDYYNLTKFYGTVKLDTMIFGVIEYCERGSLRDVLNDKi 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  728 ---DGQFTIVQL-VGMLRGVGAGMRYL-SDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAayttaggkipir 802
Cdd:cd14044    99 sypDGTFMDWEFkISVMYDIAKGMSYLhSSKTEVHGRLKSTNCVVDSRMVVKITDFGCNSILPPSKDL------------ 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  803 WTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGErPYWNMTNQDvisSVEEGYRLPAPMGC---------------PRALH 867
Cdd:cd14044   167 WTAPEHLRQAGTSQKGDVYSYGIIAQEIILRKE-TFYTAACSD---RKEKIYRVQNPKGMkpfrpdlnlesagerEREVY 242
                         250       260
                  ....*....|....*....|....
gi 341940659  868 QLMLDCWHKDRAQRPRFAHVVSVL 891
Cdd:cd14044   243 GLVKNCWEEDPEKRPDFKKIENTL 266
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
664-893 2.37e-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: 83.43  E-value: 2.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  664 AIKALKAGYTERQrqdflsEAAIMGQFDHPNIIRLEGVVTRGRlaMIVTEYMENGSLDAFLRTHDGQF-----TIVQLVG 738
Cdd:cd14000    47 ATDAMKNFRLLRQ------ELTVLSHLHHPSIVYLLGIGIHPL--MLVLELAPLGSLDHLLQQDSRSFaslgrTLQQRIA 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  739 MlrGVGAGMRYLSDLGYIHRDLAARNVLV-----DGRLVCKVSDFGLSRalEDDPEAAYTTAGGKipiRWTAPEAIAFRT 813
Cdd:cd14000   119 L--QVADGLRYLHSAMIIYRDLKSHNVLVwtlypNSAIIIKIADYGISR--QCCRMGAKGSEGTP---GFRAPEIARGNV 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  814 -FSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEegyRLPAPMG-----CPRALHQLMLDCWHKDRAQRPRFAHV 887
Cdd:cd14000   192 iYNEKVDVFSFGMLLYEILSGGAPMVGHLKFPNEFDIHG---GLRPPLKqyecaPWPEVEVLMKKCWKENPQQRPTAVTV 268

                  ....*.
gi 341940659  888 VSVLDA 893
Cdd:cd14000   269 VSILNS 274
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
636-831 2.45e-17

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: 83.71  E-value: 2.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIIGSGESGEVCYGRLQVPGQrdvPVAIKalkagyteRQRQD--FLS-EAAIMGQFDHPNIIRLEGV-VTRGRLAM-- 709
Cdd:cd14137     8 IEKVIGSGSFGVVYQAKLLETGE---VVAIK--------KVLQDkrYKNrELQIMRRLKHPNIVKLKYFfYSSGEKKDev 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  710 ---IVTEYMENgSLDAFLRTHDGQFTIVQLV-------GMLRGvgagMRYLSDLGYIHRDLAARNVLVDGR-LVCKVSDF 778
Cdd:cd14137    77 ylnLVMEYMPE-TLYRVIRHYSKNKQTIPIIyvklysyQLFRG----LAYLHSLGICHRDIKPQNLLVDPEtGVLKLCDF 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 341940659  779 GLSRALE-DDPEAAYttaggkIPIR-WTAPEAIA-FRTFSSASDVWSFGVVMWEVL 831
Cdd:cd14137   152 GSAKRLVpGEPNVSY------ICSRyYRAPELIFgATDYTTAIDIWSAGCVLAELL 201
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
640-838 2.64e-17

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: 83.30  E-value: 2.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQRDVP--VAIKALKAG--YTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYM 715
Cdd:cd14076     9 LGEGEFGKVKLGWPLPKANHRSGvqVAIKLIRRDtqQENCQTSKIMREINILKGLTHPNIVRLLDVLKTKKYIGIVLEFV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  716 ENGSL------DAFLRTHDGQFTIVQLVgmlrgvgAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRAL-EDDP 788
Cdd:cd14076    89 SGGELfdyilaRRRLKDSVACRLFAQLI-------SGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTFdHFNG 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 341940659  789 EAAYTTAGGKIpirWTAPEAIAFRTF--SSASDVWSFGVVMWEVLAyGERPY 838
Cdd:cd14076   162 DLMSTSCGSPC---YAAPELVVSDSMyaGRKADIWSCGVILYAMLA-GYLPF 209
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
636-839 2.85e-17

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: 83.40  E-value: 2.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIIGSGESGEVCYGRLQvpgQRDVPVAIKALKAGYTERQRQ--DFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTE 713
Cdd:cd05580     5 FLKTLGTGSFGRVRLVKHK---DSGKYYALKILKKAKIIKLKQveHVLNEKRILSEVRHPFIVNLLGSFQDDRNLYMVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  714 YMENGSLDAFLR------THDGQFTIVQLVGMLRgvgagmrYLSDLGYIHRDLAARNVLVD--GRLvcKVSDFGLSRALE 785
Cdd:cd05580    82 YVPGGELFSLLRrsgrfpNDVAKFYAAEVVLALE-------YLHSLDIVYRDLKPENLLLDsdGHI--KITDFGFAKRVK 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 341940659  786 DDpeaAYTTAGgkIPiRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYW 839
Cdd:cd05580   153 DR---TYTLCG--TP-EYLAPEIILSKGHGKAVDWWALGILIYEMLA-GYPPFF 199
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
634-853 3.15e-17

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: 82.66  E-value: 3.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  634 IHIEKIIGSGESGEVCYGRLQVPGQRdvpVAIKALKAgYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTE 713
Cdd:cd14190     6 IHSKEVLGGGKFGKVHTCTEKRTGLK---LAAKVINK-QNSKDKEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIVLFME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  714 YMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLV---DGRLVcKVSDFGLSRALedDPEA 790
Cdd:cd14190    82 YVEGGELFERIVDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCvnrTGHQV-KIIDFGLARRY--NPRE 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341940659  791 AYTTAGGKiPiRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWNMTNQDVISSVEEG 853
Cdd:cd14190   159 KLKVNFGT-P-EFLSPEVVNYDQVSFPTDMWSMGVITYMLLS-GLSPFLGDDDTETLNNVLMG 218
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
652-893 3.25e-17

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: 83.22  E-value: 3.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  652 RLQVPGQRDVPVAIKALKAGYTERQRQDFLS----EAAIMGQFDHPNIIRLEGVV--TRGR--LAMivtEYME---NGSL 720
Cdd:cd14001    20 RSPRGGSSRSPWAVKKINSKCDKGQRSLYQErlkeEAKILKSLNHPNIVGFRAFTksEDGSlcLAM---EYGGkslNDLI 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  721 DAFLRTHDGQFTIVQLVGMLRGVGAGMRYL-SDLGYIHRDLAARNVLVDGRL-VCKVSDFGLSRALED------DPEAAY 792
Cdd:cd14001    97 EERYEAGLGPFPAATILKVALSIARALEYLhNEKKILHGDIKSGNVLIKGDFeSVKLCDFGVSLPLTEnlevdsDPKAQY 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  793 TtagGKIPirWTAPEAI-AFRTFSSASDVWSFGVVMWEVLAYgERPYWNMTNQ---DVISSVEE------------GYRL 856
Cdd:cd14001   177 V---GTEP--WKAKEALeEGGVITDKADIFAYGLVLWEMMTL-SVPHLNLLDIeddDEDESFDEdeedeeayygtlGTRP 250
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 341940659  857 PAPMGCPRALHQLMLD----CWHKDRAQRPRFAHVVSVLDA 893
Cdd:cd14001   251 ALNLGELDDSYQKVIElfyaCTQEDPKDRPSAAHIVEALEA 291
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
639-848 3.39e-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: 83.14  E-value: 3.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  639 IIGSGESGEVcYGRLQVPGQRDVPVAIKALKAGYTERQRQDF----LSEAAIMGQFDHPNIIRLEGVVTRGRLAMI-VTE 713
Cdd:cd13990     7 LLGKGGFSEV-YKAFDLVEQRYVACKIHQLNKDWSEEKKQNYikhaLREYEIHKSLDHPRIVKLYDVFEIDTDSFCtVLE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  714 YMENGSLDAFLRTH------DGQFTIVQLVgmlrgvgAGMRYLSDL--GYIHRDLAARNVLVDGRLVC---KVSDFGLSR 782
Cdd:cd13990    86 YCDGNDLDFYLKQHksiperEARSIIMQVV-------SALKYLNEIkpPIIHYDLKPGNILLHSGNVSgeiKITDFGLSK 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341940659  783 ALEDDPEAAYT---TAGGKIPIRWTAPEAI----AFRTFSSASDVWSFGVVMWEVLaYGERPYWNMTNQDVIS 848
Cdd:cd13990   159 IMDDESYNSDGmelTSQGAGTYWYLPPECFvvgkTPPKISSKVDVWSVGVIFYQML-YGRKPFGHNQSQEAIL 230
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
640-838 3.55e-17

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: 83.27  E-value: 3.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQRdvpVAIKA--LKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGV------VTRGRLAMIV 711
Cdd:cd13989     1 LGSGGFGYVTLWKHQDTGEY---VAIKKcrQELSPSDKNRERWCLEVQIMKKLNHPNVVSARDVppelekLSPNDLPLLA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  712 TEYMENGSLDAFLRTHD-----GQFTIVQLvgmLRGVGAGMRYLSDLGYIHRDLAARNVL---VDGRLVCKVSDFGLSRA 783
Cdd:cd13989    78 MEYCSGGDLRKVLNQPEnccglKESEVRTL---LSDISSAISYLHENRIIHRDLKPENIVlqqGGGRVIYKLIDLGYAKE 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 341940659  784 LeDDPEAAYTTAGgkiPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPY 838
Cdd:cd13989   155 L-DQGSLCTSFVG---TLQYLAPELFESKKYTCTVDYWSFGTLAFECIT-GYRPF 204
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
587-829 3.73e-17

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 84.10  E-value: 3.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  587 QAPPPVFLPLNHPPGKFPETQFSAEPHTYEEPgRAGRSFTreiEASRIhieKIIGSGESGEVcYGRLQVPGQRdvPVAIK 666
Cdd:PLN00034   36 QRDPSLAVPLPLPPPSSSSSSSSSSSASGSAP-SAAKSLS---ELERV---NRIGSGAGGTV-YKVIHRPTGR--LYALK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  667 ALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLDAFLRTHDGQftivqLVGMLRGVGAG 746
Cdd:PLN00034  106 VIYGNHEDTVRRQICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSLEGTHIADEQF-----LADVARQILSG 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  747 MRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYTTAGgkiPIRWTAPEAIAF-----RTFSSASDVW 821
Cdd:PLN00034  181 IAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRILAQTMDPCNSSVG---TIAYMSPERINTdlnhgAYDGYAGDIW 257

                  ....*...
gi 341940659  822 SFGVVMWE 829
Cdd:PLN00034  258 SLGVSILE 265
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
637-873 4.04e-17

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: 82.34  E-value: 4.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  637 EKIiGSGESGEVcYGRLQVPGQRDVpVAIKA-LKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYM 715
Cdd:cd14121     1 EKL-GSGTYATV-YKAYRKSGAREV-VAVKCvSKSSLNKASTENLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  716 ENGSLDAFLRTHdGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRL--VCKVSDFGLSRALEDDpEAAYT 793
Cdd:cd14121    78 SGGDLSRFIRSR-RTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYnpVLKLADFGFAQHLKPN-DEAHS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  794 TAGGkiPIrWTAPEAIAFRTFSSASDVWSFGVVMWEVLaYGERPYWNMTnqdvISSVEEGYRLPAPMGCPRALHqLMLDC 873
Cdd:cd14121   156 LRGS--PL-YMAPEMILKKKYDARVDLWSVGVILYECL-FGRAPFASRS----FEELEEKIRSSKPIEIPTRPE-LSADC 226
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
638-866 4.29e-17

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: 83.60  E-value: 4.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVPGQRDVPVAIKAL-KAGYTERQRQDFLSEAAIMGQFDHPNIIRLE-GVVTRGRLAMIVtEYM 715
Cdd:cd05582     1 KVLGQGSFGKVFLVRKITGPDAGTLYAMKVLkKATLKVRDRVRTKMERDILADVNHPFIVKLHyAFQTEGKLYLIL-DFL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  716 ENGslDAFLR-THDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYTT 794
Cdd:cd05582    80 RGG--DLFTRlSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKESIDHEKKAYSF 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 341940659  795 AGgkiPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWNMTNQDVISSVeegyrLPAPMGCPRAL 866
Cdd:cd05582   158 CG---TVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GSLPFQGKDRKETMTMI-----LKAKLGMPQFL 220
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
640-840 4.57e-17

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: 83.11  E-value: 4.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGqRDVPVAIKALKagytERQRQDFL-SEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENG 718
Cdd:cd06659    29 IGEGSTGVVCIAREKHSG-RQVAVKMMDLR----KQQRRELLfNEVVIMRDYQHPNVVEMYKSYLVGEELWVLMEYLQGG 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  719 SLDAFLRthDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVL--VDGRLvcKVSDFGLSRALEDDPEAAYTTAG 796
Cdd:cd06659   104 ALTDIVS--QTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILltLDGRV--KLSDFGFCAQISKDVPKRKSLVG 179
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 341940659  797 GKIpirWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWN 840
Cdd:cd06659   180 TPY---WMAPEVISRCPYGTEVDIWSLGIMVIEMVD-GEPPYFS 219
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
682-831 4.97e-17

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: 81.99  E-value: 4.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  682 SEAAIMGQFDHPNIIRL-EGVVTRGRLaMIVTEYMENGSL-DAFlrTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRD 759
Cdd:cd14095    47 NEVAILRRVKHPNIVQLiEEYDTDTEL-YLVMELVKGGDLfDAI--TSSTKFTERDASRMVTDLAQALKYLHSLSIVHRD 123
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 341940659  760 LAARNVLV----DGRLVCKVSDFGLsrALEdDPEAAYTTAGgkIPIrWTAPEAIAFRTFSSASDVWSFGVVMWEVL 831
Cdd:cd14095   124 IKPENLLVveheDGSKSLKLADFGL--ATE-VKEPLFTVCG--TPT-YVAPEILAETGYGLKVDIWAAGVITYILL 193
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
669-894 5.40e-17

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: 81.80  E-value: 5.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  669 KAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMR 748
Cdd:cd14156    24 KIYKNDVDQHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCLEELLAREELPLSWREKVELACDISRGMV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  749 YLSDLGYIHRDLAARNVLV----DGRLVCkVSDFGLSRALED----DPEAAYTTAGGKIpirWTAPEAIAFRTFSSASDV 820
Cdd:cd14156   104 YLHSKNIYHRDLNSKNCLIrvtpRGREAV-VTDFGLAREVGEmpanDPERKLSLVGSAF---WMAPEMLRGEPYDRKVDV 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  821 WSFGVVMWEVLayGERPywnmTNQDVISSVEE------GYRLPAPmGCPRALHQLMLDCWHKDRAQRPRFAHVVSVLDAL 894
Cdd:cd14156   180 FSFGIVLCEIL--ARIP----ADPEVLPRTGDfgldvqAFKEMVP-GCPEPFLDLAASCCRMDAFKRPSFAELLDELEDI 252
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
638-882 5.52e-17

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: 82.07  E-value: 5.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGrlqVPGQRDVPVAIKALKAGYTERQRQDFLS----EAAIMGQFDHPNIIRLEGVVTRGRLAMIVTE 713
Cdd:cd06632     6 QLLGSGSFGSVYEG---FNGDTGDFFAVKEVSLVDDDKKSRESVKqleqEIALLSKLRHPNIVQYYGTEREEDNLYIFLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  714 YMENGSLDAFLRTHdGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALeddpEAAYT 793
Cdd:cd06632    83 YVPGGSIHKLLQRY-GAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHV----EAFSF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  794 TAGGKIPIRWTAPEAIAFR--TFSSASDVWSFGVVMWEvLAYGERPYWNMTNQDVISSVEEGYRLPA-PMGCPRALHQLM 870
Cdd:cd06632   158 AKSFKGSPYWMAPEVIMQKnsGYGLAVDIWSLGCTVLE-MATGKPPWSQYEGVAAIFKIGNSGELPPiPDHLSPDAKDFI 236
                         250
                  ....*....|..
gi 341940659  871 LDCWHKDRAQRP 882
Cdd:cd06632   237 RLCLQRDPEDRP 248
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
640-841 7.51e-17

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: 81.34  E-value: 7.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQrdvPVAIKalKAGYTERQR----QDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYM 715
Cdd:cd06607     9 IGHGSFGAVYYARNKRTSE---VVAIK--KMSYSGKQStekwQDIIKEVKFLRQLRHPNTIEYKGCYLREHTAWLVMEYC 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  716 EnGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGlSRALEDdpeAAYTTA 795
Cdd:cd06607    84 L-GSASDIVEVHKKPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFG-SASLVC---PANSFV 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 341940659  796 GgkIPIrWTAPEAIAFR---TFSSASDVWSFGVVMWEvLAYGERPYWNM 841
Cdd:cd06607   159 G--TPY-WMAPEVILAMdegQYDGKVDVWSLGITCIE-LAERKPPLFNM 203
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
640-838 8.54e-17

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: 81.44  E-value: 8.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVcygRLQVPGQRDVPVAIKALkagytERQR------QDFL-SEAAIMGQFDHPNIIRLEGV--VTRGRLaMI 710
Cdd:cd14164     8 IGEGSFSKV---KLATSQKYCCKVAIKIV-----DRRRaspdfvQKFLpRELSILRRVNHPNIVQMFECieVANGRL-YI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  711 VTEYMENGSLDAFLRTH-----DGQFTIVQLVGmlrgvgaGMRYLSDLGYIHRDLAARNVLV--DGRLVcKVSDFGLSRA 783
Cdd:cd14164    79 VMEAAATDLLQKIQEVHhipkdLARDMFAQMVG-------AVNYLHDMNIVHRDLKCENILLsaDDRKI-KIADFGFARF 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 341940659  784 LEDDPEAAYTTAGGKIpirWTAPEAIAFRTFSSAS-DVWSFGVVMWeVLAYGERPY 838
Cdd:cd14164   151 VEDYPELSTTFCGSRA---YTPPEVILGTPYDPKKyDVWSLGVVLY-VMVTGTMPF 202
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
689-891 8.73e-17

Pseudokinase domain of the unknown subfamily 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: 270947 [Multi-domain]  Cd Length: 269  Bit Score: 81.44  E-value: 8.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  689 QFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVD 768
Cdd:cd14045    58 ELDHPNLCKFIGGCIEVPNVAIITEYCPKGSLNDVLLNEDIPLNWGFRFSFATDIARGMAYLHQHKIYHGRLKSSNCVID 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  769 GRLVCKVSDFGLSRALEDDPEAAYTTAGGKIPIRWTAPEAIAFRTF--SSASDVWSFGVVMWEVLAYGErpywnmTNQDV 846
Cdd:cd14045   138 DRWVCKIADYGLTTYRKEDGSENASGYQQRLMQVYLPPENHSNTDTepTQATDVYSYAIILLEIATRND------PVPED 211
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 341940659  847 ISSVEEGYRLPAP----------MGCPRALHQLMLDCWHKDRAQRPRFAHVVSVL 891
Cdd:cd14045   212 DYSLDEAWCPPLPelisgktensCPCPADYVELIRRCRKNNPAQRPTFEQIKKTL 266
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
663-892 9.74e-17

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: 81.06  E-value: 9.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  663 VAIKAL------KAGYTERQRQdflsEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLDAFLRTHDGQFTIVQL 736
Cdd:cd14186    29 VAIKMIdkkamqKAGMVQRVRN----EVEIHCQLKHPSILELYNYFEDSNYVYLVLEMCHNGEMSRYLKNRKKPFTEDEA 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  737 VGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYTTAGGKipiRWTAPEAIAFRTFSS 816
Cdd:cd14186   105 RHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKMPHEKHFTMCGTP---NYISPEIATRSAHGL 181
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 341940659  817 ASDVWSFGVVMWEVLAyGERPYWNMTNQDVISSVEEG-YRLPAPMGcpRALHQLMLDCWHKDRAQRPRFAhvvSVLD 892
Cdd:cd14186   182 ESDVWSLGCMFYTLLV-GRPPFDTDTVKNTLNKVVLAdYEMPAFLS--REAQDLIHQLLRKNPADRLSLS---SVLD 252
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
640-838 1.09e-16

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: 80.73  E-value: 1.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQRdvpVAIKALKAgYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGS 719
Cdd:cd14103     1 LGRGKFGTVYRCVEKATGKE---LAAKFIKC-RKAKDREDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAGGE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  720 LdaFLRTHDGQFTIVQLVGML--RGVGAGMRYLSDLGYIHRDLAARNVLV---DGRLVcKVSDFGLSRALEDD------- 787
Cdd:cd14103    77 L--FERVVDDDFELTERDCILfmRQICEGVQYMHKQGILHLDLKPENILCvsrTGNQI-KIIDFGLARKYDPDkklkvlf 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 341940659  788 --PEaayttaggkipirWTAPEAIAFRTFSSASDVWSFGVVMWeVLAYGERPY 838
Cdd:cd14103   154 gtPE-------------FVAPEVVNYEPISYATDMWSVGVICY-VLLSGLSPF 192
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
638-844 1.26e-16

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: 81.19  E-value: 1.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEV--CY----GRL----QVPGQRDVPVAIKALKagyterqrqdflSEAAIMGQFDHPNIIRLEGV-VTRGR 706
Cdd:cd06626     6 NKIGEGTFGKVytAVnldtGELmamkEIRFQDNDPKTIKEIA------------DEMKVLEGLDHPNLVRYYGVeVHREE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  707 LaMIVTEYMENGSLDAFLRtHDG--------QFTIvQLVgmlrgvgAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDF 778
Cdd:cd06626    74 V-YIFMEYCQEGTLEELLR-HGRildeavirVYTL-QLL-------EGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDF 143
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 341940659  779 GLSRALED-----DPEAAYTTAGGKIpirWTAPEAIAFRTFSS---ASDVWSFGVVMWEvLAYGERPYWNMTNQ 844
Cdd:cd06626   144 GSAVKLKNntttmAPGEVNSLVGTPA---YMAPEVITGNKGEGhgrAADIWSLGCVVLE-MATGKRPWSELDNE 213
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
628-884 1.58e-16

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: 80.82  E-value: 1.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  628 EIEASRihiEKIIGSGESGEVCYGRLQvpGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRL 707
Cdd:cd14201     5 DFEYSR---KDLVGHGAFAVVFKGRHR--KKTDWEVAIKSINKKNLSKSQILLGKEIKILKELQHENIVALYDVQEMPNS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  708 AMIVTEYMENGSLDAFLRThDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVD--GR-------LVCKVSDF 778
Cdd:cd14201    80 VFLVMEYCNGGDLADYLQA-KGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSyaSRkkssvsgIRIKIADF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  779 GLSRALEDDPEAAyTTAGGKIpirWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWNMTNQDVISSVEEGYRL-P 857
Cdd:cd14201   159 GFARYLQSNMMAA-TLCGSPM---YMAPEVIMSQHYDAKADLWSIGTVIYQCLV-GKPPFQANSPQDLRMFYEKNKNLqP 233
                         250       260
                  ....*....|....*....|....*...
gi 341940659  858 A-PMGCPRALHQLMLDCWHKDRAQRPRF 884
Cdd:cd14201   234 SiPRETSPYLADLLLGLLQRNQKDRMDF 261
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
933-993 2.00e-16

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 74.64  E-value: 2.00e-16
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 341940659    933 TVGDWLDSIRMGRYRDHFAAGGYSSLGMVLRMNAQDVRALGITLMGHQKKILGSIQTMRAQ 993
Cdd:smart00454    8 SVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLKEQ 68
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
640-838 2.11e-16

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


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 80.73  E-value: 2.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGV-----VTRGRLAMIVTEY 714
Cdd:cd14039     1 LGTGGFGNVCLYQNQETGEK---IAIKSCRLELSVKNKDRWCHEIQIMKKLNHPNVVKACDVpeemnFLVNDVPLLAMEY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  715 MENGSLDAFLRTHDG--QFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVL---VDGRLVCKVSDFGLSRALedDPE 789
Cdd:cd14039    78 CSGGDLRKLLNKPENccGLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVlqeINGKIVHKIIDLGYAKDL--DQG 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 341940659  790 AAYTTAGGKipIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPY 838
Cdd:cd14039   156 SLCTSFVGT--LQYLAPELFENKSYTVTVDYWSFGTMVFECIA-GFRPF 201
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
632-837 2.20e-16

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: 81.21  E-value: 2.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  632 SRIHIEKIIGSGESGEVCYGRlQVPGQRDVpvaikALKAGYTERQRQDF----LSEAAIMGQFDHPNIIRLEGVV----- 702
Cdd:cd07866     8 RDYEILGKLGEGTFGEVYKAR-QIKTGRVV-----ALKKILMHNEKDGFpitaLREIKILKKLKHPNVVPLIDMAverpd 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  703 ----TRGRLAMiVTEYMENgSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDF 778
Cdd:cd07866    82 kskrKRGSVYM-VTPYMDH-DLSGLLENPSVKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADF 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 341940659  779 GLSRALEDDP----------EAAYTtagGKIPIRW-TAPEAIA-FRTFSSASDVWSFGVVMWEVlaYGERP 837
Cdd:cd07866   160 GLARPYDGPPpnpkggggggTRKYT---NLVVTRWyRPPELLLgERRYTTAVDIWGIGCVFAEM--FTRRP 225
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
644-843 3.12e-16

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: 79.76  E-value: 3.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  644 ESGE-VCYGRLQ---VPGQRD----VPVAIKALKAGYtERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYM 715
Cdd:cd06624     9 ESGErVVLGKGTfgvVYAARDlstqVRIAIKEIPERD-SREVQPLHEEIALHSRLSHKNIVQYLGSVSEDGFFKIFMEQV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  716 ENGSLDAFLRT-----HDGQFTIVQLVgmlRGVGAGMRYLSDLGYIHRDLAARNVLVD---GrlVCKVSDFGLSRALEDD 787
Cdd:cd06624    88 PGGSLSALLRSkwgplKDNENTIGYYT---KQILEGLKYLHDNKIVHRDIKGDNVLVNtysG--VVKISDFGTSKRLAGI 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 341940659  788 PEAAYTTAGgkiPIRWTAPEAIA--FRTFSSASDVWSFGVVMWEvLAYGERPYWNMTN 843
Cdd:cd06624   163 NPCTETFTG---TLQYMAPEVIDkgQRGYGPPADIWSLGCTIIE-MATGKPPFIELGE 216
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
683-853 3.18e-16

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: 79.90  E-value: 3.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  683 EAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLDAFLRtHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAA 762
Cdd:cd14097    50 EVDILKHVNHAHIIHLEEVFETPKRMYLVMELCEDGELKELLL-RKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKL 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  763 RNVLVDG-------RLVCKVSDFGLSRALEDDPEAAYTTAGGKiPIrWTAPEAIAFRTFSSASDVWSFGVVMWeVLAYGE 835
Cdd:cd14097   129 ENILVKSsiidnndKLNIKVTDFGLSVQKYGLGEDMLQETCGT-PI-YMAPEVISAHGYSQQCDIWSIGVIMY-MLLCGE 205
                         170
                  ....*....|....*...
gi 341940659  836 RPYWNMTNQDVISSVEEG 853
Cdd:cd14097   206 PPFVAKSEEKLFEEIRKG 223
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
640-827 3.24e-16

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: 79.66  E-value: 3.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEV--CYGRLQVPGQRdvpVAIKALKAGYTERQRQDF----LSEAAIMGQFDHPNIIR-LEGVVTRGRLAMIVT 712
Cdd:cd13994     1 IGKGATSVVriVTKKNPRSGVL---YAVKEYRRRDDESKRKDYvkrlTSEYIISSKLHHPNIVKvLDLCQDLHGKWCLVM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  713 EYMENGSLDAFLRThDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALED--DPEA 790
Cdd:cd13994    78 EYCPGGDLFTLIEK-ADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAEVFGMpaEKES 156
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 341940659  791 AYTT-AGGKIPirWTAPEAIAFRTFS-SASDVWSFGVVM 827
Cdd:cd13994   157 PMSAgLCGSEP--YMAPEVFTSGSYDgRAVDVWSCGIVL 193
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
663-847 3.45e-16

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: 79.65  E-value: 3.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  663 VAIKAL-KAGYTERQRQDFL-SEAAIMGQFDHPNIIR-LEGVVTRGRLaMIVTEYMENGSLDAFLRTHdGQFTIVQLVGM 739
Cdd:cd14162    28 VAIKIVsKKKAPEDYLQKFLpREIEVIKGLKHPNLICfYEAIETTSRV-YIIMELAENGDLLDYIRKN-GALPEPQARRW 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  740 LRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRaleddpeAAYTTAGGKIPIRWT--------APE---A 808
Cdd:cd14162   106 FRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFAR-------GVMKTKDGKPKLSETycgsyayaSPEilrG 178
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 341940659  809 IAFRTFssASDVWSFGVVMWEVLaYGERPYWNmTNQDVI 847
Cdd:cd14162   179 IPYDPF--LSDIWSMGVVLYTMV-YGRLPFDD-SNLKVL 213
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
638-838 3.59e-16

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: 79.83  E-value: 3.59e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVcYGRLQVPGQRdvPVAIKALKAGYTERQRQDFLSEAAIMGQFDH---PNIIRLEGVVTRGRLAMIVTEY 714
Cdd:cd06917     7 ELVGRGSYGAV-YRGYHVKTGR--VVALKVLNLDTDDDDVSDIQKEVALLSQLKLgqpKNIIKYYGSYLKGPSLWIIMDY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  715 MENGSLDAFLRThdGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYTT 794
Cdd:cd06917    84 CEGGSIRTLMRA--GPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQNSSKRSTF 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 341940659  795 AGgkIPIrWTAPEAIA-FRTFSSASDVWSFGVVMWEvLAYGERPY 838
Cdd:cd06917   162 VG--TPY-WMAPEVITeGKYYDTKADIWSLGITTYE-MATGNPPY 202
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
638-897 3.67e-16

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: 79.71  E-value: 3.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEV--CY----GR----LQVPGQRDVPVAIKALKAGYTERQrqdflseaaIMGQFDHPNIIRLEGVVTRGRL 707
Cdd:cd06625     6 KLLGQGAFGQVylCYdadtGRelavKQVEIDPINTEASKEVKALECEIQ---------LLKNLQHERIVQYYGCLQDEKS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  708 AMIVTEYMENGSLDAFLRTHdGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEdd 787
Cdd:cd06625    77 LSIFMEYMPGGSVKDEIKAY-GALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASKRLQ-- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  788 peaAYTTAGGKIPIR----WTAPEAIAFRTFSSASDVWSFGVVMWEVLAygERPYWN----MTNQDVISSVEEGYRLPAp 859
Cdd:cd06625   154 ---TICSSTGMKSVTgtpyWMSPEVINGEGYGRKADIWSVGCTVVEMLT--TKPPWAefepMAAIFKIATQPTNPQLPP- 227
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 341940659  860 mGCPRALHQLMLDCWHKDRAQRPrfahvvSVLDALVHS 897
Cdd:cd06625   228 -HVSEDARDFLSLIFVRNKKQRP------SAEELLSHS 258
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
640-884 3.73e-16

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: 79.33  E-value: 3.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRlqVPGQRDVPVAIKAL-KAGYTerQRQDFLS-EAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMEN 717
Cdd:cd14120     1 IGHGAFAVVFKGR--HRKKPDLPVAIKCItKKNLS--KSQNLLGkEIKILKELSHENVVALLDCQETSSSVYLVMEYCNG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  718 GSLDAFLRTHdGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVD---------GRLVCKVSDFGLSRALEDDP 788
Cdd:cd14120    77 GDLADYLQAK-GTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLShnsgrkpspNDIRLKIADFGFARFLQDGM 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  789 EAAyTTAGGKIpirWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWNMTNQDVISSVEEGYRL-PA-PMGCPRAL 866
Cdd:cd14120   156 MAA-TLCGSPM---YMAPEVIMSLQYDAKADLWSIGTIVYQCLT-GKAPFQAQTPQELKAFYEKNANLrPNiPSGTSPAL 230
                         250       260
                  ....*....|....*....|.
gi 341940659  867 HQL---MLDCWHKDRAQRPRF 884
Cdd:cd14120   231 KDLllgLLKRNPKDRIDFEDF 251
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
633-894 4.35e-16

Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KSR1 functions as a transducer of TNFalpha-stimulated C-Raf activation of ERK1/2 and NF-kB. Detected activity of KSR1 is cell type specific and context dependent. It is inactive in normal colon epithelial cells and becomes activated at the onset of inflammatory bowel disease (IBD). Similarly, KSR1 activity is undetectable prior to stimulation by EGF or ceramide in COS-7 or YAMC cells, respectively. KSR proteins are widely regarded as pseudokinases, however, this matter is up for debate as catalytic activity has been detected for KSR1 in some systems. The KSR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 79.63  E-value: 4.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  633 RIHIEKIIGSGESGEVCYGRLQvpGQrdvpVAIKALKA-GYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIV 711
Cdd:cd14152     1 QIELGELIGQGRWGKVHRGRWH--GE----VAIRLLEIdGNNQDHLKLFKKEVMNYRQTRHENVVLFMGACMHPPHLAII 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  712 TEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVD-GRLVckVSDFGL---SRALEDD 787
Cdd:cd14152    75 TSFCKGRTLYSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDnGKVV--ITDFGLfgiSGVVQEG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  788 PEAAYTtaggKIPIRWT---APEAIAFRT---------FSSASDVWSFGVVMWEVLAYGerpyWNMTNQDV------ISS 849
Cdd:cd14152   153 RRENEL----KLPHDWLcylAPEIVREMTpgkdedclpFSKAADVYAFGTIWYELQARD----WPLKNQPAealiwqIGS 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 341940659  850 VEEGYRLPAPMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVLDAL 894
Cdd:cd14152   225 GEGMKQVLTTISLGKEVTEILSACWAFDLEERPSFTLLMDMLEKL 269
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
683-893 4.38e-16

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: 79.23  E-value: 4.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  683 EAAIMGQFDHPNIIRLEGVVTRGRlaMIVTEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAA 762
Cdd:cd14068    37 ELVVLSHLHHPSLVALLAAGTAPR--MLVMELAPKGSLDALLQQDNASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKP 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  763 RNVLV-----DGRLVCKVSDFGLSR-ALEDDPEAAYTTAGgkipirWTAPE-AIAFRTFSSASDVWSFGVVMWEVLAYGE 835
Cdd:cd14068   115 HNVLLftlypNCAIIAKIADYGIAQyCCRMGIKTSEGTPG------FRAPEvARGNVIYNQQADVYSFGLLLYDILTCGE 188
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341940659  836 RPYWNMTNQDVISSVEEGYRLPAPM---GCP--RALHQLMLDCWHKDRAQRPRFAHVVSVLDA 893
Cdd:cd14068   189 RIVEGLKFPNEFDELAIQGKLPDPVkeyGCApwPGVEALIKDCLKENPQCRPTSAQVFDILNS 251
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
607-840 4.65e-16

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


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 80.08  E-value: 4.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  607 QFSAEPHTYEEPGRAgrsftREIEASRIHIekiiGSGESGEVCYGRLQVPGQRdvpVAIKalKAGYTERQRQDFL-SEAA 685
Cdd:cd06658     6 QFRAALQLVVSPGDP-----REYLDSFIKI----GEGSTGIVCIATEKHTGKQ---VAVK--KMDLRKQQRRELLfNEVV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  686 IMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLDAFLrTHDgQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNV 765
Cdd:cd06658    72 IMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGALTDIV-THT-RMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSI 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 341940659  766 LV--DGRLvcKVSDFGLSRALEDDPEAAYTTAGGKIpirWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWN 840
Cdd:cd06658   150 LLtsDGRI--KLSDFGFCAQVSKEVPKRKSLVGTPY---WMAPEVISRLPYGTEVDIWSLGIMVIEMID-GEPPYFN 220
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
640-832 4.93e-16

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: 79.67  E-value: 4.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQRdvpVAIKALKAGY-TERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENG 718
Cdd:cd07833     9 VGEGAYGVVLKCRNKATGEI---VAIKKFKESEdDEDVKKTALREVKVLRQLRHENIVNLKEAFRRKGRLYLVFEYVERT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  719 SLDAFLRTHDG------QFTIVQLvgmLRGVGagmrYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAY 792
Cdd:cd07833    86 LLELLEASPGGlppdavRSYIWQL---LQAIA----YCHSHNIIHRDIKPENILVSESGVLKLCDFGFARALTARPASPL 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 341940659  793 TTaggKIPIRW-TAPEAIAFRT-FSSASDVWSFGVVMWEVLA 832
Cdd:cd07833   159 TD---YVATRWyRAPELLVGDTnYGKPVDVWAIGCIMAELLD 197
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
638-854 5.20e-16

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: 79.65  E-value: 5.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYTERQrQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMEN 717
Cdd:cd14166     9 EVLGSGAFSEVYLVKQRSTGKL---YALKCIKKSPLSRD-SSLENEIAVLKRIKHENIVTLEDIYESTTHYYLVMQLVSG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  718 GSLdaFLRTHD-GQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLV---DGRLVCKVSDFGLSRaLEDDpeAAYT 793
Cdd:cd14166    85 GEL--FDRILErGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFGLSK-MEQN--GIMS 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 341940659  794 TAGGKiPiRWTAPEAIAFRTFSSASDVWSFGVVMWeVLAYGERPYWNMTNQDVISSVEEGY 854
Cdd:cd14166   160 TACGT-P-GYVAPEVLAQKPYSKAVDCWSIGVITY-ILLCGYPPFYEETESRLFEKIKEGY 217
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
633-832 5.49e-16

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


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 79.39  E-value: 5.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  633 RIHIEKIIGSGESGEVcygrLQV--PGQRDVPVAIKALK---AGYTERQRQdfLSEAAIMGQFD---HPNIIRLEGVVTR 704
Cdd:cd14052     1 RFANVELIGSGEFSQV----YKVseRVPTGKVYAVKKLKpnyAGAKDRLRR--LEEVSILRELTldgHDNIVQLIDSWEY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  705 GRLAMIVTEYMENGSLDAFLrTHDGQFTIV---QLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLV--DGRLvcKVSDFG 779
Cdd:cd14052    75 HGHLYIQTELCENGSLDVFL-SELGLLGRLdefRVWKILVELSLGLRFIHDHHFVHLDLKPANVLItfEGTL--KIGDFG 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 341940659  780 L--------SRALEDDPEaayttaggkipirWTAPEAIAFRTFSSASDVWSFGVVMWEVLA 832
Cdd:cd14052   152 MatvwplirGIEREGDRE-------------YIAPEILSEHMYDKPADIFSLGLILLEAAA 199
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
636-838 6.71e-16

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: 78.73  E-value: 6.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIIGSGESGEVCygRLQVPGQRDvPVAIKALKAGYteRQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYM 715
Cdd:cd14087     5 IKALIGRGSFSRVV--RVEHRVTRQ-PYAIKMIETKC--RGREVCESELNVLRRVRHTNIIQLIEVFETKERVYMVMELA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  716 ENGSLdaFLR-THDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVL-----VDGRLVckVSDFGLSRALEDDPE 789
Cdd:cd14087    80 TGGEL--FDRiIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLyyhpgPDSKIM--ITDFGLASTRKKGPN 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 341940659  790 AAYTTAGGKiPiRWTAPEAIAFRTFSSASDVWSFGVVMWeVLAYGERPY 838
Cdd:cd14087   156 CLMKTTCGT-P-EYIAPEILLRKPYTQSVDMWAVGVIAY-ILLSGTMPF 201
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
632-886 6.93e-16

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: 78.58  E-value: 6.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  632 SRIHIEKIIGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYTErQRQDFL---SEAAIMGQFDHPNIIRLEGVVTRGRLA 708
Cdd:cd14073     1 HRYELLETLGKGTYGKVKLAIERATGRE---VAIKSIKKDKIE-DEQDMVrirREIEIMSSLNHPHIIRIYEVFENKDKI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  709 MIVTEYMENGSLDAFLrTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDp 788
Cdd:cd14073    77 VIVMEYASGGELYDYI-SERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSNLYSKD- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  789 EAAYTTAGGKIpirWTAPEAIAFRTFSSAS-DVWSFGVVMWeVLAYGERPYWNMTNQDVISSVEEG-YRLPAPMGCPRAL 866
Cdd:cd14073   155 KLLQTFCGSPL---YASPEIVNGTPYQGPEvDCWSLGVLLY-TLVYGTMPFDGSDFKRLVKQISSGdYREPTQPSDASGL 230
                         250       260
                  ....*....|....*....|
gi 341940659  867 HQLMLDCWHKDRAQRPRFAH 886
Cdd:cd14073   231 IRWMLTVNPKRRATIEDIAN 250
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
439-520 8.46e-16

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 73.42  E-value: 8.46e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659    439 PSQVVVIRQERAGQTSVSLLWQEPEQPNGI--ILEYEIKYYEKDKEMQSYSTlKAVTTRATVSGLKPGTRYVFQVRARTS 516
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITgyIVGYRVEYREEGSEWKEVNV-TPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                    ....
gi 341940659    517 AGCG 520
Cdd:smart00060   80 AGEG 83
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
638-882 9.00e-16

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes 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 region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as TGFbR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. TGFbR2 acts as the receptor for TGFbeta, which is crucial in growth control and homeostasis in many different tissues. It plays roles in regulating apoptosis and in maintaining the balance between self renewal and cell loss. It also plays a key role in maintaining vascular integrity and in regulating responses to genotoxic stress. Mutations in TGFbR2 can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. The TGFbR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 78.96  E-value: 9.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRL-QVPGQRDVPVAIKALKagYTE----RQRQDFLSEAAImgqfDHPNIIRL----EGVVTRGRLA 708
Cdd:cd14055     1 KLVGKGRFAEVWKAKLkQNASGQYETVAVKIFP--YEEyaswKNEKDIFTDASL----KHENILQFltaeERGVGLDRQY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  709 MIVTEYMENGSLDAFLRTHdgQFTIVQLVGMLRGVGAGMRYL-SD--------LGYIHRDLAARNVLVDGRLVCKVSDFG 779
Cdd:cd14055    75 WLITAYHENGSLQDYLTRH--ILSWEDLCKMAGSLARGLAHLhSDrtpcgrpkIPIAHRDLKSSNILVKNDGTCVLADFG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  780 LsrALEDDPEAA---YTTAGGKIPIRWTAPEAIAFR-------TFSSAsDVWSFGVVMWEvlaygerpywnMTNQDVISS 849
Cdd:cd14055   153 L--ALRLDPSLSvdeLANSGQVGTARYMAPEALESRvnledleSFKQI-DVYSMALVLWE-----------MASRCEASG 218
                         250       260       270
                  ....*....|....*....|....*....|....
gi 341940659  850 VEEGYRLP-APMGCPRALHQLMLDCWHKDRaQRP 882
Cdd:cd14055   219 EVKPYELPfGSKVRERPCVESMKDLVLRDR-GRP 251
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
635-838 9.13e-16

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: 78.80  E-value: 9.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  635 HIEKIIGSGESGEVCYGRLQVPGQrdvPVAIKALKAGYTERQR-QDFLS-EAAIMGQFDHPNIIRLEGvvT---RGRLAM 709
Cdd:cd05581     4 KFGKPLGEGSYSTVVLAKEKETGK---EYAIKVLDKRHIIKEKkVKYVTiEKEVLSRLAHPGIVKLYY--TfqdESKLYF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  710 iVTEYMENGSLDAFLRT------HDGQFTIVQLVgmlrgvgAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRA 783
Cdd:cd05581    79 -VLEYAPNGDLLEYIRKygsldeKCTRFYTAEIV-------LALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGTAKV 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 341940659  784 L--EDDPEAAYTTAGGKIPI------------RWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPY 838
Cdd:cd05581   151 LgpDSSPESTKGDADSQIAYnqaraasfvgtaEYVSPELLNEKPAGKSSDLWALGCIIYQMLT-GKPPF 218
SAM_EPH-B6 cd09555
SAM domain of EPH-B6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
936-994 9.84e-16

SAM domain of EPH-B6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B6 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B6 receptors and appears to mediate cell-cell initiated signal transduction. Receptors of this type are highly expressed in embryo and adult nervous system, in thymus and also in T-cells. They are involved in regulation of cell adhesion and migration. (EPH-B6 receptor is unusual; it fails to show catalytic activity due to alteration in kinase domain). EPH-B6 may be considered as a biomarker in some types of tumors; EPH-B6 activates MAP kinase signaling in lung adenocarcinoma, suppresses metastasis formation in non-small cell lung cancer, and slows invasiveness in some breast cancer cell lines.


Pssm-ID: 188954  Cd Length: 69  Bit Score: 72.65  E-value: 9.84e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 341940659  936 DWLDSIRMGRYRDHFAAGGYSSLGMVLRMNAQDVRALGITLMGHQKKILGSIQTMRAQL 994
Cdd:cd09555    11 AWLSAIGLECYQDNFSKFGLCTFSDVAQLSLEDLPALGITLAGHQKKLLHHIQLLQQHL 69
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
637-831 1.18e-15

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: 78.77  E-value: 1.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  637 EKIIGSGESGEVCYGRLQVPGQrdvPVAIKALKAGytERQR------QDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMI 710
Cdd:cd07841     5 GKKLGEGTYAVVYKARDKETGR---IVAIKKIKLG--ERKEakdginFTALREIKLLQELKHPNIIGLLDVFGHKSNINL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  711 VTEYMEnGSLDAFLRTHDGQFT---IVQLVGM-LRGVgagmRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALED 786
Cdd:cd07841    80 VFEFME-TDLEKVIKDKSIVLTpadIKSYMLMtLRGL----EYLHSNWILHRDLKPNNLLIASDGVLKLADFGLARSFGS 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 341940659  787 DPEaAYTTaggKIPIRW-TAPEaIAF--RTFSSASDVWSFGVVMWEVL 831
Cdd:cd07841   155 PNR-KMTH---QVVTRWyRAPE-LLFgaRHYGVGVDMWSVGCIFAELL 197
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
933-991 2.10e-15

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 71.53  E-value: 2.10e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 341940659   933 TVGDWLDSIRMGRYRDHFAAGGYSSLGMVLRMNAQDVRALGITLMGHQKKILGSIQTMR 991
Cdd:pfam07647    8 SVADWLRSIGLEQYTDNFRDQGITGAELLLRLTLEDLKRLGITSVGHRRKILKKIQELK 66
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
636-843 2.27e-15

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: 77.30  E-value: 2.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIIGSGESGEVCYGRLQVPGQRdvpVAIKAL-KAGYTERQR-QDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTE 713
Cdd:cd05578     4 ILRVIGKGSFGKVCIVQKKDTKKM---FAMKYMnKQKCIEKDSvRNVLNELEILQELEHPFLVNLWYSFQDEEDMYMVVD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  714 YMENGSLdaflRTHDGQ---FT--IVQLvgMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDP 788
Cdd:cd05578    81 LLLGGDL----RYHLQQkvkFSeeTVKF--YICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATKLTDGT 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 341940659  789 EAayTTAGGKIPirWTAPEAIAFRTFSSASDVWSFGVVMWEVLaYGERPYWNMTN 843
Cdd:cd05578   155 LA--TSTSGTKP--YMAPEVFMRAGYSFAVDWWSLGVTAYEML-RGKRPYEIHSR 204
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
638-882 2.29e-15

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: 77.16  E-value: 2.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVPGQRDVPVAIKALKAgyTERQRQDFLSEAAIMGQFDHPNIIRL-EGVVTRGRLaMIVTEYME 716
Cdd:cd08218     6 KKIGEGSFGKALLVKSKEDGKQYVIKEINISKM--SPKEREESRKEVAVLSKMKHPNIVQYqESFEENGNL-YIVMDYCD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  717 NGSLDAFLRTHDG-QFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYTTA 795
Cdd:cd08218    83 GGDLYKRINAQRGvLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVLNSTVELARTCI 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  796 GGKIpirWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYgERPY--WNMTNqdVISSVEEGYRLPAPMGCPRALHQLMLDC 873
Cdd:cd08218   163 GTPY---YLSPEICENKPYNNKSDIWALGCVLYEMCTL-KHAFeaGNMKN--LVLKIIRGSYPPVPSRYSYDLRSLVSQL 236

                  ....*....
gi 341940659  874 WHKDRAQRP 882
Cdd:cd08218   237 FKRNPRDRP 245
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
627-885 2.37e-15

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: 77.80  E-value: 2.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  627 REIEASRIHIEKIIGSGESGEVCYGRLQVPGQrdvPVAIKAL-KAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRG 705
Cdd:cd06618    10 YKADLNDLENLGEIGSGTCGQVYKMRHKKTGH---VMAVKQMrRSGNKEENKRILMDLDVVLKSHDCPYIVKCYGYFITD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  706 RLAMIVTEYMENgSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDL-GYIHRDLAARNVLVDGRLVCKVSDFGLSRAL 784
Cdd:cd06618    87 SDVFICMELMST-CLDKLLKRIQGPIPEDILGKMTVSIVKALHYLKEKhGVIHRDVKPSNILLDESGNVKLCDFGISGRL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  785 EDDpeAAYTTAGGKIPirWTAPEAIAFRTFSS---ASDVWSFGVVMWEvLAYGERPYWNM-TNQDVISSV--EEGYRLPA 858
Cdd:cd06618   166 VDS--KAKTRSAGCAA--YMAPERIDPPDNPKydiRADVWSLGISLVE-LATGQFPYRNCkTEFEVLTKIlnEEPPSLPP 240
                         250       260
                  ....*....|....*....|....*..
gi 341940659  859 PMGCPRALHQLMLDCWHKDRAQRPRFA 885
Cdd:cd06618   241 NEGFSPDFCSFVDLCLTKDHRYRPKYR 267
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
640-841 2.59e-15

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: 78.16  E-value: 2.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRlqvPGQRDVPVAIKalKAGYTERQR----QDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYM 715
Cdd:cd06633    29 IGHGSFGAVYFAT---NSHTNEVVAIK--KMSYSGKQTnekwQDIIKEVKFLQQLKHPNTIEYKGCYLKDHTAWLVMEYC 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  716 EnGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGlsRALEDDPEAAYTTA 795
Cdd:cd06633   104 L-GSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFG--SASIASPANSFVGT 180
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 341940659  796 ggkiPIrWTAPEAIAFR---TFSSASDVWSFGVVMWEvLAYGERPYWNM 841
Cdd:cd06633   181 ----PY-WMAPEVILAMdegQYDGKVDIWSLGITCIE-LAERKPPLFNM 223
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
325-518 3.01e-15

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 80.05  E-value: 3.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  325 TRPPSAPVNL-ISSVNGTSVTLEWAPPLDPGGRSditYNaVCRrcpwalshceACGSGTRFVpQQTSLAQASLLVANLLA 403
Cdd:COG3401   230 TTPPSAPTGLtATADTPGSVTLSWDPVTESDATG---YR-VYR----------SNSGDGPFT-KVATVTTTSYTDTGLTN 294
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  404 HMNYSFWIEAVNGVSNLSPeprSAAVVNITTNQAAPSQVVVIRQERAGQTSVSLLWQEPEQPNgiILEYEIkyYEKDKEM 483
Cdd:COG3401   295 GTTYYYRVTAVDAAGNESA---PSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSDAD--VTGYNV--YRSTSGG 367
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 341940659  484 QSYSTLKAV--TTRATVSGLKPGTRYVFQVRARTSAG 518
Cdd:COG3401   368 GTYTKIAETvtTTSYTDTGLTPGTTYYYKVTAVDAAG 404
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
640-838 4.25e-15

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: 77.53  E-value: 4.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVT--RGRLAMIVTEYMEN 717
Cdd:cd13988     1 LGQGATANVFRGRHKKTGDL---YAVKVFNNLSFMRPLDVQMREFEVLKKLNHKNIVKLFAIEEelTTRHKVLVMELCPC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  718 GSLDAFLRT-------HDGQFTIVqlvgmLRGVGAGMRYLSDLGYIHRDLAARNVLV----DGRLVCKVSDFGLSRALED 786
Cdd:cd13988    78 GSLYTVLEEpsnayglPESEFLIV-----LRDVVAGMNHLRENGIVHRDIKPGNIMRvigeDGQSVYKLTDFGAARELED 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 341940659  787 DPEAA--YTTAGGKIPI---RWTAPEAIAfRTFSSASDVWSFGVVMWEVlAYGERPY 838
Cdd:cd13988   153 DEQFVslYGTEEYLHPDmyeRAVLRKDHQ-KKYGATVDLWSIGVTFYHA-ATGSLPF 207
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
635-841 4.30e-15

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: 76.19  E-value: 4.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  635 HIEKIIGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYTErQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEY 714
Cdd:cd06613     3 ELIQRIGSGTYGDVYKARNIATGEL---AAVKVIKLEPGD-DFEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVMEY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  715 MENGSL-DAFLRThdGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDdpeaayT 793
Cdd:cd06613    79 CGGGSLqDIYQVT--GPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQLTA------T 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 341940659  794 TAGGKIPI---RWTAPEAIAFR---TFSSASDVWSFGVVMWEvLAYGERPYWNM 841
Cdd:cd06613   151 IAKRKSFIgtpYWMAPEVAAVErkgGYDGKCDIWALGITAIE-LAELQPPMFDL 203
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
640-840 4.49e-15

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: 76.99  E-value: 4.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQRdvpVAIKalKAGYTERQRQDFL-SEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENG 718
Cdd:cd06657    28 IGEGSTGIVCIATVKSSGKL---VAVK--KMDLRKQQRRELLfNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGG 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  719 SLDAFLrTHDgQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLV--DGRLvcKVSDFGLSRALEDDPEAAYTTAG 796
Cdd:cd06657   103 ALTDIV-THT-RMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLthDGRV--KLSDFGFCAQVSKEVPRRKSLVG 178
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 341940659  797 GKIpirWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWN 840
Cdd:cd06657   179 TPY---WMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPYFN 218
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
633-894 5.17e-15

Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR2 interacts with the protein phosphatase calcineurin and functions in calcium-mediated ERK signaling. It also functions in energy metabolism by regulating AMP kinase and AMPK-dependent processes such as glucose uptake and fatty acid oxidation. KSR proteins act as scaffold proteins that function 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. The KSR2 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: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 76.20  E-value: 5.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  633 RIHIEKIIGSGESGEVCYGRLQvpGQrdvpVAIKALKAGY-TERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIV 711
Cdd:cd14153     1 QLEIGELIGKGRFGQVYHGRWH--GE----VAIRLIDIERdNEEQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAII 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  712 TEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVD-GRLVckVSDFGLSrALEDDPEA 790
Cdd:cd14153    75 TSLCKGRTLYSVVRDAKVVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDnGKVV--ITDFGLF-TISGVLQA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  791 AYTTAGGKIPIRW---TAPEAIAFRT---------FSSASDVWSFGVVMWEVLAYgERPYWNMTNQDVISSVEEGYR-LP 857
Cdd:cd14153   152 GRREDKLRIQSGWlchLAPEIIRQLSpeteedklpFSKHSDVFAFGTIWYELHAR-EWPFKTQPAEAIIWQVGSGMKpNL 230
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 341940659  858 APMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVLDAL 894
Cdd:cd14153   231 SQIGMGKEISDILLFCWAYEQEERPTFSKLMEMLEKL 267
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
663-838 5.46e-15

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: 75.97  E-value: 5.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  663 VAIKALKagyTERQRQDFLS-----EAAIMGQFDHPNIIRLEGV--VTRGRLaMIVTEYMENGSLDAFLRTHdGQFTIVQ 735
Cdd:cd14165    29 VAIKIID---KKKAPDDFVEkflprELEILARLNHKSIIKTYEIfeTSDGKV-YIVMELGVQGDLLEFIKLR-GALPEDV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  736 LVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDpeaayttAGGKIPIRWT--------APE 807
Cdd:cd14165   104 ARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCLRD-------ENGRIVLSKTfcgsaayaAPE 176
                         170       180       190
                  ....*....|....*....|....*....|..
gi 341940659  808 AIAFRTFS-SASDVWSFGVVMWeVLAYGERPY 838
Cdd:cd14165   177 VLQGIPYDpRIYDIWSLGVILY-IMVCGSMPY 207
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
631-831 6.29e-15

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: 77.34  E-value: 6.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  631 ASRIHIEKIIGSGESGEVCYGRLQVPGQRdvpVAIKalKAGYTERQR--QDFLSEAAIMGQFDHPNIIRLEGVVTRGRLA 708
Cdd:cd07849     4 GPRYQNLSYIGEGAYGMVCSAVHKPTGQK---VAIK--KISPFEHQTycLRTLREIKILLRFKHENIIGILDIQRPPTFE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  709 -----MIVTEYMENgSLDAFLRTHD-----GQFTIVQlvgMLRGVgagmRYLSDLGYIHRDLAARNVLVDGRLVCKVSDF 778
Cdd:cd07849    79 sfkdvYIVQELMET-DLYKLIKTQHlsndhIQYFLYQ---ILRGL----KYIHSANVLHRDLKPSNLLLNTNCDLKICDF 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 341940659  779 GLSRAleDDPEAAYTtagGK----IPIRW-TAPE-AIAFRTFSSASDVWSFGVVMWEVL 831
Cdd:cd07849   151 GLARI--ADPEHDHT---GFlteyVATRWyRAPEiMLNSKGYTKAIDIWSVGCILAEML 204
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
673-882 6.41e-15

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


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 75.93  E-value: 6.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  673 TERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLDAFLRTHDGQ-FTIVQLVGMLRGVGAGMRYLS 751
Cdd:cd08221    39 SEKERRDALNEIDILSLLNHDNIITYYNHFLDGESLFIEMEYCNGGNLHDKIAQQKNQlFPEEVVLWYLYQIVSAVSHIH 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  752 DLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYTTAGGKIpirWTAPEAIAFRTFSSASDVWSFGVVMWEVL 831
Cdd:cd08221   119 KAGILHRDIKTLNIFLTKADLVKLGDFGISKVLDSESSMAESIVGTPY---YMSPELVQGVKYNFKSDIWAVGCVLYELL 195
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 341940659  832 AYgeRPYWNMTNQ-DVISSVEEGYRLPAPMGCPRALHQLMLDCWHKDRAQRP 882
Cdd:cd08221   196 TL--KRTFDATNPlRLAVKIVQGEYEDIDEQYSEEIIQLVHDCLHQDPEDRP 245
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
639-844 6.52e-15

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: 76.77  E-value: 6.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  639 IIGSGESGEVCYGRLQVPGQrdvpvaIKALKAGYTERQRQDF----LSEAAIMGQFDHPNIIRLEGVVTRGRLAM----- 709
Cdd:cd07864    14 IIGEGTYGQVYKAKDKDTGE------LVALKKVRLDNEKEGFpitaIREIKILRQLNHRSVVNLKEIVTDKQDALdfkkd 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  710 -----IVTEYMENgSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRAL 784
Cdd:cd07864    88 kgafyLVFEYMDH-DLMGLLESGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFGLARLY 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 341940659  785 EDDPEAAYTTaggKIPIRWTAPEAIAF--RTFSSASDVWSFGVVMWEVlaYGERPYWNMTNQ 844
Cdd:cd07864   167 NSEESRPYTN---KVITLWYRPPELLLgeERYGPAIDVWSCGCILGEL--FTKKPIFQANQE 223
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
640-828 6.53e-15

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


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 75.84  E-value: 6.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYTERQRQDFLS-EAAIMGQFDHPNIIRLEGVV-TRGRLaMIVTEYMEN 717
Cdd:cd14075    10 LGSGNFSQVKLGIHQLTKEK---VAIKILDKTKLDQKTQRLLSrEISSMEKLHHPNIIRLYEVVeTLSKL-HLVMEYASG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  718 GSLDAFLRThDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALedDPEAAYTTAGG 797
Cdd:cd14075    86 GELYTKIST-EGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFSTHA--KRGETLNTFCG 162
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 341940659  798 KIPirWTAPEaiafrTFSSAS------DVWSFGVVMW 828
Cdd:cd14075   163 SPP--YAAPE-----LFKDEHyigiyvDIWALGVLLY 192
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
637-838 8.65e-15

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: 75.77  E-value: 8.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  637 EKIIGSGESGEVCY-GRLQvpgqrDVPVAIKALKAGYTE--RQRQDFLSEAAimgqfDHPNIIRLEGVVTRGRLAMIVTE 713
Cdd:cd13982     6 PKVLGYGSEGTIVFrGTFD-----GRPVAVKRLLPEFFDfaDREVQLLRESD-----EHPNVIRYFCTEKDRQFLYIALE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  714 --------YMENGslDAFLRTHdgqFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVD-----GRLVCKVSDFGL 780
Cdd:cd13982    76 lcaaslqdLVESP--RESKLFL---RPGLEPVRLLRQIASGLAHLHSLNIVHRDLKPQNILIStpnahGNVRAMISDFGL 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 341940659  781 SRALEDDPEAAYTTAGGKIPIRWTAPEAI----AFRTfSSASDVWSFGVVMWEVLAYGERPY 838
Cdd:cd13982   151 CKKLDVGRSSFSRRSGVAGTSGWIAPEMLsgstKRRQ-TRAVDIFSLGCVFYYVLSGGSHPF 211
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
636-890 9.64e-15

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: 75.84  E-value: 9.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIIGSGESGEVCYGRLQVPGqrdVPVAIKALKAG--YTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTE 713
Cdd:cd08229    28 IEKKIGRGQFSEVYRATCLLDG---VPVALKKVQIFdlMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLE 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  714 YMENGSLDAFLRTHDGQFTIVQLVGMLR---GVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEA 790
Cdd:cd08229   105 LADAGDLSRMIKHFKKQKRLIPEKTVWKyfvQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTA 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  791 AYTTAGGKIpirWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYgERPYW--NMTNQDVISSVEEGYRLPAPMG-CPRALH 867
Cdd:cd08229   185 AHSLVGTPY---YMSPERIHENGYNFKSDIWSLGCLLYEMAAL-QSPFYgdKMNLYSLCKKIEQCDYPPLPSDhYSEELR 260
                         250       260
                  ....*....|....*....|...
gi 341940659  868 QLMLDCWHKDRAQRPRFAHVVSV 890
Cdd:cd08229   261 QLVNMCINPDPEKRPDITYVYDV 283
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
620-842 9.66e-15

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 76.40  E-value: 9.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  620 RAGRSFTREIEA----SRIHIEKIIGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYTER--QRQDFLSEAAIMGQFDHP 693
Cdd:PTZ00263    2 KAAYMFTKPDTSswklSDFEMGETLGTGSFGRVRIAKHKGTGEY---YAIKCLKKREILKmkQVQHVAQEKSILMELSHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  694 NIIR-LEGVVTRGRLaMIVTEYMENGSLDAFLRT-----HD-GQFTIVQLVgmlrgvgAGMRYLSDLGYIHRDLAARNVL 766
Cdd:PTZ00263   79 FIVNmMCSFQDENRV-YFLLEFVVGGELFTHLRKagrfpNDvAKFYHAELV-------LAFEYLHSKDIIYRDLKPENLL 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 341940659  767 VDGRLVCKVSDFGLSRALeddPEAAYTTAGgkIPiRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWNMT 842
Cdd:PTZ00263  151 LDNKGHVKVTDFGFAKKV---PDRTFTLCG--TP-EYLAPEVIQSKGHGKAVDWWTMGVLLYEFIA-GYPPFFDDT 219
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
639-847 1.00e-14

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: 76.25  E-value: 1.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  639 IIGSGESGEVcYGRLQVPGQRDVPVAIKALKAGYTERQRQDFLSEAA----IMGQFDHPNIIRLEGVVTRGRLAM-IVTE 713
Cdd:cd14041    13 LLGRGGFSEV-YKAFDLTEQRYVAVKIHQLNKNWRDEKKENYHKHACreyrIHKELDHPRIVKLYDYFSLDTDSFcTVLE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  714 YMENGSLDAFLRTH------DGQFTIVQLVGMLRgvgagmrYLSDLG--YIHRDLAARNVLVDGRLVC---KVSDFGLSR 782
Cdd:cd14041    92 YCEGNDLDFYLKQHklmsekEARSIIMQIVNALK-------YLNEIKppIIHYDLKPGNILLVNGTACgeiKITDFGLSK 164
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 341940659  783 ALEDDP----EAAYTTAGGKIPIRWTAPEAIAF----RTFSSASDVWSFGVVMWEVLaYGERPY-WNMTNQDVI 847
Cdd:cd14041   165 IMDDDSynsvDGMELTSQGAGTYWYLPPECFVVgkepPKISNKVDVWSVGVIFYQCL-YGRKPFgHNQSQQDIL 237
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
646-857 1.01e-14

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: 75.38  E-value: 1.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  646 GEVCYGRLQVPGQRD-VPVAIKALKAGYTeRQRQDFL---SEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLD 721
Cdd:cd14161    12 GKGTYGRVKKARDSSgRLVAIKSIRKDRI-KDEQDLLhirREIEIMSSLNHPHIISVYEVFENSSKIVIVMEYASRGDLY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  722 AFLrTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDpEAAYTTAGGKIpi 801
Cdd:cd14161    91 DYI-SERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSNLYNQD-KFLQTYCGSPL-- 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 341940659  802 rWTAPEAIAFRTFSSAS-DVWSFGVVMWeVLAYGERPYWNMTNQDVISSVEEG-YRLP 857
Cdd:cd14161   167 -YASPEIVNGRPYIGPEvDSWSLGVLLY-ILVHGTMPFDGHDYKILVKQISSGaYREP 222
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
639-882 1.05e-14

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: 75.92  E-value: 1.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  639 IIGSGESGEVCYGRLQVPGQrdvpvaIKALK----AGYTERQRQdFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMI--VT 712
Cdd:cd06621     8 SLGEGAGGSVTKCRLRNTKT------IFALKtittDPNPDVQKQ-ILRELEINKSCASPYIVKYYGAFLDEQDSSIgiAM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  713 EYMENGSLDAF---LRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPE 789
Cdd:cd06621    81 EYCEGGSLDSIykkVKKKGGRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVSGELVNSLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  790 AAYTTAGgkipiRWTAPEAIAFRTFSSASDVWSFGVVMWEVlAYGERPYWNMTNQDV--ISSVEEGYRLPAPM--GCP-- 863
Cdd:cd06621   161 GTFTGTS-----YYMAPERIQGGPYSITSDVWSLGLTLLEV-AQNRFPFPPEGEPPLgpIELLSYIVNMPNPElkDEPen 234
                         250       260
                  ....*....|....*....|....
gi 341940659  864 -----RALHQLMLDCWHKDRAQRP 882
Cdd:cd06621   235 gikwsESFKDFIEKCLEKDGTRRP 258
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
632-890 1.09e-14

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


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 75.45  E-value: 1.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  632 SRIHIEKIIGSGESGEVCYGRLQVPGQrdvPVAIKALK--AGYTERQRQDFLSEAAIMGQFDHPNIIR-LEGVVTRGRLA 708
Cdd:cd08228     2 ANFQIEKKIGRGQFSEVYRATCLLDRK---PVALKKVQifEMMDAKARQDCVKEIDLLKQLNHPNVIKyLDSFIEDNELN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  709 mIVTEYMENGSLDAFLRTHDGQFTIVQLVGMLR---GVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALE 785
Cdd:cd08228    79 -IVLELADAGDLSQMIKYFKKQKRLIPERTVWKyfvQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  786 DDPEAAYTTAGGKIpirWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYgERPYWN--MTNQDVISSVEEGYRLPAPM-GC 862
Cdd:cd08228   158 SKTTAAHSLVGTPY---YMSPERIHENGYNFKSDIWSLGCLLYEMAAL-QSPFYGdkMNLFSLCQKIEQCDYPPLPTeHY 233
                         250       260
                  ....*....|....*....|....*...
gi 341940659  863 PRALHQLMLDCWHKDRAQRPRFAHVVSV 890
Cdd:cd08228   234 SEKLRELVSMCIYPDPDQRPDIGYVHQI 261
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
640-840 1.40e-14

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: 74.96  E-value: 1.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVcYGRLQVPGQRDVpvAIKALKAGyTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGS 719
Cdd:cd06647    15 IGQGASGTV-YTAIDVATGQEV--AIKQMNLQ-QQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  720 L-DAFLRT--HDGQFTIVqlvgmLRGVGAGMRYLSDLGYIHRDLAARNVLV--DGRLvcKVSDFGLSRALEddPEAAYTT 794
Cdd:cd06647    91 LtDVVTETcmDEGQIAAV-----CRECLQALEFLHSNQVIHRDIKSDNILLgmDGSV--KLTDFGFCAQIT--PEQSKRS 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 341940659  795 AGGKIPIrWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWN 840
Cdd:cd06647   162 TMVGTPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLN 205
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
643-885 1.50e-14

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: 75.48  E-value: 1.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  643 GESGEVCYGRLQ--VPGQRDVPVAIKALKAGYTERQRQDFLSEA-AIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENgS 719
Cdd:cd06616    12 GEIGRGAFGTVNkmLHKPSGTIMAVKRIRSTVDEKEQKRLLMDLdVVMRSSDCPYIVKFYGALFREGDCWICMELMDI-S 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  720 LDAFLRT-HDGQFTIV--QLVG--MLRGVGAgMRYL-SDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDdpEAAYT 793
Cdd:cd06616    91 LDKFYKYvYEVLDSVIpeEILGkiAVATVKA-LNYLkEELKIIHRDVKPSNILLDRNGNIKLCDFGISGQLVD--SIAKT 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  794 TAGGKIPirWTAPEAIAfrTFSSA------SDVWSFGVVMWEVlAYGERPY--WNmTNQDVISSVEEGyrlPAPMGCPRA 865
Cdd:cd06616   168 RDAGCRP--YMAPERID--PSASRdgydvrSDVWSLGITLYEV-ATGKFPYpkWN-SVFDQLTQVVKG---DPPILSNSE 238
                         250       260
                  ....*....|....*....|....*..
gi 341940659  866 LHQLMLD-------CWHKDRAQRPRFA 885
Cdd:cd06616   239 EREFSPSfvnfvnlCLIKDESKRPKYK 265
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
632-854 1.68e-14

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: 74.72  E-value: 1.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  632 SRIHIEKIIGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIV 711
Cdd:cd14083     3 DKYEFKEVLGTGAFSEVVLAEDKATGKL---VAIKCIDKKALKGKEDSLENEIAVLRKIKHPNIVQLLDIYESKSHLYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  712 TEYMENGSLdaFLR-THDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVL-----VDGRLVckVSDFGLSRaLE 785
Cdd:cd14083    80 MELVTGGEL--FDRiVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLyyspdEDSKIM--ISDFGLSK-ME 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 341940659  786 DdpEAAYTTAGGKiPiRWTAPEAIAFRTFSSASDVWSFGVVMWeVLAYGERPYWNMTNQDVISSVEEGY 854
Cdd:cd14083   155 D--SGVMSTACGT-P-GYVAPEVLAQKPYGKAVDCWSIGVISY-ILLCGYPPFYDENDSKLFAQILKAE 218
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
689-883 2.56e-14

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: 73.93  E-value: 2.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  689 QFDHPNIIRLEGV-VTR-----GRLAMIVTEYMENGSLDAFLRTHdGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAA 762
Cdd:cd14012    54 KLRHPNLVSYLAFsIERrgrsdGWKVYLLTEYAPGGSLSELLDSV-GSVPLDTARRWTLQLLEALEYLHRNGVVHKSLHA 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  763 RNVLVD---GRLVCKVSDFGLSRALEDdpeaaYTTAGGKI---PIRWTAPEAIAF-RTFSSASDVWSFGVVMWEVLAYGE 835
Cdd:cd14012   133 GNVLLDrdaGTGIVKLTDYSLGKTLLD-----MCSRGSLDefkQTYWLPPELAQGsKSPTRKTDVWDLGLLFLQMLFGLD 207
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 341940659  836 RPYWNMTNQDVISSVEegyrLPAPmgcpraLHQLMLDCWHKDRAQRPR 883
Cdd:cd14012   208 VLEKYTSPNPVLVSLD----LSAS------LQDFLSKCLSLDPKKRPT 245
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
664-894 2.85e-14

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: 74.25  E-value: 2.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  664 AIKALKAGYTErQRQDFLSEAAIMGQFDHPNIIRLE--GVVTRG---RLAMIVTEYMENGSL-DAFLRTHDGQ--FTIVQ 735
Cdd:cd13986    29 ALKKILCHSKE-DVKEAMREIENYRLFNHPNILRLLdsQIVKEAggkKEVYLLLPYYKRGSLqDEIERRLVKGtfFPEDR 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  736 LVGMLRGVGAGMRYLSDL---GYIHRDLAARNVLV--DGRLVckVSDFG---LSRA-LEDDPEAAYT--TAGGKIPIRWT 804
Cdd:cd13986   108 ILHIFLGICRGLKAMHEPelvPYAHRDIKPGNVLLseDDEPI--LMDLGsmnPARIeIEGRREALALqdWAAEHCTMPYR 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  805 APE---AIAFRTFSSASDVWSFGVVMWeVLAYGERPYwnmtnqDVISS--------VEEG-YRLPAPMGCPRALHQLMLD 872
Cdd:cd13986   186 APElfdVKSHCTIDEKTDIWSLGCTLY-ALMYGESPF------ERIFQkgdslalaVLSGnYSFPDNSRYSEELHQLVKS 258
                         250       260
                  ....*....|....*....|..
gi 341940659  873 CWHKDRAQRPRFAHVVSVLDAL 894
Cdd:cd13986   259 MLVVNPAERPSIDDLLSRVHDL 280
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
636-843 3.96e-14

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: 74.05  E-value: 3.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIiGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVV-TRGRLaMIVTEY 714
Cdd:cd07836     5 LEKL-GEGTYATVYKGRNRTTGEI---VALKEIHLDAEEGTPSTAIREISLMKELKHENIVRLHDVIhTENKL-MLVFEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  715 MENgSLDAFLRTH--DGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALeddpEAAY 792
Cdd:cd07836    80 MDK-DLKKYMDTHgvRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARAF----GIPV 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 341940659  793 TTAGGKIPIRW-TAPEAI-AFRTFSSASDVWSFGVVMWEVlaYGERPYWNMTN 843
Cdd:cd07836   155 NTFSNEVVTLWyRAPDVLlGSRTYSTSIDIWSVGCIMAEM--ITGRPLFPGTN 205
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
636-831 4.42e-14

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: 73.46  E-value: 4.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIIGSGESGEVCYGRLQVPGQRdvpVAIKAL------KAGYTERQRQdflsEAAIMGQFDHPNIIRLEGVVTRGRLAM 709
Cdd:cd14079     6 LGKTLGVGSFGKVKLAEHELTGHK---VAVKILnrqkikSLDMEEKIRR----EIQILKLFRHPHIIRLYEVIETPTDIF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  710 IVTEYMENGSLDAF------LRTHDGQFTIVQlvgMLRGVGAGMRYLsdlgYIHRDLAARNVLVDGRLVCKVSDFGLSRA 783
Cdd:cd14079    79 MVMEYVSGGELFDYivqkgrLSEDEARRFFQQ---IISGVEYCHRHM----VVHRDLKPENLLLDSNMNVKIADFGLSNI 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 341940659  784 LEDDpEAAYTTAGGkiPiRWTAPEAIAFRTFS-SASDVWSFGVVMWEVL 831
Cdd:cd14079   152 MRDG-EFLKTSCGS--P-NYAAPEVISGKLYAgPEVDVWSCGVILYALL 196
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
639-847 4.57e-14

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: 73.94  E-value: 4.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  639 IIGSGESGEVcYGRLQVPGQRDVPVAIKALKAGYTERQRQDFLSEAA----IMGQFDHPNIIRLEGVVTRGRLAM-IVTE 713
Cdd:cd14040    13 LLGRGGFSEV-YKAFDLYEQRYAAVKIHQLNKSWRDEKKENYHKHACreyrIHKELDHPRIVKLYDYFSLDTDTFcTVLE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  714 YMENGSLDAFLRTH------DGQFTIVQLVGMLRgvgagmrYLSDLG--YIHRDLAARNVLVDGRLVC---KVSDFGLSR 782
Cdd:cd14040    92 YCEGNDLDFYLKQHklmsekEARSIVMQIVNALR-------YLNEIKppIIHYDLKPGNILLVDGTACgeiKITDFGLSK 164
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341940659  783 ALEDDP---EAAYTTAGGKIPIRWTAPEAIAF----RTFSSASDVWSFGVVMWEVLaYGERPY-WNMTNQDVI 847
Cdd:cd14040   165 IMDDDSygvDGMDLTSQGAGTYWYLPPECFVVgkepPKISNKVDVWSVGVIFFQCL-YGRKPFgHNQSQQDIL 236
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
638-831 4.68e-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: 73.24  E-value: 4.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVPGQRDVPVAIKALKAgyTERQRQDFLSEAAIMGQFDHPNIIRL-EGVVTRGRLAMIVTEYME 716
Cdd:cd08223     6 RVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNA--SKRERKAAEQEAKLLSKLKHPNIVSYkESFEGEDGFLYIVMGFCE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  717 NGSLDAFLRTHDGQ-FTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYTTA 795
Cdd:cd08223    84 GGDLYTRLKEQKGVlLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLESSSDMATTLI 163
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 341940659  796 GgkIPIrWTAPEAIAFRTFSSASDVWSFGVVMWEVL 831
Cdd:cd08223   164 G--TPY-YMSPELFSNKPYNHKSDVWALGCCVYEMA 196
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
674-843 5.03e-14

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: 73.90  E-value: 5.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  674 ERQRQDFLSEAAIMGQF-DHPNIIRLEGVVTRGRLAMIVTEYMENGS-LDAFLRTHdgQFTIVQLVGMLRGVGAGMRYLS 751
Cdd:cd14177    38 DKSKRDPSEEIEILMRYgQHPNIITLKDVYDDGRYVYLVTELMKGGElLDRILRQK--FFSEREASAVLYTITKTVDYLH 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  752 DLGYIHRDLAARNVL-------VDGRLVCkvsDFGLSRALEDDPEAAYTTAggkIPIRWTAPEAIAFRTFSSASDVWSFG 824
Cdd:cd14177   116 CQGVVHRDLKPSNILymddsanADSIRIC---DFGFAKQLRGENGLLLTPC---YTANFVAPEVLMRQGYDAACDIWSLG 189
                         170
                  ....*....|....*....
gi 341940659  825 VVMWEVLAyGERPYWNMTN 843
Cdd:cd14177   190 VLLYTMLA-GYTPFANGPN 207
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
674-853 5.20e-14

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: 73.91  E-value: 5.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  674 ERQRQDFLSEAAIMGQF-DHPNIIRLEGVVTRGRLAMIVTEYMENGS-LDAFLRTHdgQFTIVQLVGMLRGVGAGMRYLS 751
Cdd:cd14175    35 DKSKRDPSEEIEILLRYgQHPNIITLKDVYDDGKHVYLVTELMRGGElLDKILRQK--FFSEREASSVLHTICKTVEYLH 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  752 DLGYIHRDLAARNVL-VD--GRLVC-KVSDFGLSRALEDDPEAAYT---TAggkipiRWTAPEAIAFRTFSSASDVWSFG 824
Cdd:cd14175   113 SQGVVHRDLKPSNILyVDesGNPESlRICDFGFAKQLRAENGLLMTpcyTA------NFVAPEVLKRQGYDEGCDIWSLG 186
                         170       180       190
                  ....*....|....*....|....*....|..
gi 341940659  825 VVMWEVLAyGERPYWNM---TNQDVISSVEEG 853
Cdd:cd14175   187 ILLYTMLA-GYTPFANGpsdTPEEILTRIGSG 217
SAM_EPH-A1 cd09542
SAM domain of EPH-A1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
933-988 5.74e-14

SAM domain of EPH-A1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A1 subfamily of the receptor tyrosine kinases is a C-terminal protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A1 receptors and appears to mediate cell-cell initiated signal transduction. Activation of these receptors leads to inhibition of cell spreading and migration in a RhoA-ROCK-dependent manner. EPH-A1 receptors are known to bind ILK (integrin-linked kinase) which is the mediator of interactions between integrin and the actin cytoskeleton. However SAM is not sufficient for this interaction; it rather plays an ancillary role. SAM domains of Eph-A1 receptors do not form homo/hetero dimers/oligomers. EphA1 gene was found expressed widely in differentiated epithelial cells. In a number of different malignant tumors EphA1 genes are downregulated. In breast carcinoma the downregulation is associated with invasive behavior of the cell.


Pssm-ID: 188941  Cd Length: 63  Bit Score: 67.34  E-value: 5.74e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 341940659  933 TVGDWLDSIRMGRYRDHFAAGGYSSLGMVLRMNAQDVRALGITLMGHQKKILGSIQ 988
Cdd:cd09542     6 SVSEWLESIRMKRYILHFRSAGLDTMECVLELTAEDLTQMGITLPGHQKRILCSIQ 61
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
640-885 5.78e-14

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: 73.46  E-value: 5.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGV------VTRGRLAMIVTE 713
Cdd:cd14038     2 LGTGGFGNVLRWINQETGEQ---VAIKQCRQELSPKNRERWCLEIQIMKRLNHPNVVAARDVpeglqkLAPNDLPLLAME 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  714 YMENGSLDAFLRTHDGQFTIVQ--LVGMLRGVGAGMRYLSDLGYIHRDLAARNVLV---DGRLVCKVSDFGLSRALeDDP 788
Cdd:cd14038    79 YCQGGDLRKYLNQFENCCGLREgaILTLLSDISSALRYLHENRIIHRDLKPENIVLqqgEQRLIHKIIDLGYAKEL-DQG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  789 EAAYTTAGgkiPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPY--------WN-----------MTNQDVISS 849
Cdd:cd14038   158 SLCTSFVG---TLQYLAPELLEQQKYTVTVDYWSFGTLAFECIT-GFRPFlpnwqpvqWHgkvrqksnediVVYEDLTGA 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 341940659  850 VEEGYRLPAPMGCPRALH-------QLMLdCWH-KDRAQRPRFA 885
Cdd:cd14038   234 VKFSSVLPTPNNLNGILAgklerwlQCML-MWHpRQRGTDPPQN 276
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
682-859 5.92e-14

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: 73.14  E-value: 5.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  682 SEAAIMGQFDHPNIIRL-EGVVTRGRLaMIVTEYMENGSL-DAFlrTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRD 759
Cdd:cd14184    48 NEVSILRRVKHPNIIMLiEEMDTPAEL-YLVMELVKGGDLfDAI--TSSTKYTERDASAMVYNLASALKYLHGLCIVHRD 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  760 LAARNVLV----DGRLVCKVSDFGLSRALEDdpeAAYTTAGGKIpirWTAPEAIAFRTFSSASDVWSFGVVMWeVLAYGE 835
Cdd:cd14184   125 IKPENLLVceypDGTKSLKLGDFGLATVVEG---PLYTVCGTPT---YVAPEIIAETGYGLKVDIWAAGVITY-ILLCGF 197
                         170       180
                  ....*....|....*....|....*..
gi 341940659  836 RPYWNMTN--QDVISSVEEGY-RLPAP 859
Cdd:cd14184   198 PPFRSENNlqEDLFDQILLGKlEFPSP 224
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
636-889 7.38e-14

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: 72.70  E-value: 7.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIIGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRL-EGVVTRGRLaMIVTEY 714
Cdd:cd08219     4 VLRVVGEGSFGRALLVQHVNSDQK---YAMKEIRLPKSSSAVEDSRKEAVLLAKMKHPNIVAFkESFEADGHL-YIVMEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  715 MENGSLDAFLRTHDGQF----TIVQ-LVGMLRGVgagmRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPE 789
Cdd:cd08219    80 CDGGDLMQKIKLQRGKLfpedTILQwFVQMCLGV----QHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSPGA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  790 AAYTTAGGKIpirWTAPEAIAFRTFSSASDVWSFGVVMWEvLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALHQL 869
Cdd:cd08219   156 YACTYVGTPY---YVPPEIWENMPYNNKSDIWSLGCILYE-LCTLKHPFQANSWKNLILKVCQGSYKPLPSHYSYELRSL 231
                         250       260
                  ....*....|....*....|
gi 341940659  870 MLDCWHKDRAQRPRFAHVVS 889
Cdd:cd08219   232 IKQMFKRNPRSRPSATTILS 251
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
640-841 7.83e-14

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: 73.52  E-value: 7.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRlqvPGQRDVPVAIKalKAGYTERQR----QDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYM 715
Cdd:cd06634    23 IGHGSFGAVYFAR---DVRNNEVVAIK--KMSYSGKQSnekwQDIIKEVKFLQKLRHPNTIEYRGCYLREHTAWLVMEYC 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  716 EnGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEddPEAAYTTA 795
Cdd:cd06634    98 L-GSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGSASIMA--PANSFVGT 174
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 341940659  796 GgkipiRWTAPEAIAFR---TFSSASDVWSFGVVMWEvLAYGERPYWNM 841
Cdd:cd06634   175 P-----YWMAPEVILAMdegQYDGKVDVWSLGITCIE-LAERKPPLFNM 217
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
631-837 8.35e-14

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: 73.94  E-value: 8.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  631 ASRIHIEKIIGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYTERQR-QDFLSEAAIMGQFDHPNII------RLEGVVT 703
Cdd:cd07855     4 GDRYEPIETIGSGAYGVVCSAIDTKSGQK---VAIKKIPNAFDVVTTaKRTLRELKILRHFKHDNIIairdilRPKVPYA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  704 RGRLAMIVTEYMENG-----SLDAFLRTHDGQFTIVQLvgmLRGvgagMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDF 778
Cdd:cd07855    81 DFKDVYVVLDLMESDlhhiiHSDQPLTLEHIRYFLYQL---LRG----LKYIHSANVIHRDLKPSNLLVNENCELKIGDF 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 341940659  779 GLSRALEDDPEAAYTTAGGKIPIRW-TAPEAI-AFRTFSSASDVWSFGVVMWEVLayGERP 837
Cdd:cd07855   154 GMARGLCTSPEEHKYFMTEYVATRWyRAPELMlSLPEYTQAIDMWSVGCIFAEML--GRRQ 212
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
640-840 8.71e-14

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: 73.22  E-value: 8.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQRdvpVAIKALKAgYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGS 719
Cdd:cd06655    27 IGQGASGTVFTAIDVATGQE---VAIKQINL-QKQPKKELIINEILVMKELKNPNIVNFLDSFLVGDELFVVMEYLAGGS 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  720 L-DAFLRTHDGQftiVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYTTAGGK 798
Cdd:cd06655   103 LtDVVTETCMDE---AQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTP 179
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 341940659  799 IpirWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWN 840
Cdd:cd06655   180 Y---WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLN 217
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
643-847 9.01e-14

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: 72.75  E-value: 9.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  643 GESGEVCYGRLQVPGQRDVPV--AIKALKAGyTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSL 720
Cdd:cd06643    11 GELGDGAFGKVYKAQNKETGIlaAAKVIDTK-SEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIEFCAGGAV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  721 DAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVL--VDGRLvcKVSDFGLS----RALEDDPEAAYTT 794
Cdd:cd06643    90 DAVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILftLDGDI--KLADFGVSakntRTLQRRDSFIGTP 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 341940659  795 aggkipiRWTAPEAIAFRT-----FSSASDVWSFGVVMWEvLAYGERPYWNMTNQDVI 847
Cdd:cd06643   168 -------YWMAPEVVMCETskdrpYDYKADVWSLGVTLIE-MAQIEPPHHELNPMRVL 217
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
636-850 9.46e-14

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: 72.34  E-value: 9.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIIGSGESGEVCygRLQVPGQRDVpVAIKALKAgYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYM 715
Cdd:cd14191     6 IEERLGSGKFGQVF--RLVEKKTKKV-WAGKFFKA-YSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEMV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  716 ENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVS--DFGLSRALEDdpeaayt 793
Cdd:cd14191    82 SGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTKIKliDFGLARRLEN------- 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 341940659  794 taGGKIPI-----RWTAPEAIAFRTFSSASDVWSFGVVMWeVLAYGERPYWNMTNQDVISSV 850
Cdd:cd14191   155 --AGSLKVlfgtpEFVAPEVINYEPIGYATDMWSIGVICY-ILVSGLSPFMGDNDNETLANV 213
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
662-831 9.82e-14

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: 72.85  E-value: 9.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  662 PVAIKAL-KAGYTER-----QRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLdaFLRthdgqftIVQ 735
Cdd:cd14096    29 PVAIKVVrKADLSSDnlkgsSRANILKEVQIMKRLSHPNIVKLLDFQESDEYYYIVLELADGGEI--FHQ-------IVR 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  736 LV--------GMLRGVGAGMRYLSDLGYIHRDLAARNVLVD-----------------------------------GRLv 772
Cdd:cd14096   100 LTyfsedlsrHVITQVASAVKYLHEIGVVHRDIKPENLLFEpipfipsivklrkadddetkvdegefipgvggggiGIV- 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 341940659  773 cKVSDFGLSRALedDPEAAYTTAGgkiPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVL 831
Cdd:cd14096   179 -KLADFGLSKQV--WDSNTKTPCG---TVGYTAPEVVKDERYSKKVDMWALGCVLYTLL 231
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
640-841 1.06e-13

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: 73.16  E-value: 1.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRlqvPGQRDVPVAIKalKAGYTERQR----QDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYM 715
Cdd:cd06635    33 IGHGSFGAVYFAR---DVRTSEVVAIK--KMSYSGKQSnekwQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVMEYC 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  716 EnGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGlSRALEDDPEAAYTTA 795
Cdd:cd06635   108 L-GSASDLLEVHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFG-SASIASPANSFVGTP 185
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 341940659  796 ggkipiRWTAPEAIAFR---TFSSASDVWSFGVVMWEvLAYGERPYWNM 841
Cdd:cd06635   186 ------YWMAPEVILAMdegQYDGKVDVWSLGITCIE-LAERKPPLFNM 227
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
638-853 1.10e-13

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: 72.13  E-value: 1.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVPGQRdvpVAIKALKAG--YTERQRQDFLSEAAI-MGQFDHPNIIRLEGVVTRGRLAMIVTEY 714
Cdd:cd05611     2 KPISKGAFGSVYLAKKRSTGDY---FAIKVLKKSdmIAKNQVTNVKAERAImMIQGESPYVAKLYYSFQSKDYLYLVMEY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  715 MENGSLDAFLRTHDG---QFTIVQLVGMLRGVGagmrYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAA 791
Cdd:cd05611    79 LNGGDCASLIKTLGGlpeDWAKQYIAEVVLGVE----DLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRNGLEKRHNK 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 341940659  792 YTTAggkIPiRWTAPEAIAFRTFSSASDVWSFGVVMWEVLaYGERPYWNMTNQDVISSVEEG 853
Cdd:cd05611   155 KFVG---TP-DYLAPETILGVGDDKMSDWWSLGCVIFEFL-FGYPPFHAETPDAVFDNILSR 211
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
643-863 1.23e-13

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: 72.76  E-value: 1.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  643 GESGEVCYGRLQVPGQRDVPV--AIKALKAGyTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSL 720
Cdd:cd06644    18 GELGDGAFGKVYKAKNKETGAlaAAKVIETK-SEEELEDYMVEIEILATCNHPYIVKLLGAFYWDGKLWIMIEFCPGGAV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  721 DAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLV--DGRLvcKVSDFGLSRALEDDPEAAYTTAGGK 798
Cdd:cd06644    97 DAIMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLtlDGDI--KLADFGVSAKNVKTLQRRDSFIGTP 174
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  799 IpirWTAPEAIAFRTFSSA-----SDVWSFGVVMWEvLAYGERPYWNMTNQDVISSVEEGYrlPAPMGCP 863
Cdd:cd06644   175 Y---WMAPEVVMCETMKDTpydykADIWSLGITLIE-MAQIEPPHHELNPMRVLLKIAKSE--PPTLSQP 238
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
640-850 1.54e-13

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: 71.97  E-value: 1.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQRDVPVAIKALKAGYTER--QRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMEN 717
Cdd:cd14194    13 LGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRgvSREDIEREVSILKEIQHPNVITLHEVYENKTDVILILELVAG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  718 GSLDAFLRTHDgQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLV----CKVSDFGLSRALE--DDPEAA 791
Cdd:cd14194    93 GELFDFLAEKE-SLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVpkprIKIIDFGLAHKIDfgNEFKNI 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 341940659  792 YTTAggkipiRWTAPEAIAFRTFSSASDVWSFGVVMWeVLAYGERPYWNMTNQDVISSV 850
Cdd:cd14194   172 FGTP------EFVAPEIVNYEPLGLEADMWSIGVITY-ILLSGASPFLGDTKQETLANV 223
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
681-853 1.64e-13

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: 71.77  E-value: 1.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  681 LSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENG---SLDAFLRTHDgQFTIVQLVGMLRGVGAGMRYLSDLGYIH 757
Cdd:cd14109    44 MREVDIHNSLDHPNIVQMHDAYDDEKLAVTVIDNLASTielVRDNLLPGKD-YYTERQVAVFVRQLLLALKHMHDLGIAH 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  758 RDLAARNVLV-DGRLvcKVSDFGLSRALEDDpeAAYTTAGGkIPiRWTAPEAIAFRTFSSASDVWSFGVVMWeVLAYGER 836
Cdd:cd14109   123 LDLRPEDILLqDDKL--KLADFGQSRRLLRG--KLTTLIYG-SP-EFVSPEIVNSYPVTLATDMWSVGVLTY-VLLGGIS 195
                         170
                  ....*....|....*..
gi 341940659  837 PYWNMTNQDVISSVEEG 853
Cdd:cd14109   196 PFLGDNDRETLTNVRSG 212
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
663-887 1.75e-13

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: 71.56  E-value: 1.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  663 VAIKAL-KAGYTERQRQDFL-SEAAIMGQFDHPNIIRLEGVV--TRGRLAMiVTEYMENGslDAF-LRTHDGQFTIVQLV 737
Cdd:cd14163    28 VAIKIIdKSGGPEEFIQRFLpRELQIVERLDHKNIIHVYEMLesADGKIYL-VMELAEDG--DVFdCVLHGGPLPEHRAK 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  738 GMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVcKVSDFGLSRALEDDPEAAYTTAGGKIPirWTAPEAI-AFRTFSS 816
Cdd:cd14163   105 ALFRQLVEAIRYCHGCGVAHRDLKCENALLQGFTL-KLTDFGFAKQLPKGGRELSQTFCGSTA--YAAPEVLqGVPHDSR 181
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 341940659  817 ASDVWSFGVVMWeVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALHQLMLDCWHKDRAQRPRFAHV 887
Cdd:cd14163   182 KGDIWSMGVVLY-VMLCAQLPFDDTDIPKMLCQQQKGVSLPGHLGVSRTCQDLLKRLLEPDMVLRPSIEEV 251
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
640-831 2.27e-13

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: 72.71  E-value: 2.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQRdvpVAIKALkagyterqRQDFLS---------EAAIMGQFDHPNIIRLEGVVTRGRLAM- 709
Cdd:cd07851    23 VGSGAYGQVCSAFDTKTGRK---VAIKKL--------SRPFQSaihakrtyrELRLLKHMKHENVIGLLDVFTPASSLEd 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  710 -----IVTEYMeNGSLDAFLRTH---DG--QFTIVQlvgMLRGvgagMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFG 779
Cdd:cd07851    92 fqdvyLVTHLM-GADLNNIVKCQklsDDhiQFLVYQ---ILRG----LKYIHSAGIIHRDLKPSNLAVNEDCELKILDFG 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 341940659  780 LSRALEDDpeaayttAGGKIPIRW-TAPEAI-AFRTFSSASDVWSFGVVMWEVL 831
Cdd:cd07851   164 LARHTDDE-------MTGYVATRWyRAPEIMlNWMHYNQTVDIWSVGCIMAELL 210
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
658-885 2.62e-13

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: 71.69  E-value: 2.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  658 QRDVPVAIKALKAGYTERQRQDFLSEAAI-MGQFDHPNIIRLEGVVTRGRLAMIVTEYMENgSLDAFLR-THDGQFTIVQ 735
Cdd:cd06617    24 PTGTIMAVKRIRATVNSQEQKRLLMDLDIsMRSVDCPYTVTFYGALFREGDVWICMEVMDT-SLDKFYKkVYDKGLTIPE 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  736 --LVGMLRGVGAGMRYL-SDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDpeAAYTTAGGKIPirWTAPEAI--- 809
Cdd:cd06617   103 diLGKIAVSIVKALEYLhSKLSVIHRDVKPSNVLINRNGQVKLCDFGISGYLVDS--VAKTIDAGCKP--YMAPERInpe 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  810 -AFRTFSSASDVWSFGVVMWEvLAYGERPY--WNMTNQDVISSVEE-GYRLPAPMGCPRaLHQLMLDCWHKDRAQRPRFA 885
Cdd:cd06617   179 lNQKGYDVKSDVWSLGITMIE-LATGRFPYdsWKTPFQQLKQVVEEpSPQLPAEKFSPE-FQDFVNKCLKKNYKERPNYP 256
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
636-854 2.87e-13

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: 71.14  E-value: 2.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIIGSGESGEVCYGRLQvpgQRDVPVAIKAL------KAGYTERQRQdflsEAAIMGQFDHPNIIRLEGVVTRGRLAM 709
Cdd:cd14116     9 IGRPLGKGKFGNVYLAREK---QSKFILALKVLfkaqleKAGVEHQLRR----EVEIQSHLRHPNILRLYGYFHDATRVY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  710 IVTEYMENGSLDAFLR---THDGQFT---IVQLVGMLRgvgagmrYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSra 783
Cdd:cd14116    82 LILEYAPLGTVYRELQklsKFDEQRTatyITELANALS-------YCHSKRVIHRDIKPENLLLGSAGELKIADFGWS-- 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 341940659  784 lEDDPEAAYTTAGGKIPirWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWNMTNQDV---ISSVEEGY 854
Cdd:cd14116   153 -VHAPSSRRTTLCGTLD--YLPPEMIEGRMHDEKVDLWSLGVLCYEFLV-GKPPFEANTYQETykrISRVEFTF 222
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
633-831 2.93e-13

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: 72.12  E-value: 2.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  633 RIHIEKIIGSGESGEVCYGRLQVPGQRdvpVAIKALKAGY---TERQRqdFLSEAAIMGQFDHPNIIRLEGVV-----TR 704
Cdd:cd07859     1 RYKIQEVIGKGSYGVVCSAIDTHTGEK---VAIKKINDVFehvSDATR--ILREIKLLRLLRHPDIVEIKHIMlppsrRE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  705 GRLAMIVTEYMEN------GSLDAFLRTHDgQFTIVQLvgmLRGvgagMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDF 778
Cdd:cd07859    76 FKDIYVVFELMESdlhqviKANDDLTPEHH-QFFLYQL---LRA----LKYIHTANVFHRDLKPKNILANADCKLKICDF 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 341940659  779 GLSR-ALEDDPEAAYTTagGKIPIRW-TAPEAIA--FRTFSSASDVWSFGVVMWEVL 831
Cdd:cd07859   148 GLARvAFNDTPTAIFWT--DYVATRWyRAPELCGsfFSKYTPAIDIWSIGCIFAEVL 202
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
639-841 3.99e-13

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: 70.79  E-value: 3.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  639 IIGSGESGEVCYGRLQVPGQRdvpVAIKALKagYTERQRQDFLSEAAIMGQF-DHPNIIRLEGV-------VTRGRLaMI 710
Cdd:cd06608    13 VIGEGTYGKVYKARHKKTGQL---AAIKIMD--IIEDEEEEIKLEINILRKFsNHPNIATFYGAfikkdppGGDDQL-WL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  711 VTEYMENGS---LDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLV--DGRLvcKVSDFGLSRALE 785
Cdd:cd06608    87 VMEYCGGGSvtdLVKGLRKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLteEAEV--KLVDFGVSAQLD 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 341940659  786 DDPEAAYTTAGgkIPIrWTAPEAIAF-----RTFSSASDVWSFGVVMWEvLAYGERPYWNM 841
Cdd:cd06608   165 STLGRRNTFIG--TPY-WMAPEVIACdqqpdASYDARCDVWSLGITAIE-LADGKPPLCDM 221
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
640-885 4.93e-13

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: 70.65  E-value: 4.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGqrdVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGS 719
Cdd:cd06622     9 LGKGNYGSVYKVLHRPTG---VTMAMKEIRLELDESKFNQIIMELDILHKAVSPYIVDFYGAFFIEGAVYMCMEYMDAGS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  720 LDAFlrTHDGQFTIVQLVGMLRGVGA----GMRYLSD-LGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEddPEAAYTT 794
Cdd:cd06622    86 LDKL--YAGGVATEGIPEDVLRRITYavvkGLKFLKEeHNIIHRDVKPTNVLVNGNGQVKLCDFGVSGNLV--ASLAKTN 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  795 AGGKipiRWTAPEAI------AFRTFSSASDVWSFGVVMWEvLAYGERPYWNMTNQDV---ISSVEEGYRLPAPMGCPRA 865
Cdd:cd06622   162 IGCQ---SYMAPERIksggpnQNPTYTVQSDVWSLGLSILE-MALGRYPYPPETYANIfaqLSAIVDGDPPTLPSGYSDD 237
                         250       260
                  ....*....|....*....|
gi 341940659  866 LHQLMLDCWHKDRAQRPRFA 885
Cdd:cd06622   238 AQDFVAKCLNKIPNRRPTYA 257
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
635-847 5.00e-13

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: 70.20  E-value: 5.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  635 HIEKIIGSGESGEVCYGRLQVPGQRdvpVAIKA-----LKAGYTERQrqdFLSEAAIMGQFDHPNIIRLEGVV-TRGRLa 708
Cdd:cd14007     3 EIGKPLGKGKFGNVYLAREKKSGFI---VALKVisksqLQKSGLEHQ---LRREIEIQSHLRHPNILRLYGYFeDKKRI- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  709 MIVTEYMENGSLDAFLRTHdGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDP 788
Cdd:cd14007    76 YLILEYAPNGELYKELKKQ-KRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSVHAPSNR 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341940659  789 EAayTTAGgkipirwT----APEAIAFRTFSSASDVWSFGVVMWEVLaYGERPyWNMTNQDVI 847
Cdd:cd14007   155 RK--TFCG-------TldylPPEMVEGKEYDYKVDIWSLGVLCYELL-VGKPP-FESKSHQET 206
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
627-831 6.08e-13

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 71.33  E-value: 6.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  627 REIEASRIHIEKIIGSGESGEVCYGRLQVPGQRdvpVAIKALK----AGYTERQRQDF---------LSEAAIMGQFDHP 693
Cdd:PTZ00024    4 FSISERYIQKGAHLGEGTYGKVEKAYDTLTGKI---VAIKKVKiieiSNDVTKDRQLVgmcgihfttLRELKIMNEIKHE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  694 NIIRLEGVVTRGRLAMIVTEYMENG---SLDAFLRthdgqFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGR 770
Cdd:PTZ00024   81 NIMGLVDVYVEGDFINLVMDIMASDlkkVVDRKIR-----LTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSK 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341940659  771 LVCKVSDFGLSRALEDDPEAAYTTAG----------GKIPIRW-TAPEAIAFRT-FSSASDVWSFGVVMWEVL 831
Cdd:PTZ00024  156 GICKIADFGLARRYGYPPYSDTLSKDetmqrreemtSKVVTLWyRAPELLMGAEkYHFAVDMWSVGCIFAELL 228
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
631-838 6.27e-13

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: 70.02  E-value: 6.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  631 ASRIHIEKIIGSGESGEVcygRLQVPGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRL-EGVVTRGRLaM 709
Cdd:cd14183     5 SERYKVGRTIGDGNFAVV---KECVERSTGREYALKIINKSKCRGKEHMIQNEVSILRRVKHPNIVLLiEEMDMPTEL-Y 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  710 IVTEYMENGSL-DAFlrTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLV----DGRLVCKVSDFGLSRAL 784
Cdd:cd14183    81 LVMELVKGGDLfDAI--TSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyehqDGSKSLKLGDFGLATVV 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 341940659  785 eDDPeaAYTTAGGKIpirWTAPEAIAFRTFSSASDVWSFGVVMWeVLAYGERPY 838
Cdd:cd14183   159 -DGP--LYTVCGTPT---YVAPEIIAETGYGLKVDIWAAGVITY-ILLCGFPPF 205
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
665-855 6.50e-13

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: 69.95  E-value: 6.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  665 IKALKAGYTERQRqdFLSEAAIMGQFDHPNIIRLEGV-VTRGRLAMI-VTEYMENGSLDAFLRTHdGQFTIVQLVGMLRG 742
Cdd:cd13983    34 IKLRKLPKAERQR--FKQEIEILKSLKHPNIIKFYDSwESKSKKEVIfITELMTSGTLKQYLKRF-KRLKLKVIKSWCRQ 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  743 VGAGMRYL--SDLGYIHRDLAARNVLVDGRL-VCKVSDFGLSRALEDDpeAAYTTAGgkipirwtAPEAIAFRTFS---- 815
Cdd:cd13983   111 ILEGLNYLhtRDPPIIHRDLKCDNIFINGNTgEVKIGDLGLATLLRQS--FAKSVIG--------TPEFMAPEMYEehyd 180
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 341940659  816 SASDVWSFGVVMWEvLAYGERPYWNMTN-QDVISSVEEGYR 855
Cdd:cd13983   181 EKVDIYAFGMCLLE-MATGEYPYSECTNaAQIYKKVTSGIK 220
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
674-859 6.75e-13

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: 70.08  E-value: 6.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  674 ERQRQDFLSEAAIMGQFD-HPNIIRLEGVVTRGRLAMIVTEYMENGSLDAFLrTHDGQFTIVQLVGMLRGVGAGMRYLSD 752
Cdd:cd14093    49 EELREATRREIEILRQVSgHPNIIELHDVFESPTFIFLVFELCRKGELFDYL-TEVVTLSEKKTRRIMRQLFEAVEFLHS 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  753 LGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYT--TAGgkipirWTAPEAIAFRTFSSAS------DVWSFG 824
Cdd:cd14093   128 LNIVHRDLKPENILLDDNLNVKISDFGFATRLDEGEKLRELcgTPG------YLAPEVLKCSMYDNAPgygkevDMWACG 201
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 341940659  825 VVMWEVLAyGERPYWNMTNQDVISSVEEG-YRLPAP 859
Cdd:cd14093   202 VIMYTLLA-GCPPFWHRKQMVMLRNIMEGkYEFGSP 236
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
664-853 7.09e-13

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: 69.81  E-value: 7.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  664 AIKAL---KAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLDAFLRTHDGqftIVQLVG-- 738
Cdd:cd14098    29 AIKQIvkrKVAGNDKNLQLFQREINILKSLEHPGIVRLIDWYEDDQHIYLVMEYVEGGDLMDFIMAWGA---IPEQHAre 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  739 MLRGVGAGMRYLSDLGYIHRDLAARNVLV--DGRLVCKVSDFGLSRALEDDpeAAYTTAGGKipIRWTAPEAIAFRT--- 813
Cdd:cd14098   106 LTKQILEAMAYTHSMGITHRDLKPENILItqDDPVIVKISDFGLAKVIHTG--TFLVTFCGT--MAYLAPEILMSKEqnl 181
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 341940659  814 ---FSSASDVWSFGVVMWeVLAYGERPYWNMTNQDVISSVEEG 853
Cdd:cd14098   182 qggYSNLVDMWSVGCLVY-VMLTGALPFDGSSQLPVEKRIRKG 223
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
640-850 7.73e-13

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: 69.82  E-value: 7.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQRDVPVAIKALKAGYTER--QRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMEN 717
Cdd:cd14105    13 LGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKASRRgvSREDIEREVSILRQVLHPNIITLHDVFENKTDVVLILELVAG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  718 GSLDAFLRTHDGqFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLV----CKVSDFGLSRALEDDPEaaYT 793
Cdd:cd14105    93 GELFDFLAEKES-LSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNVpiprIKLIDFGLAHKIEDGNE--FK 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 341940659  794 TAGGKiPiRWTAPEAIAFRTFSSASDVWSFGVVMWeVLAYGERPYWNMTNQDVISSV 850
Cdd:cd14105   170 NIFGT-P-EFVAPEIVNYEPLGLEADMWSIGVITY-ILLSGASPFLGDTKQETLANI 223
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
674-853 1.03e-12

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: 70.43  E-value: 1.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  674 ERQRQDFLSEAAIMGQF-DHPNIIRLEGVVTRGRLAMIVTEYMENGS-LDAFLRTHdgQFTIVQLVGMLRGVGAGMRYLS 751
Cdd:cd14176    53 DKSKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMKGGElLDKILRQK--FFSEREASAVLFTITKTVEYLH 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  752 DLGYIHRDLAARNVL-VD---GRLVCKVSDFGLSRALEDDPEAAYTTAggkIPIRWTAPEAIAFRTFSSASDVWSFGVVM 827
Cdd:cd14176   131 AQGVVHRDLKPSNILyVDesgNPESIRICDFGFAKQLRAENGLLMTPC---YTANFVAPEVLERQGYDAACDIWSLGVLL 207
                         170       180
                  ....*....|....*....|....*....
gi 341940659  828 WEVLAyGERPYWNM---TNQDVISSVEEG 853
Cdd:cd14176   208 YTMLT-GYTPFANGpddTPEEILARIGSG 235
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
682-882 1.10e-12

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: 69.34  E-value: 1.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  682 SEAAIMGQ---FDHPNIIRLEGVVTRGRLAMIVTEYMENGsLDAF--------LRTHDGQFTIVQLVgmlrgvgAGMRYL 750
Cdd:cd14004    54 LEIHILDTlnkRSHPNIVKLLDFFEDDEFYYLVMEKHGSG-MDLFdfierkpnMDEKEAKYIFRQVA-------DAVKHL 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  751 SDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPeaAYTTAGgkiPIRWTAPEAIAFRTFSSAS-DVWSFGVVMWe 829
Cdd:cd14004   126 HDQGIVHRDIKDENVILDGNGTIKLIDFGSAAYIKSGP--FDTFVG---TIDYAAPEVLRGNPYGGKEqDIWALGVLLY- 199
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 341940659  830 VLAYGERPYWNmtnqdvissVEEGyrLPAPMGCPRALHQ----LMLDCWHKDRAQRP 882
Cdd:cd14004   200 TLVFKENPFYN---------IEEI--LEADLRIPYAVSEdlidLISRMLNRDVGDRP 245
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
640-894 1.12e-12

Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. 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 (a pseudokinase in the case of IRAK3), 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. IRAK3 (or IRAK-M) is the only IRAK that does not show kinase activity. It is found only in monocytes and macrophages in humans, and functions as a negative regulator of TLR signaling including TLR-2 induced p38 activation. It also negatively regulates the alternative NFkB pathway in a TLR-2 specific manner. IRAK3 is downregulated in the monocytes of obese people, and is associated with high SOD2, a marker of mitochondrial oxidative stress. It is an important inhibitor of inflammation in association with obesity and metabolic syndrome. The IRAK3 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: 271062 [Multi-domain]  Cd Length: 276  Bit Score: 69.53  E-value: 1.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQvpgqrDVPVAIKALKagyTERQRQ------DFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTE 713
Cdd:cd14160     1 IGEGEIFEVYRVRIG-----NRSYAVKLFK---QEKKMQwkkhwkRFLSELEVLLLFQHPNILELAAYFTETEKFCLVYP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  714 YMENGSLDAFLRTHDGQFTIV--QLVGMLRGVGAGMRYLSDL---GYIHRDLAARNVLVDGRLVCKVSDFGLSR---ALE 785
Cdd:cd14160    73 YMQNGTLFDRLQCHGVTKPLSwhERINILIGIAKAIHYLHNSqpcTVICGNISSANILLDDQMQPKLTDFALAHfrpHLE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  786 DDPEAAYTTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYW----NMTNQDVISSVEEGYRLPAPMG 861
Cdd:cd14160   153 DQSCTINMTTALHKHLWYMPEEYIRQGKLSVKTDVYSFGIVIMEVLT-GCKVVLddpkHLQLRDLLHELMEKRGLDSCLS 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 341940659  862 --------CPRA----LHQLMLDCWHKDRAQRPRFAHVVSVLDAL 894
Cdd:cd14160   232 fldlkfppCPRNfsakLFRLAGRCTATKAKLRPDMDEVLQRLEST 276
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
635-838 1.41e-12

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: 69.96  E-value: 1.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  635 HIEKI--IGSGESGEVCYGRLQVPGQRdvpVAIKAL-KAGYTERQR-QDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMI 710
Cdd:cd05574     2 HFKKIklLGKGDVGRVYLVRLKGTGKL---FAMKVLdKEEMIKRNKvKRVLTEREILATLDHPFLPTLYASFQTSTHLCF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  711 VTEYMENGSLDAFLRTHDG--------QFTIVQLVgmlrgvgAGMRYLSDLGYIHRDLAARNVLV--DGRLVckVSDFGL 780
Cdd:cd05574    79 VMDYCPGGELFRLLQKQPGkrlpeevaRFYAAEVL-------LALEYLHLLGFVYRDLKPENILLheSGHIM--LTDFDL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  781 SRALEDDPEA--------AYTTAGGKIPIR------------------WTAPEAIAFRTFSSASDVWSFGVVMWEVLaYG 834
Cdd:cd05574   150 SKQSSVTPPPvrkslrkgSRRSSVKSIEKEtfvaepsarsnsfvgteeYIAPEVIKGDGHGSAVDWWTLGILLYEML-YG 228

                  ....
gi 341940659  835 ERPY 838
Cdd:cd05574   229 TTPF 232
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
637-828 1.52e-12

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: 68.98  E-value: 1.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  637 EKIIGSGESGEVcYGRLQVPGQRDVpvAIKAL-KAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYM 715
Cdd:cd14082     8 DEVLGSGQFGIV-YGGKHRKTGRDV--AIKVIdKLRFPTKQESQLRNEVAILQQLSHPGVVNLECMFETPERVFVVMEKL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  716 ENGSLDAFLRTHDG-------QFTIVQLVGMLRgvgagmrYLSDLGYIHRDLAARNVLV---DGRLVCKVSDFGLSRALe 785
Cdd:cd14082    85 HGDMLEMILSSEKGrlperitKFLVTQILVALR-------YLHSKNIVHCDLKPENVLLasaEPFPQVKLCDFGFARII- 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 341940659  786 ddPEAAYTTAGGKIPIrWTAPEAIAFRTFSSASDVWSFGVVMW 828
Cdd:cd14082   157 --GEKSFRRSVVGTPA-YLAPEVLRNKGYNRSLDMWSVGVIIY 196
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
640-840 1.74e-12

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: 69.37  E-value: 1.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVcYGRLQVPGQRDVPVAIKALKagyTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGS 719
Cdd:cd06654    28 IGQGASGTV-YTAMDVATGQEVAIRQMNLQ---QQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  720 L-DAFLRT--HDGQFTIVqlvgmLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYTTAG 796
Cdd:cd06654   104 LtDVVTETcmDEGQIAAV-----CRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVG 178
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 341940659  797 GKIpirWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWN 840
Cdd:cd06654   179 TPY---WMAPEVVTRKAYGPKVDIWSLGIMAIEMIE-GEPPYLN 218
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
640-889 1.94e-12

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: 68.84  E-value: 1.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYgRLQVPGQrdvPVAIKA--------------------LKAGYTERQRQDFLSEAAIMGQFDHPNIIRLE 699
Cdd:cd14067     1 LGQGGSGTVIY-RARYQGQ---PVAVKRfhikkckkrtdgsadtmlkhLRAADAMKNFSEFRQEASMLHSLQHPCIVYLI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  700 GVVTRGrlAMIVTEYMENGSLDAFLRTHDGQFTIVQLVGMLR-----GVGAGMRYLSDLGYIHRDLAARNVLV---DGR- 770
Cdd:cd14067    77 GISIHP--LCFALELAPLGSLNTVLEENHKGSSFMPLGHMLTfkiayQIAAGLAYLHKKNIIFCDLKSDNILVwslDVQe 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  771 -LVCKVSDFGLSR-ALEDDPEAAYTTAGgkipirWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWNMTNQDVIS 848
Cdd:cd14067   155 hINIKLSDYGISRqSFHEGALGVEGTPG------YQAPEIRPRIVYDEKVDMFSYGMVLYELLS-GQRPSLGHHQLQIAK 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 341940659  849 SVEEGYRlPApMGCP-----RALHQLMLDCWHKDRAQRPRFAHVVS 889
Cdd:cd14067   228 KLSKGIR-PV-LGQPeevqfFRLQALMMECWDTKPEKRPLACSVVE 271
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
663-882 2.06e-12

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: 68.44  E-value: 2.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  663 VAIKALKAgytERQR------QDFLSEAAIMGQFDHPNIIRLEGVVT---RGRLAMiVTEYMENGSLDAFLRTHDGQFTI 733
Cdd:cd14119    21 RAVKILKK---RKLRripngeANVKREIQILRRLNHRNVIKLVDVLYneeKQKLYM-VMEYCVGGLQEMLDSAPDKRLPI 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  734 VQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLV--DGRLvcKVSDFGLSRALED-DPEAAYTTAGGKiPiRWTAPEAIA 810
Cdd:cd14119    97 WQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLttDGTL--KISDFGVAEALDLfAEDDTCTTSQGS-P-AFQPPEIAN 172
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 341940659  811 F-RTFSS-ASDVWSFGVVMWEVLAyGERPYWNMTNQDVISSVEEG-YRLPApmGCPRALHQLMLDCWHKDRAQRP 882
Cdd:cd14119   173 GqDSFSGfKVDIWSAGVTLYNMTT-GKYPFEGDNIYKLFENIGKGeYTIPD--DVDPDLQDLLRGMLEKDPEKRF 244
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
636-882 2.24e-12

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: 68.10  E-value: 2.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIIGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYTERQ-RQDFLSEAAIMGQF-DHPNIIRLEGVVTRGRLAMIVTE 713
Cdd:cd14050     5 ILSKLGEGSFGEVFKVRSREDGKL---YAVKRSRSRFRGEKdRKRKLEEVERHEKLgEHPNCVRFIKAWEEKGILYIQTE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  714 YMEnGSLDAFLRTHD--GQFTIVQ-LVGMLRGVGagmrYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGL---------S 781
Cdd:cd14050    82 LCD-TSLQQYCEETHslPESEVWNiLLDLLKGLK----HLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLvveldkediH 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  782 RALEDDPeaayttaggkipiRWTAPEAIAfRTFSSASDVWSFGVVMWEVLAYGERPywnmTNQDVISSVEEGYrLPAPMG 861
Cdd:cd14050   157 DAQEGDP-------------RYMAPELLQ-GSFTKAADIFSLGITILELACNLELP----SGGDGWHQLRQGY-LPEEFT 217
                         250       260
                  ....*....|....*....|....*.
gi 341940659  862 CP-----RALHQLMLdcwHKDRAQRP 882
Cdd:cd14050   218 AGlspelRSIIKLMM---DPDPERRP 240
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
634-838 2.29e-12

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: 68.40  E-value: 2.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  634 IHIEKIIGSGESGEVCYGRLQVPGqrdVPVAIKALKAgYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTE 713
Cdd:cd14193     6 VNKEEILGGGRFGQVHKCEEKSSG---LKLAAKIIKA-RSQKEKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIVLVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  714 YMENGSLdaFLRTHDGQFTIVQL--VGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLV--CKVSDFGLSRALEddPE 789
Cdd:cd14193    82 YVDGGEL--FDRIIDENYNLTELdtILFIKQICEGIQYMHQMYILHLDLKPENILCVSREAnqVKIIDFGLARRYK--PR 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 341940659  790 AAYTTAGGKiPiRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPY 838
Cdd:cd14193   158 EKLRVNFGT-P-EFLAPEVVNYEFVSFPTDMWSLGVIAYMLLS-GLSPF 203
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
640-840 2.38e-12

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: 68.98  E-value: 2.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVcYGRLQVPGQRDVpvAIKALKAgYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGS 719
Cdd:cd06656    27 IGQGASGTV-YTAIDIATGQEV--AIKQMNL-QQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  720 L-DAFLRT--HDGQFTIVqlvgmLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYTTAG 796
Cdd:cd06656   103 LtDVVTETcmDEGQIAAV-----CRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVG 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 341940659  797 GKIpirWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWN 840
Cdd:cd06656   178 TPY---WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLN 217
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
631-881 2.50e-12

Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin receptor-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR1, also called Activin receptor-Like Kinase 2 (ALK2), and ALK1 act as receptors for bone morphogenetic proteins (BMPs) and they activate SMAD1/5/8. ACVR1 is widely expressed while ALK1 is limited mainly to endothelial cells. The specificity of BMP binding to type I receptors is affected by type II receptors. ACVR1 binds BMP6/7/9/10 and can also bind anti-Mullerian hormone (AMH) in the presence of AMHR2. ALK1 binds BMP9/10 as well as TGFbeta in endothelial cells. A missense mutation in the GS domain of ACVR1 causes fibrodysplasia ossificans progressiva, a complex and disabling disease characterized by congenital skeletal malformations and extraskeletal bone formation. ACVR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and AMH, 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, like ACVR1 and ALK1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, 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. The ACVR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 69.01  E-value: 2.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  631 ASRIHIEKIIGSGESGEVCYGRLQvpgqrDVPVAIKAlkagYTERQRQDFLSEAAIMGQ--FDHPNIIRLEG--VVTRGR 706
Cdd:cd14142     4 ARQITLVECIGKGRYGEVWRGQWQ-----GESVAVKI----FSSRDEKSWFRETEIYNTvlLRHENILGFIAsdMTSRNS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  707 LAM--IVTEYMENGSLDAFLRTHdgQFTIVQLVGMLRGVGAGMRYL--------SDLGYIHRDLAARNVLVDGRLVCKVS 776
Cdd:cd14142    75 CTQlwLITHYHENGSLYDYLQRT--TLDHQEMLRLALSAASGLVHLhteifgtqGKPAIAHRDLKSKNILVKSNGQCCIA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  777 DFGLsrALEDDPEAAYTTAGGKIPI---RWTAPEAI-------AFRTFSSAsDVWSFGVVMWEV----LAYG-----ERP 837
Cdd:cd14142   153 DLGL--AVTHSQETNQLDVGNNPRVgtkRYMAPEVLdetintdCFESYKRV-DIYAFGLVLWEVarrcVSGGiveeyKPP 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  838 YWNMTNQD--------VIssVEEGYRLPAPmgcPR--------ALHQLMLDCWHKDRAQR 881
Cdd:cd14142   230 FYDVVPSDpsfedmrkVV--CVDQQRPNIP---NRwssdptltAMAKLMKECWYQNPSAR 284
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
691-831 2.51e-12

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: 69.12  E-value: 2.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  691 DHPNIIRLEGVV--TRGRLAMIVTEYMENgSLDAFLRT------HDgQFTIVQLVGMLRGVGAGmrylsdlGYIHRDLAA 762
Cdd:cd07852    65 DHPNIIKLLNVIraENDKDIYLVFEYMET-DLHAVIRAnilediHK-QYIMYQLLKALKYLHSG-------GVIHRDLKP 135
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 341940659  763 RNVLVDGRLVCKVSDFGLSRALEDDPEAAyttaggKIPI-------RW-TAPEA-IAFRTFSSASDVWSFGVVMWEVL 831
Cdd:cd07852   136 SNILLNSDCRVKLADFGLARSLSQLEEDD------ENPVltdyvatRWyRAPEIlLGSTRYTKGVDMWSVGCILGEML 207
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
638-850 2.70e-12

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: 68.06  E-value: 2.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVPGqrdVPVAIKALKAGyTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMEN 717
Cdd:cd14192    10 EVLGGGRFGQVHKCTELSTG---LTLAAKIIKVK-GAKEREEVKNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  718 GSLdaFLRTHDGQFTIVQLVGML--RGVGAGMRYLSDLGYIHRDLAARNVLV---DGRLVcKVSDFGLSRALEddPEAAY 792
Cdd:cd14192    86 GEL--FDRITDESYQLTELDAILftRQICEGVHYLHQHYILHLDLKPENILCvnsTGNQI-KIIDFGLARRYK--PREKL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 341940659  793 TTAGGKiPiRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWNMTNQDVISSV 850
Cdd:cd14192   161 KVNFGT-P-EFLAPEVVNYDFVSFPTDMWSVGVITYMLLS-GLSPFLGETDAETMNNI 215
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
674-853 2.78e-12

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: 68.50  E-value: 2.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  674 ERQRQDFLSEAAIMGQF-DHPNIIRLEGVVTRGRLAMIVTEYMENGSL-DAFLRTHdgQFTIVQLVGMLRGVGAGMRYLS 751
Cdd:cd14178    37 DKSKRDPSEEIEILLRYgQHPNIITLKDVYDDGKFVYLVMELMRGGELlDRILRQK--CFSEREASAVLCTITKTVEYLH 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  752 DLGYIHRDLAARNVLV-------DGRLVCkvsDFGLSRALEDDPEAAYTTAggkIPIRWTAPEAIAFRTFSSASDVWSFG 824
Cdd:cd14178   115 SQGVVHRDLKPSNILYmdesgnpESIRIC---DFGFAKQLRAENGLLMTPC---YTANFVAPEVLKRQGYDAACDIWSLG 188
                         170       180       190
                  ....*....|....*....|....*....|..
gi 341940659  825 VVMWEVLAyGERPYWNM---TNQDVISSVEEG 853
Cdd:cd14178   189 ILLYTMLA-GFTPFANGpddTPEEILARIGSG 219
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
633-838 2.83e-12

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: 68.09  E-value: 2.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  633 RIHIEKIIGSGESGevcYGRLQVPGQRDVPVAIKALKAGytERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVT 712
Cdd:cd14665     1 RYELVKDIGSGNFG---VARLMRDKQTKELVAVKYIERG--EKIDENVQREIINHRSLRHPNIVRFKEVILTPTHLAIVM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  713 EYMENGSLdaFLRT-HDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDG----RLvcKVSDFGLSRA--LE 785
Cdd:cd14665    76 EYAAGGEL--FERIcNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGspapRL--KICDFGYSKSsvLH 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 341940659  786 DDPEAAYTTAGgkipirWTAPEAIAFRTFSSA-SDVWSFGVVMWeVLAYGERPY 838
Cdd:cd14665   152 SQPKSTVGTPA------YIAPEVLLKKEYDGKiADVWSCGVTLY-VMLVGAYPF 198
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
638-881 2.88e-12

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1 functions as a receptor for morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Vertebrates contain two type I BMP receptors, BMPR1a and BMPR1b. BMPR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that also includes TGFbeta, 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, like BMPR1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, 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. The BMPR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 68.66  E-value: 2.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLqvpgqRDVPVAIKALKAgyTERQ---RQDFLSEAAIMgqfDHPNI-------IRLEGVVTRgrl 707
Cdd:cd14144     1 RSVGKGRYGEVWKGKW-----RGEKVAVKIFFT--TEEAswfRETEIYQTVLM---RHENIlgfiaadIKGTGSWTQ--- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  708 AMIVTEYMENGSLDAFLRTHdgqftIVQLVGMLR---GVGAGMRYLSDLGY--------IHRDLAARNVLVDGRLVCKVS 776
Cdd:cd14144    68 LYLITDYHENGSLYDFLRGN-----TLDTQSMLKlaySAACGLAHLHTEIFgtqgkpaiAHRDIKSKNILVKKNGTCCIA 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  777 DFGLS-RALEDDPE---AAYTTAGGKipiRWTAPEAI-------AFRTFSSAsDVWSFGVVMWEV----LAYG-----ER 836
Cdd:cd14144   143 DLGLAvKFISETNEvdlPPNTRVGTK---RYMAPEVLdeslnrnHFDAYKMA-DMYSFGLVLWEIarrcISGGiveeyQL 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 341940659  837 PYWNMTNQDviSSVE--------EGYRLPAPM-----GCPRALHQLMLDCWHKDRAQR 881
Cdd:cd14144   219 PYYDAVPSD--PSYEdmrrvvcvERRRPSIPNrwssdEVLRTMSKLMSECWAHNPAAR 274
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
640-889 2.90e-12

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: 68.30  E-value: 2.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQRdvPVAIKALKA-----GYTERQRQ----DFLSEAAIMG-QFDHPNIIRLEGVVTRGRLAM 709
Cdd:cd08528     8 LGSGAFGCVYKVRKKSNGQT--LLALKEINMtnpafGRTEQERDksvgDIISEVNIIKeQLRHPNIVRYYKTFLENDRLY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  710 IVTEYMENGSL-DAF--LRTHDGQFTIVQLVGMLRGVGAGMRYL-SDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRalE 785
Cdd:cd08528    86 IVMELIEGAPLgEHFssLKEKNEHFTEDRIWNIFVQMVLALRYLhKEKQIVHRDLKPNNIMLGEDDKVTITDFGLAK--Q 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  786 DDPEAAY-TTAGGKIpiRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYgeRPYWNMTNQDVISS--VEEGYRlPAPMGC 862
Cdd:cd08528   164 KGPESSKmTSVVGTI--LYSCPEIVQNEPYGEKADIWALGCILYQMCTL--QPPFYSTNMLTLATkiVEAEYE-PLPEGM 238
                         250       260
                  ....*....|....*....|....*...
gi 341940659  863 -PRALHQLMLDCWHKDRAQRPRFAHVVS 889
Cdd:cd08528   239 ySDDITFVIRSCLTPDPEARPDIVEVSS 266
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
676-889 3.31e-12

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: 68.04  E-value: 3.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  676 QRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLdafLRTHDGQFTIVQLVG--MLRGVGAGMRYLSDL 753
Cdd:cd14187    50 QKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLELCRRRSL---LELHKRRKALTEPEAryYLRQIILGCQYLHRN 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  754 GYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYTTAGGKipiRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAy 833
Cdd:cd14187   127 RVIHRDLKLGNLFLNDDMEVKIGDFGLATKVEYDGERKKTLCGTP---NYIAPEVLSKKGHSFEVDIWSIGCIMYTLLV- 202
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 341940659  834 GERPYWNMTNQDVISSVEEG-YRLPAPMG-CPRALHQLMLdcwHKDRAQRPRFAHVVS 889
Cdd:cd14187   203 GKPPFETSCLKETYLRIKKNeYSIPKHINpVAASLIQKML---QTDPTARPTINELLN 257
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
639-881 3.33e-12

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I Receptor and Activin Type IB/IC Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR1, also called Activin receptor-Like Kinase 5 (ALK5), functions as a receptor for TGFbeta and phoshorylates SMAD2/3. TGFbeta proteins are cytokines that regulate cell growth, differentiation, and survival, and are critical in the development and progression of many human cancers. Mutations in TGFbR1 (and TGFbR2) can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. ACVR1b (also called ALK4) and ACVR1c (also called ALK7) act as receptors for activin A and B, respectively. TGFbR1, ACVR1b, and ACVR1c belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes 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, like TGFbR1, ACVR1b, and ACVR1c, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, 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. The TGFbR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 68.24  E-value: 3.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  639 IIGSGESGEVCYGRLQvpgQRDVPVAIkalkagYTERQRQDFLSEAAIMG--QFDHPNII-------RLEGVVTRGRLam 709
Cdd:cd14143     2 SIGKGRFGEVWRGRWR---GEDVAVKI------FSSREERSWFREAEIYQtvMLRHENILgfiaadnKDNGTWTQLWL-- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  710 iVTEYMENGSLDAFLRTHdgqftIVQLVGMLR---GVGAGMRYL--------SDLGYIHRDLAARNVLVDGRLVCKVSDF 778
Cdd:cd14143    71 -VSDYHEHGSLFDYLNRY-----TVTVEGMIKlalSIASGLAHLhmeivgtqGKPAIAHRDLKSKNILVKKNGTCCIADL 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  779 GLsrALEDDPE------AAYTTAGGKipiRWTAPE----AIAFRTFSS--ASDVWSFGVVMWEVlayGER---------- 836
Cdd:cd14143   145 GL--AVRHDSAtdtidiAPNHRVGTK---RYMAPEvlddTINMKHFESfkRADIYALGLVFWEI---ARRcsiggihedy 216
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  837 --PYWNMTNQDviSSVEE--------GYRLPAP---MGCP--RALHQLMLDCWHKDRAQR 881
Cdd:cd14143   217 qlPYYDLVPSD--PSIEEmrkvvceqKLRPNIPnrwQSCEalRVMAKIMRECWYANGAAR 274
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
637-859 3.39e-12

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: 68.54  E-value: 3.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  637 EKIIGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYME 716
Cdd:cd14168    15 KEVLGTGAFSEVVLAEERATGKL---FAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  717 NGSLdaFLR-THDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLV----DGRLVcKVSDFGLSRaLEDDPEAA 791
Cdd:cd14168    92 GGEL--FDRiVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYfsqdEESKI-MISDFGLSK-MEGKGDVM 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 341940659  792 YTTAGGKipiRWTAPEAIAFRTFSSASDVWSFGVVMWeVLAYGERPYWNMTNQDVISSV-EEGYRLPAP 859
Cdd:cd14168   168 STACGTP---GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFEQIlKADYEFDSP 232
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
638-881 3.48e-12

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1a, also called Activin receptor-Like Kinase 3 (ALK3), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Germline mutations in BMPR1a are associated with an increased risk to Juvenile Polyposis Syndrome, a hamartomatous disorder that may lead to gastrointestinal cancer. BMPR1a may also play an indirect role in the development of hematopoietic stem cells (HSCs) as osteoblasts are a major component of the HSC niche within the bone marrow. BMPR1a belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, 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, like BMPR1a, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, 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. The BMPR1a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 68.14  E-value: 3.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLqvpgqRDVPVAIKAlkagYTERQRQDFLSEAAIMGQ--FDHPNIIRLEGVVTRGRLA----MIV 711
Cdd:cd14220     1 RQIGKGRYGEVWMGKW-----RGEKVAVKV----FFTTEEASWFRETEIYQTvlMRHENILGFIAADIKGTGSwtqlYLI 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  712 TEYMENGSLDAFLRthdgqFTIVQLVGMLR---GVGAGMRYLSDLGY--------IHRDLAARNVLVDGRLVCKVSDFGL 780
Cdd:cd14220    72 TDYHENGSLYDFLK-----CTTLDTRALLKlaySAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGTCCIADLGL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  781 SRALEDDPEAA----YTTAGGKipiRWTAPEAI-------AFRTFSSAsDVWSFGVVMWE---------VLAYGERPYWN 840
Cdd:cd14220   147 AVKFNSDTNEVdvplNTRVGTK---RYMAPEVLdeslnknHFQAYIMA-DIYSFGLIIWEmarrcvtggIVEEYQLPYYD 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 341940659  841 MTNQDviSSVEEGYRLPAPMG-------------CPRALHQLMLDCWHKDRAQR 881
Cdd:cd14220   223 MVPSD--PSYEDMREVVCVKRlrptvsnrwnsdeCLRAVLKLMSECWAHNPASR 274
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
637-859 3.53e-12

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: 67.71  E-value: 3.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  637 EKIIGSGESGEV--CYGRLQvpGQRdvpVAIKALKAGYTERQRQDFLSEAAimgqfDHPNIIRLEGV---VTRG-RLAMI 710
Cdd:cd14172     9 KQVLGLGVNGKVleCFHRRT--GQK---CALKLLYDSPKARREVEHHWRAS-----GGPHIVHILDVyenMHHGkRCLLI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  711 VTEYMENGSLdaFLRTH---DGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGR---LVCKVSDFGLSR-- 782
Cdd:cd14172    79 IMECMEGGEL--FSRIQergDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKekdAVLKLTDFGFAKet 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  783 ----ALEDDPEAAYttaggkipirWTAPEAIAFRTFSSASDVWSFGVVMWeVLAYGERPYWNMTNQDVISSVEEGYRL-- 856
Cdd:cd14172   157 tvqnALQTPCYTPY----------YVAPEVLGPEKYDKSCDMWSLGVIMY-ILLCGFPPFYSNTGQAISPGMKRRIRMgq 225

                  ....*.
gi 341940659  857 ---PAP 859
Cdd:cd14172   226 ygfPNP 231
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
640-831 3.79e-12

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: 68.75  E-value: 3.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQrdvPVAIKAL-KAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGV-VTRGRLAMIVTEYMEN 717
Cdd:cd07856    18 VGMGAFGLVCSARDQLTGQ---NVAVKKImKPFSTPVLAKRTYRELKLLKHLRHENIISLSDIfISPLEDIYFVTELLGT 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  718 gSLDAFLRTH--DGQFTIVQLVGMLRGvgagMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRAleDDPEAAytta 795
Cdd:cd07856    95 -DLHRLLTSRplEKQFIQYFLYQILRG----LKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLARI--QDPQMT---- 163
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 341940659  796 gGKIPIR-WTAPE-AIAFRTFSSASDVWSFGVVMWEVL 831
Cdd:cd07856   164 -GYVSTRyYRAPEiMLTWQKYDVEVDIWSAGCIFAEML 200
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
638-838 3.92e-12

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: 67.86  E-value: 3.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVPGQ----RDVPVAIKALKAGYTERQRQDFLS-------EAAIMGQFDHPNIIRLEGVVTRGR 706
Cdd:cd14077     7 KTIGAGSMGKVKLAKHIRTGEkcaiKIIPRASNAGLKKEREKRLEKEISrdirtirEAALSSLLNHPHICRLRDFLRTPN 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  707 LAMIVTEYMENGSLDAFLRTHdGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALed 786
Cdd:cd14077    87 HYYMLFEYVDGGQLLDYIISH-GKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGLSNLY-- 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 341940659  787 DPEAAYTTAGGKipIRWTAPEAIAFRTFSSAS-DVWSFGVVMWeVLAYGERPY 838
Cdd:cd14077   164 DPRRLLRTFCGS--LYFAAPELLQAQPYTGPEvDVWSFGVVLY-VLVCGKVPF 213
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
743-895 3.94e-12

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: 67.52  E-value: 3.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  743 VGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRaleddPEAAYTTAGGKIPIRwTAPEAIAFRtFSSASDVWS 822
Cdd:cd13975   111 VVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFCK-----PEAMMSGSIVGTPIH-MAPELFSGK-YDNSVDVYA 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  823 FGVVMWEVLAYGER---PYWNMTNQDVI-SSVEEGYRlpapmgcPRALH-------QLMLDCWHKDRAQRPRFAHVVSVL 891
Cdd:cd13975   184 FGILFWYLCAGHVKlpeAFEQCASKDHLwNNVRKGVR-------PERLPvfdeecwNLMEACWSGDPSQRPLLGIVQPKL 256

                  ....
gi 341940659  892 DALV 895
Cdd:cd13975   257 QGIM 260
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
633-838 4.88e-12

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 69.82  E-value: 4.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  633 RIHIEKIIGSGESGEVCYG---RLQvpgqRDVpvAIKALKAGYTE----RQRqdFLSEAAIMGQFDHPNIIRLEGVVTRG 705
Cdd:NF033483    8 RYEIGERIGRGGMAEVYLAkdtRLD----RDV--AVKVLRPDLARdpefVAR--FRREAQSAASLSHPNIVSVYDVGEDG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  706 RLAMIVTEYMENGSLDAFLRTHdGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLV--DGRLvcKVSDFGLSRA 783
Cdd:NF033483   80 GIPYIVMEYVDGRTLKDYIREH-GPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILItkDGRV--KVTDFGIARA 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 341940659  784 LEddpEAAYT-------TA---------GGKIPIRwtapeaiafrtfssaSDVWSFGVVMWEVLAyGERPY 838
Cdd:NF033483  157 LS---STTMTqtnsvlgTVhylspeqarGGTVDAR---------------SDIYSLGIVLYEMLT-GRPPF 208
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
638-831 5.02e-12

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: 68.59  E-value: 5.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVPGQRdvpVAIKALKAGY---TERQRQdfLSEAAIMGQFDHPNIIRLEGVVTRGRL------A 708
Cdd:cd07850     6 KPIGSGAQGIVCAAYDTVTGQN---VAIKKLSRPFqnvTHAKRA--YRELVLMKLVNHKNIIGLLNVFTPQKSleefqdV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  709 MIVTEYMENGSLDAFLRTHDGQFTIVQLVGMLrgvgAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRaleddp 788
Cdd:cd07850    81 YLVMELMDANLCQVIQMDLDHERMSYLLYQML----CGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLAR------ 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 341940659  789 eaaytTAGGKIPIR-------WTAPEAIAFRTFSSASDVWSFGVVMWEVL 831
Cdd:cd07850   151 -----TAGTSFMMTpyvvtryYRAPEVILGMGYKENVDIWSVGCIMGEMI 195
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
638-839 5.20e-12

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 68.47  E-value: 5.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQvpGQRDVPVAIKALKAGYTERQRQ--DFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYM 715
Cdd:PTZ00426   36 RTLGTGSFGRVILATYK--NEDFPPVAIKRFEKSKIIKQKQvdHVFSERKILNYINHPFCVNLYGSFKDESYLYLVLEFV 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  716 ENGSLDAFLRTHD------GQFTIVQLVGMLRgvgagmrYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEddpE 789
Cdd:PTZ00426  114 IGGEFFTFLRRNKrfpndvGCFYAAQIVLIFE-------YLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAKVVD---T 183
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 341940659  790 AAYTTAGGKipiRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYW 839
Cdd:PTZ00426  184 RTYTLCGTP---EYIAPEILLNVGHGKAADWWTLGIFIYEILV-GCPPFY 229
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
675-838 6.08e-12

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: 66.87  E-value: 6.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  675 RQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLDAFLR------THDGQFTIVQLVgmlrgvgAGMR 748
Cdd:cd05572    35 RQQEHIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLGGELWTILRdrglfdEYTARFYTACVV-------LAFE 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  749 YLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDpEAAYTTAGgkIPiRWTAPEAIAFRTFSSASDVWSFGVVMW 828
Cdd:cd05572   108 YLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKKLGSG-RKTWTFCG--TP-EYVAPEIILNKGYDFSVDYWSLGILLY 183
                         170
                  ....*....|
gi 341940659  829 EVLAyGERPY 838
Cdd:cd05572   184 ELLT-GRPPF 192
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
638-838 6.99e-12

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: 67.46  E-value: 6.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVPGQRdVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMEN 717
Cdd:cd05612     7 KTIGTGTFGRVHLVRDRISEHY-YALKVMAIPEVIRLKQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYMLMEYVPG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  718 GSLDAFLRTHdGQFTivqlVGMLRGVGA----GMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDdpeAAYT 793
Cdd:cd05612    86 GELFSYLRNS-GRFS----NSTGLFYASeivcALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKLRD---RTWT 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 341940659  794 TAGgkIPiRWTAPEAIAFRTFSSASDVWSFGVVMWEVLA-----YGERPY 838
Cdd:cd05612   158 LCG--TP-EYLAPEVIQSKGHNKAVDWWALGILIYEMLVgyppfFDDNPF 204
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
663-831 1.35e-11

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: 66.09  E-value: 1.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  663 VAIKALKAGYTERQRQ--DFLSEAAIMGQFDHPNIIRL-EGVVTRGRLAMiVTEYMENGSLDAFLRT------HDGQFTI 733
Cdd:cd05579    21 YAIKVIKKRDMIRKNQvdSVLAERNILSQAQNPFVVKLyYSFQGKKNLYL-VMEYLPGGDLYSLLENvgaldeDVARIYI 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  734 VQLVgmlrgvgAGMRYLSDLGYIHRDLAARNVLVD--GRLvcKVSDFGLSRA-LEDD----PEAAYTTAGGKIPIR---- 802
Cdd:cd05579   100 AEIV-------LALEYLHSHGIIHRDLKPDNILIDanGHL--KLTDFGLSKVgLVRRqiklSIQKKSNGAPEKEDRrivg 170
                         170       180       190
                  ....*....|....*....|....*....|..
gi 341940659  803 ---WTAPEAIAFRTFSSASDVWSFGVVMWEVL 831
Cdd:cd05579   171 tpdYLAPEILLGQGHGKTVDWWSLGVILYEFL 202
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
673-859 1.48e-11

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: 66.29  E-value: 1.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  673 TERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSL--DAFLRTH----DGQFTIVQLVGMLRgvgag 746
Cdd:cd14086    40 SARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFDLVTGGELfeDIVAREFyseaDASHCIQQILESVN----- 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  747 mrYLSDLGYIHRDLAARNVLVDGRL---VCKVSDFGLSRALEDDPEAAYTTAGGKIpirWTAPEAIAFRTFSSASDVWSF 823
Cdd:cd14086   115 --HCHQNGIVHRDLKPENLLLASKSkgaAVKLADFGLAIEVQGDQQAWFGFAGTPG---YLSPEVLRKDPYGKPVDIWAC 189
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 341940659  824 GVVMWeVLAYGERPYWNMTNQDVISSVEEG-YRLPAP 859
Cdd:cd14086   190 GVILY-ILLVGYPPFWDEDQHRLYAQIKAGaYDYPSP 225
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
636-858 1.50e-11

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: 65.90  E-value: 1.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIIGSGESGEVCYGRLQVPGQRdvpVAIKAL-KAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVV-TRGRLAMIVtE 713
Cdd:cd14074     7 LEETLGRGHFAVVKLARHVFTGEK---VAVKVIdKTKLDDVSKAHLFQEVRCMKLVQHPNVVRLYEVIdTQTKLYLIL-E 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  714 YMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVC-KVSDFGLSRALEddPEAAY 792
Cdd:cd14074    83 LGDGGDMYDYIMKHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQGLvKLTDFGFSNKFQ--PGEKL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 341940659  793 TTAGGKIPirWTAPEAIAFRTFSS-ASDVWSFGVVMWeVLAYGERPYWNMTNQDVISSVEEG-YRLPA 858
Cdd:cd14074   161 ETSCGSLA--YSAPEILLGDEYDApAVDIWSLGVILY-MLVCGQPPFQEANDSETLTMIMDCkYTVPA 225
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
682-850 1.55e-11

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: 66.07  E-value: 1.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  682 SEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLdaFLRTHD-GQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDL 760
Cdd:cd14169    50 NEIAVLRRINHENIVSLEDIYESPTHLYLAMELVTGGEL--FDRIIErGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDL 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  761 AARNVLV-----DGRLVckVSDFGLSRaLEDDpeAAYTTAGGKiPiRWTAPEAIAFRTFSSASDVWSFGVVMWeVLAYGE 835
Cdd:cd14169   128 KPENLLYatpfeDSKIM--ISDFGLSK-IEAQ--GMLSTACGT-P-GYVAPELLEQKPYGKAVDVWAIGVISY-ILLCGY 199
                         170
                  ....*....|....*
gi 341940659  836 RPYWNMTNQDVISSV 850
Cdd:cd14169   200 PPFYDENDSELFNQI 214
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
639-829 1.58e-11

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: 66.62  E-value: 1.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  639 IIGSGESGEVCYGRLQVPGQrdvpvaIKALKAGYTERQRQDF----LSEAAIMGQFDHPNIIRLEGVVTRGRLA------ 708
Cdd:cd07865    19 KIGQGTFGEVFKARHRKTGQ------IVALKKVLMENEKEGFpitaLREIKILQLLKHENVVNLIEICRTKATPynrykg 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  709 --MIVTEYMENgSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALED 786
Cdd:cd07865    93 siYLVFEFCEH-DLAGLLSNKNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGLARAFSL 171
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 341940659  787 DPEAAYTTAGGKIPIRW-TAPE-AIAFRTFSSASDVWSFGVVMWE 829
Cdd:cd07865   172 AKNSQPNRYTNRVVTLWyRPPElLLGERDYGPPIDMWGAGCIMAE 216
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
663-853 1.84e-11

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: 65.37  E-value: 1.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  663 VAIKALKagYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLDAFLRtHDGQFTIVQLVGMLRG 742
Cdd:cd14006    21 FAAKFIP--KRDKKKEAVLREISILNQLQHPRIIQLHEAYESPTELVLILELCSGGELLDRLA-ERGSLSEEEVRTYMRQ 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  743 VGAGMRYLSDLGYIHRDLAARNVLVDGRLV--CKVSDFGLSRALEDD---------PEAAyttaggkipirwtAPEAIAF 811
Cdd:cd14006    98 LLEGLQYLHNHHILHLDLKPENILLADRPSpqIKIIDFGLARKLNPGeelkeifgtPEFV-------------APEIVNG 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 341940659  812 RTFSSASDVWSFGVVMWeVLAYGERPYWNMTNQDVISSVEEG 853
Cdd:cd14006   165 EPVSLATDMWSIGVLTY-VLLSGLSPFLGEDDQETLANISAC 205
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
636-850 1.91e-11

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: 65.75  E-value: 1.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIIGSGESGEVCYGRLQVPGQRDVPVAIKALKAGYTER--QRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTE 713
Cdd:cd14196     9 IGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRgvSREEIEREVSILRQVLHPNIITLHDVYENRTDVVLILE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  714 YMENGSLDAFLRTHDgQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLV----CKVSDFGLSRALEDDPE 789
Cdd:cd14196    89 LVSGGELFDFLAQKE-SLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIEDGVE 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 341940659  790 aaYTTAGGKiPiRWTAPEAIAFRTFSSASDVWSFGVVMWeVLAYGERPYWNMTNQDVISSV 850
Cdd:cd14196   168 --FKNIFGT-P-EFVAPEIVNYEPLGLEADMWSIGVITY-ILLSGASPFLGDTKQETLANI 223
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
638-841 1.99e-11

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: 65.39  E-value: 1.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEV--CYGRlqVPGQRdvpVAIKALKAGYTERQRQDFLSEAAimgqfDHPNIIRL----EGVVTRGRLAMIV 711
Cdd:cd14089     7 QVLGLGINGKVleCFHK--KTGEK---FALKVLRDNPKARREVELHWRAS-----GCPHIVRIidvyENTYQGRKCLLVV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  712 TEYMENGSL-DAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGR---LVCKVSDFGLsrALEDD 787
Cdd:cd14089    77 MECMEGGELfSRIQERADSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKgpnAILKLTDFGF--AKETT 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 341940659  788 PEAAYTTaggkiPI---RWTAPEAIAFRTFSSASDVWSFGVVMWeVLAYGERPYWNM 841
Cdd:cd14089   155 TKKSLQT-----PCytpYYVAPEVLGPEKYDKSCDMWSLGVIMY-ILLCGYPPFYSN 205
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
639-829 2.28e-11

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: 65.76  E-value: 2.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  639 IIGSGESGEVCYGRlQVPGQRDVpvAIKALKAGYTERQ-RQDFLSEAAIMGQ---FDHPNIIRLEGV-----VTRGRLAM 709
Cdd:cd07838     6 EIGEGAYGTVYKAR-DLQDGRFV--ALKKVRVPLSEEGiPLSTIREIALLKQlesFEHPNVVRLLDVchgprTDRELKLT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  710 IVTEYMENgSLDAFLRTHD----GQFTIVQLVG-MLRGVgagmRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRAL 784
Cdd:cd07838    83 LVFEHVDQ-DLATYLDKCPkpglPPETIKDLMRqLLRGL----DFLHSHRIVHRDLKPQNILVTSDGQVKLADFGLARIY 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 341940659  785 EDdpEAAYTtaggkiPIRWT----APEAIAFRTFSSASDVWSFGVVMWE 829
Cdd:cd07838   158 SF--EMALT------SVVVTlwyrAPEVLLQSSYATPVDMWSVGCIFAE 198
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
640-837 2.39e-11

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-3 shows a restricted pattern of expression and is present in brain, kidney, and intestine. It is elevated in Alzheimer's disease (AD) and has been shown to associate with paired helical filaments (PHFs) and stimulate Tau phosphorylation. As AD progresses, phosphorylated Tau aggregates and forms PHFs, which leads to the formation of neurofibrillary tangles. In human glioma cells, PCTAIRE-3 induces cell cycle arrest and cell death. PCTAIRE-3 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 65.80  E-value: 2.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENG- 718
Cdd:cd07871    13 LGEGTYATVFKGRSKLTENL---VALKEIRLEHEEGAPCTAIREVSLLKNLKHANIVTLHDIIHTERCLTLVFEYLDSDl 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  719 --SLD---AFLRTHDGQFTIVQLvgmLRGvgagMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRAlEDDPEAAYT 793
Cdd:cd07871    90 kqYLDncgNLMSMHNVKIFMFQL---LRG----LSYCHKRKILHRDLKPQNLLINEKGELKLADFGLARA-KSVPTKTYS 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 341940659  794 TaggKIPIRWTAPEAIAFRT--FSSASDVWSFGVVMWEvLAYGeRP 837
Cdd:cd07871   162 N---EVVTLWYRPPDVLLGSteYSTPIDMWGVGCILYE-MATG-RP 202
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
668-830 2.44e-11

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 66.94  E-value: 2.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  668 LKAGyterQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLA-MIVTEYMENgsLDAFLRTHDgQFTIVQLVGMLRGVGAG 746
Cdd:PHA03212  122 IKAG----QRGGTATEAHILRAINHPSIIQLKGTFTYNKFTcLILPRYKTD--LYCYLAAKR-NIAICDILAIERSVLRA 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  747 MRYLSDLGYIHRDLAARNVLVD--GRlVCkVSDFGLSRALEDDPEAAYTTAGGKIPIrwTAPEAIAFRTFSSASDVWSFG 824
Cdd:PHA03212  195 IQYLHENRIIHRDIKAENIFINhpGD-VC-LGDFGAACFPVDINANKYYGWAGTIAT--NAPELLARDPYGPAVDIWSAG 270

                  ....*.
gi 341940659  825 VVMWEV 830
Cdd:PHA03212  271 IVLFEM 276
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
638-883 2.60e-11

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: 65.31  E-value: 2.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVcYgRLQVPGQRdvpvaIKALK----AGYTERQRQDFLSEAAIMGQF-DHPNIIRL---EGVVTRGRLAM 709
Cdd:cd14131     7 KQLGKGGSSKV-Y-KVLNPKKK-----IYALKrvdlEGADEQTLQSYKNEIELLKKLkGSDRIIQLydyEVTDEDDYLYM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  710 IvteyMENGSLD--AFLRTHDGQ-----FTIVQLVGMLRGVgagmRYLSDLGYIHRDLAARN-VLVDGRLvcKVSDFGLS 781
Cdd:cd14131    80 V----MECGEIDlaTILKKKRPKpidpnFIRYYWKQMLEAV----HTIHEEGIVHSDLKPANfLLVKGRL--KLIDFGIA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  782 RALEDDpeaayTT-------AGgkiPIRWTAPEAIAFRTFSS----------ASDVWSFGVVMWEvLAYGERPYWNMTN- 843
Cdd:cd14131   150 KAIQND-----TTsivrdsqVG---TLNYMSPEAIKDTSASGegkpkskigrPSDVWSLGCILYQ-MVYGKTPFQHITNp 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 341940659  844 -QDVISSVEEGYRLPAPMGCPRALHQLMLDCWHKDRAQRPR 883
Cdd:cd14131   221 iAKLQAIIDPNHEIEFPDIPNPDLIDVMKRCLQRDPKKRPS 261
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
636-831 2.85e-11

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: 65.60  E-value: 2.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIiGSGESGEVCYGRLQVPGQRdvpVAIKALKAGY-TERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEY 714
Cdd:cd07860     5 VEKI-GEGTYGVVYKARNKLTGEV---VALKKIRLDTeTEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  715 MeNGSLDAFLR-THDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALeDDPEAAYT 793
Cdd:cd07860    81 L-HQDLKKFMDaSALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAF-GVPVRTYT 158
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 341940659  794 TAggKIPIRWTAPEA-IAFRTFSSASDVWSFGVVMWEVL 831
Cdd:cd07860   159 HE--VVTLWYRAPEIlLGCKYYSTAVDIWSLGCIFAEMV 195
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
633-838 3.27e-11

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: 64.79  E-value: 3.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  633 RIHIEKIIGSGESGevcYGRLQVPGQRDVPVAIKalkagYTER-QRQDFLSEAAIMGQ--FDHPNIIRLEGVVTRGRLAM 709
Cdd:cd14662     1 RYELVKDIGSGNFG---VARLMRNKETKELVAVK-----YIERgLKIDENVQREIINHrsLRHPNIIRFKEVVLTPTHLA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  710 IVTEYMENGSLdaFLRTHD-GQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDG----RLvcKVSDFGLSRA- 783
Cdd:cd14662    73 IVMEYAAGGEL--FERICNaGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGspapRL--KICDFGYSKSs 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 341940659  784 -LEDDPEAAYTTAGgkipirWTAPEAIAFRTFS-SASDVWSFGVVMWeVLAYGERPY 838
Cdd:cd14662   149 vLHSQPKSTVGTPA------YIAPEVLSRKEYDgKVADVWSCGVTLY-VMLVGAYPF 198
EphA2_TM pfam14575
Ephrin type-A receptor 2 transmembrane domain; Epha2_TM represents the left-handed dimer ...
561-631 3.35e-11

Ephrin type-A receptor 2 transmembrane domain; Epha2_TM represents the left-handed dimer transmembrane domain of of EphA2 receptor. This domain oligomerises and is important for the active signalling process.


Pssm-ID: 464211  Cd Length: 72  Bit Score: 59.92  E-value: 3.35e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 341940659   561 ICKKRHCGYSKAFQDSDEEKMHYqngqapppvflplnhppgKFPETQFSAEPHTYEEPGRAGRSFTREIEA 631
Cdd:pfam14575   20 IRRRRCCGRKKSQDDDEEEFHQY------------------KPPGRKTYIDPHTYEDPNQAVLEFAKEIDA 72
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
674-859 3.68e-11

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: 64.99  E-value: 3.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  674 ERQRQDFLSEAAIMGQF-DHPNIIRLEGVVTRGRLAMIVTEYMENGSLDAFLrTHDGQFTIVQLVGMLRGVGAGMRYLSD 752
Cdd:cd14181    56 EEVRSSTLKEIHILRQVsGHPSIITLIDSYESSTFIFLVFDLMRRGELFDYL-TEKVTLSEKETRSIMRSLLEAVSYLHA 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  753 LGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYT--TAGgkipirWTAPEAI------AFRTFSSASDVWSFG 824
Cdd:cd14181   135 NNIVHRDLKPENILLDDQLHIKLSDFGFSCHLEPGEKLRELcgTPG------YLAPEILkcsmdeTHPGYGKEVDLWACG 208
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 341940659  825 VVMWEVLAyGERPYWNMTNQDVISSVEEG-YRLPAP 859
Cdd:cd14181   209 VILFTLLA-GSPPFWHRRQMLMLRMIMEGrYQFSSP 243
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
632-831 4.08e-11

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: 64.98  E-value: 4.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  632 SRIHIEKIiGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIV 711
Cdd:cd07870     1 SYLNLEKL-GEGSYATVYKGISRINGQL---VALKVISMKTEEGVPFTAIREASLLKGLKHANIVLLHDIIHTKETLTFV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  712 TEYMENgSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRAlEDDPEAA 791
Cdd:cd07870    77 FEYMHT-DLAQYMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLARA-KSIPSQT 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 341940659  792 YTTAggKIPIRWTAPEAIAFRT-FSSASDVWSFGVVMWEVL 831
Cdd:cd07870   155 YSSE--VVTLWYRPPDVLLGATdYSSALDIWGAGCIFIEML 193
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
633-837 4.27e-11

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: 65.50  E-value: 4.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  633 RIHIEKIIGSGESGEVCYGRlQVPGQRDVPVAIKAL-----KAGYTERQrqdfLSEAAIMGQF-DHPNIIRL--EGVVTR 704
Cdd:cd07857     1 RYELIKELGQGAYGIVCSAR-NAETSEEETVAIKKItnvfsKKILAKRA----LRELKLLRHFrGHKNITCLydMDIVFP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  705 GRL--AMIVTEYMEnGSLDAFLRTHDG------QFTIVQLVgmlrgvgAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVS 776
Cdd:cd07857    76 GNFneLYLYEELME-ADLHQIIRSGQPltdahfQSFIYQIL-------CGLKYIHSANVLHRDLKPGNLLVNADCELKIC 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 341940659  777 DFGLSRALEDDPE--AAYTTagGKIPIRW-TAPE-AIAFRTFSSASDVWSFGVVMWEVLayGERP 837
Cdd:cd07857   148 DFGLARGFSENPGenAGFMT--EYVATRWyRAPEiMLSFQSYTKAIDVWSVGCILAELL--GRKP 208
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
638-831 4.76e-11

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: 65.36  E-value: 4.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGrlqVPGQRDVPVAIKALkagYTERQRQDFLSEA----AIMGQFDHPNIIRLEGVVT------RGRL 707
Cdd:cd07880    21 KQVGSGAYGTVCSA---LDRRTGAKVAIKKL---YRPFQSELFAKRAyrelRLLKHMKHENVIGLLDVFTpdlsldRFHD 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  708 AMIVTEYMenGSLDAFLRTHDG------QFTIVQlvgMLRGvgagMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLS 781
Cdd:cd07880    95 FYLVMPFM--GTDLGKLMKHEKlsedriQFLVYQ---MLKG----LKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLA 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 341940659  782 RalEDDPEAAyttagGKIPIRW-TAPEAI-AFRTFSSASDVWSFGVVMWEVL 831
Cdd:cd07880   166 R--QTDSEMT-----GYVVTRWyRAPEVIlNWMHYTQTVDIWSVGCIMAEML 210
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
632-858 5.22e-11

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: 65.38  E-value: 5.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  632 SRIHIEKIIGSGESGEVCYGRLQVPGQrdvPVAIKAL-KAGYTER-QRQDFLSEAAIMGQFDHPNIIRLegVVT---RGR 706
Cdd:cd05573     1 DDFEVIKVIGRGAFGEVWLVRDKDTGQ---VYAMKILrKSDMLKReQIAHVRAERDILADADSPWIVRL--HYAfqdEDH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  707 LAMiVTEYMENGSLDAFLRTHD------GQFTIVQLVgmlrgvgAGMRYLSDLGYIHRDLAARNVLVD--GRLvcKVSDF 778
Cdd:cd05573    76 LYL-VMEYMPGGDLMNLLIKYDvfpeetARFYIAELV-------LALDSLHKLGFIHRDIKPDNILLDadGHI--KLADF 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  779 GLSRALEDDPEAAY---------TTAGGKIPIRWT-----------------APEAIAFRTFSSASDVWSFGVVMWEVLa 832
Cdd:cd05573   146 GLCTKMNKSGDRESylndsvntlFQDNVLARRRPHkqrrvraysavgtpdyiAPEVLRGTGYGPECDWWSLGVILYEML- 224
                         250       260
                  ....*....|....*....|....*....
gi 341940659  833 YGERPYWNMTNQDV---ISSVEEGYRLPA 858
Cdd:cd05573   225 YGFPPFYSDSLVETyskIMNWKESLVFPD 253
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
692-888 5.71e-11

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: 64.58  E-value: 5.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  692 HPNIIRLEGVVTRGRLAMIVTEYMENGSL-DAFLRthDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLV--- 767
Cdd:cd14091    53 HPNIITLRDVYDDGNSVYLVTELLRGGELlDRILR--QKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYade 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  768 DGRLVC-KVSDFGLSRALEDD------PeaAYTTaggkipiRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWN 840
Cdd:cd14091   131 SGDPESlRICDFGFAKQLRAEngllmtP--CYTA-------NFVAPEVLKKQGYDAACDIWSLGVLLYTMLA-GYTPFAS 200
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 341940659  841 MTN---QDVISSVEEG-YRLPAPMGC-----PRALHQLMLdcwHKDRAQRPRFAHVV 888
Cdd:cd14091   201 GPNdtpEVILARIGSGkIDLSGGNWDhvsdsAKDLVRKML---HVDPSQRPTAAQVL 254
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
636-872 7.08e-11

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: 64.07  E-value: 7.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIIGSGESGEVCYGRLQVPGQRdvpVAIKALKagyTERQRQD------FLSEAAIMGQFDHPNIIRLEGVVTRGRLAM 709
Cdd:cd14070     6 IGRKLGEGSFAKVREGLHAVTGEK---VAIKVID---KKKAKKDsyvtknLRREGRIQQMIRHPNITQLLDILETENSYY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  710 IVTEYMENGSLdaFLRTHDGQ-FTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRA--LED 786
Cdd:cd14070    80 LVMELCPGGNL--MHRIYDKKrLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNCagILG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  787 DPEAAYTTAGGKIpirWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYwnmtnqdvisSVEegyrlpaPMGCpRAL 866
Cdd:cd14070   158 YSDPFSTQCGSPA---YAAPELLARKKYGPKVDVWSIGVNMYAMLT-GTLPF----------TVE-------PFSL-RAL 215

                  ....*.
gi 341940659  867 HQLMLD 872
Cdd:cd14070   216 HQKMVD 221
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
740-870 7.70e-11

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: 63.79  E-value: 7.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  740 LRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYTTAGGKipiRWTAPEAIAFRTFSSASD 819
Cdd:cd14189   107 LKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARLEPPEQRKKTICGTP---NYLAPEVLLRQGHGPESD 183
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 341940659  820 VWSFGVVMWEVLAyGERPYWNMTNQDVISSVEE-GYRLPAPMGCPrALHQLM 870
Cdd:cd14189   184 VWSLGCVMYTLLC-GNPPFETLDLKETYRCIKQvKYTLPASLSLP-ARHLLA 233
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
646-840 7.90e-11

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: 63.50  E-value: 7.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  646 GEVCYGR--LQVPGQRDVPVAIKALKAGYTerQRQDFLSEAAIMGQF-DHPNIIRLEGVVTRGRLA-MIVTEYMENGSLD 721
Cdd:cd13987     2 GEGTYGKvlLAVHKGSGTKMALKFVPKPST--KLKDFLREYNISLELsVHPHIIKTYDVAFETEDYyVFAQEYAPYGDLF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  722 AFLRTHDG------QFTIVQlvgmlrgVGAGMRYLSDLGYIHRDLAARNVLV---DGRLVcKVSDFGLSRAleddpeaay 792
Cdd:cd13987    80 SIIPPQVGlpeervKRCAAQ-------LASALDFMHSKNLVHRDIKPENVLLfdkDCRRV-KLCDFGLTRR--------- 142
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 341940659  793 ttAGGKIPIRW-----TAPE------AIAFRTFSSaSDVWSFGVVM---------WEVLAYGERPYWN 840
Cdd:cd13987   143 --VGSTVKRVSgtipyTAPEvceakkNEGFVVDPS-IDVWAFGVLLfccltgnfpWEKADSDDQFYEE 207
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
638-831 8.86e-11

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: 63.74  E-value: 8.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVPgqrDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIR-----LEGVVTRGRLAM--- 709
Cdd:cd14048    12 QCLGRGGFGVVFEAKNKVD---DCNYAVKRIRLPNNELAREKVLREVRALAKLDHPGIVRyfnawLERPPEGWQEKMdev 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  710 ---IVTEYMENGSLDAFLRthdGQFTIVQ-----LVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLS 781
Cdd:cd14048    89 ylyIQMQLCRKENLKDWMN---RRCTMESrelfvCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVGDFGLV 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 341940659  782 RAL-EDDPE-------AAYTTAGGKIPIR-WTAPEAIAFRTFSSASDVWSFGVVMWEVL 831
Cdd:cd14048   166 TAMdQGEPEqtvltpmPAYAKHTGQVGTRlYMSPEQIHGNQYSEKVDIFALGLILFELI 224
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
633-827 1.02e-10

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: 63.52  E-value: 1.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  633 RIHIEKIIGSGESGEVcygRLQVPGQRDVPVAIKAL-KAGYTER-----QRQDFLSEAAIMGQF-DHPNIIRLEGVVTRG 705
Cdd:cd13993     1 RYQLISPIGEGAYGVV---YLAVDLRTGRKYAIKCLyKSGPNSKdgndfQKLPQLREIDLHRRVsRHPNIITLHDVFETE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  706 RLAMIVTEYMENGSL------DAF--LRTHDGQFTIVQLVgmlrgvgAGMRYLSDLGYIHRDLAARNVLVDGR-LVCKVS 776
Cdd:cd13993    78 VAIYIVLEYCPNGDLfeaiteNRIyvGKTELIKNVFLQLI-------DAVKHCHSLGIYHRDIKPENILLSQDeGTVKLC 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 341940659  777 DFGLSRALEDDPEAAYTTAggkipiRWTAPEAIAF-----RTFSSAS-DVWSFGVVM 827
Cdd:cd13993   151 DFGLATTEKISMDFGVGSE------FYMAPECFDEvgrslKGYPCAAgDIWSLGIIL 201
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
638-838 1.06e-10

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: 64.35  E-value: 1.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVPGQRDVPVAIKALKAGYTERQRQDFL---SEAAIMGQFDHPNIIRLE-GVVTRGRLAMIVtE 713
Cdd:cd05584     2 KVLGKGGYGKVFQVRKTTGSDKGKIFAMKVLKKASIVRNQKDTAhtkAERNILEAVKHPFIVDLHyAFQTGGKLYLIL-E 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  714 YMENGSLDAFLRThDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYT 793
Cdd:cd05584    81 YLSGGELFMHLER-EGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCKESIHDGTVTHT 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 341940659  794 TAGgkiPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPY 838
Cdd:cd05584   160 FCG---TIEYMAPEILTRSGHGKAVDWWSLGALMYDMLT-GAPPF 200
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
407-535 1.10e-10

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 65.41  E-value: 1.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  407 YSFWIEAVNGvSNLSPEPRSAAVVNITTNQAAPSQVVVIRQeraGQTSVSLLWQEPEQPNgiILEYEIkyYEKDKEMQSY 486
Cdd:COG3401   205 YYYRVAATDT-GGESAPSNEVSVTTPTTPPSAPTGLTATAD---TPGSVTLSWDPVTESD--ATGYRV--YRSNSGDGPF 276
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 341940659  487 STLKAVT-TRATVSGLKPGTRYVFQVRARTSAGC-GRFSQAMEVETGKPRP 535
Cdd:COG3401   277 TKVATVTtTSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSNVVSVTTDLTPP 327
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
640-831 1.17e-10

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: 64.30  E-value: 1.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYTE--RQRQDFlSEAAIMGQFDHPNIIRLEGVVTRG------RLAMIV 711
Cdd:cd07878    23 VGSGAYGSVCSAYDTRLRQK---VAVKKLSRPFQSliHARRTY-RELRLLKHMKHENVIGLLDVFTPAtsienfNEVYLV 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  712 TEYM--ENGSLDAFLRTHDG--QFTIVQLvgmLRGvgagMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDD 787
Cdd:cd07878    99 TNLMgaDLNNIVKCQKLSDEhvQFLIYQL---LRG----LKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLARQADDE 171
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 341940659  788 peaayttAGGKIPIRW-TAPE-AIAFRTFSSASDVWSFGVVMWEVL 831
Cdd:cd07878   172 -------MTGYVATRWyRAPEiMLNWMHYNQTVDIWSVGCIMAELL 210
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
683-838 1.21e-10

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: 63.43  E-value: 1.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  683 EAAIMGQFDHPNIIRLEGVV---TRGRLAMiVTEYMENGSLDAFlrTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRD 759
Cdd:cd14200    73 EIAILKKLDHVNIVKLIEVLddpAEDNLYM-VFDLLRKGPVMEV--PSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRD 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  760 LAARNVLV--DGRLvcKVSDFGLSRALEDDPEAAYTTAGGKIpirWTAPEAIA--FRTFS-SASDVWSFGVVMWeVLAYG 834
Cdd:cd14200   150 IKPSNLLLgdDGHV--KIADFGVSNQFEGNDALLSSTAGTPA---FMAPETLSdsGQSFSgKALDVWAMGVTLY-CFVYG 223

                  ....
gi 341940659  835 ERPY 838
Cdd:cd14200   224 KCPF 227
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
638-831 1.23e-10

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: 64.28  E-value: 1.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVPGqrdVPVAIKALKAGY-TERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRL------AMI 710
Cdd:cd07876    27 KPIGSGAQGIVCAAFDTVLG---INVAVKKLSRPFqNQTHAKRAYRELVLLKCVNHKNIISLLNVFTPQKSleefqdVYL 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  711 VTEYMENGSLDAFLRTHDGQFTIVQLVGMLrgvgAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDpea 790
Cdd:cd07876   104 VMELMDANLCQVIHMELDHERMSYLLYQML----CGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTACTN--- 176
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 341940659  791 aYTTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVL 831
Cdd:cd07876   177 -FMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELV 216
STKc_IRAK2 cd14157
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; ...
657-831 1.38e-10

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: 63.32  E-value: 1.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  657 GQRD-VPVAIKALKAGYTERQRQD---FLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLDAFLRTHDGQ-- 730
Cdd:cd14157    12 GYRHgKQYVIKRLKETECESPKSTerfFQTEVQICFRCCHPNILPLLGFCVESDCHCLIYPYMPNGSLQDRLQQQGGShp 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  731 FTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLsRALEDDPEAAYTTAGGKIpIRWTA---PE 807
Cdd:cd14157    92 LPWEQRLSISLGLLKAVQHLHNFGILHGNIKSSNVLLDGNLLPKLGHSGL-RLCPVDKKSVYTMMKTKV-LQISLaylPE 169
                         170       180
                  ....*....|....*....|....*.
gi 341940659  808 AIaFR--TFSSASDVWSFGVVMWEVL 831
Cdd:cd14157   170 DF-VRhgQLTEKVDIFSCGVVLAEIL 194
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
711-852 1.48e-10

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: 63.86  E-value: 1.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  711 VTEYMENGSLdAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRalEDDPEA 790
Cdd:cd05616    79 VMEYVNGGDL-MYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCK--ENIWDG 155
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 341940659  791 AYTTAGGKIPiRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWNMTNQDVISSVEE 852
Cdd:cd05616   156 VTTKTFCGTP-DYIAPEIIAYQPYGKSVDWWAFGVLLYEMLA-GQAPFEGEDEDELFQSIME 215
SAM_EPH-A3 cd09544
SAM domain of EPH-A3 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
933-990 1.52e-10

SAM domain of EPH-A3 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A3 subfamily of receptor tyrosine kinases is a C-terminal putative protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A3 receptors and appears to mediate cell-cell initiated signal transduction. EPH-A3 receptors bind SH2/SH3 containing adaptor protein Nck1 and this adaptor is a key factor in EPH-A3 mediated signaling. However SAM domain is not implemented in this interaction. Activation of EPH-A3 receptors inhibits outgrowth and cell migration. Mutations in SAM domain may play a role in development of hepatocellular carcinoma. Expression of EPH-A3 is associated with lymphocytic leukemia and defines the subset of rhabdomyosarcoma tumors. EPH-A3 receptors are attractive targets for drug design.


Pssm-ID: 188943  Cd Length: 63  Bit Score: 57.76  E-value: 1.52e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 341940659  933 TVGDWLDSIRMGRYRDHFAAGGYSSLGMVLRMNAQDVRALGITLMGHQKKILGSIQTM 990
Cdd:cd09544     4 TTGDWLNGARTAHCKEIFTGVEYSSCDTIAKISTDDMKKVGVTVVGPQKKIVSSIKTL 61
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
692-852 1.55e-10

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: 63.52  E-value: 1.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  692 HPNIIRLEGVVTRGRLAMIVTEYMENGSLdaFLRTHDGQ-FTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLV--- 767
Cdd:cd14179    61 HPNIVKLHEVYHDQLHTFLVMELLKGGEL--LERIKKKQhFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFtde 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  768 DGRLVCKVSDFGLSRALEDDPEAAYTTAggkIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWNMTNQDVI 847
Cdd:cd14179   139 SDNSEIKIIDFGFARLKPPDNQPLKTPC---FTLHYAAPELLNYNGYDESCDLWSLGVILYTMLS-GQVPFQCHDKSLTC 214

                  ....*
gi 341940659  848 SSVEE 852
Cdd:cd14179   215 TSAEE 219
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
635-831 1.62e-10

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: 62.79  E-value: 1.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  635 HIEKIIGSGESGEVCYGRLQVPGQRdvpVAIK-----ALKAGYTERQRqdflsEAAIMGQFDHPNIIRLEGVVTRGRLAM 709
Cdd:cd14078     6 ELHETIGSGGFAKVKLATHILTGEK---VAIKimdkkALGDDLPRVKT-----EIEALKNLSHQHICRLYHVIETDNKIF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  710 IVTEYMENGSLDAFLRTHDgQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPE 789
Cdd:cd14078    78 MVLEYCPGGELFDYIVAKD-RLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCAKPKGGMD 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 341940659  790 AAYTTAGGKiPIrWTAPEAIAFRTF-SSASDVWSFGVVMWEVL 831
Cdd:cd14078   157 HHLETCCGS-PA-YAAPELIQGKPYiGSEADVWSMGVLLYALL 197
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
690-841 1.75e-10

Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity.STRAD-beta is also referred to as ALS2CR2 (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 2 protein), since the human gene encoding it is located within the juvenile ALS2 critical region on chromosome 2q33-q34. It is not linked to the development of ALS2. 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. The STRAD-beta 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: 270864 [Multi-domain]  Cd Length: 328  Bit Score: 63.74  E-value: 1.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  690 FDHPNIIRLEGVVTRGRLAMIVTEYMENGSLDAFLRTHDGQFTIVQLVG-MLRGVGAGMRYLSDLGYIHRDLAARNVLVD 768
Cdd:cd08226    56 FRHPNIMTHWTVFTEGSWLWVISPFMAYGSARGLLKTYFPEGMNEALIGnILYGAIKALNYLHQNGCIHRSVKASHILIS 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  769 G----------RLVCKVSDFGLSRALEDDPEaaYTTAggKIPirWTAPEAIA--FRTFSSASDVWSFGVVMWEvLAYGER 836
Cdd:cd08226   136 GdglvslsglsHLYSMVTNGQRSKVVYDFPQ--FSTS--VLP--WLSPELLRqdLHGYNVKSDIYSVGITACE-LARGQV 208

                  ....*
gi 341940659  837 PYWNM 841
Cdd:cd08226   209 PFQDM 213
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
638-837 1.86e-10

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: 63.40  E-value: 1.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVcygRL-QVPGQRDVpVAIKAL-KAGYTER-QRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEY 714
Cdd:cd05599     7 KVIGRGAFGEV---RLvRKKDTGHV-YAMKKLrKSEMLEKeQVAHVRAERDILAEADNPWVVKLYYSFQDEENLYLIMEF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  715 MENGSLDAFLRTHD------GQFTIVQLVgmlrgvgAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDP 788
Cdd:cd05599    83 LPGGDMMTLLMKKDtlteeeTRFYIAETV-------LAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCTGLKKSH 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 341940659  789 eAAYTTAGgkIPiRWTAPEAIAFRTFSSASDVWSFGVVMWEVLA-----YGERP 837
Cdd:cd05599   156 -LAYSTVG--TP-DYIAPEVFLQKGYGKECDWWSLGVIMYEMLIgyppfCSDDP 205
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
675-838 1.88e-10

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: 62.66  E-value: 1.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  675 RQRQDFL-SEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSL-DAFLRT-----HDGQFTIVQLVGMLrgvgagm 747
Cdd:cd14185    39 KGKEDMIeSEILIIKSLSHPNIVKLFEVYETEKEIYLILEYVRGGDLfDAIIESvkfteHDAALMIIDLCEAL------- 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  748 RYLSDLGYIHRDLAARNVLV----DGRLVCKVSDFGLSRALEddpEAAYTTAGGKIpirWTAPEAIAFRTFSSASDVWSF 823
Cdd:cd14185   112 VYIHSKHIVHRDLKPENLLVqhnpDKSTTLKLADFGLAKYVT---GPIFTVCGTPT---YVAPEILSEKGYGLEVDMWAA 185
                         170
                  ....*....|....*
gi 341940659  824 GVVMWeVLAYGERPY 838
Cdd:cd14185   186 GVILY-ILLCGFPPF 199
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
676-888 2.25e-10

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: 62.34  E-value: 2.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  676 QRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLDAFLRTHDgQFTIVQLVGMLRGVGAGMRYLSDLGY 755
Cdd:cd14188    44 QREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRRSMAHILKARK-VLTEPEVRYYLRQIVSGLKYLHEQEI 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  756 IHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYTTAGGKipiRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAygE 835
Cdd:cd14188   123 LHRDLKLGNFFINENMELKVGDFGLAARLEPLEHRRRTICGTP---NYLSPEVLNKQGHGCESDIWALGCVMYTMLL--G 197
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 341940659  836 RPYWNMTN-QDVISSVEEG-YRLPAPMGCPRalHQLMLDCWHKDRAQRPRFAHVV 888
Cdd:cd14188   198 RPPFETTNlKETYRCIREArYSLPSSLLAPA--KHLIASMLSKNPEDRPSLDEII 250
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
638-839 2.25e-10

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: 62.35  E-value: 2.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEV--CY----GR----LQVPGQRDVPVAIKALKAGYTERQrqdflseaaIMGQFDHPNIIRLEGVVT--RG 705
Cdd:cd06653     8 KLLGRGAFGEVylCYdadtGRelavKQVPFDPDSQETSKEVNALECEIQ---------LLKNLRHDRIVQYYGCLRdpEE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  706 RLAMIVTEYMENGSLDAFLRTHdGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALe 785
Cdd:cd06653    79 KKLSIFVEYMPGGSVKDQLKAY-GALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRI- 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 341940659  786 ddpEAAYTTAGGKIPIR----WTAPEAIAFRTFSSASDVWSFGVVMWEVLAygERPYW 839
Cdd:cd06653   157 ---QTICMSGTGIKSVTgtpyWMSPEVISGEGYGRKADVWSVACTVVEMLT--EKPPW 209
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
639-852 2.39e-10

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: 63.48  E-value: 2.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  639 IIGSGESGEVCYGRLQvpgQRDVPVAIKALKAGYTeRQRQDF---LSEAAIMGQFDHPNII-RLEGVVTRGRLAMIVTEY 714
Cdd:cd05615    17 VLGKGSFGKVMLAERK---GSDELYAIKILKKDVV-IQDDDVectMVEKRVLALQDKPPFLtQLHSCFQTVDRLYFVMEY 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  715 MENGSLDAFLRtHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRalEDDPEAAYTT 794
Cdd:cd05615    93 VNGGDLMYHIQ-QVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCK--EHMVEGVTTR 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 341940659  795 AGGKIPiRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWNMTNQDVISSVEE 852
Cdd:cd05615   170 TFCGTP-DYIAPEIIAYQPYGRSVDWWAYGVLLYEMLA-GQPPFDGEDEDELFQSIME 225
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
640-831 2.40e-10

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: 63.52  E-value: 2.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYTE--RQRQDFlSEAAIMGQFDHPNIIRLEGVVTRGRL------AMIV 711
Cdd:cd07877    25 VGSGAYGSVCAAFDTKTGLR---VAVKKLSRPFQSiiHAKRTY-RELRLLKHMKHENVIGLLDVFTPARSleefndVYLV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  712 TEYMeNGSLDAFLR----THDG-QFTIVQLvgmLRGvgagMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALED 786
Cdd:cd07877   101 THLM-GADLNNIVKcqklTDDHvQFLIYQI---LRG----LKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDD 172
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 341940659  787 DpeaayttAGGKIPIRW-TAPE-AIAFRTFSSASDVWSFGVVMWEVL 831
Cdd:cd07877   173 E-------MTGYVATRWyRAPEiMLNWMHYNQTVDIWSVGCIMAELL 212
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
637-839 2.46e-10

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: 62.77  E-value: 2.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  637 EKI--IGSGESGEVCYGRLQVPGQrdvPVAIKAlkagYTERQ-----RQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAM 709
Cdd:cd07847     4 EKLskIGEGSYGVVFKCRNRETGQ---IVAIKK----FVESEddpviKKIALREIRMLKQLKHPNLVNLIEVFRRKRKLH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  710 IVTEYMENGSLDAfLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALeDDPE 789
Cdd:cd07847    77 LVFEYCDHTVLNE-LEKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARIL-TGPG 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 341940659  790 AAYTTAggkIPIRW-TAPEAIAFRT-FSSASDVWSFGVVMWEVLAyGErPYW 839
Cdd:cd07847   155 DDYTDY---VATRWyRAPELLVGDTqYGPPVDVWAIGCVFAELLT-GQ-PLW 201
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
627-838 2.93e-10

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: 62.19  E-value: 2.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  627 REIEASRIHIEKIIGSGESGEVCYGRLQvpgQRDVPVAIKALKAGYTERQ--RQDFLSEAAIMGQFDHPNIIRLEGVVTR 704
Cdd:cd14117     1 RKFTIDDFDIGRPLGKGKFGNVYLAREK---QSKFIVALKVLFKSQIEKEgvEHQLRREIEIQSHLRHPNILRLYNYFHD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  705 GRLAMIVTEYMENGSLDAFLRTHdGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSral 784
Cdd:cd14117    78 RKRIYLILEYAPRGELYKELQKH-GRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWS--- 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 341940659  785 EDDPEAAYTTAGGKIPirWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPY 838
Cdd:cd14117   154 VHAPSLRRRTMCGTLD--YLPPEMIEGRTHDEKVDLWCIGVLCYELLV-GMPPF 204
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
638-831 3.13e-10

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: 63.00  E-value: 3.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYterQRQDFLSEA----AIMGQFDHPNIIRLEGVVTRGRLA----- 708
Cdd:cd07879    21 KQVGSGAYGSVCSAIDKRTGEK---VAIKKLSRPF---QSEIFAKRAyrelTLLKHMQHENVIGLLDVFTSAVSGdefqd 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  709 -MIVTEYMENgSLDAFLRTHDGQFTIVQLV-GMLRGvgagMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRAled 786
Cdd:cd07879    95 fYLVMPYMQT-DLQKIMGHPLSEDKVQYLVyQMLCG----LKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLARH--- 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 341940659  787 dPEAAYTtagGKIPIRW-TAPEAI-AFRTFSSASDVWSFGVVMWEVL 831
Cdd:cd07879   167 -ADAEMT---GYVVTRWyRAPEVIlNWMHYNQTVDIWSVGCIMAEML 209
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
683-852 3.45e-10

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: 62.19  E-value: 3.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  683 EAAIMGQFDHPNIIRL-EGVVTRGRLAMIVtEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLA 761
Cdd:cd14104    46 EISILNIARHRNILRLhESFESHEELVMIF-EFISGVDIFERITTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIR 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  762 ARNVLVDGRL--VCKVSDFGLSRALE--DDPEAAYTTAggkipiRWTAPEAIAFRTFSSASDVWSFGVVMWeVLAYGERP 837
Cdd:cd14104   125 PENIIYCTRRgsYIKIIEFGQSRQLKpgDKFRLQYTSA------EFYAPEVHQHESVSTATDMWSLGCLVY-VLLSGINP 197
                         170
                  ....*....|....*
gi 341940659  838 YWNMTNQDVISSVEE 852
Cdd:cd14104   198 FEAETNQQTIENIRN 212
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
676-845 3.56e-10

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: 61.98  E-value: 3.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  676 QRQDFLSEAAIMGQ-FDHPNIIRLEGVV-TRGRLAmIVTEYMENGSLDAFLrTHDGQFTIVQLVGMLRGVGAGMRYLSDL 753
Cdd:cd14106    50 CRNEILHEIAVLELcKDCPRVVNLHEVYeTRSELI-LILELAAGGELQTLL-DEEECLTEADVRRLMRQILEGVQYLHER 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  754 GYIHRDLAARNVLVDGRLVC---KVSDFGLSRALEDDPEaayttaggkipIR-------WTAPEAIAFRTFSSASDVWSF 823
Cdd:cd14106   128 NIVHLDLKPQNILLTSEFPLgdiKLCDFGISRVIGEGEE-----------IReilgtpdYVAPEILSYEPISLATDMWSI 196
                         170       180
                  ....*....|....*....|..
gi 341940659  824 GVVMWeVLAYGERPYWNMTNQD 845
Cdd:cd14106   197 GVLTY-VLLTGHSPFGGDDKQE 217
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
638-839 3.72e-10

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: 61.60  E-value: 3.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEV--CY----GR----LQVPGQRDVPVAIKALKAGYTERQrqdflseaaIMGQFDHPNIIRLEGVV--TRG 705
Cdd:cd06652     8 KLLGQGAFGRVylCYdadtGRelavKQVQFDPESPETSKEVNALECEIQ---------LLKNLLHERIVQYYGCLrdPQE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  706 RLAMIVTEYMENGSLDAFLRTHdGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALE 785
Cdd:cd06652    79 RTLSIFMEYMPGGSIKDQLKSY-GALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGASKRLQ 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 341940659  786 DDPEAAYTTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAygERPYW 839
Cdd:cd06652   158 TICLSGTGMKSVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLT--EKPPW 209
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
677-837 3.75e-10

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: 62.45  E-value: 3.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  677 RQDFLSEAAIMGQFDHPNIIRLEGV-VTRGRLAmIVTEYMENGSLDAFLRTHD-------GQFTIvqlvgmlrGVGAGMR 748
Cdd:cd06615    43 RNQIIRELKVLHECNSPYIVGFYGAfYSDGEIS-ICMEHMDGGSLDQVLKKAGripenilGKISI--------AVLRGLT 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  749 YLSD-LGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDdpEAAYTTAGGKipiRWTAPEAIAFRTFSSASDVWSFGVVM 827
Cdd:cd06615   114 YLREkHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLID--SMANSFVGTR---SYMSPERLQGTHYTVQSDIWSLGLSL 188
                         170
                  ....*....|
gi 341940659  828 WEvLAYGERP 837
Cdd:cd06615   189 VE-MAIGRYP 197
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
673-897 4.15e-10

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: 61.66  E-value: 4.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  673 TERQRQDFLSEAAIMGQFDHPNIIRL----EGVVTRGRLAMIVTEYMENGSLDAFLRthdgQFTIVQ---LVGMLRGVGA 745
Cdd:cd14031    49 TKAEQQRFKEEAEMLKGLQHPNIVRFydswESVLKGKKCIVLVTELMTSGTLKTYLK----RFKVMKpkvLRSWCRQILK 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  746 GMRYLSDLG--YIHRDLAARNVLVDGRL-VCKVSDFGLSRALeddpEAAYTTAGGKIPiRWTAPEAIAfRTFSSASDVWS 822
Cdd:cd14031   125 GLQFLHTRTppIIHRDLKCDNIFITGPTgSVKIGDLGLATLM----RTSFAKSVIGTP-EFMAPEMYE-EHYDESVDVYA 198
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 341940659  823 FGVVMWEvLAYGERPYWNMTN-QDVISSVEEGYRlPAPMG--CPRALHQLMLDCWHKDRAQRprfahvVSVLDALVHS 897
Cdd:cd14031   199 FGMCMLE-MATSEYPYSECQNaAQIYRKVTSGIK-PASFNkvTDPEVKEIIEGCIRQNKSER------LSIKDLLNHA 268
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
636-863 4.51e-10

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 61.76  E-value: 4.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIiGSGESGEVCYGRLQVPGQrdvpvaIKALKAGYTERQRQDFLS----EAAIMGQFDHPNIIRLEGVVTRGRLAMIV 711
Cdd:PLN00009    7 VEKI-GEGTYGVVYKARDRVTNE------TIALKKIRLEQEDEGVPStairEISLLKEMQHGNIVRLQDVVHSEKRLYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  712 TEYmengsLDAFLRTH---------DGQFTIVQLVGMLRGVGagmrYLSDLGYIHRDLAARNVLVDGRL-VCKVSDFGLS 781
Cdd:PLN00009   80 FEY-----LDLDLKKHmdsspdfakNPRLIKTYLYQILRGIA----YCHSHRVLHRDLKPQNLLIDRRTnALKLADFGLA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  782 RALeDDPEAAYTTAggKIPIRWTAPEA-IAFRTFSSASDVWSFGVVMWEvlaygerpywnMTNQDVI----SSVEEGYRL 856
Cdd:PLN00009  151 RAF-GIPVRTFTHE--VVTLWYRAPEIlLGSRHYSTPVDIWSVGCIFAE-----------MVNQKPLfpgdSEIDELFKI 216

                  ....*..
gi 341940659  857 PAPMGCP 863
Cdd:PLN00009  217 FRILGTP 223
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
633-882 4.66e-10

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: 61.58  E-value: 4.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  633 RIHIEKIIGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYTERQRQdFLSEAAIMGQF-DHPNIIRL--EGVVTRG--RL 707
Cdd:cd13985     1 RYQVTKQLGEGGFSYVYLAHDVNTGRR---YALKRMYFNDEEQLRV-AIKEIEIMKRLcGHPNIVQYydSAILSSEgrKE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  708 AMIVTEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLG--YIHRDLAARNVLVDGRLVCKVSDFGLS---- 781
Cdd:cd13985    77 VLLLMEYCPGSLVDILEKSPPSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFGSAtteh 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  782 --------RALEDDPEAAYTTaggkipIRWTAPEAI-AFRTF--SSASDVWSFGVVMWeVLAYGERPYwnmTNQDVISSV 850
Cdd:cd13985   157 ypleraeeVNIIEEEIQKNTT------PMYRAPEMIdLYSKKpiGEKADIWALGCLLY-KLCFFKLPF---DESSKLAIV 226
                         250       260       270
                  ....*....|....*....|....*....|..
gi 341940659  851 EEGYRLPAPMGCPRALHQLMLDCWHKDRAQRP 882
Cdd:cd13985   227 AGKYSIPEQPRYSPELHDLIRHMLTPDPAERP 258
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
638-838 4.79e-10

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: 62.27  E-value: 4.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYT--ERQRQDFLSEAAIMG-QFDHPNIIRLEGVVTRGRLAMIVTEY 714
Cdd:cd05620     1 KVLGKGSFGKVLLAELKGKGEY---FAVKALKKDVVliDDDVECTMVEKRVLAlAWENPFLTHLYCTFQTKEHLFFVMEF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  715 MENGSLdAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYTT 794
Cdd:cd05620    78 LNGGDL-MFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKENVFGDNRASTF 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 341940659  795 AGGKipiRWTAPEAIAFRTFSSASDVWSFGVVMWEVLaYGERPY 838
Cdd:cd05620   157 CGTP---DYIAPEILQGLKYTFSVDWWSFGVLLYEML-IGQSPF 196
pknD PRK13184
serine/threonine-protein kinase PknD;
633-881 5.50e-10

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 63.64  E-value: 5.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  633 RIHIEKIIGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYTE--RQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMI 710
Cdd:PRK13184    3 RYDIIRLIGKGGMGEVYLAYDPVCSRR---VALKKIREDLSEnpLLKKRFLREAKIAADLIHPGIVPVYSICSDGDPVYY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  711 VTEYMENGSLDAFLRT----------HDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVD--GRLVckVSDF 778
Cdd:PRK13184   80 TMPYIEGYTLKSLLKSvwqkeslskeLAEKTSVGAFLSIFHKICATIEYVHSKGVLHRDLKPDNILLGlfGEVV--ILDW 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  779 G--LSRALEDDPEAAYT-----------TAGGKI--PIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYgERPYWN--- 840
Cdd:PRK13184  158 GaaIFKKLEEEDLLDIDvdernicyssmTIPGKIvgTPDYMAPERLLGVPASESTDIYALGVILYQMLTL-SFPYRRkkg 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 341940659  841 --MTNQDVISSVEE--GYRlpapmGCPRALHQLMLDCWHKDRAQR 881
Cdd:PRK13184  237 rkISYRDVILSPIEvaPYR-----EIPPFLSQIAMKALAVDPAER 276
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
640-831 5.65e-10

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: 61.52  E-value: 5.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYTERQRQ-DFLSEAAIMG---QFDHPNIIRLEGVVTRGRL--AMIVTE 713
Cdd:cd07863     8 IGVGAYGTVYKARDPHSGHF---VALKSVRVQTNEDGLPlSTVREVALLKrleAFDHPNIVRLMDVCATSRTdrETKVTL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  714 YMENgsLDAFLRTHDGQ-----FTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRaleddp 788
Cdd:cd07863    85 VFEH--VDQDLRTYLDKvpppgLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLAR------ 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 341940659  789 eaAYTTAGGKIPIRWT----APEAIAFRTFSSASDVWSFGVVMWEVL 831
Cdd:cd07863   157 --IYSCQMALTPVVVTlwyrAPEVLLQSTYATPVDMWSVGCIFAEMF 201
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
636-829 6.14e-10

Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK, CDK2, and CDK3. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression while the CDK1/cyclin B complex is critical for G2 to M phase transition. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. Studies in knockout mice revealed that CDK1 can compensate for the loss of the cdk2 gene as it can also bind cyclin E and drive G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 61.54  E-value: 6.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIiGSGESGEVCYGRLQVPGQrdvpvaIKALKAGYTERQRQDFLS----EAAIMGQFDHPNIIRLEGVVTRGRLAMIV 711
Cdd:cd07835     4 LEKI-GEGTYGVVYKARDKLTGE------IVALKKIRLETEDEGVPStairEISLLKELNHPNIVRLLDVVHSENKLYLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  712 TEYMeNGSLDAFLRTHDGQFTIVQLVG-----MLRGVGagmrYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALeD 786
Cdd:cd07835    77 FEFL-DLDLKKYMDSSPLTGLDPPLIKsylyqLLQGIA----FCHSHRVLHRDLKPQNLLIDTEGALKLADFGLARAF-G 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 341940659  787 DPEAAYTTaggKIPIRW-TAPEA-IAFRTFSSASDVWSFGVVMWE 829
Cdd:cd07835   151 VPVRTYTH---EVVTLWyRAPEIlLGSKHYSTPVDIWSVGCIFAE 192
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
638-882 6.28e-10

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: 61.66  E-value: 6.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVPGQRdvpVAIKALKAgyTERQRQDFLSEAAIMGQFDH-PNIIRLEGV-VTRGRLAM-----I 710
Cdd:cd06637    12 ELVGNGTYGQVYKGRHVKTGQL---AAIKVMDV--TGDEEEEIKQEINMLKKYSHhRNIATYYGAfIKKNPPGMddqlwL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  711 VTEYMENGSLDAFLRTHDGQFTIVQLVGML-RGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPE 789
Cdd:cd06637    87 VMEFCGAGSVTDLIKNTKGNTLKEEWIAYIcREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVG 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  790 AAYTTAGGKIpirWTAPEAIAF-----RTFSSASDVWSFGVVMWEvLAYGERPYWNMTNQDVISSVEegyRLPAP----M 860
Cdd:cd06637   167 RRNTFIGTPY---WMAPEVIACdenpdATYDFKSDLWSLGITAIE-MAEGAPPLCDMHPMRALFLIP---RNPAPrlksK 239
                         250       260
                  ....*....|....*....|..
gi 341940659  861 GCPRALHQLMLDCWHKDRAQRP 882
Cdd:cd06637   240 KWSKKFQSFIESCLVKNHSQRP 261
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
640-830 6.49e-10

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: 61.56  E-value: 6.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPgqrDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENgS 719
Cdd:cd07873    10 LGEGTYATVYKGRSKLT---DNLVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYLDK-D 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  720 LDAFL-------RTHDGQFTIVQLvgmLRGvgagMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRAlEDDPEAAY 792
Cdd:cd07873    86 LKQYLddcgnsiNMHNVKLFLFQL---LRG----LAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARA-KSIPTKTY 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 341940659  793 TTaggKIPIRWTAPEAIAFRT--FSSASDVWSFGVVMWEV 830
Cdd:cd07873   158 SN---EVVTLWYRPPDILLGStdYSTQIDMWGVGCIFYEM 194
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
692-853 7.83e-10

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: 61.43  E-value: 7.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  692 HPNIIRLEGVVTRGRLAMIVTEYMENGSLDAFLRTHDgQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLV---- 767
Cdd:cd14180    60 HPNIVALHEVLHDQYHTYLVMELLRGGELLDRIKKKA-RFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYades 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  768 DGRLVcKVSDFGLSRALEDDPEAAYTTAggkIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWNMTNQ--- 844
Cdd:cd14180   139 DGAVL-KVIDFGFARLRPQGSRPLQTPC---FTLQYAAPELFSNQGYDESCDLWSLGVILYTMLS-GQVPFQSKRGKmfh 213
                         170
                  ....*....|...
gi 341940659  845 ----DVISSVEEG 853
Cdd:cd14180   214 nhaaDIMHKIKEG 226
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
640-832 7.88e-10

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: 61.13  E-value: 7.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYTERQRQDFLSEAAIMGQF-DHPNIIRLEGVV---TRGRLAMIVtEYM 715
Cdd:cd07831     7 IGEGTFSEVLKAQSRKTGKY---YAIKCMKKHFKSLEQVNNLREIQALRRLsPHPNILRLIEVLfdrKTGRLALVF-ELM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  716 EnGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVcKVSDFGLSRALEDD-PEAAYtt 794
Cdd:cd07831    83 D-MNLYELIKGRKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDDIL-KLADFGSCRGIYSKpPYTEY-- 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 341940659  795 aggkIPIRW-TAPEAIAfrT---FSSASDVWSFGVVMWEVLA 832
Cdd:cd07831   159 ----ISTRWyRAPECLL--TdgyYGPKMDIWAVGCVFFEILS 194
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
691-888 8.20e-10

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: 61.16  E-value: 8.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  691 DHPNIIRLEGVVTR-----GRLAMIVTEYMENGSLDAFLRT--HDGQFTIVQLVG-MLRGVGAGMRYLSDLGYIHRDLAA 762
Cdd:cd06639    77 NHPNVVKFYGMFYKadqyvGGQLWLVLELCNGGSVTELVKGllKCGQRLDEAMISyILYGALLGLQHLHNNRIIHRDVKG 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  763 RNVLVDGRLVCKVSDFGLSRALEDDPEAAYTTAGGKIpirWTAPEAIAFR-----TFSSASDVWSFGVVMWEvLAYGERP 837
Cdd:cd06639   157 NNILLTTEGGVKLVDFGVSAQLTSARLRRNTSVGTPF---WMAPEVIACEqqydySYDARCDVWSLGITAIE-LADGDPP 232
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 341940659  838 YWNMtnqdviSSVEEGYRLPA--------PMGCPRALHQLMLDCWHKDRAQRPRFAHVV 888
Cdd:cd06639   233 LFDM------HPVKALFKIPRnppptllnPEKWCRGFSHFISQCLIKDFEKRPSVTHLL 285
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
756-882 8.83e-10

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 62.34  E-value: 8.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  756 IHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYTTAGGKIPIrWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYgE 835
Cdd:PTZ00267  191 MHRDLKSANIFLMPTGIIKLGDFGFSKQYSDSVSLDVASSFCGTPY-YLAPELWERKRYSKKADMWSLGVILYELLTL-H 268
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 341940659  836 RPYWNMTNQDVISSVEEGYRLPAPMGCPRALHQLMLDCWHKDRAQRP 882
Cdd:PTZ00267  269 RPFKGPSQREIMQQVLYGKYDPFPCPVSSGMKALLDPLLSKNPALRP 315
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
636-896 9.25e-10

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: 60.80  E-value: 9.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIIGSGESGEVCYGRLQVPGQRdvpVAIKALKAgyTERQRQDFLSEAAIMGQF-DHPNIIRLEGV-----VTRGRLAM 709
Cdd:cd06638    22 IIETIGKGTYGKVFKVLNKKNGSK---AAVKILDP--IHDIDEEIEAEYNILKALsDHPNVVKFYGMyykkdVKNGDQLW 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  710 IVTEYMENGSL----DAFLRTHDGQFTIVqLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALE 785
Cdd:cd06638    97 LVLELCNGGSVtdlvKGFLKRGERMEEPI-IAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  786 DDPEAAYTTAGGKIpirWTAPEAIAFR-----TFSSASDVWSFGVVMWEvLAYGERPYWNMTNQDVISSVeegyrlpaPM 860
Cdd:cd06638   176 STRLRRNTSVGTPF---WMAPEVIACEqqldsTYDARCDVWSLGITAIE-LGDGDPPLADLHPMRALFKI--------PR 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 341940659  861 GCPRALHQLML----------DCWHKDRAQRPrfahvvSVLDALVH 896
Cdd:cd06638   244 NPPPTLHQPELwsnefndfirKCLTKDYEKRP------TVSDLLQH 283
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
636-866 9.76e-10

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: 61.48  E-value: 9.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIIGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYT--ERQRQDFLSEAAIMG-QFDHPNIIRLEGVVTRGRLAMIVT 712
Cdd:cd05619     9 LHKMLGKGSFGKVFLAELKGTNQF---FAIKALKKDVVlmDDDVECTMVEKRVLSlAWEHPFLTHLFCTFQTKENLFFVM 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  713 EYMENGSLDAFLRT-HdgQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRalEDDPEAA 791
Cdd:cd05619    86 EYLNGGDLMFHIQScH--KFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCK--ENMLGDA 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 341940659  792 YTTAGGKIPiRWTAPEAIAFRTFSSASDVWSFGVVMWEVLaYGERPYWNMTNQDVISSVeegyRLPAPMgCPRAL 866
Cdd:cd05619   162 KTSTFCGTP-DYIAPEILLGQKYNTSVDWWSFGVLLYEML-IGQSPFHGQDEEELFQSI----RMDNPF-YPRWL 229
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
638-881 1.25e-09

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: 60.79  E-value: 1.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVPGQRdvpVAIKALKAGY--TERQRQDFLSEAAIMGQFDHPNIIRLE-GVVTRGRLAMiVTEY 714
Cdd:cd05595     1 KLLGKGTFGKVILVREKATGRY---YAMKILRKEViiAKDEVAHTVTESRVLQNTRHPFLTALKyAFQTHDRLCF-VMEY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  715 MENGSLDAFLR-----THD-GQFTIVQLVgmlrgvgAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDP 788
Cdd:cd05595    77 ANGGELFFHLSrervfTEDrARFYGAEIV-------SALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGITDG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  789 EAAYTTAGGKipiRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWNMTNQDVISSV-EEGYRLPAPMGcPRAlH 867
Cdd:cd05595   150 ATMKTFCGTP---EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHERLFELIlMEEIRFPRTLS-PEA-K 223
                         250
                  ....*....|....
gi 341940659  868 QLMLDCWHKDRAQR 881
Cdd:cd05595   224 SLLAGLLKKDPKQR 237
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
638-833 1.28e-09

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: 61.26  E-value: 1.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVpgqRDVPVAIKALKAGY-TERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRL------AMI 710
Cdd:cd07874    23 KPIGSGAQGIVCAAYDAV---LDRNVAIKKLSRPFqNQTHAKRAYRELVLMKCVNHKNIISLLNVFTPQKSleefqdVYL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  711 VTEYMENGSLDAFLRTHDGQFTIVQLVGMLrgvgAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRAleddPEA 790
Cdd:cd07874   100 VMELMDANLCQVIQMELDHERMSYLLYQML----CGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLART----AGT 171
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 341940659  791 AYTTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAY 833
Cdd:cd07874   172 SFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRH 214
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
636-830 1.33e-09

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: 60.51  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIiGSGESGEVCYGRLQVPGQrdvpvaIKALKAGYTERQRQDFLS----EAAIMGQFDHPNIIRLEGVVTRGRLAMIV 711
Cdd:cd07861     5 IEKI-GEGTYGVVYKGRNKKTGQ------IVAMKKIRLESEEEGVPStairEISLLKELQHPNIVCLEDVLMQENRLYLV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  712 TEYMengSLDafLRTH-----DGQFTIVQLV-GMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALe 785
Cdd:cd07861    78 FEFL---SMD--LKKYldslpKGKYMDAELVkSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARAF- 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 341940659  786 ddpeaayttaggKIPIR----------WTAPEAIAFRT-FSSASDVWSFGVVMWEV 830
Cdd:cd07861   152 ------------GIPVRvythevvtlwYRAPEVLLGSPrYSTPVDIWSIGTIFAEM 195
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
638-882 1.34e-09

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 62.45  E-value: 1.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVcygrLQVPGQRDVPV-AIKALK-AGYTERQRQDFLSEAAIMGQFDHPNIIR-LEGVVTRGRLAM-IVTE 713
Cdd:PTZ00266   19 KKIGNGRFGEV----FLVKHKRTQEFfCWKAISyRGLKEREKSQLVIEVNVMRELKHKNIVRyIDRFLNKANQKLyILME 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  714 YMENGSLDAFLRTHDGQFTIVQ---LVGMLRGVGAGMRYLSDLG-------YIHRDLAARNVL----------------- 766
Cdd:PTZ00266   95 FCDAGDLSRNIQKCYKMFGKIEehaIVDITRQLLHALAYCHNLKdgpngerVLHRDLKPQNIFlstgirhigkitaqann 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  767 VDGRLVCKVSDFGLSRALEDDpEAAYTTAGgkIPIRWTaPEAIAFRT--FSSASDVWSFGVVMWEvLAYGERPYWNMTN- 843
Cdd:PTZ00266  175 LNGRPIAKIGDFGLSKNIGIE-SMAHSCVG--TPYYWS-PELLLHETksYDDKSDMWALGCIIYE-LCSGKTPFHKANNf 249
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 341940659  844 QDVISSVEEGYRLPAPmGCPRALHQLMLDCWHKDRAQRP 882
Cdd:PTZ00266  250 SQLISELKRGPDLPIK-GKSKELNILIKNLLNLSAKERP 287
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
638-841 1.51e-09

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: 60.02  E-value: 1.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVPGQRdvpVAIKALKAgyTERQRQDFLSEAAIMGQFDH-PNIIRLEGVVTRGRLA------MI 710
Cdd:cd06636    22 EVVGNGTYGQVYKGRHVKTGQL---AAIKVMDV--TEDEEEEIKLEINMLKKYSHhRNIATYYGAFIKKSPPghddqlWL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  711 VTEYMENGSLDAFLRTHDGQFTIVQLVGML-RGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPE 789
Cdd:cd06636    97 VMEFCGAGSVTDLVKNTKGNALKEDWIAYIcREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVG 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 341940659  790 AAYTTAGGKIpirWTAPEAIAF-----RTFSSASDVWSFGVVMWEvLAYGERPYWNM 841
Cdd:cd06636   177 RRNTFIGTPY---WMAPEVIACdenpdATYDYRSDIWSLGITAIE-MAEGAPPLCDM 229
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
683-838 1.72e-09

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: 60.07  E-value: 1.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  683 EAAIMGQFDHPNIIRLEGVV---TRGRLAMiVTEYMENGsldAFLRT-HDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHR 758
Cdd:cd14118    64 EIAILKKLDHPNVVKLVEVLddpNEDNLYM-VFELVDKG---AVMEVpTDNPLSEETARSYFRDIVLGIEYLHYQKIIHR 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  759 DLAARNVLV--DGRLvcKVSDFGLSRALEDDPEAAYTTAGgkIPIrWTAPEAIA--FRTFSS-ASDVWSFGVVMWeVLAY 833
Cdd:cd14118   140 DIKPSNLLLgdDGHV--KIADFGVSNEFEGDDALLSSTAG--TPA-FMAPEALSesRKKFSGkALDIWAMGVTLY-CFVF 213

                  ....*
gi 341940659  834 GERPY 838
Cdd:cd14118   214 GRCPF 218
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
640-850 1.82e-09

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: 59.63  E-value: 1.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQRDVPVAIKALKAGYTER--QRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMEN 717
Cdd:cd14195    13 LGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSSRRgvSREEIEREVNILREIQHPNIITLHDIFENKTDVVLILELVSG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  718 GSLDAFLRTHDgQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLV----CKVSDFGLSRALEDDPEaaYT 793
Cdd:cd14195    93 GELFDFLAEKE-SLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVpnprIKLIDFGIAHKIEAGNE--FK 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 341940659  794 TAGGKiPiRWTAPEAIAFRTFSSASDVWSFGVVMWeVLAYGERPYWNMTNQDVISSV 850
Cdd:cd14195   170 NIFGT-P-EFVAPEIVNYEPLGLEADMWSIGVITY-ILLSGASPFLGETKQETLTNI 223
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
673-843 1.91e-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: 59.71  E-value: 1.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  673 TERQRQDFLSEAAIMGQFDHPNIIRL----EGVVTRGRLAMIVTEYMENGSLDAFLRthdgQFTIVQ---LVGMLRGVGA 745
Cdd:cd14032    40 TKVERQRFKEEAEMLKGLQHPNIVRFydfwESCAKGKRCIVLVTELMTSGTLKTYLK----RFKVMKpkvLRSWCRQILK 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  746 GMRYLSDLG--YIHRDLAARNVLVDGRL-VCKVSDFGLSRAleddPEAAYTTAGGKIPiRWTAPEAIAfRTFSSASDVWS 822
Cdd:cd14032   116 GLLFLHTRTppIIHRDLKCDNIFITGPTgSVKIGDLGLATL----KRASFAKSVIGTP-EFMAPEMYE-EHYDESVDVYA 189
                         170       180
                  ....*....|....*....|.
gi 341940659  823 FGVVMWEvLAYGERPYWNMTN 843
Cdd:cd14032   190 FGMCMLE-MATSEYPYSECQN 209
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
628-831 2.04e-09

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: 60.46  E-value: 2.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  628 EIEASRIHIeKIIGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYTER---QRQdfLSEAAIMGQFDHPNIIRLEGVVT- 703
Cdd:cd07858     2 EVDTKYVPI-KPIGRGAYGIVCSAKNSETNEK---VAIKKIANAFDNRidaKRT--LREIKLLRHLDHENVIAIKDIMPp 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  704 RGRLAM----IVTEYMENgSLDAFLRTHDG------QFTIVQLvgmLRGvgagMRYLSDLGYIHRDLAARNVLVDGRLVC 773
Cdd:cd07858    76 PHREAFndvyIVYELMDT-DLHQIIRSSQTlsddhcQYFLYQL---LRG----LKYIHSANVLHRDLKPSNLLLNANCDL 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  774 KVSDFGLSRALEDDPEaaYTTAggKIPIRW-TAPEAI-AFRTFSSASDVWSFGVVMWEVL 831
Cdd:cd07858   148 KICDFGLARTTSEKGD--FMTE--YVVTRWyRAPELLlNCSEYTTAIDVWSVGCIFAELL 203
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
644-852 2.08e-09

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: 59.60  E-value: 2.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  644 ESGEVCYGRLQVPGQRDVPVAIKALKAGYTERQ---RQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSL 720
Cdd:cd14113    11 EVAELGRGRFSVVKKCDQRGTKRAVATKFVNKKlmkRDQVTHELGVLQSLQHPQLVGLLDTFETPTSYILVLEMADQGRL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  721 -DAFLRThdGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRL---VCKVSDFGLSRALEDDPEAAYTTAG 796
Cdd:cd14113    91 lDYVVRW--GNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLskpTIKLADFGDAVQLNTTYYIHQLLGS 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 341940659  797 GKipirWTAPEAIAFRTFSSASDVWSFGVVMWeVLAYGERPYWNmtnqdviSSVEE 852
Cdd:cd14113   169 PE----FAAPEIILGNPVSLTSDLWSIGVLTY-VLLSGVSPFLD-------ESVEE 212
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
678-860 2.18e-09

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: 59.86  E-value: 2.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  678 QDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLdAF--LRTHDGQFTIVQLVG--MLRGVGAGMRYLSDL 753
Cdd:cd14094    50 EDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADL-CFeiVKRADAGFVYSEAVAshYMRQILEALRYCHDN 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  754 GYIHRDLAARNVL---VDGRLVCKVSDFGLSRALeddPEAAYTTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEV 830
Cdd:cd14094   129 NIIHRDVKPHCVLlasKENSAPVKLGGFGVAIQL---GESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFIL 205
                         170       180       190
                  ....*....|....*....|....*....|.
gi 341940659  831 LAyGERPYWNmTNQDVISSVEEG-YRLPAPM 860
Cdd:cd14094   206 LS-GCLPFYG-TKERLFEGIIKGkYKMNPRQ 234
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
632-830 2.35e-09

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: 59.62  E-value: 2.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  632 SRIHIEKIIGSGESGEVCYGRLQvpgQRDVPVAIKALK-AGYTERQRQDFLSEAAIMGQFDHPNIIRL-EGVVTRGRLaM 709
Cdd:cd07848     1 NKFEVLGVVGEGAYGVVLKCRHK---ETKEIVAIKKFKdSEENEEVKETTLRELKMLRTLKQENIVELkEAFRRRGKL-Y 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  710 IVTEYMENGSLDAFLRTHDG------QFTIVQLVgmlrgvgAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRA 783
Cdd:cd07848    77 LVFEYVEKNMLELLEEMPNGvppekvRSYIYQLI-------KAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARN 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 341940659  784 LEDDPEAAYTTAggkIPIRW-TAPEAIAFRTFSSASDVWSFGVVMWEV 830
Cdd:cd07848   150 LSEGSNANYTEY---VATRWyRSPELLLGAPYGKAVDMWSVGCILGEL 194
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
683-838 2.35e-09

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: 59.13  E-value: 2.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  683 EAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAA 762
Cdd:cd14114    49 EIQIMNQLHHPKLINLHDAFEDDNEMVLILEFLSGGELFERIAAEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKP 128
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 341940659  763 RNVLVDGRLV--CKVSDFGLSRALEDDPEAAYTTAGGKipirWTAPEAIAFRTFSSASDVWSFGVVMWeVLAYGERPY 838
Cdd:cd14114   129 ENIMCTTKRSneVKLIDFGLATHLDPKESVKVTTGTAE----FAAPEIVEREPVGFYTDMWAVGVLSY-VLLSGLSPF 201
fn3 pfam00041
Fibronectin type III domain;
329-422 2.53e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 54.73  E-value: 2.53e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659   329 SAPVNL-ISSVNGTSVTLEWAPPLDPGGrsDITYNAVcrrcpwalsHCEACGSGTRFVPQQTSLAQASLLVANLLAHMNY 407
Cdd:pfam00041    1 SAPSNLtVTDVTSTSLTVSWTPPPDGNG--PITGYEV---------EYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEY 69
                           90
                   ....*....|....*
gi 341940659   408 SFWIEAVNGVSNLSP 422
Cdd:pfam00041   70 EVRVQAVNGGGEGPP 84
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
638-838 2.57e-09

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: 59.72  E-value: 2.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYTERQRQ--DFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYM 715
Cdd:cd14209     7 KTLGTGSFGRVMLVRHKETGNY---YAMKILDKQKVVKLKQveHTLNEKRILQAINFPFLVKLEYSFKDNSNLYMVMEYV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  716 ENGSLDAFLRtHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDdpeAAYTTA 795
Cdd:cd14209    84 PGGEMFSHLR-RIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRVKG---RTWTLC 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 341940659  796 GgkIPiRWTAPEAIAFRTFSSASDVWSFGVVMWEvLAYGERPY 838
Cdd:cd14209   160 G--TP-EYLAPEIILSKGYNKAVDWWALGVLIYE-MAAGYPPF 198
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
639-831 2.58e-09

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: 59.36  E-value: 2.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  639 IIGSGESGEVCYGRLQVPGQrdvPVAIKAlkagYTERQRQDFLSEAAI-----MGQFDHPNIIRLEGVVTRGRLAMIVTE 713
Cdd:cd07846     8 LVGEGSYGMVMKCRHKETGQ---IVAIKK----FLESEDDKMVKKIAMreikmLKQLRHENLVNLIEVFRRKKRWYLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  714 YMENGSLDAFLRTHDG-QFTIVQ--LVGMLRGVGagmrYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEdDPEA 790
Cdd:cd07846    81 FVDHTVLDDLEKYPNGlDESRVRkyLFQILRGID----FCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLA-APGE 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 341940659  791 AYTTaggKIPIRW-TAPEAIAFRT-FSSASDVWSFGVVMWEVL 831
Cdd:cd07846   156 VYTD---YVATRWyRAPELLVGDTkYGKAVDVWAVGCLVTEML 195
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
638-881 2.61e-09

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: 59.98  E-value: 2.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVPGQRdvpVAIKAL--KAGYTERQRQDFLSE-AAIMGQFDHPNIIRLEGVVTRGRLAMIVTEY 714
Cdd:cd05603     1 KVIGKGSFGKVLLAKRKCDGKF---YAVKVLqkKTILKKKEQNHIMAErNVLLKNLKHPFLVGLHYSFQTSEKLYFVLDY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  715 MENGSLDAFLRtHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSR-ALEddPEAAYT 793
Cdd:cd05603    78 VNGGELFFHLQ-RERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKeGME--PEETTS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  794 TAGGKiPiRWTAPEAIAFRTFSSASDVWSFGVVMWEVLaYGERPYWnmtNQDVISSVEEGYRLP--APMGCPRALHQLML 871
Cdd:cd05603   155 TFCGT-P-EYLAPEVLRKEPYDRTVDWWCLGAVLYEML-YGLPPFY---SRDVSQMYDNILHKPlhLPGGKTVAACDLLQ 228
                         250
                  ....*....|
gi 341940659  872 DCWHKDRAQR 881
Cdd:cd05603   229 GLLHKDQRRR 238
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
632-881 2.87e-09

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: 60.03  E-value: 2.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  632 SRIHIEKIIGSGESGEVCYGRLQvpgQRDVPVAIKAL--KAGYTERQRQDFLSEA-AIMGQFDHPNIIRLE-GVVTRGRL 707
Cdd:cd05602     7 SDFHFLKVIGKGSFGKVLLARHK---SDEKFYAVKVLqkKAILKKKEEKHIMSERnVLLKNVKHPFLVGLHfSFQTTDKL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  708 AMIVtEYMENGSLDAFLRtHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRAlEDD 787
Cdd:cd05602    84 YFVL-DYINGGELFYHLQ-RERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKE-NIE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  788 PEAAYTTAGGKiPiRWTAPEAIAFRTFSSASDVWSFGVVMWEVLaYGERPYWNMTNQDVISSVeegyrLPAPM----GCP 863
Cdd:cd05602   161 PNGTTSTFCGT-P-EYLAPEVLHKQPYDRTVDWWCLGAVLYEML-YGLPPFYSRNTAEMYDNI-----LNKPLqlkpNIT 232
                         250
                  ....*....|....*...
gi 341940659  864 RALHQLMLDCWHKDRAQR 881
Cdd:cd05602   233 NSARHLLEGLLQKDRTKR 250
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
677-837 2.96e-09

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: 59.68  E-value: 2.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  677 RQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLDAFLRTHdGQFTiVQLVGMLR-GVGAGMRYLSDLGY 755
Cdd:cd06650    47 RNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKKA-GRIP-EQILGKVSiAVIKGLTYLREKHK 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  756 I-HRDLAARNVLVDGRLVCKVSDFGLSRALEDdpEAAYTTAGGKipiRWTAPEAIAFRTFSSASDVWSFGVVMWEvLAYG 834
Cdd:cd06650   125 ImHRDVKPSNILVNSRGEIKLCDFGVSGQLID--SMANSFVGTR---SYMSPERLQGTHYSVQSDIWSMGLSLVE-MAVG 198

                  ...
gi 341940659  835 ERP 837
Cdd:cd06650   199 RYP 201
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
638-846 3.00e-09

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: 60.09  E-value: 3.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVPGQRdvpVAIKALKAGY--TERQRQDFLSEAAIMGQFDHPNIIRLE-GVVTRGRLAMIVtEY 714
Cdd:cd05593    21 KLLGKGTFGKVILVREKASGKY---YAMKILKKEViiAKDEVAHTLTESRVLKNTRHPFLTSLKySFQTKDRLCFVM-EY 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  715 MENGSLdAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYTT 794
Cdd:cd05593    97 VNGGEL-FFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTF 175
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 341940659  795 AGGKipiRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWNMTNQDV 846
Cdd:cd05593   176 CGTP---EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKL 223
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
634-832 3.19e-09

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: 59.62  E-value: 3.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  634 IHIEKIiGSGESGEVCYGRLQVPgqrDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTE 713
Cdd:cd07872     9 IKLEKL-GEGTYATVFKGRSKLT---ENLVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIVHTDKSLTLVFE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  714 YMENgSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRAlEDDPEAAYT 793
Cdd:cd07872    85 YLDK-DLKQYMDDCGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARA-KSVPTKTYS 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 341940659  794 TaggKIPIRWTAPEAIAFRT--FSSASDVWSFGVVMWEVLA 832
Cdd:cd07872   163 N---EVVTLWYRPPDVLLGSseYSTQIDMWGVGCIFFEMAS 200
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
640-831 3.50e-09

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 59.32  E-value: 3.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENgS 719
Cdd:cd07869    13 LGEGSYATVYKGKSKVNGKL---VALKVIRLQEEEGTPFTAIREASLLKGLKHANIVLLHDIIHTKETLTLVFEYVHT-D 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  720 LDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRAlEDDPEAAYTTaggKI 799
Cdd:cd07869    89 LCQYMDKHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARA-KSVPSHTYSN---EV 164
                         170       180       190
                  ....*....|....*....|....*....|....
gi 341940659  800 PIRWTAPEAIAFRT--FSSASDVWSFGVVMWEVL 831
Cdd:cd07869   165 VTLWYRPPDVLLGSteYSTCLDMWGVGCIFVEMI 198
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
636-838 3.96e-09

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: 59.25  E-value: 3.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIIGSGESGEVCYGRLQVPGqrDVpVAIKALKAGYTERQRQD--FLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTE 713
Cdd:cd05601     5 VKNVIGRGHFGEVQVVKEKATG--DI-YAMKVLKKSETLAQEEVsfFEEERDIMAKANSPWITKLQYAFQDSENLYLVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  714 YMENGSLDAFLRTHDGQFT-------IVQLVGMLRGvgagmryLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALED 786
Cdd:cd05601    82 YHPGGDLLSLLSRYDDIFEesmarfyLAELVLAIHS-------LHSMGYVHRDIKPENILIDRTGHIKLADFGSAAKLSS 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 341940659  787 DpeaayTTAGGKIPI---RWTAPEAIAFRTFSSAS------DVWSFGVVMWEVLaYGERPY 838
Cdd:cd05601   155 D-----KTVTSKMPVgtpDYIAPEVLTSMNGGSKGtygvecDWWSLGIVAYEML-YGKTPF 209
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
638-839 4.00e-09

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: 58.94  E-value: 4.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEV--CY----GR----LQVPGQRDVPVAIKALKAGYTERQrqdflseaaIMGQFDHPNIIRLEGVV-TRG- 705
Cdd:cd06651    13 KLLGQGAFGRVylCYdvdtGRelaaKQVQFDPESPETSKEVSALECEIQ---------LLKNLQHERIVQYYGCLrDRAe 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  706 RLAMIVTEYMENGSLDAFLRTHdGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALE 785
Cdd:cd06651    84 KTLTIFMEYMPGGSVKDQLKAY-GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQ 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 341940659  786 DDPEAAYTTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAygERPYW 839
Cdd:cd06651   163 TICMSGTGIRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLT--EKPPW 214
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
640-864 4.06e-09

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: 58.89  E-value: 4.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQRDVpvAIKALKAGYTERQRQ-DFLSEAAIMGQ---FDHPNIIRLEGVVTRGRL-----AMI 710
Cdd:cd07862     9 IGEGAYGKVFKARDLKNGGRFV--ALKRVRVQTGEEGMPlSTIREVAVLRHletFEHPNVVRLFDVCTVSRTdretkLTL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  711 VTEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALeddpEA 790
Cdd:cd07862    87 VFEHVDQDLTTYLDKVPEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLARIY----SF 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 341940659  791 AYTTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVlaYGERPYWNmTNQDV--ISSVEEGYRLPAPMGCPR 864
Cdd:cd07862   163 QMALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEM--FRRKPLFR-GSSDVdqLGKILDVIGLPGEEDWPR 235
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
439-516 4.42e-09

Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple acid phosphatase proteins.


Pssm-ID: 465220 [Multi-domain]  Cd Length: 93  Bit Score: 54.34  E-value: 4.42e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659   439 PSQVVVIRQERAgqTSVSLLWQEPEQPNGIILEYEIKYYEKDK----EMQSYSTLKAVT---TRATVSGLKPGTRYVFQV 511
Cdd:pfam16656    1 PEQVHLSLTGDS--TSMTVSWVTPSAVTSPVVQYGTSSSALTStataTSSTYTTGDGGTgyiHRATLTGLEPGTTYYYRV 78

                   ....*
gi 341940659   512 RARTS 516
Cdd:pfam16656   79 GDDNG 83
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
629-839 4.42e-09

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: 59.63  E-value: 4.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  629 IEASRIHIEKIIGSGESGEVCYGRLQvpGQRDVpVAIKALkAGYTERQRQD---FLSEAAIMGQFDHPNIIRLEGVVTRG 705
Cdd:cd05622    70 MKAEDYEVVKVIGRGAFGEVQLVRHK--STRKV-YAMKLL-SKFEMIKRSDsafFWEERDIMAFANSPWVVQLFYAFQDD 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  706 RLAMIVTEYMENGSLDAFLRTHD-----GQFTIVQLVGMLRGVGAgmrylsdLGYIHRDLAARNVLVDGRLVCKVSDFGL 780
Cdd:cd05622   146 RYLYMVMEYMPGGDLVNLMSNYDvpekwARFYTAEVVLALDAIHS-------MGFIHRDVKPDNMLLDKSGHLKLADFGT 218
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341940659  781 SRALEDDPEAAYTTAGGKiPiRWTAPEAIAFRT----FSSASDVWSFGVVMWEVLAyGERPYW 839
Cdd:cd05622   219 CMKMNKEGMVRCDTAVGT-P-DYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLV-GDTPFY 278
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
664-829 4.78e-09

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: 58.53  E-value: 4.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  664 AIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSL-DAFlrtHDGQF-TIVQLVGMLR 741
Cdd:cd14046    35 AIKKIKLRSESKNNSRILREVMLLSRLNHQHVVRYYQAWIERANLYIQMEYCEKSTLrDLI---DSGLFqDTDRLWRLFR 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  742 GVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYTTAGGKIPIR---------------WTAP 806
Cdd:cd14046   112 QILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLATSNKLNVELATQDINKSTSAAlgssgdltgnvgtalYVAP 191
                         170       180
                  ....*....|....*....|....*
gi 341940659  807 E--AIAFRTFSSASDVWSFGVVMWE 829
Cdd:cd14046   192 EvqSGTKSTYNEKVDMYSLGIIFFE 216
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
640-831 5.21e-09

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: 58.27  E-value: 5.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYTERQRqdflsEAAIMGQFDHPNIIRLEG-----------------VV 702
Cdd:cd14047    14 IGSGGFGQVFKAKHRIDGKT---YAIKRVKLNNEKAER-----EVKALAKLDHPNIVRYNGcwdgfdydpetsssnssRS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  703 TRGRLaMIVTEYMENGSLDAFLRTHDGQFTI-VQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLS 781
Cdd:cd14047    86 KTKCL-FIQMEFCEKGTLESWIEKRNGEKLDkVLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVKIGDFGLV 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 341940659  782 RALEDDPEaaytTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVL 831
Cdd:cd14047   165 TSLKNDGK----RTKSKGTLSYMSPEQISSQDYGKEVDIYALGLILFELL 210
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
636-837 5.39e-09

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK5 is unusual in that it is regulated by non-cyclin proteins, p35 and p39. It is highly expressed in the nervous system and is critical in normal neural development and function. It plays a role in neuronal migration and differentiation, and is also important in synaptic plasticity and learning. CDK5 also participates in protecting against cell death and promoting angiogenesis. Impaired CDK5 activity is implicated in Alzheimer's disease, amyotrophic lateral sclerosis, Parkinson's disease, Huntington's disease and acute neuronal injury. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 58.60  E-value: 5.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIiGSGESGEVCYGRLQVPGQrdvpvaIKALKagyteRQRQD---------FLSEAAIMGQFDHPNIIRLEGVVTRGR 706
Cdd:cd07839     5 LEKI-GEGTYGTVFKAKNRETHE------IVALK-----RVRLDdddegvpssALREICLLKELKHKNIVRLYDVLHSDK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  707 LAMIVTEYMENgSLDAFLRTHDGQF--TIVQ--LVGMLRGvgagMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSR 782
Cdd:cd07839    73 KLTLVFEYCDQ-DLKKYFDSCNGDIdpEIVKsfMFQLLKG----LAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLAR 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 341940659  783 ALeddpeaayttaggKIPIR---------WTAPEAIAF--RTFSSASDVWSFGVVMWEvLAYGERP 837
Cdd:cd07839   148 AF-------------GIPVRcysaevvtlWYRPPDVLFgaKLYSTSIDMWSAGCIFAE-LANAGRP 199
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
640-841 5.55e-09

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: 58.52  E-value: 5.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYTErqrqDF---LSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYME 716
Cdd:cd06645    19 IGSGTYGDVYKARNVNTGEL---AAIKVIKLEPGE----DFavvQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICMEFCG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  717 NGSLDAFLRThDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSraleddPEAAYTTAG 796
Cdd:cd06645    92 GGSLQDIYHV-TGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVS------AQITATIAK 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 341940659  797 GKIPI---RWTAPEAIAFRT---FSSASDVWSFGVVMWEvLAYGERPYWNM 841
Cdd:cd06645   165 RKSFIgtpYWMAPEVAAVERkggYNQLCDIWAVGITAIE-LAELQPPMFDL 214
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
639-882 5.93e-09

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: 58.22  E-value: 5.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  639 IIGSGESGEVCYGrLQVPGQRdvpVAIK--ALKAGY---TERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTE 713
Cdd:cd06631     8 VLGKGAYGTVYCG-LTSTGQL---IAVKqvELDTSDkekAEKEYEKLQEEVDLLKTLKHVNIVGYLGTCLEDNVVSIFME 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  714 YMENGSLDAFLRTHdGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALeddpeAAYT 793
Cdd:cd06631    84 FVPGGSIASILARF-GALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAKRL-----CINL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  794 TAGGKIPI--------RWTAPEAIAFRTFSSASDVWSFGVVMWEvLAYGERPYWNMTNQDVISSVEEGYRLPAPMG---C 862
Cdd:cd06631   158 SSGSQSQLlksmrgtpYWMAPEVINETGHGRKSDIWSIGCTVFE-MATGKPPWADMNPMAAIFAIGSGRKPVPRLPdkfS 236
                         250       260
                  ....*....|....*....|
gi 341940659  863 PRAlHQLMLDCWHKDRAQRP 882
Cdd:cd06631   237 PEA-RDFVHACLTRDQDERP 255
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
692-840 6.04e-09

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: 58.39  E-value: 6.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  692 HPNIIRLEGVVTRGRLAMIVTEYMENGSLDAFLrTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRL 771
Cdd:cd14182    69 HPNIIQLKDTYETNTFFFLVFDLMKKGELFDYL-TEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDM 147
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 341940659  772 VCKVSDFGLSRALeDDPEAAYTTAGGKipiRWTAPEAIA------FRTFSSASDVWSFGVVMWEVLAyGERPYWN 840
Cdd:cd14182   148 NIKLTDFGFSCQL-DPGEKLREVCGTP---GYLAPEIIEcsmddnHPGYGKEVDMWSTGVIMYTLLA-GSPPFWH 217
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
638-834 6.06e-09

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: 59.29  E-value: 6.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVPGQRdvpVAIKALKAGY-TERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRL------AMI 710
Cdd:cd07875    30 KPIGSGAQGIVCAAYDAILERN---VAIKKLSRPFqNQTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQKSleefqdVYI 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  711 VTEYMENGSLDAFLRTHDGQFTIVQLVGMLrgvgAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRAleddPEA 790
Cdd:cd07875   107 VMELMDANLCQVIQMELDHERMSYLLYQML----CGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLART----AGT 178
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 341940659  791 AYTTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYG 834
Cdd:cd07875   179 SFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGG 222
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
746-852 6.19e-09

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: 58.77  E-value: 6.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  746 GMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRalEDDPEAAYTTAGGKIPiRWTAPEAIAFRTFSSASDVWSFGV 825
Cdd:cd05570   108 ALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCK--EGIWGGNTTSTFCGTP-DYIAPEILREQDYGFSVDWWALGV 184
                          90       100
                  ....*....|....*....|....*..
gi 341940659  826 VMWEVLAyGERPYWNMTNQDVISSVEE 852
Cdd:cd05570   185 LLYEMLA-GQSPFEGDDEDELFEAILN 210
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
746-831 6.97e-09

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: 58.99  E-value: 6.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  746 GMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDpEAAYTTAgGKIPIRWTAPEAI-AFRTFSSASDVWSFG 824
Cdd:cd07853   115 GLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVEEPD-ESKHMTQ-EVVTQYYRAPEILmGSRHYTSAVDIWSVG 192

                  ....*..
gi 341940659  825 VVMWEVL 831
Cdd:cd07853   193 CIFAELL 199
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
703-838 7.14e-09

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: 58.56  E-value: 7.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  703 TRGRLaMIVTEYMENGSLdAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSR 782
Cdd:cd05587    68 TMDRL-YFVMEYVNGGDL-MYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCK 145
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 341940659  783 ALEDDPEAAYTTAGGKIPIrwtAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPY 838
Cdd:cd05587   146 EGIFGGKTTRTFCGTPDYI---APEIIAYQPYGKSVDWWAYGVLLYEMLA-GQPPF 197
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
328-417 7.30e-09

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 53.39  E-value: 7.30e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659    328 PSAPVNL-ISSVNGTSVTLEWAPPLDPGGRSDITYNAVCRRcpwalshceacGSGTRFVPQQTSLAQASLLVANLLAHMN 406
Cdd:smart00060    1 PSPPSNLrVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYR-----------EEGSEWKEVNVTPSSTSYTLTGLKPGTE 69
                            90
                    ....*....|.
gi 341940659    407 YSFWIEAVNGV 417
Cdd:smart00060   70 YEFRVRAVNGA 80
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
934-989 7.47e-09

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 52.63  E-value: 7.47e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 341940659  934 VGDWLDSIRMGRYRDHFAAGgYSSLGMVLRMNAQDVRALGITLMGHQKKILGSIQT 989
Cdd:cd09487     2 VAEWLESLGLEQYADLFRKN-EIDGDALLLLTDEDLKELGITSPGHRKKILRAIQR 56
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
680-841 9.23e-09

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: 58.08  E-value: 9.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  680 FLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLDAFLRTH--DGqFTIVQLVGMLRGVGAGMRYLSDLGYIH 757
Cdd:cd08216    46 LQQEILTSRQLQHPNILPYVTSFVVDNDLYVVTPLMAYGSCRDLLKTHfpEG-LPELAIAFILRDVLNALEYIHSKGYIH 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  758 RDLAARNVLVDGRlvCKVSDFGLSRALEDDPEAAYTTAGGKIPIR------WTAPEAIA--FRTFSSASDVWSFGVVMWE 829
Cdd:cd08216   125 RSVKASHILISGD--GKVVLSGLRYAYSMVKHGKRQRVVHDFPKSseknlpWLSPEVLQqnLLGYNEKSDIYSVGITACE 202
                         170
                  ....*....|..
gi 341940659  830 vLAYGERPYWNM 841
Cdd:cd08216   203 -LANGVVPFSDM 213
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
677-837 1.01e-08

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: 58.14  E-value: 1.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  677 RQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLDAFLRthDGQFTIVQLVGMLR-GVGAGMRYLSDLGY 755
Cdd:cd06649    47 RNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLK--EAKRIPEEILGKVSiAVLRGLAYLREKHQ 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  756 I-HRDLAARNVLVDGRLVCKVSDFGLSRALEDdpEAAYTTAGGKipiRWTAPEAIAFRTFSSASDVWSFGVVMWEvLAYG 834
Cdd:cd06649   125 ImHRDVKPSNILVNSRGEIKLCDFGVSGQLID--SMANSFVGTR---SYMSPERLQGTHYSVQSDIWSMGLSLVE-LAIG 198

                  ...
gi 341940659  835 ERP 837
Cdd:cd06649   199 RYP 201
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
673-843 1.04e-08

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: 57.75  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  673 TERQRQDFLSEAAIMGQFDHPNIIRL----EGVVTRGRLAMIVTEYMENGSLDAFLRthdgQFTIVQ---LVGMLRGVGA 745
Cdd:cd14030    64 SKSERQRFKEEAGMLKGLQHPNIVRFydswESTVKGKKCIVLVTELMTSGTLKTYLK----RFKVMKikvLRSWCRQILK 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  746 GMRYLSDLG--YIHRDLAARNVLVDGRL-VCKVSDFGLSRAleddPEAAYTTAGGKIPiRWTAPEAIAfRTFSSASDVWS 822
Cdd:cd14030   140 GLQFLHTRTppIIHRDLKCDNIFITGPTgSVKIGDLGLATL----KRASFAKSVIGTP-EFMAPEMYE-EKYDESVDVYA 213
                         170       180
                  ....*....|....*....|.
gi 341940659  823 FGVVMWEvLAYGERPYWNMTN 843
Cdd:cd14030   214 FGMCMLE-MATSEYPYSECQN 233
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
638-838 1.19e-08

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: 57.70  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRlQVPGQRDVPV-AIKALKAGY------------TERQRQDFLSEAaimgqfdhPNIIRLE-GVVT 703
Cdd:cd05613     6 KVLGTGAYGKVFLVR-KVSGHDAGKLyAMKVLKKATivqkaktaehtrTERQVLEHIRQS--------PFLVTLHyAFQT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  704 RGRLAMIVtEYMENGSLDAFLRTHDgQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRA 783
Cdd:cd05613    77 DTKLHLIL-DYINGGELFTHLSQRE-RFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKE 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 341940659  784 -LEDDPEAAYTTAGgkiPIRWTAPEAI--AFRTFSSASDVWSFGVVMWEVLAyGERPY 838
Cdd:cd05613   155 fLLDENERAYSFCG---TIEYMAPEIVrgGDSGHDKAVDWWSLGVLMYELLT-GASPF 208
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
635-833 1.24e-08

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: 57.68  E-value: 1.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  635 HIEKIIGSGESGEVcYGRLQVPGQRDVPVAIKALKagyTERQRQDFLSEAAI-----MGQFDHPNIIRLEGVV---TRGR 706
Cdd:cd07842     3 EIEGCIGRGTYGRV-YKAKRKNGKDGKEYAIKKFK---GDKEQYTGISQSACreialLRELKHENVVSLVEVFlehADKS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  707 LAMIVtEYMEN--GSLDAFLRTHDGqftiVQL-VGMLRG----VGAGMRYLSDLGYIHRDLAARNVLVDG----RLVCKV 775
Cdd:cd07842    79 VYLLF-DYAEHdlWQIIKFHRQAKR----VSIpPSMVKSllwqILNGIHYLHSNWVLHRDLKPANILVMGegpeRGVVKI 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 341940659  776 SDFGLSRALEDDPEAAYTTAGGKIPIRWTAPEAI-AFRTFSSASDVWSFGVVMWEVLAY 833
Cdd:cd07842   154 GDLGLARLFNAPLKPLADLDPVVVTIWYRAPELLlGARHYTKAIDIWAIGCIFAELLTL 212
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
638-881 1.48e-08

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: 57.73  E-value: 1.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVPGQRdvpVAIKALKAGY--TERQRQDFLSEAAIMGQFDHPNIIRLE-GVVTRGRLAMiVTEY 714
Cdd:cd05594    31 KLLGKGTFGKVILVKEKATGRY---YAMKILKKEVivAKDEVAHTLTENRVLQNSRHPFLTALKySFQTHDRLCF-VMEY 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  715 MENGSLdAFLRTHDGQFTivqlvgMLRGVGAGMRYLSDLGYIH-------RDLAARNVLVDGRLVCKVSDFGLSRALEDD 787
Cdd:cd05594   107 ANGGEL-FFHLSRERVFS------EDRARFYGAEIVSALDYLHseknvvyRDLKLENLMLDKDGHIKITDFGLCKEGIKD 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  788 PEAAYTTAGGKipiRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWNMTNQDVISSV-EEGYRLPAPMGcPRAl 866
Cdd:cd05594   180 GATMKTFCGTP---EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELIlMEEIRFPRTLS-PEA- 253
                         250
                  ....*....|....*
gi 341940659  867 HQLMLDCWHKDRAQR 881
Cdd:cd05594   254 KSLLSGLLKKDPKQR 268
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
639-857 1.69e-08

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: 57.31  E-value: 1.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  639 IIGSGESGEVCYGRLQVPGQRdvpVAIKALKAG-YTERQRQDFL-SEAAIM---GQFDHPNIIRLEGVVTRGRLAMIVTE 713
Cdd:cd05589     6 VLGRGHFGKVLLAEYKPTGEL---FAIKALKKGdIIARDEVESLmCEKRIFetvNSARHPFLVNLFACFQTPEHVCFVME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  714 YMENGslDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRalEDDPEAAYT 793
Cdd:cd05589    83 YAAGG--DLMMHIHEDVFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK--EGMGFGDRT 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 341940659  794 TAGGKIPiRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWNMTNQDVISS-VEEGYRLP 857
Cdd:cd05589   159 STFCGTP-EFLAPEVLTDTSYTRAVDWWGLGVLIYEMLV-GESPFPGDDEEEVFDSiVNDEVRYP 221
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
635-852 1.90e-08

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: 56.51  E-value: 1.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  635 HIEKIIGSGESGEV--CYGRLQvpgqrDVPVAIKALKaGYTERQRQDfLSEAAIM------GQFDHPNIIRLEGVVTRGR 706
Cdd:cd14133     2 EVLEVLGKGTFGQVvkCYDLLT-----GEEVALKIIK-NNKDYLDQS-LDEIRLLellnkkDKADKYHIVRLKDVFYFKN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  707 LAMIVTEYMENgSLDAFLRTHDGQ-FTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDG--RLVCKVSDFGLSRA 783
Cdd:cd14133    75 HLCIVFELLSQ-NLYEFLKQNKFQyLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASysRCQIKIIDFGSSCF 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  784 LEDdpeAAYTTaggkIPIR-WTAPEAIAFRTFSSASDVWSFGVVMWEvLAYGERPYWNMTNQDVISSVEE 852
Cdd:cd14133   154 LTQ---RLYSY----IQSRyYRAPEVILGLPYDEKIDMWSLGCILAE-LYTGEPLFPGASEVDQLARIIG 215
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
747-838 2.10e-08

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: 57.24  E-value: 2.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  747 MRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRA-LEDDPEAAYTTAGgkiPIRWTAPEAIAFRT-FSSASDVWSFG 824
Cdd:cd05614   118 LEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKEfLTEEKERTYSFCG---TIEYMAPEIIRGKSgHGKAVDWWSLG 194
                          90
                  ....*....|....
gi 341940659  825 VVMWEVLAyGERPY 838
Cdd:cd05614   195 ILMFELLT-GASPF 207
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
673-843 2.19e-08

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: 56.55  E-value: 2.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  673 TERQRqdFLSEAAIMGQFDHPNIIRLEG---VVTRGRLAMI-VTEYMENGSLDAFLRTHDgQFTIVQLVGMLRGVGAGMR 748
Cdd:cd14033    42 GERQR--FSEEVEMLKGLQHPNIVRFYDswkSTVRGHKCIIlVTELMTSGTLKTYLKRFR-EMKLKLLQRWSRQILKGLH 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  749 YLSDLG--YIHRDLAARNVLVDGRL-VCKVSDFGLSRAleddPEAAYTTAGGKIPiRWTAPEAIAfRTFSSASDVWSFGV 825
Cdd:cd14033   119 FLHSRCppILHRDLKCDNIFITGPTgSVKIGDLGLATL----KRASFAKSVIGTP-EFMAPEMYE-EKYDEAVDVYAFGM 192
                         170
                  ....*....|....*...
gi 341940659  826 VMWEvLAYGERPYWNMTN 843
Cdd:cd14033   193 CILE-MATSEYPYSECQN 209
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
636-840 2.20e-08

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: 56.76  E-value: 2.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  636 IEKIIGSGESgEVCYGRLQVPGQRdvPVAIKALKAGYterQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYM 715
Cdd:cd14085     7 IESELGRGAT-SVVYRCRQKGTQK--PYAVKKLKKTV---DKKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLELV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  716 ENGSLdaFLR-THDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLV-----DGRLvcKVSDFGLSRALEDDpe 789
Cdd:cd14085    81 TGGEL--FDRiVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYatpapDAPL--KIADFGLSKIVDQQ-- 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 341940659  790 AAYTTAGGKiPiRWTAPEAIAFRTFSSASDVWSFGVVMWeVLAYGERPYWN 840
Cdd:cd14085   155 VTMKTVCGT-P-GYCAPEILRGCAYGPEVDMWSVGVITY-ILLCGFEPFYD 202
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
658-838 2.39e-08

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: 56.51  E-value: 2.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  658 QRDVPVAIKALKAGYTERQR--QDFLSEAAIMGQFDHPNIIRLEGVV---TRGRLAMiVTEYMENGSL-----DAFLRTH 727
Cdd:cd14199    48 RRPPPRGARAAPEGCTQPRGpiERVYQEIAILKKLDHPNVVKLVEVLddpSEDHLYM-VFELVKQGPVmevptLKPLSED 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  728 DGQFTIVQLVgmlrgvgAGMRYLSDLGYIHRDLAARNVLV--DGRLvcKVSDFGLSRALEDDPEAAYTTAGGKIpirWTA 805
Cdd:cd14199   127 QARFYFQDLI-------KGIEYLHYQKIIHRDVKPSNLLVgeDGHI--KIADFGVSNEFEGSDALLTNTVGTPA---FMA 194
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 341940659  806 PEAIA--FRTFS-SASDVWSFGVVMWeVLAYGERPY 838
Cdd:cd14199   195 PETLSetRKIFSgKALDVWAMGVTLY-CFVFGQCPF 229
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
638-850 2.82e-08

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: 56.99  E-value: 2.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVcygRLQVPGQRDVPVAIKAL-KAGYTERQRQDFL-SEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYM 715
Cdd:cd05627     8 KVIGRGAFGEV---RLVQKKDTGHIYAMKILrKADMLEKEQVAHIrAERDILVEADGAWVVKMFYSFQDKRNLYLIMEFL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  716 ENGSLDAFLRTHDG------QFTIVQLVgmlrgvgAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLS-------- 781
Cdd:cd05627    85 PGGDMMTLLMKKDTlseeatQFYIAETV-------LAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCtglkkahr 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  782 ----RALEDDP-----------------------EAAYTTAGGKipiRWTAPEAIAFRTFSSASDVWSFGVVMWEVLaYG 834
Cdd:cd05627   158 tefyRNLTHNPpsdfsfqnmnskrkaetwkknrrQLAYSTVGTP---DYIAPEVFMQTGYNKLCDWWSLGVIMYEML-IG 233
                         250
                  ....*....|....*.
gi 341940659  835 ERPYWNMTNQDVISSV 850
Cdd:cd05627   234 YPPFCSETPQETYRKV 249
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
638-840 2.96e-08

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: 56.51  E-value: 2.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVPGQRdvpVAIKAL--KAGYTERQRQDFLSEA-AIMGQFDHPNIIRLEGVVTRGRLAMIVTEY 714
Cdd:cd05604     2 KVIGKGSFGKVLLAKRKRDGKY---YAVKVLqkKVILNRKEQKHIMAERnVLLKNVKHPFLVGLHYSFQTTDKLYFVLDF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  715 MENGSLdAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRalEDDPEAAYTT 794
Cdd:cd05604    79 VNGGEL-FFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCK--EGISNSDTTT 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 341940659  795 AGGKIPiRWTAPEAIAFRTFSSASDVWSFGVVMWEVLaYGERPYWN 840
Cdd:cd05604   156 TFCGTP-EYLAPEVIRKQPYDNTVDWWCLGSVLYEML-YGLPPFYC 199
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
628-839 2.99e-08

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: 56.93  E-value: 2.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  628 EIEASRIHIEKIIGSGESGEVCYGRLQVPGQrdvpVAIKALKAGYTERQRQD---FLSEAAIMGQFDHPNIIRLEGVVTR 704
Cdd:cd05621    48 QMKAEDYDVVKVIGRGAFGEVQLVRHKASQK----VYAMKLLSKFEMIKRSDsafFWEERDIMAFANSPWVVQLFCAFQD 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  705 GRLAMIVTEYMENGSLDAFLRTHD-----GQFTIVQLVGMLRGVGAgmrylsdLGYIHRDLAARNVLVDGRLVCKVSDFG 779
Cdd:cd05621   124 DKYLYMVMEYMPGGDLVNLMSNYDvpekwAKFYTAEVVLALDAIHS-------MGLIHRDVKPDNMLLDKYGHLKLADFG 196
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 341940659  780 LSRALEDDPEAAYTTAGGKiPiRWTAPEAIAFRT----FSSASDVWSFGVVMWEVLAyGERPYW 839
Cdd:cd05621   197 TCMKMDETGMVHCDTAVGT-P-DYISPEVLKSQGgdgyYGRECDWWSVGVFLFEMLV-GDTPFY 257
STKc_TTBK2 cd14129
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze ...
633-854 3.11e-08

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: 55.83  E-value: 3.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  633 RIHIEKIIGSGESGEVcYGRLQVPGQRDVpvaikALKAGYTERQRQDFLSEAAIMGQF---DHpnIIRLEGVVTRGRLAM 709
Cdd:cd14129     1 RWKVLRKIGGGGFGEI-YDALDLLTRENV-----ALKVESAQQPKQVLKMEVAVLKKLqgkDH--VCRFIGCGRNDRFNY 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  710 IVTEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVdGRL-----VCKVSDFGLSRAL 784
Cdd:cd14129    73 VVMQLQGRNLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAM-GRFpstcrKCYMLDFGLARQF 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341940659  785 ED---DPEAAYTTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWNMTNQDVISSVEEGY 854
Cdd:cd14129   152 TNscgDVRPPRAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVV-GQLPWRKIKDKEQVGSIKERY 223
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
638-840 3.16e-08

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: 56.60  E-value: 3.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVPGQRdvpVAIKALK---------AGYTerqrqdfLSEAAIMGQFDHPNIIRLE-GVVTRGRL 707
Cdd:cd05571     1 KVLGKGTFGKVILCREKATGEL---YAIKILKkeviiakdeVAHT-------LTENRVLQNTRHPFLTSLKySFQTNDRL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  708 AMiVTEYMENGSLDAFLRtHDGQFTIVQLvgmlRGVGA----GMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRa 783
Cdd:cd05571    71 CF-VMEYVNGGELFFHLS-RERVFSEDRT----RFYGAeivlALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCK- 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 341940659  784 lEDDPEAAYTTAGGKIPiRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWN 840
Cdd:cd05571   144 -EEISYGATTKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYN 197
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
624-839 3.19e-08

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: 56.62  E-value: 3.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  624 SFTREIEASRIHIE-----KIIGSGESGEVCYGRLQVPGQrdvPVAIKALKAgyTER-QRQD---FLSEAAIMGQFDHPN 694
Cdd:cd05596    13 KPVNEITKLRMNAEdfdviKVIGRGAFGEVQLVRHKSTKK---VYAMKLLSK--FEMiKRSDsafFWEERDIMAHANSEW 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  695 IIRLEGVVTRGRLAMIVTEYMENGSLDAFLRTHD-----GQFTIVQLVGMLRGVgagmrylSDLGYIHRDLAARNVLVDG 769
Cdd:cd05596    88 IVQLHYAFQDDKYLYMVMDYMPGGDLVNLMSNYDvpekwARFYTAEVVLALDAI-------HSMGFVHRDVKPDNMLLDA 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 341940659  770 RLVCKVSDFGLSRALEDDPEAAYTTAGGKiPiRWTAPEAI----AFRTFSSASDVWSFGVVMWEVLaYGERPYW 839
Cdd:cd05596   161 SGHLKLADFGTCMKMDKDGLVRSDTAVGT-P-DYISPEVLksqgGDGVYGRECDWWSVGVFLYEML-VGDTPFY 231
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
640-912 3.67e-08

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: 56.10  E-value: 3.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEvCYGRLQVPGQRDVPVAIKALKA---GYTERQRQDFLSEAAIMGQFD-HPNIIRLEGVVTRGRLAMIVT--- 712
Cdd:cd14020     8 LGQGSSAS-VYRVSSGRGADQPTSALKEFQLdhqGSQESGDYGFAKERAALEQLQgHRNIVTLYGVFTNHYSANVPSrcl 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  713 --EYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVC-KVSDFGLSRAlEDDPE 789
Cdd:cd14020    87 llELLDVSVSELLLRSSNQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAEDECfKLIDFGLSFK-EGNQD 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  790 AAYTTAGGkipirWTAPEAIAFRTF-----------SSASDVWSFGVVMWEVlaygerpYWNMTNQDVISSVEegYRLPA 858
Cdd:cd14020   166 VKYIQTDG-----YRAPEAELQNCLaqaglqsetecTSAVDLWSLGIVLLEM-------FSGMKLKHTVRSQE--WKDNS 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 341940659  859 PMGCPRALHQLMLDCwhkdrAQRPRFaHVVSVLDALVHSPESLRATATVSRCPP 912
Cdd:cd14020   232 SAIIDHIFASNAVVN-----PAIPAY-HLRDLIKSMLHNDPGKRATAEAALCSP 279
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
677-838 4.97e-08

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: 55.33  E-value: 4.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  677 RQDFLSEAAIMG-QFDHPNIIRLEGVVTRGRLAMIVTEYMENGSL-DAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLG 754
Cdd:cd14197    52 RMEIIHEIAVLElAQANPWVINLHEVYETASEMILVLEYAAGGEIfNQCVADREEAFKEKDVKRLMKQILEGVSFLHNNN 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  755 YIHRDLAARNVLVDGRLV---CKVSDFGLSRALEDDPEAAYTTAGGKipirWTAPEAIAFRTFSSASDVWSFGVVMWeVL 831
Cdd:cd14197   132 VVHLDLKPQNILLTSESPlgdIKIVDFGLSRILKNSEELREIMGTPE----YVAPEILSYEPISTATDMWSIGVLAY-VM 206

                  ....*..
gi 341940659  832 AYGERPY 838
Cdd:cd14197   207 LTGISPF 213
SAM_AIDA1AB-like_repeat2 cd09500
SAM domain of AIDA1AB-like proteins, repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
928-987 5.75e-08

SAM domain of AIDA1AB-like proteins, repeat 2; SAM (sterile alpha motif) domain repeat 2 of AIDA1AB-like proteins is a protein-protein interaction domain. AIDA1AB-like proteins have two tandem SAM domains. They may form an intramolecular head-to-tail homodimer. One of two basic motifs of the nuclear localization signal (NLS) is located within helix 5 of the SAM2 (motif HKRK). This signal plays a role in decoupling of SAM2 from SAM1, thus facilitating translocation of this type proteins into the nucleus. SAM domains of the AIDA1AB-like subfamily can directly bind ubiquitin and participate in regulating the degradation of ubiquitinated EphA receptors, particularly EPH-A8 receptor. Additionally AIDA1AB-like proteins may participate in the regulation of nucleoplasmic coilin protein interactions.


Pssm-ID: 188899  Cd Length: 65  Bit Score: 50.38  E-value: 5.75e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341940659  928 GNGDLTVGDWLDSIRMGRYRDHFAAGGYSSLGMVLR---MNAQDVraLGITLMGHQKKILGSI 987
Cdd:cd09500     2 GNSPASVSEWLDSIGLGDYIETFLKHGYTSMERVKRiweVELTNV--LEINKLGHRKRILASL 62
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
693-840 6.93e-08

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: 55.43  E-value: 6.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  693 PNIIRL----EGVVTRGRLAMIVTEYMENGSLDAFLRTH-DGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLV 767
Cdd:cd14170    55 PHIVRIvdvyENLYAGRKCLLIVMECLDGGELFSRIQDRgDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLY 134
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 341940659  768 DGR---LVCKVSDFGLSRALEDDPEAA---YTTaggkipiRWTAPEAIAFRTFSSASDVWSFGVVMWeVLAYGERPYWN 840
Cdd:cd14170   135 TSKrpnAILKLTDFGFAKETTSHNSLTtpcYTP-------YYVAPEVLGPEKYDKSCDMWSLGVIMY-ILLCGYPPFYS 205
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
623-861 7.15e-08

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: 55.79  E-value: 7.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  623 RSFTREIEASRIH-----IEKIIGSGESGEVCYGRLQvpgQRDVPVAIKALKAGYTERQRQD--FLSEAAIMGQFDHPNI 695
Cdd:cd05624    58 KPFTQLVKEMQLHrddfeIIKVIGRGAFGEVAVVKMK---NTERIYAMKILNKWEMLKRAETacFREERNVLVNGDCQWI 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  696 IRLEGVVTRGRLAMIVTEYMENGSLDAFLRTHD-------GQFTIVQLVgmlrgvgAGMRYLSDLGYIHRDLAARNVLVD 768
Cdd:cd05624   135 TTLHYAFQDENYLYLVMDYYVGGDLLTLLSKFEdklpedmARFYIGEMV-------LAIHSIHQLHYVHRDIKPDNVLLD 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  769 GRLVCKVSDFGLSRALEDDPEAAYTTAGGKiPiRWTAPEAI-----AFRTFSSASDVWSFGVVMWEVLaYGERPYWNMTN 843
Cdd:cd05624   208 MNGHIRLADFGSCLKMNDDGTVQSSVAVGT-P-DYISPEILqamedGMGKYGPECDWWSLGVCMYEML-YGETPFYAESL 284
                         250       260
                  ....*....|....*....|.
gi 341940659  844 QDVISSV---EEGYRLPAPMG 861
Cdd:cd05624   285 VETYGKImnhEERFQFPSHVT 305
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
631-881 7.74e-08

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1b, also called Activin receptor-Like Kinase 6 (ALK6), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Mutations in BMPR1b that led to inhibition of chondrogenesis can cause Brachydactyly (BD) type A2, a dominant hand malformation characterized by shortening and lateral deviation of the index fingers. A point mutation in the BMPR1b kinase domain is also associated with the Booroola phenotype, characterized by precocious differentiation of ovarian follicles. BMPR1b belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, 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, like BMPR1b, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, 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. The BMPR1b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271121 [Multi-domain]  Cd Length: 305  Bit Score: 55.06  E-value: 7.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  631 ASRIHIEKIIGSGESGEVCYGRLqvpgqRDVPVAIKALkagYTERQ----RQDFLSEAAIMgqfDHPNIIRLEGVVTRGR 706
Cdd:cd14219     4 AKQIQMVKQIGKGRYGEVWMGKW-----RGEKVAVKVF---FTTEEaswfRETEIYQTVLM---RHENILGFIAADIKGT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  707 LA----MIVTEYMENGSLDAFLRThdgqfTIVQLVGMLRGVGAGMRYLSDL-----------GYIHRDLAARNVLVDGRL 771
Cdd:cd14219    73 GSwtqlYLITDYHENGSLYDYLKS-----TTLDTKAMLKLAYSSVSGLCHLhteifstqgkpAIAHRDLKSKNILVKKNG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  772 VCKVSDFGLS-RALEDDPEAAY---TTAGGKipiRWTAPEAI-------AFRTFSSAsDVWSFGVVMWEVlaygerpywn 840
Cdd:cd14219   148 TCCIADLGLAvKFISDTNEVDIppnTRVGTK---RYMPPEVLdeslnrnHFQSYIMA-DMYSFGLILWEV---------- 213
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 341940659  841 mTNQDVISSVEEGYRLP-------------------------------APMGCPRALHQLMLDCWHKDRAQR 881
Cdd:cd14219   214 -ARRCVSGGIVEEYQLPyhdlvpsdpsyedmreivcikrlrpsfpnrwSSDECLRQMGKLMTECWAHNPASR 284
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
638-840 7.93e-08

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: 54.91  E-value: 7.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVPGQRDVPVAI--KALKAGYTERQRqdfLSEAAIMGQFDHPNIIRLE-GVVTRGRLAMIVTeY 714
Cdd:cd05607     8 RVLGKGGFGEVCAVQVKNTGQMYACKKLdkKRLKKKSGEKMA---LLEKEILEKVNSPFIVSLAyAFETKTHLCLVMS-L 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  715 MENGSLDaFLRTHDGQ--FTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALeddPEAAY 792
Cdd:cd05607    84 MNGGDLK-YHIYNVGErgIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEV---KEGKP 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 341940659  793 TT--AGGKipiRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPYWN 840
Cdd:cd05607   160 ITqrAGTN---GYMAPEILKEESYSYPVDWFAMGCSIYEMVA-GRTPFRD 205
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
638-838 1.01e-07

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: 54.64  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVPGQRdvpVAIKALKAGYTERQRQD--FLSEAAIMGQFDHPNIIRLE-GVVTRGRLAMIVTeY 714
Cdd:cd05630     6 RVLGKGGFGEVCACQVRATGKM---YACKKLEKKRIKKRKGEamALNEKQILEKVNSRFVVSLAyAYETKDALCLVLT-L 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  715 MENGSLDaFLRTHDGQ--FTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDpeaay 792
Cdd:cd05630    82 MNGGDLK-FHIYHMGQagFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEG----- 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 341940659  793 TTAGGKI-PIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPY 838
Cdd:cd05630   156 QTIKGRVgTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIA-GQSPF 201
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
677-854 1.06e-07

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: 54.54  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  677 RQDFLSEAAIM-GQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSL-DAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLG 754
Cdd:cd14198    51 RAEILHEIAVLeLAKSNPRVVNLHEVYETTSEIILILEYAAGGEIfNLCVPDLAEMVSENDIIRLIRQILEGVYYLHQNN 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  755 YIHRDLAARNVLVD-----GRLvcKVSDFGLSRALEDDPEAAYTTAGGKipirWTAPEAIAFRTFSSASDVWSFGVVMWe 829
Cdd:cd14198   131 IVHLDLKPQNILLSsiyplGDI--KIVDFGMSRKIGHACELREIMGTPE----YLAPEILNYDPITTATDMWNIGVIAY- 203
                         170       180
                  ....*....|....*....|....*...
gi 341940659  830 VLAYGERPYWNMTNQDV---ISSVEEGY 854
Cdd:cd14198   204 MLLTHESPFVGEDNQETflnISQVNVDY 231
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
690-841 1.14e-07

Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. 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. A mutation which results in a truncation of a C-terminal part of the human STRAD-alpha pseudokinase domain and disrupts its association with LKB1, leads to PMSE (polyhydramnios, megalencephaly, symptomatic epilepsy) syndrome. Several splice variants of STRAD-alpha exist which exhibit different effects on the localization and activation of LKB1. 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. The STRAD alpha 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: 173767 [Multi-domain]  Cd Length: 327  Bit Score: 54.95  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  690 FDHPNIIRLEGVVTRGRLAMIVTEYMENGSLDAFLRTH--DGqFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVL- 766
Cdd:cd08227    56 FNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHfmDG-MSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILi 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  767 -VDGRLVCK--VSDFGL------SRALEDDPEAAYTTaggkipIRWTAPEAIA--FRTFSSASDVWSFGVVMWEvLAYGE 835
Cdd:cd08227   135 sVDGKVYLSglRSNLSMinhgqrLRVVHDFPKYSVKV------LPWLSPEVLQqnLQGYDAKSDIYSVGITACE-LANGH 207

                  ....*.
gi 341940659  836 RPYWNM 841
Cdd:cd08227   208 VPFKDM 213
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
692-832 1.19e-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: 54.66  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  692 HPNIIRLEGVVTRGRLA----MIVTEYMENGSLDAFLRTHDGQFTIVQLVG--MLRGVG------AGMRYLSDLGYIHRD 759
Cdd:cd14141    48 HENILQFIGAEKRGTNLdvdlWLITAFHEKGSLTDYLKANVVSWNELCHIAqtMARGLAylhediPGLKDGHKPAIAHRD 127
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 341940659  760 LAARNVLVDGRLVCKVSDFGLSRALEDDPEAAyTTAGGKIPIRWTAPE----AIAF-RTFSSASDVWSFGVVMWEVLA 832
Cdd:cd14141   128 IKSKNVLLKNNLTACIADFGLALKFEAGKSAG-DTHGQVGTRRYMAPEvlegAINFqRDAFLRIDMYAMGLVLWELAS 204
SAM_caskin1,2_repeat2 cd09498
SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 ...
933-991 1.37e-07

SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 proteins is a protein-protein interaction domain. Caskin has two tandem SAM domains. Caskin protein is known to interact with membrane-associated guanylate kinase CASK, and may play a role in neural development, synaptic protein targeting, and regulation of gene expression.


Pssm-ID: 188897  Cd Length: 71  Bit Score: 49.60  E-value: 1.37e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 341940659  933 TVGDWLDSIRMGRYRDHFAAGGYSSLGMVLRMNAQDVRALGITLMGHQKKILGSIQTMR 991
Cdd:cd09498     9 DLLEWLSLLGLPQYHKVLVENGYDSIDFVTDLTWEDLQDIGITKLGHQKKLMLAIKKLK 67
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
638-838 1.37e-07

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: 54.70  E-value: 1.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  638 KIIGSGESGEVCYGRLQVPGQRdvpVAIKALK-----------AGYTERQrqdFLSEAAImgqfdHPNIIRLEGVVTRGR 706
Cdd:cd05592     1 KVLGKGSFGKVMLAELKGTNQY---FAIKALKkdvvledddveCTMIERR---VLALASQ-----HPFLTHLFCTFQTES 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  707 LAMIVTEYMENGSLdAFLRTHDGQFTIVQLvgmlRGVGA----GMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSR 782
Cdd:cd05592    70 HLFFVMEYLNGGDL-MFHIQQSGRFDEDRA----RFYGAeiicGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCK 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 341940659  783 ALEDDPEAAYTTAGgkIPiRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAyGERPY 838
Cdd:cd05592   145 ENIYGENKASTFCG--TP-DYIAPEILKGQKYNQSVDWWSFGVLLYEMLI-GQSPF 196
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
622-839 1.82e-07

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: 54.64  E-value: 1.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  622 GRSFTREIEASRIHIE-----KIIGSGESGEVCYGRLQvpgQRDVPVAIKALKAGYTERQRQD--FLSEAAIMGQFDHPN 694
Cdd:cd05623    57 AKPFTSKVKQMRLHKEdfeilKVIGRGAFGEVAVVKLK---NADKVFAMKILNKWEMLKRAETacFREERDVLVNGDSQW 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  695 IIRLEGVVTRGRLAMIVTEYMENGSLDAFLRTHD-------GQFTIVQLVGMLRGVgagmrylSDLGYIHRDLAARNVLV 767
Cdd:cd05623   134 ITTLHYAFQDDNNLYLVMDYYVGGDLLTLLSKFEdrlpedmARFYLAEMVLAIDSV-------HQLHYVHRDIKPDNILM 206
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 341940659  768 DGRLVCKVSDFGLSRALEDDPEAAYTTAGGKiPiRWTAPEAIAFR-----TFSSASDVWSFGVVMWEVLaYGERPYW 839
Cdd:cd05623   207 DMNGHIRLADFGSCLKLMEDGTVQSSVAVGT-P-DYISPEILQAMedgkgKYGPECDWWSLGVCMYEML-YGETPFY 280
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
640-831 1.83e-07

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: 54.40  E-value: 1.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  640 IGSGESGEVCYGrlqVPGQRDVPVAIKalKAGYTERQR-QDFLSEAAIMGQFDHPNIIRL--------------EGVVTR 704
Cdd:cd07854    13 LGCGSNGLVFSA---VDSDCDKRVAVK--KIVLTDPQSvKHALREIKIIRRLDHDNIVKVyevlgpsgsdltedVGSLTE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  705 GRLAMIVTEYM--------ENGSLDAflrTHDGQFTiVQLvgmLRGvgagMRYLSDLGYIHRDLAARNVLVDGR-LVCKV 775
Cdd:cd07854    88 LNSVYIVQEYMetdlanvlEQGPLSE---EHARLFM-YQL---LRG----LKYIHSANVLHRDLKPANVFINTEdLVLKI 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 341940659  776 SDFGLSRALedDPE---AAYTTAGgkIPIRW-TAPE-AIAFRTFSSASDVWSFGVVMWEVL 831
Cdd:cd07854   157 GDFGLARIV--DPHyshKGYLSEG--LVTKWyRSPRlLLSPNNYTKAIDMWAAGCIFAEML 213
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
312-525 2.68e-05

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 48.07  E-value: 2.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  312 YYR-AALD------PPSAA-----CTRPPSAPVNL-ISSVNGTSVTLEWAPPLDPggrsDITYNAVCRrcpwalshceAC 378
Cdd:COG3401   299 YYRvTAVDaagnesAPSNVvsvttDLTPPAAPSGLtATAVGSSSITLSWTASSDA----DVTGYNVYR----------ST 364
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940659  379 GSGTRFVPQQTSLAQASLLVANLLAHMNYSFWIEAVNGVSNLSPEPRSAAVVNITTNQ-----AAPSQVVVIRQERAGQT 453
Cdd:COG3401   365 SGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASgesltASVDAVPLTDVAGATAA 444
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 341940659  454 SVSLLWQEPEQPNGIILEYEIKYYEKDKEMQSYSTLKAVTTRA---TVSGLKPGTRYVFQVRARTSAGCGRFSQA 525
Cdd:COG3401   445 ASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTAnlsVTTGSLVGGSGASSVTNSVSVIGASAAAA 519
 
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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