NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|157822719|ref|NP_001102438|]
View 

protein-tyrosine kinase 6 [Rattus norvegicus]

Protein Classification

protein kinase family protein; choline kinase family protein( domain architecture ID 10185615)

protein kinase family protein containing Src homology 2 (SH2) domain(s), may catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine and/or tyrosine residues on protein substrates; similar to Syk-like subfamily of tyrosine-protein kinases| choline kinase (ChoK) family protein similar to ChoK that catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC), and sphingomyelin (SM)

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
184-444 1.57e-164

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 cd05148:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 261  Bit Score: 463.83  E-value: 1.57e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 184 WERPREEFTLCKKLGSGYFGEVFEGLWKGLVRVAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYII 263
Cdd:cd05148    1 WERPREEFTLERKLGSGYFGEVWEGLWKNRVRVAIKILKSDDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGEPVYII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 264 TELMPKGSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYL 343
Cdd:cd05148   81 TELMEKGSLLAFLRSPEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLARLIKEDVYL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 344 SRDHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLSC 423
Cdd:cd05148  161 SSDKKIPYKWTAPEAASHGTFSTKSDVWSFGILLYEMFTYGQVPYPGMNNHEVYDQITAGYRMPCPAKCPQEIYKIMLEC 240
                        250       260
                 ....*....|....*....|.
gi 157822719 424 WSRDPKQRPCFKDLCEKLSGI 444
Cdd:cd05148  241 WAAEPEDRPSFKALREELDNI 261
SH2_PTK6_Brk cd10358
Src homology 2 domain found in protein-tyrosine kinase-6 (PTK6) which is also known as breast ...
75-174 1.01e-53

Src homology 2 domain found in protein-tyrosine kinase-6 (PTK6) which is also known as breast tumor kinase (Brk); Human protein-tyrosine kinase-6 (PTK6, also known as breast tumor kinase (Brk)) is a member of the non-receptor protein-tyrosine kinase family and is expressed in two-thirds of all breast tumors. PTK6 (9). PTK6 contains a SH3 domain, a SH2 domain, and catalytic domains. For the case of the non-receptor protein-tyrosine kinases, the SH2 domain is typically involved in negative regulation of kinase activity by binding to a phosphorylated tyrosine residue near to the C terminus. The C-terminal sequence of PTK6 (PTSpYENPT where pY is phosphotyrosine) is thought to be a self-ligand for the SH2 domain. The structure of the SH2 domain resembles other SH2 domains except for a centrally located four-stranded antiparallel beta-sheet (strands betaA, betaB, betaC, and betaD). There are also differences in the loop length which might be responsible for PTK6 ligand specificity. There are two possible means of regulation of PTK6: autoinhibitory with the phosphorylation of Tyr playing a role in its negative regulation and autophosphorylation at this site, though it has been shown that PTK6 might phosphorylate signal transduction-associated proteins Sam68 and signal transducing adaptor family member 2 (STAP/BKS) in vivo. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


:

Pssm-ID: 198221  Cd Length: 100  Bit Score: 174.94  E-value: 1.01e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719  75 SEPWFFGCISRSEAMHRLQSEDYPKGTFLIRVSQKPGADYVLSVWDAEAVRHYRIWRNSAGRLHLNEVVSFSSLSELVNY 154
Cdd:cd10358    1 SEPWFFGCISRSEAVRRLQAEGNATGAFLIRVSEKPSADYVLSVRDTQAVRHYKIWRRAGGRLHLNEAVSFLSLPELVNY 80
                         90       100
                 ....*....|....*....|
gi 157822719 155 HKTHNLSPGLQLSMACWKLK 174
Cdd:cd10358   81 HRAQSLSHGLRLAAPCRKHE 100
SH3_Brk cd11847
Src homology 3 domain of Brk (Breast tumor kinase) Protein Tyrosine Kinase (PTK), also called ...
12-69 1.43e-27

Src homology 3 domain of Brk (Breast tumor kinase) Protein Tyrosine Kinase (PTK), also called PTK6; Brk is a cytoplasmic (or non-receptor) PTK with limited homology to Src kinases. It has been found to be overexpressed in a majority of breast tumors. It plays roles in normal cell differentiation, proliferation, survival, migration, and cell cycle progression. Brk substrates include RNA-binding proteins (SLM-1/2, Sam68), transcription factors (STAT3/5), and signaling molecules (Akt, paxillin, IRS-4). 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). However, Brk lacks the N-terminal myristoylation site. The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


:

Pssm-ID: 212781 [Multi-domain]  Cd Length: 58  Bit Score: 104.18  E-value: 1.43e-27
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 157822719  12 KYVGLWDFKARTDEELSFQAGDLLHVTRKEEQWWWATLLDAEGKALAEGYVPHNYLAE 69
Cdd:cd11847    1 IYKALWDFKARGDEELSFQAGDQFRIAERSGDWWTALKLDRAGGVVAQGFVPNNYLAR 58
 
Name Accession Description Interval E-value
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
184-444 1.57e-164

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: 463.83  E-value: 1.57e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 184 WERPREEFTLCKKLGSGYFGEVFEGLWKGLVRVAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYII 263
Cdd:cd05148    1 WERPREEFTLERKLGSGYFGEVWEGLWKNRVRVAIKILKSDDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGEPVYII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 264 TELMPKGSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYL 343
Cdd:cd05148   81 TELMEKGSLLAFLRSPEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLARLIKEDVYL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 344 SRDHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLSC 423
Cdd:cd05148  161 SSDKKIPYKWTAPEAASHGTFSTKSDVWSFGILLYEMFTYGQVPYPGMNNHEVYDQITAGYRMPCPAKCPQEIYKIMLEC 240
                        250       260
                 ....*....|....*....|.
gi 157822719 424 WSRDPKQRPCFKDLCEKLSGI 444
Cdd:cd05148  241 WAAEPEDRPSFKALREELDNI 261
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
192-441 5.46e-129

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: 373.42  E-value: 5.46e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719   192 TLCKKLGSGYFGEVFEGLWKGL-----VRVAVKVISRDNLLHQHT-FQAEIQAMKKLRHKHILSLYAVATAGDPVYIITE 265
Cdd:smart00221   2 TLGKKLGEGAFGEVYKGTLKGKgdgkeVEVAVKTLKEDASEQQIEeFLREARIMRKLDHPNIVKLLGVCTEEEPLMIVME 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719   266 LMPKGSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKE-DIYLS 344
Cdd:smart00221  82 YMPGGDLLDYLRKNRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDdDYYKV 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719   345 RDHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLSCW 424
Cdd:smart00221 162 KGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEEPYPGMSNAEVLEYLKKGYRLPKPPNCPPELYKLMLQCW 241
                          250
                   ....*....|....*..
gi 157822719   425 SRDPKQRPCFKDLCEKL 441
Cdd:smart00221 242 AEDPEDRPTFSELVEIL 258
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
191-441 2.59e-125

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: 364.13  E-value: 2.59e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719  191 FTLCKKLGSGYFGEVFEGLWKGL-----VRVAVKVISRDNLLHQHT-FQAEIQAMKKLRHKHILSLYAVATAGDPVYIIT 264
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGEgentkIKVAVKTLKEGADEEEREdFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719  265 ELMPKGSLLQLLRDSDEKdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLS 344
Cdd:pfam07714  81 EYMPGGDLLDFLRKHKRK-LTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDIYDDDYYR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719  345 RDHN--VPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLS 422
Cdd:pfam07714 160 KRGGgkLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEFLEDGYRLPQPENCPDELYDLMKQ 239
                         250
                  ....*....|....*....
gi 157822719  423 CWSRDPKQRPCFKDLCEKL 441
Cdd:pfam07714 240 CWAYDPEDRPTFSELVEDL 258
SH2_PTK6_Brk cd10358
Src homology 2 domain found in protein-tyrosine kinase-6 (PTK6) which is also known as breast ...
75-174 1.01e-53

Src homology 2 domain found in protein-tyrosine kinase-6 (PTK6) which is also known as breast tumor kinase (Brk); Human protein-tyrosine kinase-6 (PTK6, also known as breast tumor kinase (Brk)) is a member of the non-receptor protein-tyrosine kinase family and is expressed in two-thirds of all breast tumors. PTK6 (9). PTK6 contains a SH3 domain, a SH2 domain, and catalytic domains. For the case of the non-receptor protein-tyrosine kinases, the SH2 domain is typically involved in negative regulation of kinase activity by binding to a phosphorylated tyrosine residue near to the C terminus. The C-terminal sequence of PTK6 (PTSpYENPT where pY is phosphotyrosine) is thought to be a self-ligand for the SH2 domain. The structure of the SH2 domain resembles other SH2 domains except for a centrally located four-stranded antiparallel beta-sheet (strands betaA, betaB, betaC, and betaD). There are also differences in the loop length which might be responsible for PTK6 ligand specificity. There are two possible means of regulation of PTK6: autoinhibitory with the phosphorylation of Tyr playing a role in its negative regulation and autophosphorylation at this site, though it has been shown that PTK6 might phosphorylate signal transduction-associated proteins Sam68 and signal transducing adaptor family member 2 (STAP/BKS) in vivo. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198221  Cd Length: 100  Bit Score: 174.94  E-value: 1.01e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719  75 SEPWFFGCISRSEAMHRLQSEDYPKGTFLIRVSQKPGADYVLSVWDAEAVRHYRIWRNSAGRLHLNEVVSFSSLSELVNY 154
Cdd:cd10358    1 SEPWFFGCISRSEAVRRLQAEGNATGAFLIRVSEKPSADYVLSVRDTQAVRHYKIWRRAGGRLHLNEAVSFLSLPELVNY 80
                         90       100
                 ....*....|....*....|
gi 157822719 155 HKTHNLSPGLQLSMACWKLK 174
Cdd:cd10358   81 HRAQSLSHGLRLAAPCRKHE 100
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
191-432 7.47e-45

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 162.87  E-value: 7.47e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEGLWKGLVR-VAVKVISRDNLLHQHT---FQAEIQAMKKLRHKHILSLYAVATAGDPVYIITEL 266
Cdd:COG0515    9 YRILRLLGRGGMGVVYLARDLRLGRpVALKVLRPELAADPEArerFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 267 MPKGSLLQLLRDsdEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVkEDIYLSRD 346
Cdd:COG0515   89 VEGESLADLLRR--RGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARAL-GGATLTQT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 347 HNVPYK--WTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRVDAGYRMPCPL---ECPPNIHKLML 421
Cdd:COG0515  166 GTVVGTpgYMAPEQARGEPVDPRSDVYSLGVTLYELLT-GRPPFDGDSPAELLRAHLREPPPPPSElrpDLPPALDAIVL 244
                        250
                 ....*....|.
gi 157822719 422 SCWSRDPKQRP 432
Cdd:COG0515  245 RALAKDPEERY 255
SH3_Brk cd11847
Src homology 3 domain of Brk (Breast tumor kinase) Protein Tyrosine Kinase (PTK), also called ...
12-69 1.43e-27

Src homology 3 domain of Brk (Breast tumor kinase) Protein Tyrosine Kinase (PTK), also called PTK6; Brk is a cytoplasmic (or non-receptor) PTK with limited homology to Src kinases. It has been found to be overexpressed in a majority of breast tumors. It plays roles in normal cell differentiation, proliferation, survival, migration, and cell cycle progression. Brk substrates include RNA-binding proteins (SLM-1/2, Sam68), transcription factors (STAT3/5), and signaling molecules (Akt, paxillin, IRS-4). 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). However, Brk lacks the N-terminal myristoylation site. The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212781 [Multi-domain]  Cd Length: 58  Bit Score: 104.18  E-value: 1.43e-27
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 157822719  12 KYVGLWDFKARTDEELSFQAGDLLHVTRKEEQWWWATLLDAEGKALAEGYVPHNYLAE 69
Cdd:cd11847    1 IYKALWDFKARGDEELSFQAGDQFRIAERSGDWWTALKLDRAGGVVAQGFVPNNYLAR 58
SH2 smart00252
Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides ...
76-161 2.73e-25

Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides via 2 surface pockets. Specificity is provided via interaction with residues that are distinct from the phosphotyrosine. Only a single occurrence of a SH2 domain has been found in S. cerevisiae.


Pssm-ID: 214585 [Multi-domain]  Cd Length: 84  Bit Score: 98.84  E-value: 2.73e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719    76 EPWFFGCISRSEAMHRLQSEdyPKGTFLIRVSQKPGADYVLSVWDAEAVRHYRIWRNSAGRLHLNEVVSFSSLSELVNYH 155
Cdd:smart00252   1 QPWYHGFISREEAEKLLKNE--GDGDFLVRDSESSPGDYVLSVRVKGKVKHYRIRRNEDGKFYLEGGRKFPSLVELVEHY 78

                   ....*.
gi 157822719   156 KTHNLS 161
Cdd:smart00252  79 QKNSLG 84
SH2 pfam00017
SH2 domain;
78-155 7.64e-19

SH2 domain;


Pssm-ID: 425423 [Multi-domain]  Cd Length: 77  Bit Score: 80.72  E-value: 7.64e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157822719   78 WFFGCISRSEAMHRLQSEDyPKGTFLIRVSQ-KPGaDYVLSVWDAEAVRHYRIWRNSAGRLHLNEVVSFSSLSELVNYH 155
Cdd:pfam00017   1 WYHGKISRQEAERLLLNGK-PDGTFLVRESEsTPG-GYTLSVRDDGKVKHYKIQSTDNGGYYISGGVKFSSLAELVEHY 77
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
295-437 1.52e-18

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 88.00  E-value: 1.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 295 QVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARL----VKEDIylSRDH-NVPYkWTAPEALSRGHYSIKSD 369
Cdd:PTZ00283 151 QVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFGFSKMyaatVSDDV--GRTFcGTPY-YVAPEIWRRKPYSKKAD 227
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157822719 370 VWSFGVLLHEIFSRgQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLSCWSRDPKQRPCFKDL 437
Cdd:PTZ00283 228 MFSLGVLLYELLTL-KRPFDGENMEEVMHKTLAGRYDPLPPSISPEMQEIVTALLSSDPKRRPSSSKL 294
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
195-390 8.72e-18

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 85.62  E-value: 8.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWKGLVR-VAVKVIsRDNLLHQHTFQA----EIQAMKKLRHKHILSLYAVATAGDPVYIITELMPK 269
Cdd:NF033483  13 ERIGRGGMAEVYLAKDTRLDRdVAVKVL-RPDLARDPEFVArfrrEAQSAASLSHPNIVSVYDVGEDGGIPYIVMEYVDG 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 270 GSLLQLLRDsdEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDI-------- 341
Cdd:NF033483  92 RTLKDYIRE--HGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIARALSSTTmtqtnsvl 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 157822719 342 ----YLSrdhnvpykwtaPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPG 390
Cdd:NF033483 170 gtvhYLS-----------PEQARGGTVDARSDIYSLGIVLYEMLT-GRPPFDG 210
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
10-68 2.26e-13

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 64.48  E-value: 2.26e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719    10 GPKYVGLWDFKARTDEELSFQAGDLLHVTRKEEQ-WWWATLLDaeGKalaEGYVPHNYLA 68
Cdd:smart00326   2 GPQVRALYDYTAQDPDELSFKKGDIITVLEKSDDgWWKGRLGR--GK---EGLFPSNYVE 56
 
Name Accession Description Interval E-value
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
184-444 1.57e-164

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: 463.83  E-value: 1.57e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 184 WERPREEFTLCKKLGSGYFGEVFEGLWKGLVRVAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYII 263
Cdd:cd05148    1 WERPREEFTLERKLGSGYFGEVWEGLWKNRVRVAIKILKSDDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGEPVYII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 264 TELMPKGSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYL 343
Cdd:cd05148   81 TELMEKGSLLAFLRSPEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLARLIKEDVYL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 344 SRDHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLSC 423
Cdd:cd05148  161 SSDKKIPYKWTAPEAASHGTFSTKSDVWSFGILLYEMFTYGQVPYPGMNNHEVYDQITAGYRMPCPAKCPQEIYKIMLEC 240
                        250       260
                 ....*....|....*....|.
gi 157822719 424 WSRDPKQRPCFKDLCEKLSGI 444
Cdd:cd05148  241 WAAEPEDRPSFKALREELDNI 261
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
195-441 8.05e-133

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: 382.79  E-value: 8.05e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWKGLVRVAVKVisrdnlLHQHT-----FQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPK 269
Cdd:cd05034    1 KKLGAGQFGEVWMGVWNGTTKVAVKT------LKPGTmspeaFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELMSK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 270 GSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSRDH-N 348
Cdd:cd05034   75 GSLLDYLRTGEGRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLARLIEDDEYTAREGaK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 349 VPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLSCWSRDP 428
Cdd:cd05034  155 FPIKWTAPEAALYGRFTIKSDVWSFGILLYEIVTYGRVPYPGMTNREVLEQVERGYRMPKPPGCPDELYDIMLQCWKKEP 234
                        250
                 ....*....|...
gi 157822719 429 KQRPCFKDLCEKL 441
Cdd:cd05034  235 EERPTFEYLQSFL 247
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
192-441 5.46e-129

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: 373.42  E-value: 5.46e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719   192 TLCKKLGSGYFGEVFEGLWKGL-----VRVAVKVISRDNLLHQHT-FQAEIQAMKKLRHKHILSLYAVATAGDPVYIITE 265
Cdd:smart00221   2 TLGKKLGEGAFGEVYKGTLKGKgdgkeVEVAVKTLKEDASEQQIEeFLREARIMRKLDHPNIVKLLGVCTEEEPLMIVME 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719   266 LMPKGSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKE-DIYLS 344
Cdd:smart00221  82 YMPGGDLLDYLRKNRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDdDYYKV 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719   345 RDHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLSCW 424
Cdd:smart00221 162 KGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEEPYPGMSNAEVLEYLKKGYRLPKPPNCPPELYKLMLQCW 241
                          250
                   ....*....|....*..
gi 157822719   425 SRDPKQRPCFKDLCEKL 441
Cdd:smart00221 242 AEDPEDRPTFSELVEIL 258
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
182-441 7.86e-128

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: 370.97  E-value: 7.86e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 182 DDWERPREEFTLCKKLGSGYFGEVFEGLWKGLVRVAVKVISRDNLlHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVY 261
Cdd:cd05068    1 DQWEIDRKSLKLLRKLGSGQFGEVWEGLWNNTTPVAVKTLKPGTM-DPEDFLREAQIMKKLRHPKLIQLYAVCTLEEPIY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 262 IITELMPKGSLLQLLRDsDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVK-ED 340
Cdd:cd05068   80 IITELMKHGSLLEYLQG-KGRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGLARVIKvED 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 341 IYLSR-DHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKL 419
Cdd:cd05068  159 EYEAReGAKFPIKWTAPEAANYNRFSIKSDVWSFGILLTEIVTYGRIPYPGMTNAEVLQQVERGYRMPCPPNCPPQLYDI 238
                        250       260
                 ....*....|....*....|..
gi 157822719 420 MLSCWSRDPKQRPCFKDLCEKL 441
Cdd:cd05068  239 MLECWKADPMERPTFETLQWKL 260
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
192-441 3.82e-126

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 366.09  E-value: 3.82e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719   192 TLCKKLGSGYFGEVFEGLWKGL-----VRVAVKVISRDNLLHQHT-FQAEIQAMKKLRHKHILSLYAVATAGDPVYIITE 265
Cdd:smart00219   2 TLGKKLGEGAFGEVYKGKLKGKggkkkVEVAVKTLKEDASEQQIEeFLREARIMRKLDHPNVVKLLGVCTEEEPLYIVME 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719   266 LMPKGSLLQLLRDSDEKdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSR 345
Cdd:smart00219  82 YMEGGDLLSYLRKNRPK-LSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDYYRK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719   346 DH-NVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLSCW 424
Cdd:smart00219 161 RGgKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEYLKNGYRLPQPPNCPPELYDLMLQCW 240
                          250
                   ....*....|....*..
gi 157822719   425 SRDPKQRPCFKDLCEKL 441
Cdd:smart00219 241 AEDPEDRPTFSELVEIL 257
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
191-441 2.59e-125

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: 364.13  E-value: 2.59e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719  191 FTLCKKLGSGYFGEVFEGLWKGL-----VRVAVKVISRDNLLHQHT-FQAEIQAMKKLRHKHILSLYAVATAGDPVYIIT 264
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGEgentkIKVAVKTLKEGADEEEREdFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719  265 ELMPKGSLLQLLRDSDEKdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLS 344
Cdd:pfam07714  81 EYMPGGDLLDFLRKHKRK-LTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDIYDDDYYR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719  345 RDHN--VPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLS 422
Cdd:pfam07714 160 KRGGgkLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEFLEDGYRLPQPENCPDELYDLMKQ 239
                         250
                  ....*....|....*....
gi 157822719  423 CWSRDPKQRPCFKDLCEKL 441
Cdd:pfam07714 240 CWAYDPEDRPTFSELVEDL 258
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
195-441 2.76e-119

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: 348.76  E-value: 2.76e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWKGL----VRVAVKVISRD-NLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPK 269
Cdd:cd00192    1 KKLGEGAFGEVYKGKLKGGdgktVDVAVKTLKEDaSESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYMEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 270 GSLLQLLR-------DSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIY 342
Cdd:cd00192   81 GDLLDFLRksrpvfpSPEPSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRDIYDDDY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 343 LSRDHN--VPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLM 420
Cdd:cd00192  161 YRKKTGgkLPIRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTLGATPYPGLSNEEVLEYLRKGYRLPKPENCPDELYELM 240
                        250       260
                 ....*....|....*....|.
gi 157822719 421 LSCWSRDPKQRPCFKDLCEKL 441
Cdd:cd00192  241 LSCWQLDPEDRPTFSELVERL 261
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
195-437 2.88e-102

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: 304.92  E-value: 2.88e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWKGLVRVAVKVIsRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAgDPVYIITELMPKGSLLQ 274
Cdd:cd14203    1 VKLGQGCFGEVWMGTWNGTTKVAIKTL-KPGTMSPEAFLEEAQIMKKLRHDKLVQLYAVVSE-EPIYIVTEFMSKGSLLD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 275 LLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSRD-HNVPYKW 353
Cdd:cd14203   79 FLKDGEGKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQgAKFPIKW 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 354 TAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLSCWSRDPKQRPC 433
Cdd:cd14203  159 TAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPPGCPESLHELMCQCWRKDPEERPT 238

                 ....
gi 157822719 434 FKDL 437
Cdd:cd14203  239 FEYL 242
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
183-437 1.32e-97

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: 293.72  E-value: 1.32e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 183 DWERPREEFTLCKKLGSGYFGEVFEGLWKGLVRVAVKVIsRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAgDPVYI 262
Cdd:cd05067    1 EWEVPRETLKLVERLGAGQFGEVWMGYYNGHTKVAIKSL-KQGSMSPDAFLAEANLMKQLQHQRLVRLYAVVTQ-EPIYI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 263 ITELMPKGSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIY 342
Cdd:cd05067   79 ITEYMENGSLVDFLKTPSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLIEDNEY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 343 LSRD-HNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLML 421
Cdd:cd05067  159 TAREgAKFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVTHGRIPYPGMTNPEVIQNLERGYRMPRPDNCPEELYQLMR 238
                        250
                 ....*....|....*.
gi 157822719 422 SCWSRDPKQRPCFKDL 437
Cdd:cd05067  239 LCWKERPEDRPTFEYL 254
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
184-444 4.43e-97

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: 291.95  E-value: 4.43e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 184 WERPREEFTLCKKLGSGYFGEVFEGLWKGLvRVAVKVIsRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYII 263
Cdd:cd05039    1 WAINKKDLKLGELIGKGEFGDVMLGDYRGQ-KVAVKCL-KDDSTAAQAFLAEASVMTTLRHPNLVQLLGVVLEGNGLYIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 264 TELMPKGSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYL 343
Cdd:cd05039   79 TEYMAKGSLVDYLRSRGRAVITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAKEASSNQDG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 344 SRdhnVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLSC 423
Cdd:cd05039  159 GK---LPIKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVVPHVEKGYRMEAPEGCPPEVYKVMKNC 235
                        250       260
                 ....*....|....*....|.
gi 157822719 424 WSRDPKQRPCFKDLCEKLSGI 444
Cdd:cd05039  236 WELDPAKRPTFKQLREKLEHI 256
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
184-434 5.45e-95

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: 287.32  E-value: 5.45e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 184 WERPREEFTLCKKLGSGYFGEVFEGLWKGLVRVAVKVISRDNLLHQhTFQAEIQAMKKLRHKHILSLYAVATAGDPVYII 263
Cdd:cd05072    2 WEIPRESIKLVKKLGAGQFGEVWMGYYNNSTKVAVKTLKPGTMSVQ-AFLEEANLMKTLQHDKLVRLYAVVTKEEPIYII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 264 TELMPKGSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYL 343
Cdd:cd05072   81 TEYMAKGSLLDFLKSDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIEDNEYT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 344 SRD-HNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLS 422
Cdd:cd05072  161 AREgAKFPIKWTAPEAINFGSFTIKSDVWSFGILLYEIVTYGKIPYPGMSNSDVMSALQRGYRMPRMENCPDELYDIMKT 240
                        250
                 ....*....|..
gi 157822719 423 CWSRDPKQRPCF 434
Cdd:cd05072  241 CWKEKAEERPTF 252
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
182-435 1.24e-94

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: 286.58  E-value: 1.24e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 182 DDWERPREEFTLCKKLGSGYFGEVFEGLWKGLVRVAVKVISRDNLLHQhTFQAEIQAMKKLRHKHILSLYAVATAgDPVY 261
Cdd:cd05069    5 DAWEIPRESLRLDVKLGQGCFGEVWMGTWNGTTKVAIKTLKPGTMMPE-AFLQEAQIMKKLRHDKLVPLYAVVSE-EPIY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 262 IITELMPKGSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDI 341
Cdd:cd05069   83 IVTEFMGKGSLLDFLKEGDGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNE 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 342 YLSRD-HNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLM 420
Cdd:cd05069  163 YTARQgAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMVNREVLEQVERGYRMPCPQGCPESLHELM 242
                        250
                 ....*....|....*
gi 157822719 421 LSCWSRDPKQRPCFK 435
Cdd:cd05069  243 KLCWKKDPDERPTFE 257
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
182-437 5.35e-93

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: 282.35  E-value: 5.35e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 182 DDWERPREEFTLCKKLGSGYFGEVFEGLWKGLVRVAVKVIsRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAgDPVY 261
Cdd:cd05071    2 DAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTL-KPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSE-EPIY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 262 IITELMPKGSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDI 341
Cdd:cd05071   80 IVTEYMSKGSLLDFLKGEMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 342 YLSRD-HNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLM 420
Cdd:cd05071  160 YTARQgAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPCPPECPESLHDLM 239
                        250
                 ....*....|....*..
gi 157822719 421 LSCWSRDPKQRPCFKDL 437
Cdd:cd05071  240 CQCWRKEPEERPTFEYL 256
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
182-437 6.05e-92

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: 279.65  E-value: 6.05e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 182 DDWERPREEFTLCKKLGSGYFGEVFEGLWKGLVRVAVKVIsRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAgDPVY 261
Cdd:cd05070    2 DVWEIPRESLQLIKRLGNGQFGEVWMGTWNGNTKVAIKTL-KPGTMSPESFLEEAQIMKKLKHDKLVQLYAVVSE-EPIY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 262 IITELMPKGSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDI 341
Cdd:cd05070   80 IVTEYMSKGSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 342 YLSRD-HNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLM 420
Cdd:cd05070  160 YTARQgAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPQDCPISLHELM 239
                        250
                 ....*....|....*..
gi 157822719 421 LSCWSRDPKQRPCFKDL 437
Cdd:cd05070  240 IHCWKKDPEERPTFEYL 256
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
184-444 1.15e-91

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: 278.54  E-value: 1.15e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 184 WERPREEFTLCKKLGSGYFGEVFEGLWKGLVR-VAVKVISRDNLlHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYI 262
Cdd:cd05052    1 WEIERTDITMKHKLGGGQYGEVYEGVWKKYNLtVAVKTLKEDTM-EVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 263 ITELMPKGSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIY 342
Cdd:cd05052   80 ITEFMPYGNLLDYLRECNREELNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 343 LSRD-HNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLML 421
Cdd:cd05052  160 TAHAgAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKGYRMERPEGCPPKVYELMR 239
                        250       260
                 ....*....|....*....|...
gi 157822719 422 SCWSRDPKQRPCFKDLCEKLSGI 444
Cdd:cd05052  240 ACWQWNPSDRPSFAEIHQALETM 262
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
195-441 1.44e-89

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: 272.78  E-value: 1.44e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWKGL-VRVAVKViSRDNLL--HQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGS 271
Cdd:cd05041    1 EKIGRGNFGDVYRGVLKPDnTEVAVKT-CRETLPpdLKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 272 LLQLLRDSdEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSRD--HNV 349
Cdd:cd05041   80 LLTFLRKK-GARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSREEEDGEYTVSDglKQI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 350 PYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLSCWSRDPK 429
Cdd:cd05041  159 PIKWTAPEALNYGRYTSESDVWSFGILLWEIFSLGATPYPGMSNQQTREQIESGYRMPAPELCPEAVYRLMLQCWAYDPE 238
                        250
                 ....*....|..
gi 157822719 430 QRPCFKDLCEKL 441
Cdd:cd05041  239 NRPSFSEIYNEL 250
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
190-441 2.05e-85

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: 262.00  E-value: 2.05e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLCKKLGSGYFGEVFEGLWKGLVRVAVKVIsRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPK 269
Cdd:cd05059    5 ELTFLKELGSGQFGVVHLGKWRGKIDVAIKMI-KEGSMSEDDFIEEAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEYMAN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 270 GSLLQLLRDSDEKdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYL-SRDHN 348
Cdd:cd05059   84 GCLLNYLRERRGK-FQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARYVLDDEYTsSVGTK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 349 VPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLSCWSRDP 428
Cdd:cd05059  163 FPVKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSEGKMPYERFSNSEVVEHISQGYRLYRPHLAPTEVYTIMYSCWHEKP 242
                        250
                 ....*....|...
gi 157822719 429 KQRPCFKDLCEKL 441
Cdd:cd05059  243 EERPTFKILLSQL 255
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
182-435 1.32e-84

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: 260.34  E-value: 1.32e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 182 DDWERPREEFTLCKKLGSGYFGEVFEGLWKGLVRVAVKVIsRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAgDPVY 261
Cdd:cd05073    4 DAWEIPRESLKLEKKLGAGQFGEVWMATYNKHTKVAVKTM-KPGSMSVEAFLAEANVMKTLQHDKLVKLHAVVTK-EPIY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 262 IITELMPKGSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDI 341
Cdd:cd05073   82 IITEFMAKGSLLDFLKSDEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVIEDNE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 342 YLSRD-HNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLM 420
Cdd:cd05073  162 YTAREgAKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTYGRIPYPGMSNPEVIRALERGYRMPRPENCPEELYNIM 241
                        250
                 ....*....|....*
gi 157822719 421 LSCWSRDPKQRPCFK 435
Cdd:cd05073  242 MRCWKNRPEERPTFE 256
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
197-441 6.14e-84

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: 257.85  E-value: 6.14e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGLVrVAVKVISRDNLLHQH--TFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSLLQ 274
Cdd:cd13999    1 IGSGSFGEVYKGKWRGTD-VAIKKLKVEDDNDELlkEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSLYD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 275 LLRDsDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSRDHNVPYKWT 354
Cdd:cd13999   80 LLHK-KKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKMTGVVGTPRWM 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 355 APEALSRGHYSIKSDVWSFGVLLHEIFSRgQMPYPGMSN-HETFLRVDAGYRMPCPLECPPNIHKLMLSCWSRDPKQRPC 433
Cdd:cd13999  159 APEVLRGEPYTEKADVYSFGIVLWELLTG-EVPFKELSPiQIAAAVVQKGLRPPIPPDCPPELSKLIKRCWNEDPEKRPS 237

                 ....*...
gi 157822719 434 FKDLCEKL 441
Cdd:cd13999  238 FSEIVKRL 245
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
184-441 9.46e-81

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: 251.57  E-value: 9.46e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 184 WERPREEFTLCKKLGSGYFGEVFEGLWKGL-------VRVAVKVISRDNllHQHTFQ---AEIQAMKKL-RHKHILSLYA 252
Cdd:cd05053    7 WELPRDRLTLGKPLGEGAFGQVVKAEAVGLdnkpnevVTVAVKMLKDDA--TEKDLSdlvSEMEMMKMIgKHKNIINLLG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 253 VATAGDPVYIITELMPKGSLLQLLRD--------------SDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNV 318
Cdd:cd05053   85 ACTQDGPLYVVVEYASKGNLREFLRArrppgeeaspddprVPEEQLTQKDLVSFAYQVARGMEYLASKKCIHRDLAARNV 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 319 LVTENNLCKVGDFGLARLVKE-DIYLSR-DHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHET 396
Cdd:cd05053  165 LVTEDNVMKIADFGLARDIHHiDYYRKTtNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEEL 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 157822719 397 FLRVDAGYRMPCPLECPPNIHKLMLSCWSRDPKQRPCFKDLCEKL 441
Cdd:cd05053  245 FKLLKEGHRMEKPQNCTQELYMLMRDCWHEVPSQRPTFKQLVEDL 289
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
192-442 9.43e-79

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: 245.36  E-value: 9.43e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 192 TLCKKLGSGYFGEVFEGLW----KGLVRVAVKVI---SRDNllHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIIT 264
Cdd:cd05033    7 TIEKVIGGGEFGEVCSGSLklpgKKEIDVAIKTLksgYSDK--QRLDFLTEASIMGQFDHPNVIRLEGVVTKSRPVMIVT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 265 ELMPKGSLLQLLRDSDEKdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLV--KEDIY 342
Cdd:cd05033   85 EYMENGSLDKFLRENDGK-FTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLSRRLedSEATY 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 343 LSRDHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLS 422
Cdd:cd05033  164 TTKGGKIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSYGERPYWDMSNQDVIKAVEDGYRLPPPMDCPSALYQLMLD 243
                        250       260
                 ....*....|....*....|
gi 157822719 423 CWSRDPKQRPCFKDLCEKLS 442
Cdd:cd05033  244 CWQKDRNERPTFSQIVSTLD 263
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
197-442 1.48e-78

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: 244.53  E-value: 1.48e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGLVRVAVKVISRDnlLHQH---TFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSLL 273
Cdd:cd05085    4 LGKGNFGEVYKGTLKDKTPVAVKTCKED--LPQElkiKFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVPGGDFL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 274 QLLRDSDEkDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSRD-HNVPYK 352
Cdd:cd05085   82 SFLRKKKD-ELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQEDDGVYSSSGlKQIPIK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 353 WTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLSCWSRDPKQRP 432
Cdd:cd05085  161 WTAPEALNYGRYSSESDVWSFGILLWETFSLGVCPYPGMTNQQAREQVEKGYRMSAPQRCPEDIYKIMQRCWDYNPENRP 240
                        250
                 ....*....|
gi 157822719 433 CFKDLCEKLS 442
Cdd:cd05085  241 KFSELQKELA 250
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
184-441 2.00e-78

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: 244.01  E-value: 2.00e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 184 WERPREEFTLCKKLGSGYFGEVFEGLWKGLvRVAVKVISRDnlLHQHTFQAEIQAMKKLRHKHILSLYAVATAgDPVYII 263
Cdd:cd05083    1 WLLNLQKLTLGEIIGEGEFGAVLQGEYMGQ-KVAVKNIKCD--VTAQAFLEETAVMTKLQHKNLVRLLGVILH-NGLYIV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 264 TELMPKGSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYL 343
Cdd:cd05083   77 MELMSKGNLVNFLRSRGRALVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAKVGSMGVDN 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 344 SRdhnVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLSC 423
Cdd:cd05083  157 SR---LPVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFSYGRAPYPKMSVKEVKEAVEKGYRMEPPEGCPPDVYSIMTSC 233
                        250
                 ....*....|....*...
gi 157822719 424 WSRDPKQRPCFKDLCEKL 441
Cdd:cd05083  234 WEAEPGKRPSFKKLREKL 251
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
184-444 5.16e-78

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: 243.35  E-value: 5.16e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 184 WERPREEFTLCKKLGSGYFGEVFEGLWKGlVRVAVKVISRDNLlhQHTFQAEIQAMKKLRHKHILSLYAVATAGD-PVYI 262
Cdd:cd05082    1 WALNMKELKLLQTIGKGEFGDVMLGDYRG-NKVAVKCIKNDAT--AQAFLAEASVMTQLRHSNLVQLLGVIVEEKgGLYI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 263 ITELMPKGSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLArlvKEDIY 342
Cdd:cd05082   78 VTEYMAKGSLVDYLRSRGRSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLT---KEASS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 343 LSRDHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLS 422
Cdd:cd05082  155 TQDTGKLPVKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVVPRVEKGYKMDAPDGCPPAVYDVMKN 234
                        250       260
                 ....*....|....*....|..
gi 157822719 423 CWSRDPKQRPCFKDLCEKLSGI 444
Cdd:cd05082  235 CWHLDAAMRPSFLQLREQLEHI 256
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
195-442 2.61e-77

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: 241.48  E-value: 2.61e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWKG----LVRVAVKVISRDNLLHQHT---FQAEIQAMKKLRHKHILSLYAVATAgDPVYIITELM 267
Cdd:cd05040    1 EKLGDGSFGVVRRGEWTTpsgkVIQVAVKCLKSDVLSQPNAmddFLKEVNAMHSLDHPNLIRLYGVVLS-SPLMMVTELA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 268 PKGSLLQLLRDsDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVK--EDIYLSR 345
Cdd:cd05040   80 PLGSLLDRLRK-DQGHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLMRALPqnEDHYVMQ 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 346 DH-NVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVD-AGYRMPCPLECPPNIHKLMLSC 423
Cdd:cd05040  159 EHrKVPFAWCAPESLKTRKFSHASDVWMFGVTLWEMFTYGEEPWLGLNGSQILEKIDkEGERLERPDDCPQDIYNVMLQC 238
                        250
                 ....*....|....*....
gi 157822719 424 WSRDPKQRPCFKDLCEKLS 442
Cdd:cd05040  239 WAHKPADRPTFVALRDFLP 257
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
195-441 8.25e-77

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: 240.40  E-value: 8.25e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWKGL-------VRVAVKVISRDNLLH-QHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITEL 266
Cdd:cd05044    1 KFLGSGAFGEVFEGTAKDIlgdgsgeTKVAVKTLRKGATDQeKAEFLKEAHLMSNFKHPNILKLLGVCLDNDPQYIILEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 267 MPKGSLLQLLRDSDEKD-----LPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLC----KVGDFGLAR-L 336
Cdd:cd05044   81 MEGGDLLSYLRAARPTAftpplLTLKDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVSSKDYRervvKIGDFGLARdI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 337 VKEDIYLSRDHN-VPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPN 415
Cdd:cd05044  161 YKNDYYRKEGEGlLPVRWMAPESLVDGVFTTQSDVWAFGVLMWEILTLGQQPYPARNNLEVLHFVRAGGRLDQPDNCPDD 240
                        250       260
                 ....*....|....*....|....*.
gi 157822719 416 IHKLMLSCWSRDPKQRPCFKDLCEKL 441
Cdd:cd05044  241 LYELMLRCWSTDPEERPSFARILEQL 266
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
184-442 1.48e-76

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: 240.32  E-value: 1.48e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 184 WERPREEFTLCKKLGSGYFGEVFEGLWKGLV------RVAVKVISRDNLLHQHT-FQAEIQAMKKLRHKHILSLYAVATA 256
Cdd:cd05032    1 WELPREKITLIRELGQGSFGMVYEGLAKGVVkgepetRVAIKTVNENASMRERIeFLNEASVMKEFNCHHVVRLLGVVST 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 257 GDPVYIITELMPKGSLLQLLRDSDEKD-----LPILELVDF---ASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKV 328
Cdd:cd05032   81 GQPTLVVMELMAKGDLKSYLRSRRPEAennpgLGPPTLQKFiqmAAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVKI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 329 GDFGLARLVKEDIYLSRDHN--VPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRM 406
Cdd:cd05032  161 GDFGMTRDIYETDYYRKGGKglLPVRWMAPESLKDGVFTTKSDVWSFGVVLWEMATLAEQPYQGLSNEEVLKFVIDGGHL 240
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 157822719 407 PCPLECPPNIHKLMLSCWSRDPKQRPCFKDLCEKLS 442
Cdd:cd05032  241 DLPENCPDKLLELMRMCWQYNPKMRPTFLEIVSSLK 276
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
195-444 1.62e-75

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: 236.86  E-value: 1.62e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWK----GLVRVAVKVISRDNLLHQHT-FQAEIQAMKKLRHKHILSLYAVaTAGDPVYIITELMPK 269
Cdd:cd05060    1 KELGHGNFGSVRKGVYLmksgKEVEVAVKTLKQEHEKAGKKeFLREASVMAQLDHPCIVRLIGV-CKGEPLMLVMELAPL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 270 GSLLQLLRDsdEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVK--EDIYLSRDH 347
Cdd:cd05060   80 GPLLKYLKK--RREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSRALGagSDYYRATTA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 348 NV-PYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLSCWSR 426
Cdd:cd05060  158 GRwPLKWYAPECINYGKFSSKSDVWSYGVTLWEAFSYGAKPYGEMKGPEVIAMLESGERLPRPEECPQEIYSIMLSCWKY 237
                        250
                 ....*....|....*...
gi 157822719 427 DPKQRPCFKDLCEKLSGI 444
Cdd:cd05060  238 RPEDRPTFSELESTFRRD 255
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
195-441 3.74e-75

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: 235.60  E-value: 3.74e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEG-LWKGLVRVAVKViSRDNLL--HQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGS 271
Cdd:cd05084    2 ERIGRGNFGEVFSGrLRADNTPVAVKS-CRETLPpdLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 272 LLQLLRdSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSRD--HNV 349
Cdd:cd05084   81 FLTFLR-TEGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSREEEDGVYAATGgmKQI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 350 PYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLSCWSRDPK 429
Cdd:cd05084  160 PVKWTAPEALNYGRYSSESDVWSFGILLWETFSLGAVPYANLSNQQTREAVEQGVRLPCPENCPDEVYRLMEQCWEYDPR 239
                        250
                 ....*....|..
gi 157822719 430 QRPCFKDLCEKL 441
Cdd:cd05084  240 KRPSFSTVHQDL 251
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
178-445 6.27e-74

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: 234.86  E-value: 6.27e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 178 LPHWDDWERPREEFTLCKKLGSGYFGEVFEGLWKGL--------VRVAVKVIsRDNLLHQH--TFQAEIQAMKKL-RHKH 246
Cdd:cd05099    1 LPLDPKWEFPRDRLVLGKPLGEGCFGQVVRAEAYGIdksrpdqtVTVAVKML-KDNATDKDlaDLISEMELMKLIgKHKN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 247 ILSLYAVATAGDPVYIITELMPKGSLLQLLR--------------DSDEKDLPILELVDFASQVAEGMCYLESQNYIHRD 312
Cdd:cd05099   80 IINLLGVCTQEGPLYVIVEYAAKGNLREFLRarrppgpdytfditKVPEEQLSFKDLVSCAYQVARGMEYLESRRCIHRD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 313 LAARNVLVTENNLCKVGDFGLARLVKEDIYLSRDHN--VPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPG 390
Cdd:cd05099  160 LAARNVLVTEDNVMKIADFGLARGVHDIDYYKKTSNgrLPVKWMAPEALFDRVYTHQSDVWSFGILMWEIFTLGGSPYPG 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 157822719 391 MSNHETFLRVDAGYRMPCPLECPPNIHKLMLSCWSRDPKQRPCFKDLCEKLSGIT 445
Cdd:cd05099  240 IPVEELFKLLREGHRMDKPSNCTHELYMLMRECWHAVPTQRPTFKQLVEALDKVL 294
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
178-441 2.18e-73

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: 232.76  E-value: 2.18e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 178 LPHWDDWERPREEFTLCKKLGSGYFGEVFEGLWKGL------VRVAVKVI-SRDNLLHQHTFQAEIQAMKKL-RHKHILS 249
Cdd:cd05055   24 LPYDLKWEFPRNNLSFGKTLGAGAFGKVVEATAYGLsksdavMKVAVKMLkPTAHSSEREALMSELKIMSHLgNHENIVN 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 250 LYAVATAGDPVYIITELMPKGSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVG 329
Cdd:cd05055  104 LLGACTIGGPILVITEYCCYGDLLNFLRRKRESFLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTHGKIVKIC 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 330 DFGLARLVKEDI-YLSR-DHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLR-VDAGYRM 406
Cdd:cd05055  184 DFGLARDIMNDSnYVVKgNARLPVKWMAPESIFNCVYTFESDVWSYGILLWEIFSLGSNPYPGMPVDSKFYKlIKEGYRM 263
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 157822719 407 PCPLECPPNIHKLMLSCWSRDPKQRPCFKDLCEKL 441
Cdd:cd05055  264 AQPEHAPAEIYDIMKTCWDADPLKRPTFKQIVQLI 298
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
189-442 3.13e-72

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: 228.30  E-value: 3.13e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFEGLWKGLVRVAVKVIsRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMP 268
Cdd:cd05112    4 SELTFVQEIGSGQFGLVHLGYWLNKDKVAIKTI-REGAMSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFME 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 269 KGSLLQLLRdSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSRD-H 347
Cdd:cd05112   83 HGCLSDYLR-TQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTRFVLDDQYTSSTgT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 348 NVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLSCWSRD 427
Cdd:cd05112  162 KFPVKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSEGKIPYENRSNSEVVEDINAGFRLYKPRLASTHVYEIMNHCWKER 241
                        250
                 ....*....|....*
gi 157822719 428 PKQRPCFKDLCEKLS 442
Cdd:cd05112  242 PEDRPSFSLLLRQLA 256
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
185-442 3.05e-71

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: 226.50  E-value: 3.05e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 185 ERPREEFTLCKKLGSGYFGEVFEGLWKGL------VRVAVKVI----SRDNLLhqhTFQAEIQAMKKLRHKHILSLYAVA 254
Cdd:cd05036    2 EVPRKNLTLIRALGQGAFGEVYEGTVSGMpgdpspLQVAVKTLpelcSEQDEM---DFLMEALIMSKFNHPNIVRCIGVC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 255 TAGDPVYIITELMPKGSLLQLLRDSDEK-----DLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVT---ENNLC 326
Cdd:cd05036   79 FQRLPRFILLELMAGGDLKSFLRENRPRpeqpsSLTMLDLLQLAQDVAKGCRYLEENHFIHRDIAARNCLLTckgPGRVA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 327 KVGDFGLARlvkeDIYLSRDHN------VPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRV 400
Cdd:cd05036  159 KIGDFGMAR----DIYRADYYRkggkamLPVKWMPPEAFLDGIFTSKTDVWSFGVLLWEIFSLGYMPYPGKSNQEVMEFV 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 157822719 401 DAGYRMPCPLECPPNIHKLMLSCWSRDPKQRPCFKDLCEKLS 442
Cdd:cd05036  235 TSGGRMDPPKNCPGPVYRIMTQCWQHIPEDRPNFSTILERLN 276
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
188-444 2.47e-69

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: 221.14  E-value: 2.47e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 188 REEFTLCKKLGSGYFGEVFEGLWKGL----VRVAVKVISRD-NLLHQHTFQAEIQAMKKLRHKHILSLYAVATAgDPVYI 262
Cdd:cd05056    5 REDITLGRCIGEGQFGDVYQGVYMSPenekIAVAVKTCKNCtSPSVREKFLQEAYIMRQFDHPHIVKLIGVITE-NPVWI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 263 ITELMPKGSLLQLLRDSDEKdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVK-EDI 341
Cdd:cd05056   84 VMELAPLGELRSYLQVNKYS-LDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRYMEdESY 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 342 YLSRDHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLML 421
Cdd:cd05056  163 YKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMLGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMT 242
                        250       260
                 ....*....|....*....|...
gi 157822719 422 SCWSRDPKQRPCFKDLCEKLSGI 444
Cdd:cd05056  243 KCWAYDPSKRPRFTELKAQLSDI 265
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
195-437 3.50e-69

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: 221.00  E-value: 3.50e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWK----GLVRVAVKVISRDNLLHQHT-FQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPK 269
Cdd:cd05063   11 KVIGAGEFGEVFRGILKmpgrKEVAVAIKTLKPGYTEKQRQdFLSEASIMGQFSHHNIIRLEGVVTKFKPAMIITEYMEN 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 270 GSLLQLLRDSDeKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKED---IYLSRD 346
Cdd:cd05063   91 GALDKYLRDHD-GEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRVLEDDpegTYTTSG 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 347 HNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLSCWSR 426
Cdd:cd05063  170 GKIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSFGERPYWDMSNHEVMKAINDGFRLPAPMDCPSAVYQLMLQCWQQ 249
                        250
                 ....*....|.
gi 157822719 427 DPKQRPCFKDL 437
Cdd:cd05063  250 DRARRPRFVDI 260
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
188-437 1.67e-67

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: 216.28  E-value: 1.67e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 188 REEFTLCKKLGSGYFGEVFEGLWKGLVRVAVKVIsRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELM 267
Cdd:cd05113    3 PKDLTFLKELGTGQFGVVKYGKWRGQYDVAIKMI-KEGSMSEDEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 268 PKGSLLQLLRDSdEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSR-D 346
Cdd:cd05113   82 ANGCLLNYLREM-RKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVLDDEYTSSvG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 347 HNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLSCWSR 426
Cdd:cd05113  161 SKFPVRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSLGKMPYERFTNSETVEHVSQGLRLYRPHLASEKVYTIMYSCWHE 240
                        250
                 ....*....|.
gi 157822719 427 DPKQRPCFKDL 437
Cdd:cd05113  241 KADERPTFKIL 251
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
187-441 7.54e-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: 215.32  E-value: 7.54e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 187 PREEFTLCKKLGSGYFGEVFEGLWKGL-----VRVAVKVISRD-NLLHQHTFQAEIQAMKKLRHKHILSLYAVATA--GD 258
Cdd:cd05038    2 EERHLKFIKQLGEGHFGSVELCRYDPLgdntgEQVAVKSLQPSgEEQHMSDFKREIEILRTLDHEYIVKYKGVCESpgRR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 259 PVYIITELMPKGSLLQLLRD-SDEKDLPilELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLV 337
Cdd:cd05038   82 SLRLIMEYLPSGSLRDYLQRhRDQIDLK--RLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAKVL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 338 KED---IYLSRDHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRG---QMPYP----------GMSNHETFLR-V 400
Cdd:cd05038  160 PEDkeyYYVKEPGESPIFWYAPECLRESRFSSASDVWSFGVTLYELFTYGdpsQSPPAlflrmigiaqGQMIVTRLLElL 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 157822719 401 DAGYRMPCPLECPPNIHKLMLSCWSRDPKQRPCFKDLCEKL 441
Cdd:cd05038  240 KSGERLPRPPSCPDEVYDLMKECWEYEPQDRPSFSDLILII 280
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
187-441 8.86e-67

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: 215.02  E-value: 8.86e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 187 PREEFTLCKKLGSGYFGEVFEGLWKGLVR------VAVKVI--SRDNLLHQhTFQAEIQAMKKLRHKHILSLYAVATAGD 258
Cdd:cd05049    3 KRDTIVLKRELGEGAFGKVFLGECYNLEPeqdkmlVAVKTLkdASSPDARK-DFEREAELLTNLQHENIVKFYGVCTEGD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 259 PVYIITELMPKGSLLQLLR------------DSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLC 326
Cdd:cd05049   82 PLLMVFEYMEHGDLNKFLRshgpdaaflaseDSAPGELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLVGTNLVV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 327 KVGDFGLARlvkeDIYLSRDHNV------PYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRV 400
Cdd:cd05049  162 KIGDFGMSR----DIYSTDYYRVgghtmlPIRWMPPESILYRKFTTESDVWSFGVVLWEIFTYGKQPWFQLSNTEVIECI 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 157822719 401 DAGYRMPCPLECPPNIHKLMLSCWSRDPKQRPCFKDLCEKL 441
Cdd:cd05049  238 TQGRLLQRPRTCPSEVYAVMLGCWKREPQQRLNIKDIHKRL 278
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
195-441 1.17e-66

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: 214.35  E-value: 1.17e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWK----GLVRVAVKVISRDNLLHQH-TFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPK 269
Cdd:cd05066   10 KVIGAGEFGEVCSGRLKlpgkREIPVAIKTLKAGYTEKQRrDFLSEASIMGQFDHPNIIHLEGVVTRSKPVMIVTEYMEN 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 270 GSLLQLLRDSDEKdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKED---IYLSRD 346
Cdd:cd05066   90 GSLDAFLRKHDGQ-FTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDpeaAYTTRG 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 347 HNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLSCWSR 426
Cdd:cd05066  169 GKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWEMSNQDVIKAIEEGYRLPAPMDCPAALHQLMLDCWQK 248
                        250
                 ....*....|....*
gi 157822719 427 DPKQRPCFKDLCEKL 441
Cdd:cd05066  249 DRNERPKFEQIVSIL 263
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
178-444 5.80e-66

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: 214.11  E-value: 5.80e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 178 LPHWDDWERPREEFTLCKKLGSGYFGEVFEGLWKGL--------VRVAVKVIsRDNLLHQ--HTFQAEIQAMKKL-RHKH 246
Cdd:cd05101   13 LPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIdkdkpkeaVTVAVKML-KDDATEKdlSDLVSEMEMMKMIgKHKN 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 247 ILSLYAVATAGDPVYIITELMPKGSLLQLLRDS--------------DEKDLPILELVDFASQVAEGMCYLESQNYIHRD 312
Cdd:cd05101   92 IINLLGACTQDGPLYVIVEYASKGNLREYLRARrppgmeysydinrvPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRD 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 313 LAARNVLVTENNLCKVGDFGLARLVKEDIYLSRDHN--VPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPG 390
Cdd:cd05101  172 LAARNVLVTENNVMKIADFGLARDINNIDYYKKTTNgrLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPG 251
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 157822719 391 MSNHETFLRVDAGYRMPCPLECPPNIHKLMLSCWSRDPKQRPCFKDLCEKLSGI 444
Cdd:cd05101  252 IPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRI 305
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
190-444 1.37e-65

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: 211.26  E-value: 1.37e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLCKKLGSGYFGEVFEGLWKGLVRVAVKVIsRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPK 269
Cdd:cd05114    5 ELTFMKELGSGLFGVVRLGKWRAQYKVAIKAI-REGAMSEEDFIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMEN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 270 GSLLQLLRDSDEKDLPILeLVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSRD-HN 348
Cdd:cd05114   84 GCLLNYLRQRRGKLSRDM-LLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRYVLDDQYTSSSgAK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 349 VPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLSCWSRDP 428
Cdd:cd05114  163 FPVKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTEGKMPFESKSNYEVVEMVSRGHRLYRPKLASKSVYEVMYSCWHEKP 242
                        250
                 ....*....|....*.
gi 157822719 429 KQRPCFKDLCEKLSGI 444
Cdd:cd05114  243 EGRPTFADLLRTITEI 258
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
184-441 1.43e-65

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: 212.14  E-value: 1.43e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 184 WERPREEFTLCKKLGSGYFGEVFEGLWKGLV------RVAVKVISRDNLLHQHT-FQAEIQAMKKLRHKHILSLYAVATA 256
Cdd:cd05061    1 WEVSREKITLLRELGQGSFGMVYEGNARDIIkgeaetRVAVKTVNESASLRERIeFLNEASVMKGFTCHHVVRLLGVVSK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 257 GDPVYIITELMPKG---SLLQLLRDSDEKD----LPIL-ELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKV 328
Cdd:cd05061   81 GQPTLVVMELMAHGdlkSYLRSLRPEAENNpgrpPPTLqEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 329 GDFGLARLVKEDIYLSRDHN--VPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRV-DAGYr 405
Cdd:cd05061  161 GDFGMTRDIYETDYYRKGGKglLPVRWMAPESLKDGVFTTSSDMWSFGVVLWEITSLAEQPYQGLSNEQVLKFVmDGGY- 239
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 157822719 406 MPCPLECPPNIHKLMLSCWSRDPKQRPCFKDLCEKL 441
Cdd:cd05061  240 LDQPDNCPERVTDLMRMCWQFNPKMRPTFLEIVNLL 275
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
190-441 1.45e-65

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: 211.85  E-value: 1.45e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLC-----KKLGSGYFGEVFEGLWKGL------VRVAVKVISRDNLLH-QHTFQAEIQAMKKLRHKHILSLYAVATAG 257
Cdd:cd05048    1 EIPLSavrflEELGEGAFGKVYKGELLGPsseesaISVAIKTLKENASPKtQQDFRREAELMSDLQHPNIVCLLGVCTKE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 258 DPVYIITELMPKGSLLQLL-----------RDSDEKDLPILELVDF---ASQVAEGMCYLESQNYIHRDLAARNVLVTEN 323
Cdd:cd05048   81 QPQCMLFEYMAHGDLHEFLvrhsphsdvgvSSDDDGTASSLDQSDFlhiAIQIAAGMEYLSSHHYVHRDLAARNCLVGDG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 324 NLCKVGDFGLARLVKEDIYLSRDHN--VPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVD 401
Cdd:cd05048  161 LTVKISDFGLSRDIYSSDYYRVQSKslLPVRWMPPEAILYGKFTTESDVWSFGVVLWEIFSYGLQPYYGYSNQEVIEMIR 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 157822719 402 AGYRMPCPLECPPNIHKLMLSCWSRDPKQRPCFKDLCEKL 441
Cdd:cd05048  241 SRQLLPCPEDCPARVYSLMVECWHEIPSRRPRFKEIHTRL 280
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
197-441 4.91e-64

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: 207.41  E-value: 4.91e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGLVR----VAVKVISRDNLLHQH-TFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGS 271
Cdd:cd05065   12 IGAGEFGEVCRGRLKLPGKreifVAIKTLKSGYTEKQRrDFLSEASIMGQFDHPNIIHLEGVVTKSRPVMIITEFMENGA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 272 LLQLLRDSDEKdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKED----IYLSR-D 346
Cdd:cd05065   92 LDSFLRQNDGQ-FTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLEDDtsdpTYTSSlG 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 347 HNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLSCWSR 426
Cdd:cd05065  171 GKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVINAIEQDYRLPPPMDCPTALHQLMLDCWQK 250
                        250
                 ....*....|....*
gi 157822719 427 DPKQRPCFKDLCEKL 441
Cdd:cd05065  251 DRNLRPKFGQIVNTL 265
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
178-444 1.46e-63

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: 207.56  E-value: 1.46e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 178 LPHWDDWERPREEFTLCKKLGSGYFGEVFEGLWKGL--------VRVAVKVISRDNLLHQHT-FQAEIQAMKKL-RHKHI 247
Cdd:cd05098    2 LPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLdkdkpnrvTKVAVKMLKSDATEKDLSdLISEMEMMKMIgKHKNI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 248 LSLYAVATAGDPVYIITELMPKGSLLQLLR--------------DSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDL 313
Cdd:cd05098   82 INLLGACTQDGPLYVIVEYASKGNLREYLQarrppgmeycynpsHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 314 AARNVLVTENNLCKVGDFGLARLVKEDIYLSRDHN--VPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGM 391
Cdd:cd05098  162 AARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNgrLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPGV 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 157822719 392 SNHETFLRVDAGYRMPCPLECPPNIHKLMLSCWSRDPKQRPCFKDLCEKLSGI 444
Cdd:cd05098  242 PVEELFKLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRI 294
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
184-442 3.39e-63

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: 206.19  E-value: 3.39e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 184 WERPREEFTLCKKLGSGYFGEVFEGLWKGLVR------VAVKVISRDNLLHQHtfQAEIQAMKKLRH-KHILS----LYA 252
Cdd:cd05054    2 WEFPRDRLKLGKPLGRGAFGKVIQASAFGIDKsatcrtVAVKMLKEGATASEH--KALMTELKILIHiGHHLNvvnlLGA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 253 VATAGDPVYIITELMPKGSLLQLLR---------------------DSDE---KDLPILELVDFASQVAEGMCYLESQNY 308
Cdd:cd05054   80 CTKPGGPLMVIVEFCKFGNLSNYLRskreefvpyrdkgardveeeeDDDElykEPLTLEDLICYSFQVARGMEFLASRKC 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 309 IHRDLAARNVLVTENNLCKVGDFGLARlvkeDIYLSRDH------NVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFS 382
Cdd:cd05054  160 IHRDLAARNILLSENNVVKICDFGLAR----DIYKDPDYvrkgdaRLPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFS 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157822719 383 RGQMPYPGMSNHETFL-RVDAGYRMPCPLECPPNIHKLMLSCWSRDPKQRPCFKDLCEKLS 442
Cdd:cd05054  236 LGASPYPGVQMDEEFCrRLKEGTRMRAPEYTTPEIYQIMLDCWHGEPKERPTFSELVEKLG 296
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
190-446 5.93e-62

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: 202.64  E-value: 5.93e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLCKKLGSGYFGEVFEGLWKGL-----VRVAVKVISRDNllHQHTFQA---EIQAMKKLRHKHILSLYAVATaGDPVY 261
Cdd:cd05057    8 ELEKGKVLGSGAFGTVYKGVWIPEgekvkIPVAIKVLREET--GPKANEEildEAYVMASVDHPHLVRLLGICL-SSQVQ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 262 IITELMPKGSLLQLLRDSDEKdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARL--VKE 339
Cdd:cd05057   85 LITQLMPLGCLLDYVRNHRDN-IGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGLAKLldVDE 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 340 DIYLSRDHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKL 419
Cdd:cd05057  164 KEYHAEGGKVPIKWMALESIQYRIYTHKSDVWSYGVTVWELMTFGAKPYEGIPAVEIPDLLEKGERLPQPPICTIDVYMV 243
                        250       260
                 ....*....|....*....|....*..
gi 157822719 420 MLSCWSRDPKQRPCFKDLCEKLSGITR 446
Cdd:cd05057  244 LVKCWMIDAESRPTFKELANEFSKMAR 270
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
178-444 7.11e-62

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: 204.10  E-value: 7.11e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 178 LPHWDDWERPREEFTLCKKLGSGYFGEVFEGLWKGL--------VRVAVKVISRDNLLHQHT-FQAEIQAMKKL-RHKHI 247
Cdd:cd05100    1 LPADPKWELSRTRLTLGKPLGEGCFGQVVMAEAIGIdkdkpnkpVTVAVKMLKDDATDKDLSdLVSEMEMMKMIgKHKNI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 248 LSLYAVATAGDPVYIITELMPKGSLLQLLRDS--------------DEKDLPILELVDFASQVAEGMCYLESQNYIHRDL 313
Cdd:cd05100   81 INLLGACTQDGPLYVLVEYASKGNLREYLRARrppgmdysfdtcklPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 314 AARNVLVTENNLCKVGDFGLARLVKEDIYLSRDHN--VPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGM 391
Cdd:cd05100  161 AARNVLVTEDNVMKIADFGLARDVHNIDYYKKTTNgrLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGI 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 157822719 392 SNHETFLRVDAGYRMPCPLECPPNIHKLMLSCWSRDPKQRPCFKDLCEKLSGI 444
Cdd:cd05100  241 PVEELFKLLKEGHRMDKPANCTHELYMIMRECWHAVPSQRPTFKQLVEDLDRV 293
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
191-439 2.13e-61

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 200.06  E-value: 2.13e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719   191 FTLCKKLGSGYFGEVFEGLWKGL-VRVAVKVISRDNLL-HQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMP 268
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTgKLVAIKVIKKKKIKkDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719   269 KGSLLQLLRDsdEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSRDHN 348
Cdd:smart00220  81 GGDLFDLLKK--RGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKLTTFVG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719   349 VPYkWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRV---DAGYRMPCPLECPPNIHKLMLSCWS 425
Cdd:smart00220 159 TPE-YMAPEVLLGKGYGKAVDIWSLGVILYELLT-GKPPFPGDDQLLELFKKigkPKPPFPPPEWDISPEAKDLIRKLLV 236
                          250
                   ....*....|....
gi 157822719   426 RDPKQRPCFKDLCE 439
Cdd:smart00220 237 KDPEKRLTAEEALQ 250
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
187-442 2.21e-61

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: 200.77  E-value: 2.21e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 187 PREEFTLCKKLGSGYFGEVFEGLWKGLVR------VAVKVI-SRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDP 259
Cdd:cd05046    3 PRSNLQEITTLGRGEFGEVFLAKAKGIEEeggetlVLVKALqKTKDENLQSEFRRELDMFRKLSHKNVVRLLGLCREAEP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 260 VYIITELMPKGSLLQLLRDSDEKDLPIL-------ELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFG 332
Cdd:cd05046   83 HYMILEYTDLGDLKQFLRATKSKDEKLKppplstkQKVALCTQIALGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 333 LARLV-KEDIYLSRDHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAG-YRMPCPL 410
Cdd:cd05046  163 LSKDVyNSEYYKLRNALIPLRWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTQGELPFYGLSDEEVLNRLQAGkLELPVPE 242
                        250       260       270
                 ....*....|....*....|....*....|..
gi 157822719 411 ECPPNIHKLMLSCWSRDPKQRPCFKDLCEKLS 442
Cdd:cd05046  243 GCPSRLYKLMTRCWAVNPKDRPSFSELVSALG 274
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
193-441 1.61e-60

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: 199.03  E-value: 1.61e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 193 LCKKLGSGYFGEVFEGL------WKGLVRVAVKVISRD-NLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITE 265
Cdd:cd05045    4 LGKTLGEGEFGKVVKATafrlkgRAGYTTVAVKMLKENaSSSELRDLLSEFNLLKQVNHPHVIKLYGACSQDGPLLLIVE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMPKGSLLQLLRDS----------------------DEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTEN 323
Cdd:cd05045   84 YAKYGSLRSFLRESrkvgpsylgsdgnrnssyldnpDERALTMGDLISFAWQISRGMQYLAEMKLVHRDLAARNVLVAEG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 324 NLCKVGDFGLARLV-KEDIYLSRDHN-VPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVD 401
Cdd:cd05045  164 RKMKISDFGLSRDVyEEDSYVKRSKGrIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIAPERLFNLLK 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 157822719 402 AGYRMPCPLECPPNIHKLMLSCWSRDPKQRPCFKDLCEKL 441
Cdd:cd05045  244 TGYRMERPENCSEEMYNLMLTCWKQEPDKRPTFADISKEL 283
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
178-442 3.56e-60

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: 200.84  E-value: 3.56e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 178 LPHWDDWERPREEFTLCKKLGSGYFGEVFEGLWKGL------VRVAVKVI-SRDNLLHQHTFQAEIQAMKKL-RHKHILS 249
Cdd:cd05106   27 LPYNEKWEFPRDNLQFGKTLGAGAFGKVVEATAFGLgkednvLRVAVKMLkASAHTDEREALMSELKILSHLgQHKNIVN 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 250 LYAVATAGDPVYIITELMPKGSLLQLLR-------------------DSDEKD--------------------------- 283
Cdd:cd05106  107 LLGACTHGGPVLVITEYCCYGDLLNFLRkkaetflnfvmalpeisetSSDYKNitlekkyirsdsgfssqgsdtyvemrp 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 284 ----------------------LPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDI 341
Cdd:cd05106  187 vsssssqssdskdeedtedswpLDLDDLLRFSSQVAQGMDFLASKNCIHRDVAARNVLLTDGRVAKICDFGLARDIMNDS 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 342 -YLSR-DHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLR-VDAGYRMPCPLECPPNIHK 418
Cdd:cd05106  267 nYVVKgNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGKSPYPGILVNSKFYKmVKRGYQMSRPDFAPPEIYS 346
                        330       340
                 ....*....|....*....|....
gi 157822719 419 LMLSCWSRDPKQRPCFKDLCEKLS 442
Cdd:cd05106  347 IMKMCWNLEPTERPTFSQISQLIQ 370
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
191-445 5.74e-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: 191.98  E-value: 5.74e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEGLWKG----LVRVAVKVISRDNLLHQHT--FQAEIQAMKKLRHKHILSLYAVATAGD------ 258
Cdd:cd05035    1 LKLGKILGEGEFGSVMEAQLKQddgsQLKVAVKTMKVDIHTYSEIeeFLSEAACMKDFDHPNVMRLIGVCFTASdlnkpp 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 259 -PVyIITELMPKGSLLQLLRDS----DEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGL 333
Cdd:cd05035   81 sPM-VILPFMKHGDLHSYLLYSrlggLPEKLPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVADFGL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 334 ARLVKEDIYLSRDH--NVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLE 411
Cdd:cd05035  160 SRKIYSGDYYRQGRisKMPVKWIALESLADNVYTSKSDVWSFGVTMWEIATRGQTPYPGVENHEIYDYLRNGNRLKQPED 239
                        250       260       270
                 ....*....|....*....|....*....|....
gi 157822719 412 CPPNIHKLMLSCWSRDPKQRPCFKDLCEKLSGIT 445
Cdd:cd05035  240 CLDEVYFLMYFCWTVDPKDRPTFTKLREVLENIL 273
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
184-437 8.74e-58

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: 191.79  E-value: 8.74e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 184 WERPREEFTLCKKLGSGYFGEVFEGLWKGLV------RVAVKVISRDNLLHQHT-FQAEIQAMKKLRHKHILSLYAVATA 256
Cdd:cd05062    1 WEVAREKITMSRELGQGSFGMVYEGIAKGVVkdepetRVAIKTVNEAASMRERIeFLNEASVMKEFNCHHVVRLLGVVSQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 257 GDPVYIITELMPKGSLLQLLRD--SDEKDLPIL------ELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKV 328
Cdd:cd05062   81 GQPTLVIMELMTRGDLKSYLRSlrPEMENNPVQappslkKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVKI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 329 GDFGLARLVKEDIYLSRDHN--VPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRM 406
Cdd:cd05062  161 GDFGMTRDIYETDYYRKGGKglLPVRWMSPESLKDGVFTTYSDVWSFGVVLWEIATLAEQPYQGMSNEQVLRFVMEGGLL 240
                        250       260       270
                 ....*....|....*....|....*....|.
gi 157822719 407 PCPLECPPNIHKLMLSCWSRDPKQRPCFKDL 437
Cdd:cd05062  241 DKPDNCPDMLFELMRMCWQYNPKMRPSFLEI 271
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
185-438 6.91e-57

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: 189.86  E-value: 6.91e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 185 ERPREEFTLCKKLGSGYFGEV---------------FEGLWK--GLVRVAVKVISRD-NLLHQHTFQAEIQAMKKLRHKH 246
Cdd:cd05051    1 EFPREKLEFVEKLGEGQFGEVhlceanglsdltsddFIGNDNkdEPVLVAVKMLRPDaSKNAREDFLKEVKIMSQLKDPN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 247 ILSLYAVATAGDPVYIITELMPKGSLLQLLRDSDEKD----------LPILELVDFASQVAEGMCYLESQNYIHRDLAAR 316
Cdd:cd05051   81 IVRLLGVCTRDEPLCMIVEYMENGDLNQFLQKHEAETqgasatnsktLSYGTLLYMATQIASGMKYLESLNFVHRDLATR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 317 NVLVTENNLCKVGDFGLAR-LVKEDIYLSRDHNV-PYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFS--RGQmPYPGMS 392
Cdd:cd05051  161 NCLVGPNYTIKIADFGMSRnLYSGDYYRIEGRAVlPIRWMAWESILLGKFTTKSDVWAFGVTLWEILTlcKEQ-PYEHLT 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 157822719 393 ------NHETFLRVDAGYR-MPCPLECPPNIHKLMLSCWSRDPKQRPCFKDLC 438
Cdd:cd05051  240 deqvieNAGEFFRDDGMEVyLSRPPNCPKEIYELMLECWRRDEEDRPTFREIH 292
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
197-437 7.12e-57

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: 187.09  E-value: 7.12e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGL-VRVAVKVISRDNLLHQ-HTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSLLQ 274
Cdd:cd00180    1 LGKGSFGKVYKARDKETgKKVAVKVIPKEKLKKLlEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSLKD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 275 LLRdSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSRDHN--VPYK 352
Cdd:cd00180   81 LLK-ENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTTGgtTPPY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 353 WTAPEALSRGHYSIKSDVWSFGVLLHEIfsrgqmpypgmsnhetflrvdagyrmpcplecpPNIHKLMLSCWSRDPKQRP 432
Cdd:cd00180  160 YAPPELLGGRYYGPKVDIWSLGVILYEL---------------------------------EELKDLIRRMLQYDPKKRP 206

                 ....*
gi 157822719 433 CFKDL 437
Cdd:cd00180  207 SAKEL 211
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
192-442 1.03e-56

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: 188.59  E-value: 1.03e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 192 TLCKKLGSGYFGEVFEGLWKGLVR----VAVKVIsRDNLL--HQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITE 265
Cdd:cd05064    8 KIERILGTGRFGELCRGCLKLPSKrelpVAIHTL-RAGCSdkQRRGFLAEALTLGQFDHSNIVRLEGVITRGNTMMIVTE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMPKGSLLQLLRdSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFG-LARLVKEDIYLS 344
Cdd:cd05064   87 YMSNGALDSFLR-KHEGQLVAGQLMGMLPGLASGMKYLSEMGYVHKGLAAHKVLVNSDLVCKISGFRrLQEDKSEAIYTT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 345 RDHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLSCW 424
Cdd:cd05064  166 MSGKSPVLWAAPEAIQYHHFSSASDVWSFGIVMWEVMSYGERPYWDMSGQDVIKAVEDGFRLPAPRNCPNLLHQLMLDCW 245
                        250
                 ....*....|....*...
gi 157822719 425 SRDPKQRPCFKDLCEKLS 442
Cdd:cd05064  246 QKERGERPRFSQIHSILS 263
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
190-446 3.37e-56

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: 187.52  E-value: 3.37e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLCKKLGSGYFGEVFEGLWK---GLVRVAVK-----VISRDNLlhqHTFQAEIQAMKKLRHKHILSLYAVATAG---- 257
Cdd:cd05075    1 KLALGKTLGEGEFGSVMEGQLNqddSVLKVAVKtmkiaICTRSEM---EDFLSEAVCMKEFDHPNVMRLIGVCLQNtese 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 258 ---DPVyIITELMPKGSLLQLLRDSDEKD----LPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGD 330
Cdd:cd05075   78 gypSPV-VILPFMKHGDLHSFLLYSRLGDcpvyLPTQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVAD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 331 FGLARLVKEDIYL--SRDHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPC 408
Cdd:cd05075  157 FGLSKKIYNGDYYrqGRISKMPVKWIAIESLADRVYTTKSDVWSFGVTMWEIATRGQTPYPGVENSEIYDYLRQGNRLKQ 236
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 157822719 409 PLECPPNIHKLMLSCWSRDPKQRPCFKDLCEKLSGITR 446
Cdd:cd05075  237 PPDCLDGLYELMSSCWLLNPKDRPSFETLRCELEKILK 274
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
187-444 4.03e-56

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: 187.43  E-value: 4.03e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 187 PREEFTLCKKLGSGYFGEVFEGLWK----GLVRVAVKVISRDNLLHQ--HTFQAEIQAMKKLRHKHILSLYAVATAGDPV 260
Cdd:cd05074    7 QEQQFTLGRMLGKGEFGSVREAQLKsedgSFQKVAVKMLKADIFSSSdiEEFLREAACMKEFDHPNVIKLIGVSLRSRAK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 261 ------YIITELMPKGSLLQLL---RDSDEK-DLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGD 330
Cdd:cd05074   87 grlpipMVILPFMKHGDLHTFLlmsRIGEEPfTLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNENMTVCVAD 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 331 FGLARLVKEDIYLSRD--HNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPC 408
Cdd:cd05074  167 FGLSKKIYSGDYYRQGcaSKLPVKWLALESLADNVYTTHSDVWAFGVTMWEIMTRGQTPYAGVENSEIYNYLIKGNRLKQ 246
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 157822719 409 PLECPPNIHKLMLSCWSRDPKQRPCFKDLCEKLSGI 444
Cdd:cd05074  247 PPDCLEDVYELMCQCWSPEPKCRPSFQHLRDQLELI 282
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
185-437 4.22e-56

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: 187.73  E-value: 4.22e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 185 ERPREEFTLCKKLGSGYFGEVFEGLWKGLV------RVAVKVISRD-NLLHQHTFQAEIQAMKKLRHKHILSLYAVATAG 257
Cdd:cd05050    1 EYPRNNIEYVRDIGQGAFGRVFQARAPGLLpyepftMVAVKMLKEEaSADMQADFQREAALMAEFDHPNIVKLLGVCAVG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 258 DPVYIITELMPKGSLLQLLRDSDEK--------------------DLPILELVDFASQVAEGMCYLESQNYIHRDLAARN 317
Cdd:cd05050   81 KPMCLLFEYMAYGDLNEFLRHRSPRaqcslshstssarkcglnplPLSCTEQLCIAKQVAAGMAYLSERKFVHRDLATRN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 318 VLVTENNLCKVGDFGLARLVKEDIYLSRDHN--VPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHE 395
Cdd:cd05050  161 CLVGENMVVKIADFGLSRNIYSADYYKASENdaIPIRWMPPESIFYNRYTTESDVWAYGVVLWEIFSYGMQPYYGMAHEE 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 157822719 396 TFLRVDAGYRMPCPLECPPNIHKLMLSCWSRDPKQRPCFKDL 437
Cdd:cd05050  241 VIYYVRDGNVLSCPDNCPLELYNLMRLCWSKLPSDRPSFASI 282
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
188-441 7.86e-56

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: 186.71  E-value: 7.86e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 188 REEFTLCKKLGSGYFGEVFEGLWKGL------VRVAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVY 261
Cdd:cd05092    4 RRDIVLKWELGEGAFGKVFLAECHNLlpeqdkMLVAVKALKEATESARQDFQREAELLTVLQHQHIVRFYGVCTEGEPLI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 262 IITELMPKGSLLQLLRdSDEKDLPILE--------------LVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCK 327
Cdd:cd05092   84 MVFEYMRHGDLNRFLR-SHGPDAKILDggegqapgqltlgqMLQIASQIASGMVYLASLHFVHRDLATRNCLVGQGLVVK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 328 VGDFGLARlvkeDIYLSRDHNV------PYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVD 401
Cdd:cd05092  163 IGDFGMSR----DIYSTDYYRVggrtmlPIRWMPPESILYRKFTTESDIWSFGVVLWEIFTYGKQPWYQLSNTEAIECIT 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 157822719 402 AGYRMPCPLECPPNIHKLMLSCWSRDPKQRPCFKDLCEKL 441
Cdd:cd05092  239 QGRELERPRTCPPEVYAIMQGCWQREPQQRHSIKDIHSRL 278
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
184-441 9.48e-55

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: 185.95  E-value: 9.48e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 184 WERPREEFTLCKKLGSGYFGEVFEGLWKGLVR------VAVKVISRDNLLHQHtfQAEIQAMKKLRH-KHILS----LYA 252
Cdd:cd05103    2 WEFPRDRLKLGKPLGRGAFGQVIEADAFGIDKtatcrtVAVKMLKEGATHSEH--RALMSELKILIHiGHHLNvvnlLGA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 253 VATAGDPVYIITELMPKGSLLQLLR------------------------------------------------------- 277
Cdd:cd05103   80 CTKPGGPLMVIVEFCKFGNLSAYLRskrsefvpyktkgarfrqgkdyvgdisvdlkrrldsitssqssassgfveeksls 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 278 DSDEKD----------LPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSR-- 345
Cdd:cd05103  160 DVEEEEagqedlykdfLTLEDLICYSFQVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDPDYVRkg 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 346 DHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFL-RVDAGYRMPCPLECPPNIHKLMLSCW 424
Cdd:cd05103  240 DARLPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFSLGASPYPGVKIDEEFCrRLKEGTRMRAPDYTTPEMYQTMLDCW 319
                        330
                 ....*....|....*..
gi 157822719 425 SRDPKQRPCFKDLCEKL 441
Cdd:cd05103  320 HGEPSQRPTFSELVEHL 336
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
184-441 1.28e-54

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: 185.21  E-value: 1.28e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 184 WERPREEFTLCKKLGSGYFGEVFEGLWKGLVR------VAVKVISRDNLLHQhtFQAEIQAMKKL----RHKHILSLYAV 253
Cdd:cd14207    2 WEFARERLKLGKSLGRGAFGKVVQASAFGIKKsptcrvVAVKMLKEGATASE--YKALMTELKILihigHHLNVVNLLGA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 254 AT-AGDPVYIITELMPKGSLLQLLR------------------------------------------------------- 277
Cdd:cd14207   80 CTkSGGPLMVIVEYCKYGNLSNYLKskrdffvtnkdtslqeelikekkeaeptggkkkrlesvtssesfassgfqedksl 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 278 ---DSDEKD------LPIL--ELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARlvkeDIYLSRD 346
Cdd:cd14207  160 sdvEEEEEDsgdfykRPLTmeDLISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLAR----DIYKNPD 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 347 H------NVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFL-RVDAGYRMPCPLECPPNIHKL 419
Cdd:cd14207  236 YvrkgdaRLPLKWMAPESIFDKIYSTKSDVWSYGVLLWEIFSLGASPYPGVQIDEDFCsKLKEGIRMRAPEFATSEIYQI 315
                        330       340
                 ....*....|....*....|..
gi 157822719 420 MLSCWSRDPKQRPCFKDLCEKL 441
Cdd:cd14207  316 MLDCWQGDPNERPRFSELVERL 337
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
195-434 3.20e-54

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: 181.70  E-value: 3.20e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLW---KGLVRVAVKVISRD--NLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYI--ITELM 267
Cdd:cd05116    1 GELGSGNFGTVKKGYYqmkKVVKTVAVKILKNEanDPALKDELLREANVMQQLDNPYIVRMIGICEAESWMLVmeMAELG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 268 PKGSLLQLLRDSDEKDlpILELVdfaSQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKED--IYLSR 345
Cdd:cd05116   81 PLNKFLQKNRHVTEKN--ITELV---HQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKALRADenYYKAQ 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 346 DHNV-PYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLSCW 424
Cdd:cd05116  156 THGKwPVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSYGQKPYKGMKGNEVTQMIEKGERMECPAGCPPEMYDLMKLCW 235
                        250
                 ....*....|
gi 157822719 425 SRDPKQRPCF 434
Cdd:cd05116  236 TYDVDERPGF 245
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
197-444 4.19e-54

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: 181.52  E-value: 4.19e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLW----KGLVRVAVKVISRDNLLHQ-HTFQAEIQAMKKLRHKHILSLYAVA--TAGDPVyIITELMPK 269
Cdd:cd05058    3 IGKGHFGCVYHGTLidsdGQKIHCAVKSLNRITDIEEvEQFLKEGIIMKDFSHPNVLSLLGIClpSEGSPL-VVLPYMKH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 270 GSLLQLLRdSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLS-RDHN 348
Cdd:cd05058   82 GDLRNFIR-SETHNPTVKDLIGFGLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLARDIYDKEYYSvHNHT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 349 ---VPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLSCWS 425
Cdd:cd05058  161 gakLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPDVDSFDITVYLLQGRRLLQPEYCPDPLYEVMLSCWH 240
                        250
                 ....*....|....*....
gi 157822719 426 RDPKQRPCFKDLCEKLSGI 444
Cdd:cd05058  241 PKPEMRPTFSELVSRISQI 259
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
178-441 5.00e-54

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: 184.72  E-value: 5.00e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 178 LPHWDDWERPREEFTLCKKLGSGYFGEVFEGLWKGLVR------VAVKVI-SRDNLLHQHTFQAEIQAMKKL-RHKHILS 249
Cdd:cd05104   24 LPYDHKWEFPRDRLRFGKTLGAGAFGKVVEATAYGLAKadsamtVAVKMLkPSAHSTEREALMSELKVLSYLgNHINIVN 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 250 LYAVATAGDPVYIITELMPKGSLLQLLR---------------------------------------------------- 277
Cdd:cd05104  104 LLGACTVGGPTLVITEYCCYGDLLNFLRrkrdsficpkfedlaeaalyrnllhqremacdslneymdmkpsvsyvvptka 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 278 ---------------------DSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARL 336
Cdd:cd05104  184 dkrrgvrsgsyvdqdvtseilEEDELALDTEDLLSFSYQVAKGMEFLASKNCIHRDLAARNILLTHGRITKICDFGLARD 263
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 337 VKEDI-YLSR-DHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLR-VDAGYRMPCPLECP 413
Cdd:cd05104  264 IRNDSnYVVKgNARLPVKWMAPESIFECVYTFESDVWSYGILLWEIFSLGSSPYPGMPVDSKFYKmIKEGYRMDSPEFAP 343
                        330       340
                 ....*....|....*....|....*...
gi 157822719 414 PNIHKLMLSCWSRDPKQRPCFKDLCEKL 441
Cdd:cd05104  344 SEMYDIMRSCWDADPLKRPTFKQIVQLI 371
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
185-441 7.46e-54

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: 182.11  E-value: 7.46e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 185 ERPREEFTLCKKLGSGYFGEVF----EGLWKGL-------------VRVAVKVISRD-NLLHQHTFQAEIQAMKKLRHKH 246
Cdd:cd05095    1 EFPRKLLTFKEKLGEGQFGEVHlceaEGMEKFMdkdfalevsenqpVLVAVKMLRADaNKNARNDFLKEIKIMSRLKDPN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 247 ILSLYAVATAGDPVYIITELMPKGSLLQLLR----DSDEKDLPILELVDF------ASQVAEGMCYLESQNYIHRDLAAR 316
Cdd:cd05095   81 IIRLLAVCITDDPLCMITEYMENGDLNQFLSrqqpEGQLALPSNALTVSYsdlrfmAAQIASGMKYLSSLNFVHRDLATR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 317 NVLVTENNLCKVGDFGLAR-LVKEDIYLSRDHNV-PYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQ-MPYPGMSN 393
Cdd:cd05095  161 NCLVGKNYTIKIADFGMSRnLYSGDYYRIQGRAVlPIRWMSWESILLGKFTTASDVWAFGVTLWETLTFCReQPYSQLSD 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 157822719 394 HET------FLRvDAGYR--MPCPLECPPNIHKLMLSCWSRDPKQRPCFKDLCEKL 441
Cdd:cd05095  241 EQVientgeFFR-DQGRQtyLPQPALCPDSVYKLMLSCWRRDTKDRPSFQEIHTLL 295
SH2_PTK6_Brk cd10358
Src homology 2 domain found in protein-tyrosine kinase-6 (PTK6) which is also known as breast ...
75-174 1.01e-53

Src homology 2 domain found in protein-tyrosine kinase-6 (PTK6) which is also known as breast tumor kinase (Brk); Human protein-tyrosine kinase-6 (PTK6, also known as breast tumor kinase (Brk)) is a member of the non-receptor protein-tyrosine kinase family and is expressed in two-thirds of all breast tumors. PTK6 (9). PTK6 contains a SH3 domain, a SH2 domain, and catalytic domains. For the case of the non-receptor protein-tyrosine kinases, the SH2 domain is typically involved in negative regulation of kinase activity by binding to a phosphorylated tyrosine residue near to the C terminus. The C-terminal sequence of PTK6 (PTSpYENPT where pY is phosphotyrosine) is thought to be a self-ligand for the SH2 domain. The structure of the SH2 domain resembles other SH2 domains except for a centrally located four-stranded antiparallel beta-sheet (strands betaA, betaB, betaC, and betaD). There are also differences in the loop length which might be responsible for PTK6 ligand specificity. There are two possible means of regulation of PTK6: autoinhibitory with the phosphorylation of Tyr playing a role in its negative regulation and autophosphorylation at this site, though it has been shown that PTK6 might phosphorylate signal transduction-associated proteins Sam68 and signal transducing adaptor family member 2 (STAP/BKS) in vivo. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198221  Cd Length: 100  Bit Score: 174.94  E-value: 1.01e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719  75 SEPWFFGCISRSEAMHRLQSEDYPKGTFLIRVSQKPGADYVLSVWDAEAVRHYRIWRNSAGRLHLNEVVSFSSLSELVNY 154
Cdd:cd10358    1 SEPWFFGCISRSEAVRRLQAEGNATGAFLIRVSEKPSADYVLSVRDTQAVRHYKIWRRAGGRLHLNEAVSFLSLPELVNY 80
                         90       100
                 ....*....|....*....|
gi 157822719 155 HKTHNLSPGLQLSMACWKLK 174
Cdd:cd10358   81 HRAQSLSHGLRLAAPCRKHE 100
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
178-444 3.27e-53

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: 183.30  E-value: 3.27e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 178 LPHWDDWERPREEFTLCKKLGSGYFGEVFEGLWKGLVR------VAVKVI---SRDNllHQHTFQAEIQAMKKL-RHKHI 247
Cdd:cd05105   26 LPYDSRWEFPRDGLVLGRILGSGAFGKVVEGTAYGLSRsqpvmkVAVKMLkptARSS--EKQALMSELKIMTHLgPHLNI 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 248 LSLYAVATAGDPVYIITEL------------------------------------------------------------- 266
Cdd:cd05105  104 VNLLGACTKSGPIYIITEYcfygdlvnylhknrdnflsrhpekpkkdldifginpadestrsyvilsfenkgdymdmkqa 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 267 ---------------------------------MPKGSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDL 313
Cdd:cd05105  184 dttqyvpmleikeaskysdiqrsnydrpasykgSNDSEVKNLLSDDGSEGLTTLDLLSFTYQVARGMEFLASKNCVHRDL 263
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 314 AARNVLVTENNLCKVGDFGLARLVKEDI-YLSRDHN-VPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGM 391
Cdd:cd05105  264 AARNVLLAQGKIVKICDFGLARDIMHDSnYVSKGSTfLPVKWMAPESIFDNLYTTLSDVWSYGILLWEIFSLGGTPYPGM 343
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 157822719 392 SNHETFL-RVDAGYRMPCPLECPPNIHKLMLSCWSRDPKQRPCFKDLCEKLSGI 444
Cdd:cd05105  344 IVDSTFYnKIKSGYRMAKPDHATQEVYDIMVKCWNSEPEKRPSFLHLSDIVESL 397
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
184-441 3.60e-52

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: 178.63  E-value: 3.60e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 184 WERPREEFTLCKKLGSGYFGEVFEGLWKGLVR------VAVKVISRDNLLHQHtfQAEIQAMKKL----RHKHILSLYAV 253
Cdd:cd05102    2 WEFPRDRLRLGKVLGHGAFGKVVEASAFGIDKssscetVAVKMLKEGATASEH--KALMSELKILihigNHLNVVNLLGA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 254 ATAGD-PVYIITELMPKGSLLQLLRDSDEKDLPILE-------------------------------------------- 288
Cdd:cd05102   80 CTKPNgPLMVIVEFCKYGNLSNFLRAKREGFSPYRErsprtrsqvrsmveavradrrsrqgsdrvasftestsstnqprq 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 289 --------------LVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARlvkeDIYLSRDH------N 348
Cdd:cd05102  160 evddlwqspltmedLICYSFQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLAR----DIYKDPDYvrkgsaR 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 349 VPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFL-RVDAGYRMPCPLECPPNIHKLMLSCWSRD 427
Cdd:cd05102  236 LPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSLGASPYPGVQINEEFCqRLKDGTRMRAPEYATPEIYRIMLSCWHGD 315
                        330
                 ....*....|....
gi 157822719 428 PKQRPCFKDLCEKL 441
Cdd:cd05102  316 PKERPTFSDLVEIL 329
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
195-446 7.87e-51

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: 173.60  E-value: 7.87e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLW--KG---LVRVAVKVIsrDNLLHQHTFQA---EIQAMKKLRHKHILSLYAVAtAGDPVYIITEL 266
Cdd:cd05111   13 KVLGSGVFGTVHKGIWipEGdsiKIPVAIKVI--QDRSGRQSFQAvtdHMLAIGSLDHAYIVRLLGIC-PGASLQLVTQL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 267 MPKGSLLQLLRDSDEKDLPILeLVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKED--IYLS 344
Cdd:cd05111   90 LPLGSLLDHVRQHRGSLGPQL-LLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQVQVADFGVADLLYPDdkKYFY 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 345 RDHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLSCW 424
Cdd:cd05111  169 SEAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWEMMTFGAEPYAGMRLAEVPDLLEKGERLAQPQICTIDVYMVMVKCW 248
                        250       260
                 ....*....|....*....|..
gi 157822719 425 SRDPKQRPCFKDLCEKLSGITR 446
Cdd:cd05111  249 MIDENIRPTFKELANEFTRMAR 270
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
188-437 1.14e-50

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: 173.27  E-value: 1.14e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 188 REEFTLCKKLGSGYFGEVFEGLWKGL------VRVAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVY 261
Cdd:cd05094    4 RRDIVLKRELGEGAFGKVFLAECYNLsptkdkMLVAVKTLKDPTLAARKDFQREAELLTNLQHDHIVKFYGVCGDGDPLI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 262 IITELMPKGSLLQLLRD--------------SDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCK 327
Cdd:cd05094   84 MVFEYMKHGDLNKFLRAhgpdamilvdgqprQAKGELGLSQMLHIATQIASGMVYLASQHFVHRDLATRNCLVGANLLVK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 328 VGDFGLAR-LVKEDIYLSRDHN-VPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYR 405
Cdd:cd05094  164 IGDFGMSRdVYSTDYYRVGGHTmLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEVIECITQGRV 243
                        250       260       270
                 ....*....|....*....|....*....|..
gi 157822719 406 MPCPLECPPNIHKLMLSCWSRDPKQRPCFKDL 437
Cdd:cd05094  244 LERPRVCPKEVYDIMLGCWQREPQQRLNIKEI 275
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
185-441 1.83e-50

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: 172.50  E-value: 1.83e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 185 ERPREEFTLCKKLGSGYFGEVFEG--LWKGLVR---VAVKVISRDNLLHQHT-FQAEIQAMKKLRHKHILSLYAVATAGD 258
Cdd:cd05090    1 ELPLSAVRFMEELGECAFGKIYKGhlYLPGMDHaqlVAIKTLKDYNNPQQWNeFQQEASLMTELHHPNIVCLLGVVTQEQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 259 PVYIITELMPKGSLLQLL------------RDSDEKDLPILELVDF---ASQVAEGMCYLESQNYIHRDLAARNVLVTEN 323
Cdd:cd05090   81 PVCMLFEFMNQGDLHEFLimrsphsdvgcsSDEDGTVKSSLDHGDFlhiAIQIAAGMEYLSSHFFVHKDLAARNILVGEQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 324 NLCKVGDFGLAR-LVKEDIYLSRDHNV-PYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVD 401
Cdd:cd05090  161 LHVKISDLGLSReIYSSDYYRVQNKSLlPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVR 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 157822719 402 AGYRMPCPLECPPNIHKLMLSCWSRDPKQRPCFKDLCEKL 441
Cdd:cd05090  241 KRQLLPCSEDCPPRMYSLMTECWQEIPSRRPRFKDIHARL 280
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
197-437 6.81e-50

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: 171.23  E-value: 6.81e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGL-----VRVAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVA-TAGDP-VYIITELMPK 269
Cdd:cd05081   12 LGKGNFGSVELCRYDPLgdntgALVAVKQLQHSGPDQQRDFQREIQILKALHSDFIVKYRGVSyGPGRRsLRLVMEYLPS 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 270 GSLlqllRDSDEKDLPILE---LVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKED--IYLS 344
Cdd:cd05081   92 GCL----RDFLQRHRARLDasrLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLLPLDkdYYVV 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 345 RDH-NVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQmpyPGMSNHETFLR-----------------VDAGYRM 406
Cdd:cd05081  168 REPgQSPIFWYAPESLSDNIFSRQSDVWSFGVVLYELFTYCD---KSCSPSAEFLRmmgcerdvpalcrllelLEEGQRL 244
                        250       260       270
                 ....*....|....*....|....*....|.
gi 157822719 407 PCPLECPPNIHKLMLSCWSRDPKQRPCFKDL 437
Cdd:cd05081  245 PAPPACPAEVHELMKLCWAPSPQDRPSFSAL 275
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
197-442 7.81e-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: 170.61  E-value: 7.81e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWK--GL-VRVAVKVISRDNLLHQH-TFQAEIQAMKKL-RHKHILSLYAVATAGDPVYIITELMPKGS 271
Cdd:cd05047    3 IGEGNFGQVLKARIKkdGLrMDAAIKRMKEYASKDDHrDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPHGN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 272 LLQLLRDSD--EKD------------LPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARlv 337
Cdd:cd05047   83 LLDFLRKSRvlETDpafaianstastLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR-- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 338 KEDIYLSRDHN-VPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNI 416
Cdd:cd05047  161 GQEVYVKKTMGrLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPLNCDDEV 240
                        250       260
                 ....*....|....*....|....*.
gi 157822719 417 HKLMLSCWSRDPKQRPCFKDLCEKLS 442
Cdd:cd05047  241 YDLMRQCWREKPYERPSFAQILVSLN 266
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
188-444 8.85e-50

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: 170.89  E-value: 8.85e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 188 REEFTLCKKLGSGYFGEVFEGLWK----GLVRVAVKVISRDNLLHQHT--FQAEIQAMKKLRHKHILSLYAVATAGDPVY 261
Cdd:cd14204    6 RNLLSLGKVLGEGEFGSVMEGELQqpdgTNHKVAVKTMKLDNFSQREIeeFLSEAACMKDFNHPNVIRLLGVCLEVGSQR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 262 I-----ITELMPKGSLLQ-LLR---DSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFG 332
Cdd:cd14204   86 IpkpmvILPFMKYGDLHSfLLRsrlGSGPQHVPLQTLLKFMIDIALGMEYLSSRNFLHRDLAARNCMLRDDMTVCVADFG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 333 LARLVKEDIYL--SRDHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPL 410
Cdd:cd14204  166 LSKKIYSGDYYrqGRIAKMPVKWIAVESLADRVYTVKSDVWAFGVTMWEIATRGMTPYPGVQNHEIYDYLLHGHRLKQPE 245
                        250       260       270
                 ....*....|....*....|....*....|....
gi 157822719 411 ECPPNIHKLMLSCWSRDPKQRPCFKDLCEKLSGI 444
Cdd:cd14204  246 DCLDELYDIMYSCWRSDPTDRPTFTQLRENLEKL 279
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
196-441 1.12e-49

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: 170.13  E-value: 1.12e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 196 KLGSGYFGEVFEGLWK---GLVRVAVKVISRDNLLH-QHTFQAEIQAMKKLRHKHILSLYAVATAgDPVYIITELMPKGS 271
Cdd:cd05115   11 ELGSGNFGCVKKGVYKmrkKQIDVAIKVLKQGNEKAvRDEMMREAQIMHQLDNPYIVRMIGVCEA-EALMLVMEMASGGP 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 272 LLQLLrdSDEKD-LPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKED--IYLSRDHN 348
Cdd:cd05115   90 LNKFL--SGKKDeITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSKALGADdsYYKARSAG 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 349 V-PYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLSCWSRD 427
Cdd:cd05115  168 KwPLKWYAPECINFRKFSSRSDVWSYGVTMWEAFSYGQKPYKKMKGPEVMSFIEQGKRMDCPAECPPEMYALMSDCWIYK 247
                        250
                 ....*....|....
gi 157822719 428 PKQRPCFKDLCEKL 441
Cdd:cd05115  248 WEDRPNFLTVEQRM 261
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
195-441 1.49e-49

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: 170.20  E-value: 1.49e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWKGLV------RVAVKVIS-RDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELM 267
Cdd:cd05091   12 EELGEDRFGKVYKGHLFGTApgeqtqAVAIKTLKdKAEGPLREEFRHEAMLRSRLQHPNIVCLLGVVTKEQPMSMIFSYC 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 268 PKGSLLQLL-----------RDSDEKDLPILELVDF---ASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGL 333
Cdd:cd05091   92 SHGDLHEFLvmrsphsdvgsTDDDKTVKSTLEPADFlhiVTQIAAGMEYLSSHHVVHKDLATRNVLVFDKLNVKISDLGL 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 334 ARLV-KEDIY-LSRDHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLE 411
Cdd:cd05091  172 FREVyAADYYkLMGNSLLPIRWMSPEAIMYGKFSIDSDIWSYGVVLWEVFSYGLQPYCGYSNQDVIEMIRNRQVLPCPDD 251
                        250       260       270
                 ....*....|....*....|....*....|
gi 157822719 412 CPPNIHKLMLSCWSRDPKQRPCFKDLCEKL 441
Cdd:cd05091  252 CPAWVYTLMLECWNEFPSRRPRFKDIHSRL 281
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
190-446 2.91e-49

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: 169.43  E-value: 2.91e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLCKKLGSGYFGEVFEGLW-----KGLVRVAVKVIsRDNLLHQHTFQA--EIQAMKKLRHKHILSLYAVATAGDpVYI 262
Cdd:cd05109    8 ELKKVKVLGSGAFGTVYKGIWipdgeNVKIPVAIKVL-RENTSPKANKEIldEAYVMAGVGSPYVCRLLGICLTST-VQL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 263 ITELMPKGSLLQLLRDSDEKdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARL--VKED 340
Cdd:cd05109   86 VTQLMPYGCLLDYVRENKDR-IGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLARLldIDET 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 341 IYLSRDHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLM 420
Cdd:cd05109  165 EYHADGGKVPIKWMALESILHRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIM 244
                        250       260
                 ....*....|....*....|....*.
gi 157822719 421 LSCWSRDPKQRPCFKDLCEKLSGITR 446
Cdd:cd05109  245 VKCWMIDSECRPRFRELVDEFSRMAR 270
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
195-441 3.09e-49

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: 169.31  E-value: 3.09e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVfeglwkGLVR-----------VAVKVISRDN-LLHQHTFQAEIQAMKKLRHKHILSLYAVAT--AGDPV 260
Cdd:cd05080   10 RDLGEGHFGKV------SLYCydptndgtgemVAVKALKADCgPQHRSGWKQEIDILKTLYHENIVKYKGCCSeqGGKSL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 261 YIITELMPKGSLLQLLrdsDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKE- 339
Cdd:cd05080   84 QLIMEYVPLGSLRDYL---PKHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAKAVPEg 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 340 DIY--LSRDHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQmpyPGMSNHETFLR-----------------V 400
Cdd:cd05080  161 HEYyrVREDGDSPVFWYAPECLKEYKFYYASDVWSFGVTLYELLTHCD---SSQSPPTKFLEmigiaqgqmtvvrlielL 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 157822719 401 DAGYRMPCPLECPPNIHKLMLSCWSRDPKQRPCFKDLCEKL 441
Cdd:cd05080  238 ERGERLPCPDKCPQEVYHLMKNCWETEASFRPTFENLIPIL 278
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
190-446 3.71e-49

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: 170.20  E-value: 3.71e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLCKKLGSGYFGEVFEGLW-----KGLVRVAVKVI--SRDNLLHQHTFQaEIQAMKKLRHKHILSLYAVATAgDPVYI 262
Cdd:cd05108    8 EFKKIKVLGSGAFGTVYKGLWipegeKVKIPVAIKELreATSPKANKEILD-EAYVMASVDNPHVCRLLGICLT-STVQL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 263 ITELMPKGSLLQLLRDSDEKdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLV--KED 340
Cdd:cd05108   86 ITQLMPFGCLLDYVREHKDN-IGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLgaEEK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 341 IYLSRDHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLM 420
Cdd:cd05108  165 EYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIM 244
                        250       260
                 ....*....|....*....|....*.
gi 157822719 421 LSCWSRDPKQRPCFKDLCEKLSGITR 446
Cdd:cd05108  245 VKCWMIDADSRPKFRELIIEFSKMAR 270
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
178-437 9.46e-49

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: 171.35  E-value: 9.46e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 178 LPHWDDWERPREEFTLCKKLGSGYFGEVFEGLWKGL------VRVAVKVI-SRDNLLHQHTFQAEIQAMKKL-RHKHILS 249
Cdd:cd05107   26 LPYDSAWEMPRDNLVLGRTLGSGAFGRVVEATAHGLshsqstMKVAVKMLkSTARSSEKQALMSELKIMSHLgPHLNIVN 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 250 LYAVATAGDPVYIITE---------------------------------------LMPKGSLLQLLRDSD------EKDL 284
Cdd:cd05107  106 LLGACTKGGPIYIITEycrygdlvdylhrnkhtflqyyldknrddgslisggstpLSQRKSHVSLGSESDggymdmSKDE 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 285 PI---------------------------------------------------LELVDFASQVAEGMCYLESQNYIHRDL 313
Cdd:cd05107  186 SAdyvpmqdmkgtvkyadiessnyespydqylpsapertrrdtlinespalsyMDLVGFSYQVANGMEFLASKNCVHRDL 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 314 AARNVLVTENNLCKVGDFGLAR-LVKEDIYLSRDHN-VPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGM 391
Cdd:cd05107  266 AARNVLICEGKLVKICDFGLARdIMRDSNYISKGSTfLPLKWMAPESIFNNLYTTLSDVWSFGILLWEIFTLGGTPYPEL 345
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 157822719 392 SNHETFLR-VDAGYRMPCPLECPPNIHKLMLSCWSRDPKQRPCFKDL 437
Cdd:cd05107  346 PMNEQFYNaIKRGYRMAKPAHASDEIYEIMQKCWEEKFEIRPDFSQL 392
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
185-437 2.03e-48

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: 167.46  E-value: 2.03e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 185 ERPREEFTLCKKLGSGYFGEVF----EGLWKGL-----------VRVAVKVISRD-NLLHQHTFQAEIQAMKKLRHKHIL 248
Cdd:cd05097    1 EFPRQQLRLKEKLGEGQFGEVHlceaEGLAEFLgegapefdgqpVLVAVKMLRADvTKTARNDFLKEIKIMSRLKNPNII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 249 SLYAVATAGDPVYIITELMPKGSLLQLLRDSD-------EKDLP---ILELVDFASQVAEGMCYLESQNYIHRDLAARNV 318
Cdd:cd05097   81 RLLGVCVSDDPLCMITEYMENGDLNQFLSQREiestfthANNIPsvsIANLLYMAVQIASGMKYLASLNFVHRDLATRNC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 319 LVTENNLCKVGDFGLAR-LVKEDIYLSRDHNV-PYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSR-GQMPYPGMSNHE 395
Cdd:cd05097  161 LVGNHYTIKIADFGMSRnLYSGDYYRIQGRAVlPIRWMAWESILLGKFTTASDVWAFGVTLWEMFTLcKEQPYSLLSDEQ 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157822719 396 T------FLRvDAG---YRMPCPLeCPPNIHKLMLSCWSRDPKQRPCFKDL 437
Cdd:cd05097  241 VientgeFFR-NQGrqiYLSQTPL-CPSPVFKLMMRCWSRDIKDRPTFNKI 289
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
195-444 3.51e-48

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: 166.73  E-value: 3.51e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWKGLVR-----VAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVA-TAG-DPVYIITELM 267
Cdd:cd14205   10 QQLGKGNFGSVEMCRYDPLQDntgevVAVKKLQHSTEEHLRDFEREIEILKSLQHDNIVKYKGVCySAGrRNLRLIMEYL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 268 PKGSLLQLLRDSDEKdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLV---KEDIYLS 344
Cdd:cd14205   90 PYGSLRDYLQKHKER-IDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLpqdKEYYKVK 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 345 RDHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQmpyPGMSNHETFLR------------------VDAGYRM 406
Cdd:cd14205  169 EPGESPIFWYAPESLTESKFSVASDVWSFGVVLYELFTYIE---KSKSPPAEFMRmigndkqgqmivfhlielLKNNGRL 245
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 157822719 407 PCPLECPPNIHKLMLSCWSRDPKQRPCFKDLCEKLSGI 444
Cdd:cd14205  246 PRPDGCPDEIYMIMTECWNNNVNQRPSFRDLALRVDQI 283
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
189-442 5.53e-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: 166.71  E-value: 5.53e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFEGLWK--GL-VRVAVKVISRDNLLHQH-TFQAEIQAMKKL-RHKHILSLYAVATAGDPVYII 263
Cdd:cd05089    2 EDIKFEDVIGEGNFGQVIKAMIKkdGLkMNAAIKMLKEFASENDHrDFAGELEVLCKLgHHPNIINLLGACENRGYLYIA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 264 TELMPKGSLLQLLRDSD--EKD------------LPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVG 329
Cdd:cd05089   82 IEYAPYGNLLDFLRKSRvlETDpafakehgtastLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSKIA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 330 DFGLARlvKEDIYLSRDHN-VPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPC 408
Cdd:cd05089  162 DFGLSR--GEEVYVKKTMGrLPVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRMEK 239
                        250       260       270
                 ....*....|....*....|....*....|....
gi 157822719 409 PLECPPNIHKLMLSCWSRDPKQRPCFKDLCEKLS 442
Cdd:cd05089  240 PRNCDDEVYELMRQCWRDRPYERPPFSQISVQLS 273
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
191-432 2.63e-47

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: 163.53  E-value: 2.63e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEGLWKGLVR-VAVKVISRDNLLHQHT---FQAEIQAMKKLRHKHILSLYAVATAGDPVYIITEL 266
Cdd:cd14014    2 YRLVRLLGRGGMGEVYRARDTLLGRpVAIKVLRPELAEDEEFrerFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 267 MPKGSLLQLLRdsDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDiYLSRD 346
Cdd:cd14014   82 VEGGSLADLLR--ERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDS-GLTQT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 347 HNVPYK--WTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRVDAGYRMPCPL---ECPPNIHKLML 421
Cdd:cd14014  159 GSVLGTpaYMAPEQARGGPVDPRSDIYSLGVVLYELLT-GRPPFDGDSPAAVLAKHLQEAPPPPSPlnpDVPPALDAIIL 237
                        250
                 ....*....|.
gi 157822719 422 SCWSRDPKQRP 432
Cdd:cd14014  238 RALAKDPEERP 248
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
188-442 4.14e-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: 163.78  E-value: 4.14e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 188 REEFTLCKKLGSGYFGEVFEGLW---KGLVR-VAVK-VISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATA-GDPVY 261
Cdd:cd05043    5 RERVTLSDLLQEGTFGRIFHGILrdeKGKEEeVLVKtVKDHASEIQVTMLLQESSLLYGLSHQNLLPILHVCIEdGEKPM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 262 IITELMPKGSL---LQLLRDSDEKD---LPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLAR 335
Cdd:cd05043   85 VLYPYMNWGNLklfLQQCRLSEANNpqaLSTQQLVHMALQIACGMSYLHRRGVIHKDIAARNCVIDDELQVKITDNALSR 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 336 LVKEDIY--LSRDHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECP 413
Cdd:cd05043  165 DLFPMDYhcLGDNENRPIKWMSLESLVNKEYSSASDVWSFGVLLWELMTLGQTPYVEIDPFEMAAYLKDGYRLAQPINCP 244
                        250       260
                 ....*....|....*....|....*....
gi 157822719 414 PNIHKLMLSCWSRDPKQRPCFKDLCEKLS 442
Cdd:cd05043  245 DELFAVMACCWALDPEERPSFQQLVQCLT 273
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
188-446 4.82e-47

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: 163.67  E-value: 4.82e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 188 REEFTLCKKLGSGYFGEVFEGLWKGL------VRVAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVY 261
Cdd:cd05093    4 RHNIVLKRELGEGAFGKVFLAECYNLcpeqdkILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 262 IITELMPKGSLLQLLR-----------DSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGD 330
Cdd:cd05093   84 MVFEYMKHGDLNKFLRahgpdavlmaeGNRPAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGD 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 331 FGLARLV-KEDIYLSRDHN-VPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPC 408
Cdd:cd05093  164 FGMSRDVySTDYYRVGGHTmLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQR 243
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 157822719 409 PLECPPNIHKLMLSCWSRDPKQRPCFKDLCEKLSGITR 446
Cdd:cd05093  244 PRTCPKEVYDLMLGCWQREPHMRLNIKEIHSLLQNLAK 281
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
195-444 7.61e-46

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: 160.48  E-value: 7.61e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVF------EGLWKGlVRVAVKVI---SRDNllHQHTFQAEIQAMKKLRHKHILSLYAVAT--AGDPVYII 263
Cdd:cd05079   10 RDLGEGHFGKVElcrydpEGDNTG-EQVAVKSLkpeSGGN--HIADLKKEIEILRNLYHENIVKYKGICTedGGNGIKLI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 264 TELMPKGSLLQLLRDSDEKdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKED--- 340
Cdd:cd05079   87 MEFLPSGSLKEYLPRNKNK-INLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDkey 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 341 IYLSRDHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSnheTFLR-----------------VDAG 403
Cdd:cd05079  166 YTVKDDLDSPVFWYAPECLIQSKFYIASDVWSFGVTLYELLTYCDSESSPMT---LFLKmigpthgqmtvtrlvrvLEEG 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 157822719 404 YRMPCPLECPPNIHKLMLSCWSRDPKQRPCFKDLCEKLSGI 444
Cdd:cd05079  243 KRLPRPPNCPEEVYQLMRKCWEFQPSKRTTFQNLIEGFEAI 283
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
190-439 1.20e-45

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: 158.93  E-value: 1.20e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLCKKLGSGYFGEVFEGL-WK-GLVrVAVKVISRDNLLHQ--HTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITE 265
Cdd:cd06627    1 NYQLGDLIGRGAFGSVYKGLnLNtGEF-VAIKQISLEKIPKSdlKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMPKGSLLQLLRDSDekDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLA-RLVKEDiylS 344
Cdd:cd06627   80 YVENGSLASIIKKFG--KFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVAtKLNEVE---K 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 345 RDHNV---PYkWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLML 421
Cdd:cd06627  155 DENSVvgtPY-WMAPEVIEMSGVTTASDIWSVGCTVIELLT-GNPPYYDLQPMAALFRIVQDDHPPLPENISPELRDFLL 232
                        250
                 ....*....|....*...
gi 157822719 422 SCWSRDPKQRPCFKDLCE 439
Cdd:cd06627  233 QCFQKDPTLRPSAKELLK 250
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
191-432 7.47e-45

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 162.87  E-value: 7.47e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEGLWKGLVR-VAVKVISRDNLLHQHT---FQAEIQAMKKLRHKHILSLYAVATAGDPVYIITEL 266
Cdd:COG0515    9 YRILRLLGRGGMGVVYLARDLRLGRpVALKVLRPELAADPEArerFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 267 MPKGSLLQLLRDsdEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVkEDIYLSRD 346
Cdd:COG0515   89 VEGESLADLLRR--RGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARAL-GGATLTQT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 347 HNVPYK--WTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRVDAGYRMPCPL---ECPPNIHKLML 421
Cdd:COG0515  166 GTVVGTpgYMAPEQARGEPVDPRSDVYSLGVTLYELLT-GRPPFDGDSPAELLRAHLREPPPPPSElrpDLPPALDAIVL 244
                        250
                 ....*....|.
gi 157822719 422 SCWSRDPKQRP 432
Cdd:COG0515  245 RALAKDPEERY 255
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
190-446 4.44e-44

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: 156.38  E-value: 4.44e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLCKKLGSGYFGEVFEGLW-----KGLVRVAVKVISRDNLLHQHT-FQAEIQAMKKLRHKHILSLYAVATAgDPVYII 263
Cdd:cd05110    8 ELKRVKVLGSGAFGTVYKGIWvpegeTVKIPVAIKILNETTGPKANVeFMDEALIMASMDHPHLVRLLGVCLS-PTIQLV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 264 TELMPKGSLLQLLRDSDEKDLPILeLVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVK--EDI 341
Cdd:cd05110   87 TQLMPHGCLLDYVHEHKDNIGSQL-LLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLARLLEgdEKE 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 342 YLSRDHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLML 421
Cdd:cd05110  166 YNADGGKMPIKWMALECIHYRKFTHQSDVWSYGVTIWELMTFGGKPYDGIPTREIPDLLEKGERLPQPPICTIDVYMVMV 245
                        250       260
                 ....*....|....*....|....*
gi 157822719 422 SCWSRDPKQRPCFKDLCEKLSGITR 446
Cdd:cd05110  246 KCWMIDADSRPKFKELAAEFSRMAR 270
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
185-437 6.08e-44

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: 155.86  E-value: 6.08e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 185 ERPREEFTLCKKLGSGYFGEVFE----------------GLWKGL-VRVAVKVISRD-NLLHQHTFQAEIQAMKKLRHKH 246
Cdd:cd05096    1 KFPRGHLLFKEKLGEGQFGEVHLcevvnpqdlptlqfpfNVRKGRpLLVAVKILRPDaNKNARNDFLKEVKILSRLKDPN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 247 ILSLYAVATAGDPVYIITELMPKGSLLQLL------------RDSDEKDLPIL-----ELVDFASQVAEGMCYLESQNYI 309
Cdd:cd05096   81 IIRLLGVCVDEDPLCMITEYMENGDLNQFLsshhlddkeengNDAVPPAHCLPaisysSLLHVALQIASGMKYLSSLNFV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 310 HRDLAARNVLVTENNLCKVGDFGLAR-LVKEDIYLSRDHNV-PYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQ-M 386
Cdd:cd05096  161 HRDLATRNCLVGENLTIKIADFGMSRnLYAGDYYRIQGRAVlPIRWMAWECILMGKFTTASDVWAFGVTLWEILMLCKeQ 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 157822719 387 PYPGMSNHET------FLRvDAGYR--MPCPLECPPNIHKLMLSCWSRDPKQRPCFKDL 437
Cdd:cd05096  241 PYGELTDEQVienageFFR-DQGRQvyLFRPPPCPQGLYELMLQCWSRDCRERPSFSDI 298
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
190-437 8.58e-44

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: 153.90  E-value: 8.58e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLCKKLGSGYFGEVFEGLWK-GLVRVAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMP 268
Cdd:cd05122    1 LFEILEKIGKGGFGVVYKARHKkTGQIVAIKKINLESKEKKESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEFCS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 269 KGSLLQLLrdsDEKDLPILElvdfaSQVA-------EGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDI 341
Cdd:cd05122   81 GGSLKDLL---KNTNKTLTE-----QQIAyvckevlKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSDGK 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 342 ylSRDHNV--PYkWTAPEALSRGHYSIKSDVWSFGVLLHEIFsRGQMPYPGMSNHETFLRVDAG--YRMPCPLECPPNIH 417
Cdd:cd05122  153 --TRNTFVgtPY-WMAPEVIQGKPYGFKADIWSLGITAIEMA-EGKPPYSELPPMKALFLIATNgpPGLRNPKKWSKEFK 228
                        250       260
                 ....*....|....*....|
gi 157822719 418 KLMLSCWSRDPKQRPCFKDL 437
Cdd:cd05122  229 DFLKKCLQKDPEKRPTAEQL 248
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
190-437 9.32e-44

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: 154.22  E-value: 9.32e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLCKKLGSGYFGEVFEGLWK--GLVrVAVKVI--SRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITE 265
Cdd:cd06606    1 RWKKGELLGKGSFGSVYLALNLdtGEL-MAVKEVelSGDSEEELEALEREIRILSSLKHPNIVRYLGTERTENTLNIFLE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMPKGSLLQLLRDsdEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSR 345
Cdd:cd06606   80 YVPGGSLASLLKK--FGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRLAEIATGEG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 346 DHNV---PYkWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLrvdagYRMPCPLEcPPNIHK---- 418
Cdd:cd06606  158 TKSLrgtPY-WMAPEVIRGEGYGRAADIWSLGCTVIEMAT-GKPPWSELGNPVAAL-----FKIGSSGE-PPPIPEhlse 229
                        250       260
                 ....*....|....*....|...
gi 157822719 419 ----LMLSCWSRDPKQRPCFKDL 437
Cdd:cd06606  230 eakdFLRKCLQRDPKKRPTADEL 252
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
197-437 1.58e-41

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: 149.76  E-value: 1.58e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWK--GL-VRVAVKVI----SRDNllhQHTFQAEIQAMKKL-RHKHILSLYAVATAGDPVYIITELMP 268
Cdd:cd05088   15 IGEGNFGQVLKARIKkdGLrMDAAIKRMkeyaSKDD---HRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 269 KGSLLQLLRDSD--EKD------------LPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLA 334
Cdd:cd05088   92 HGNLLDFLRKSRvlETDpafaianstastLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 335 RlvKEDIYLSRDHN-VPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECP 413
Cdd:cd05088  172 R--GQEVYVKKTMGrLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPLNCD 249
                        250       260
                 ....*....|....*....|....
gi 157822719 414 PNIHKLMLSCWSRDPKQRPCFKDL 437
Cdd:cd05088  250 DEVYDLMRQCWREKPYERPSFAQI 273
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
197-435 3.75e-41

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: 146.49  E-value: 3.75e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGlVRVAVKVISRDNllhqhtfQAEIQAMKKLRHKHILSLYAVATAGdPVY-IITELMPKGSLLQL 275
Cdd:cd14059    1 LGSGAQGAVFLGKFRG-EEVAVKKVRDEK-------ETDIKHLRKLNHPNIIKFKGVCTQA-PCYcILMEYCPYGQLYEV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 276 LRDSDEkdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKE-DIYLSRDHNVpyKWT 354
Cdd:cd14059   72 LRAGRE--ITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKELSEkSTKMSFAGTV--AWM 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 355 APEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRVDA-GYRMPCPLECPPNIHKLMLSCWSRDPKQRPC 433
Cdd:cd14059  148 APEVIRNEPCSEKVDIWSFGVVLWELLT-GEIPYKDVDSSAIIWGVGSnSLQLPVPSTCPDGFKLLMKQCWNSKPRNRPS 226

                 ..
gi 157822719 434 FK 435
Cdd:cd14059  227 FR 228
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
197-444 6.54e-41

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: 146.38  E-value: 6.54e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGLVrVAVKV----------ISRDNLLHQhtfqAEIQAMkkLRHKHILSLYAVATAGDPVYIITEL 266
Cdd:cd14061    2 IGVGGFGKVYRGIWRGEE-VAVKAarqdpdedisVTLENVRQE----ARLFWM--LRHPNIIALRGVCLQPPNLCLVMEY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 267 MPKGSLLQLLrdsDEKDLPILELVDFASQVAEGMCYLESQN---YIHRDLAARNVLVTE--------NNLCKVGDFGLAR 335
Cdd:cd14061   75 ARGGALNRVL---AGRKIPPHVLVDWAIQIARGMNYLHNEApvpIIHRDLKSSNILILEaienedleNKTLKITDFGLAR 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 336 LVKEDIYLSRDHNvpYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSnhetFLRVDAGYRM-----PCPL 410
Cdd:cd14061  152 EWHKTTRMSAAGT--YAWMAPEVIKSSTFSKASDVWSYGVLLWELLT-GEVPYKGID----GLAVAYGVAVnkltlPIPS 224
                        250       260       270
                 ....*....|....*....|....*....|....
gi 157822719 411 ECPPNIHKLMLSCWSRDPKQRPCFKDLCEKLSGI 444
Cdd:cd14061  225 TCPEPFAQLMKDCWQPDPHDRPSFADILKQLENI 258
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
197-447 2.67e-40

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: 144.89  E-value: 2.67e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGLVrVAVKVIsrDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSLLQLL 276
Cdd:cd14058    1 VGRGSFGVVCKARWRNQI-VAVKII--ESESEKKAFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSLYNVL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 277 RDSDEKdlPILEL---VDFASQVAEGMCYLES---QNYIHRDLAARNVLVTEN-NLCKVGDFGLArlvkEDIYLSRDHNV 349
Cdd:cd14058   78 HGKEPK--PIYTAahaMSWALQCAKGVAYLHSmkpKALIHRDLKPPNLLLTNGgTVLKICDFGTA----CDISTHMTNNK 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 350 -PYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRgQMPYPGMSNHETFL--RVDAGYRMPCPLECPPNIHKLMLSCWSR 426
Cdd:cd14058  152 gSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITR-RKPFDHIGGPAFRImwAVHNGERPPLIKNCPKPIESLMTRCWSK 230
                        250       260
                 ....*....|....*....|.
gi 157822719 427 DPKQRPCFKDLCEKLSGITRY 447
Cdd:cd14058  231 DPEKRPSMKEIVKIMSHLMQF 251
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
182-446 9.63e-40

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: 144.05  E-value: 9.63e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 182 DDWERPREEFTLCKKLGSGYFGEVFEGLWKGLVRVAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILsLYAVATAGDPVY 261
Cdd:cd14151    1 DDWEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 262 IITELMPKGSLLQLLRDSDEKdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEdi 341
Cdd:cd14151   80 IVTQWCEGSSLYHHLHIIETK-FEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSR-- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 342 yLSRDHNV-----PYKWTAPEAL---SRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLR-VDAGYRMP----C 408
Cdd:cd14151  157 -WSGSHQFeqlsgSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRDQIIFmVGRGYLSPdlskV 234
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 157822719 409 PLECPPNIHKLMLSCWSRDPKQRPCFKDLCEKLSGITR 446
Cdd:cd14151  235 RSNCPKAMKRLMAECLKKKRDERPLFPQILASIELLAR 272
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
198-441 4.09e-39

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: 141.25  E-value: 4.09e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 198 GSGYFGEVFEGLWKGLVR-VAVKVISRdnllhqhtFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSLLQLL 276
Cdd:cd14060    2 GGGSFGSVYRAIWVSQDKeVAVKKLLK--------IEKEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLFDYL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 277 RDSDEKDLPILELVDFASQVAEGMCYLESQ---NYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSRDHNVPykW 353
Cdd:cd14060   74 NSNESEEMDMDQIMTWATDIAKGMHYLHMEapvKVIHRDLKSRNVVIAADGVLKICDFGASRFHSHTTHMSLVGTFP--W 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 354 TAPEALSRGHYSIKSDVWSFGVLLHEIFSRgQMPYPGMSNHE-TFLRVDAGYRMPCPLECPPNIHKLMLSCWSRDPKQRP 432
Cdd:cd14060  152 MAPEVIQSLPVSETCDTYSYGVVLWEMLTR-EVPFKGLEGLQvAWLVVEKNERPTIPSSCPRSFAELMRRCWEADVKERP 230

                 ....*....
gi 157822719 433 CFKDLCEKL 441
Cdd:cd14060  231 SFKQIIGIL 239
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
191-432 6.39e-39

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: 141.07  E-value: 6.39e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEGLWKGL-VRVAVKVISRDNLLH--QHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELM 267
Cdd:cd05117    2 YELGKVLGRGSFGVVRLAVHKKTgEEYAVKIIDKKKLKSedEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVMELC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 268 PKGSLLQLLRDS---DEKDlpilelvdfAS----QVAEGMCYLESQNYIHRDLAARNVLVT---ENNLCKVGDFGLARLV 337
Cdd:cd05117   82 TGGELFDRIVKKgsfSERE---------AAkimkQILSAVAYLHSQGIVHRDLKPENILLAskdPDSPIKIIDFGLAKIF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 338 KEDIYLSRDHNVPYkWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRVDAG-YRMPCPleCPPNI 416
Cdd:cd05117  153 EEGEKLKTVCGTPY-YVAPEVLKGKGYGKKCDIWSLGVILYILLC-GYPPFYGETEQELFEKILKGkYSFDSP--EWKNV 228
                        250       260
                 ....*....|....*....|
gi 157822719 417 HK----LMLSCWSRDPKQRP 432
Cdd:cd05117  229 SEeakdLIKRLLVVDPKKRL 248
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
197-444 3.77e-38

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: 139.72  E-value: 3.77e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGLVRVAVKVISRDNLLHQHT-FQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSLLQL 275
Cdd:cd14066    1 IGSGGFGTVYKGVLENGTVVAVKRLNEMNCAASKKeFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGSLEDR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 276 LRDSDEKD-LPILELVDFASQVAEGMCYLESQNY---IHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSRDH---- 347
Cdd:cd14066   81 LHCHKGSPpLPWPQRLKIAKGIARGLEYLHEECPppiIHGDIKSSNILLDEDFEPKLTDFGLARLIPPSESVSKTSavkg 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 348 NVPYKwtAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPypgMSNH---------------------ETFLRVDAGYRM 406
Cdd:cd14066  161 TIGYL--APEYIRTGRVSTKSDVYSFGVVLLELLT-GKPA---VDENrenasrkdlvewveskgkeelEDILDKRLVDDD 234
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 157822719 407 PCPLECPPNIHKLMLSCWSRDPKQRPCFKDLCEKLSGI 444
Cdd:cd14066  235 GVEEEEVEALLRLALLCTRSDPSLRPSMKEVVQMLEKL 272
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
190-444 5.71e-38

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: 139.02  E-value: 5.71e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLCKKLGSGYFGEVFEGLWKGlVRVAVKVISRD------NLLHQHTFQAEIQAMkkLRHKHILSLYAVATAGDPVYII 263
Cdd:cd14145    7 ELVLEEIIGIGGFGKVYRAIWIG-DEVAVKAARHDpdedisQTIENVRQEAKLFAM--LKHPNIIALRGVCLKEPNLCLV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 264 TELMPKGSLLQLLRDsdeKDLPILELVDFASQVAEGMCYLESQN---YIHRDLAARNVLVTE--------NNLCKVGDFG 332
Cdd:cd14145   84 MEFARGGPLNRVLSG---KRIPPDILVNWAVQIARGMNYLHCEAivpVIHRDLKSSNILILEkvengdlsNKILKITDFG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 333 LARLVKEDIYLSRDHNvpYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNhetfLRVDAGYRM-----P 407
Cdd:cd14145  161 LAREWHRTTKMSAAGT--YAWMAPEVIRSSMFSKGSDVWSYGVLLWELLT-GEVPFRGIDG----LAVAYGVAMnklslP 233
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 157822719 408 CPLECPPNIHKLMLSCWSRDPKQRPCFKDLCEKLSGI 444
Cdd:cd14145  234 IPSTCPEPFARLMEDCWNPDPHSRPPFTNILDQLTAI 270
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
197-444 8.06e-38

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: 138.63  E-value: 8.06e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGLvRVAVKVISRDN----LLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSL 272
Cdd:cd14146    2 IGVGGFGKVYRATWKGQ-EVAVKAARQDPdediKATAESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARGGTL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 273 LQLLRDSDE-------KDLPILELVDFASQVAEGMCYLESQNY---IHRDLAARNVLVTE--------NNLCKVGDFGLA 334
Cdd:cd14146   81 NRALAAANAapgprraRRIPPHILVNWAVQIARGMLYLHEEAVvpiLHRDLKSSNILLLEkiehddicNKTLKITDFGLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 335 RLVKEDIYLSRDHNvpYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNhetfLRVDAG-----YRMPCP 409
Cdd:cd14146  161 REWHRTTKMSAAGT--YAWMAPEVIKSSLFSKGSDIWSYGVLLWELLT-GEVPYRGIDG----LAVAYGvavnkLTLPIP 233
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 157822719 410 LECPPNIHKLMLSCWSRDPKQRPCFKDLCEKLSGI 444
Cdd:cd14146  234 STCPEPFAKLMKECWEQDPHIRPSFALILEQLTAI 268
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
197-441 8.53e-38

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: 137.91  E-value: 8.53e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGLVRVAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAgDPVYIITELMPKGSLLQLL 276
Cdd:cd14062    1 IGSGSFGTVYKGRWHGDVAVKKLNVTDPTPSQLQAFKNEVAVLRKTRHVNILLFMGYMTK-PQLAIVTQWCEGSSLYKHL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 277 RdSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARlVKEDIYLSRDHNVPYK---W 353
Cdd:cd14062   80 H-VLETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLAT-VKTRWSGSQQFEQPTGsilW 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 354 TAPEAL---SRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFL-RVDAGYRMP----CPLECPPNIHKLMLSCWS 425
Cdd:cd14062  158 MAPEVIrmqDENPYSFQSDVYAFGIVLYELLT-GQLPYSHINNRDQILfMVGRGYLRPdlskVRSDTPKALRRLMEDCIK 236
                        250
                 ....*....|....*.
gi 157822719 426 RDPKQRPCFKDLCEKL 441
Cdd:cd14062  237 FQRDERPLFPQILASL 252
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
197-444 1.00e-37

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: 138.20  E-value: 1.00e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGlVRVAVKVISRD-----NLLHQHTFQ-AEIQAMkkLRHKHILSLYAVATAGDPVYIITELMPKG 270
Cdd:cd14148    2 IGVGGFGKVYKGLWRG-EEVAVKAARQDpdediAVTAENVRQeARLFWM--LQHPNIIALRGVCLNPPHLCLVMEYARGG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 271 SLLQLLRDsdeKDLPILELVDFASQVAEGMCYLESQNY---IHRDLAARNVLVTE--------NNLCKVGDFGLARLVKE 339
Cdd:cd14148   79 ALNRALAG---KKVPPHVLVNWAVQIARGMNYLHNEAIvpiIHRDLKSSNILILEpienddlsGKTLKITDFGLAREWHK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 340 DIYLSRDHNvpYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNhetfLRVDAGYRM-----PCPLECPP 414
Cdd:cd14148  156 TTKMSAAGT--YAWMAPEVIRLSLFSKSSDVWSFGVLLWELLT-GEVPYREIDA----LAVAYGVAMnkltlPIPSTCPE 228
                        250       260       270
                 ....*....|....*....|....*....|
gi 157822719 415 NIHKLMLSCWSRDPKQRPCFKDLCEKLSGI 444
Cdd:cd14148  229 PFARLLEECWDPDPHGRPDFGSILKRLEDI 258
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
190-446 1.11e-37

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: 138.23  E-value: 1.11e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLCKKLGSGYFGEVFEGLWKGLVRVAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAgdPVY-IITELMP 268
Cdd:cd14150    1 EVSMLKRIGTGSFGTVFRGKWHGDVAVKILKVTEPTPEQLQAFKNEMQVLRKTRHVNILLFMGFMTR--PNFaIITQWCE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 269 KGSLLQLLRDSDEKdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARlVKEDIYLSRDHN 348
Cdd:cd14150   79 GSSLYRHLHVTETR-FDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLAT-VKTRWSGSQQVE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 349 VPYK---WTAPEAL---SRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFL-RVDAGYRMP----CPLECPPNIH 417
Cdd:cd14150  157 QPSGsilWMAPEVIrmqDTNPYSFQSDVYAYGVVLYELMS-GTLPYSNINNRDQIIfMVGRGYLSPdlskLSSNCPKAMK 235
                        250       260
                 ....*....|....*....|....*....
gi 157822719 418 KLMLSCWSRDPKQRPCFKDLCEKLSGITR 446
Cdd:cd14150  236 RLLIDCLKFKREERPLFPQILVSIELLQR 264
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
197-441 1.33e-37

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: 137.62  E-value: 1.33e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGLVRVAV-KVISRDNllHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSLLQL 275
Cdd:cd14065    1 LGKGFFGEVYKVTHRETGKVMVmKELKRFD--EQRSFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTLEEL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 276 LRDSDEKdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCK---VGDFGLARLVKEDIYLSRDHNVPYK 352
Cdd:cd14065   79 LKSMDEQ-LPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREANRGRnavVADFGLAREMPDEKTKKPDRKKRLT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 353 ------WTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETF-LRVDAgYRMPCPLECPPNIHKLMLSCWS 425
Cdd:cd14065  158 vvgspyWMAPEMLRGESYDEKVDVFSFGIVLCEIIGRVPADPDYLPRTMDFgLDVRA-FRTLYVPDCPPSFLPLAIRCCQ 236
                        250
                 ....*....|....*.
gi 157822719 426 RDPKQRPCFKDLCEKL 441
Cdd:cd14065  237 LDPEKRPSFVELEHHL 252
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
195-432 2.42e-37

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: 136.88  E-value: 2.42e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWK--GLvRVAVKVISRDNLLHQHT--FQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKG 270
Cdd:cd14003    6 KTLGEGSFGKVKLARHKltGE-KVAIKIIDKSKLKEEIEekIKREIEIMKLLNHPNIIKLYEVIETENKIYLVMEYASGG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 271 SLLQLLRDsdEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYL-SRDHNV 349
Cdd:cd14003   85 ELFDYIVN--NGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEFRGGSLLkTFCGTP 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 350 PYkwTAPEALSRGHY-SIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRVDAGYrMPCPLECPPNIHKLMLSCWSRDP 428
Cdd:cd14003  163 AY--AAPEVLLGRKYdGPKADVWSLGVILYAMLT-GYLPFDDDNDSKLFRKILKGK-YPIPSHLSPDARDLIRRMLVVDP 238

                 ....
gi 157822719 429 KQRP 432
Cdd:cd14003  239 SKRI 242
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
197-447 2.92e-37

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: 137.25  E-value: 2.92e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWK--GLVRVAVKVISRDNLLhQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSLLQ 274
Cdd:cd14154    1 LGKGFFGQAIKVTHRetGEVMVMKELIRFDEEA-QRNFLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGGTLKD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 275 LLRDSDEKdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSRDHNV----- 349
Cdd:cd14154   80 VLKDMARP-LPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLARLIVEERLPSGNMSPsetlr 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 350 ----------------PYkWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETF-LRVDaGYRMP-CPlE 411
Cdd:cd14154  159 hlkspdrkkrytvvgnPY-WMAPEMLNGRSYDEKVDIFSFGIVLCEIIGRVEADPDYLPRTKDFgLNVD-SFREKfCA-G 235
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 157822719 412 CPPNIHKLMLSCWSRDPKQRPCFKDLCEKLSGITRY 447
Cdd:cd14154  236 CPPPFFKLAFLCCDLDPEKRPPFETLEEWLEALYLH 271
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
197-434 3.36e-37

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: 136.81  E-value: 3.36e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGL---WKGLVRVAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSLL 273
Cdd:cd13978    1 LGSGGFGTVSKARhvsWFGMVAIKCLHSSPNCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSLK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 274 QLLrDSDEKDLPILELVDFASQVAEGMCYLESQN--YIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSR------ 345
Cdd:cd13978   81 SLL-EREIQDVPWSLRFRIIHEIALGMNFLHNMDppLLHHDLKPENILLDNHFHVKISDFGLSKLGMKSISANRrrgten 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 346 DHNVPYkWTAPEALSRGHY--SIKSDVWSFGVLLHEIFSRgQMPYPGMSNH-ETFLRVDAGYR-------MPCPLECPPN 415
Cdd:cd13978  160 LGGTPI-YMAPEAFDDFNKkpTSKSDVYSFAIVIWAVLTR-KEPFENAINPlLIMQIVSKGDRpslddigRLKQIENVQE 237
                        250
                 ....*....|....*....
gi 157822719 416 IHKLMLSCWSRDPKQRPCF 434
Cdd:cd13978  238 LISLMIRCWDGNPDARPTF 256
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
190-439 1.05e-35

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: 132.60  E-value: 1.05e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLCKKLGSGYFGEVFeglwkgLVR-------VAVKVISRDNLL---HQHTFQAEIQAMKKLRHKHILSLYAVATAGDP 259
Cdd:cd14007    1 DFEIGKPLGKGKFGNVY------LARekksgfiVALKVISKSQLQksgLEHQLRREIEIQSHLRHPNILRLYGYFEDKKR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 260 VYIITELMPKGSLLQLLRDS---DEKdlpilELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARL 336
Cdd:cd14007   75 IYLILEYAPNGELYKELKKQkrfDEK-----EAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSVH 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 337 VKEDI---------YLsrdhnvpykwtAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLR-VDAGYRM 406
Cdd:cd14007  150 APSNRrktfcgtldYL-----------PPEMVEGKEYDYKVDIWSLGVLCYELLV-GKPPFESKSHQETYKRiQNVDIKF 217
                        250       260       270
                 ....*....|....*....|....*....|...
gi 157822719 407 PCPLecPPNIHKLMLSCWSRDPKQRPCFKDLCE 439
Cdd:cd14007  218 PSSV--SPEAKDLISKLLQKDPSKRLSLEQVLN 248
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
189-444 1.36e-35

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: 132.46  E-value: 1.36e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFEGLWKGLVrVAVKVISRDN----LLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIIT 264
Cdd:cd14147    3 QELRLEEVIGIGGFGKVYRGSWRGEL-VAVKAARQDPdediSVTAESVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 265 ELMPKGSLLQLLRDsdeKDLPILELVDFASQVAEGMCYLESQNY---IHRDLAARNVLVTEN--NLC------KVGDFGL 333
Cdd:cd14147   82 EYAAGGPLSRALAG---RRVPPHVLVNWAVQIARGMHYLHCEALvpvIHRDLKSNNILLLQPieNDDmehktlKITDFGL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 334 ARLVKEDIYLSRDHNvpYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNhetfLRVDAG-----YRMPC 408
Cdd:cd14147  159 AREWHKTTQMSAAGT--YAWMAPEVIKASTFSKGSDVWSFGVLLWELLT-GEVPYRGIDC----LAVAYGvavnkLTLPI 231
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 157822719 409 PLECPPNIHKLMLSCWSRDPKQRPCFKDLCEKLSGI 444
Cdd:cd14147  232 PSTCPEPFAQLMADCWAQDPHRRPDFASILQQLEAL 267
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
195-437 1.97e-35

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: 132.09  E-value: 1.97e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWKGlvRVAVKV--ISRDNLLHQHTFQAEIQAMKKLRHKHILsLYAVATAGDPVY-IITELMPKGS 271
Cdd:cd14063    6 EVIGKGRFGRVHRGRWHG--DVAIKLlnIDYLNEEQLEAFKEEVAAYKNTRHDNLV-LFMGACMDPPHLaIVTSLCKGRT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 272 LLQLLRDSDEKdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVtENNLCKVGDFGLARLVKEDIYLSRDHN--V 349
Cdd:cd14063   83 LYSLIHERKEK-FDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFL-ENGRVVITDFGLFSLSGLLQPGRREDTlvI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 350 PYKWT---APEA-------LSRGH---YSIKSDVWSFGVLLHEIFSRGqMPYPGMSNHETFLRVDAGYRMPCP-LECPPN 415
Cdd:cd14063  161 PNGWLcylAPEIiralspdLDFEEslpFTKASDVYAFGTVWYELLAGR-WPFKEQPAESIIWQVGCGKKQSLSqLDIGRE 239
                        250       260
                 ....*....|....*....|..
gi 157822719 416 IHKLMLSCWSRDPKQRPCFKDL 437
Cdd:cd14063  240 VKDILMQCWAYDPEKRPTFSDL 261
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
191-432 4.21e-35

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: 131.05  E-value: 4.21e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFeglwkgLVR-------VAVKVISRDNLLHQHTFQA--EIQAMKKLRHKHILSLYAVATAGDPVY 261
Cdd:cd08215    2 YEKIRVIGKGSFGSAY------LVRrksdgklYVLKEIDLSNMSEKEREEAlnEVKLLSKLKHPNIVKYYESFEENGKLC 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 262 IITELMPKGSLLQLLRDSDEKDLPILE--LVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKE 339
Cdd:cd08215   76 IVMEYADGGDLAQKIKKQKKKGQPFPEeqILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKVLES 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 340 DI-----------YLSrdhnvpykwtaPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRVDAGYRMPC 408
Cdd:cd08215  156 TTdlaktvvgtpyYLS-----------PELCENKPYNYKSDIWALGCVLYELCT-LKHPFEANNLPALVYKIVKGQYPPI 223
                        250       260
                 ....*....|....*....|....
gi 157822719 409 PLECPPNIHKLMLSCWSRDPKQRP 432
Cdd:cd08215  224 PSQYSSELRDLVNSMLQKDPEKRP 247
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
183-432 9.99e-35

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: 130.20  E-value: 9.99e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 183 DWERPReeftLCKKLGSGYFGEVFEGLWKGlVRVAVKVI--SRDNLLHQHTFQAEIQAMKkLRHKHI---LSLYAVATAG 257
Cdd:cd13979    1 DWEPLR----LQEPLGSGGFGSVYKATYKG-ETVAVKIVrrRRKNRASRQSFWAELNAAR-LRHENIvrvLAAETGTDFA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 258 DPVYIITELMPKGSLLQLLrDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLV 337
Cdd:cd13979   75 SLGLIIMEYCGNGTLQQLI-YEGSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSVKL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 338 KE--DIYLSRDHNV-PYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRgQMPYPGMSNHETFLRVDAGYRmPCpleCPP 414
Cdd:cd13979  154 GEgnEVGTPRSHIGgTYTYRAPELLKGERVTPKADIYSFGITLWQMLTR-ELPYAGLRQHVLYAVVAKDLR-PD---LSG 228
                        250       260
                 ....*....|....*....|....*.
gi 157822719 415 NIH--------KLMLSCWSRDPKQRP 432
Cdd:cd13979  229 LEDsefgqrlrSLISRCWSAQPAERP 254
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
195-442 1.37e-34

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: 130.02  E-value: 1.37e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEG-LWKGL--VRVAVKVI-SRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKG 270
Cdd:cd05042    1 QEIGNGWFGKVLLGeIYSGTsvAQVVVKELkASANPKEQDTFLKEGQPYRILQHPNILQCLGQCVEAIPYLLVMEFCDLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 271 SLLQLLRDSDEKDLP---ILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARL-VKEDIYLSRD 346
Cdd:cd05042   81 DLKAYLRSEREHERGdsdTRTLQRMACEVAAGLAHLHKLNFVHSDLALRNCLLTSDLTVKIGDYGLAHSrYKEDYIETDD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 347 HN-VPYKWTAPEALSRGH-------YSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRV--DAGYRMPCP-LECP-- 413
Cdd:cd05042  161 KLwFPLRWTAPELVTEFHdrllvvdQTKYSNIWSLGVTLWELFENGAQPYSNLSDLDVLAQVvrEQDTKLPKPqLELPys 240
                        250       260
                 ....*....|....*....|....*....
gi 157822719 414 PNIHKLMLSCWsRDPKQRPCFKDLCEKLS 442
Cdd:cd05042  241 DRWYEVLQFCW-LSPEQRPAAEDVHLLLT 268
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
189-432 1.65e-34

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: 129.21  E-value: 1.65e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFEG--LWKGLVrVAVKVISRDNLLHQHT---FQAEIQAMKKLRHKHILSLYAVATAGDPVYII 263
Cdd:cd14099    1 KRYRRGKFLGKGGFAKCYEVtdMSTGKV-YAGKVVPKSSLTKPKQrekLKSEIKIHRSLKHPNIVKFHDCFEDEENVYIL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 264 TELMPKGSLLQLLRDsdEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDI-- 341
Cdd:cd14099   80 LELCSNGSLMELLKR--RKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARLEYDGer 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 342 ---------YLsrdhnvpykwtAPEALSRG-HYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRVDAG-YRMPCPL 410
Cdd:cd14099  158 kktlcgtpnYI-----------APEVLEKKkGHSFEVDIWSLGVILYTLLV-GKPPFETSDVKETYKRIKKNeYSFPSHL 225
                        250       260
                 ....*....|....*....|..
gi 157822719 411 ECPPNIHKLMLSCWSRDPKQRP 432
Cdd:cd14099  226 SISDEAKDLIRSMLQPDPTKRP 247
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
197-437 2.86e-34

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: 128.92  E-value: 2.86e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWK--GLVRVAVKVISRDNLLhQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSLLQ 274
Cdd:cd14221    1 LGKGCFGQAIKVTHRetGEVMVMKELIRFDEET-QRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLRG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 275 LLRDSDEKdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKED----IYLSRDHNV- 349
Cdd:cd14221   80 IIKSMDSH-YPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLARLMVDEktqpEGLRSLKKPd 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 350 ----------PYkWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETF-LRVDAGYRMPCPLECPPNIHK 418
Cdd:cd14221  159 rkkrytvvgnPY-WMAPEMINGRSYDEKVDVFSFGIVLCEIIGRVNADPDYLPRTMDFgLNVRGFLDRYCPPNCPPSFFP 237
                        250
                 ....*....|....*....
gi 157822719 419 LMLSCWSRDPKQRPCFKDL 437
Cdd:cd14221  238 IAVLCCDLDPEKRPSFSKL 256
Pkinase pfam00069
Protein kinase domain;
191-439 3.19e-34

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 127.36  E-value: 3.19e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719  191 FTLCKKLGSGYFGEVFEGLWKGLVR-VAVKVISRDNLLH--QHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELM 267
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKiVAIKKIKKEKIKKkkDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719  268 PKGSLLQLLRdsDEKDLPILELVDFASQVAEGMcylesqnyiHRDLAARNVLVTENnlckvgdfglarlvkediylsrdh 347
Cdd:pfam00069  81 EGGSLFDLLS--EKGAFSEREAKFIMKQILEGL---------ESGSSLTTFVGTPW------------------------ 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719  348 nvpykWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLR-VDAGYRMPC-PLECPPNIHKLMLSCWS 425
Cdd:pfam00069 126 -----YMAPEVLGGNPYGPKVDVWSLGCILYELLT-GKPPFPGINGNEIYELiIDQPYAFPElPSNLSEEAKDLLKKLLK 199
                         250
                  ....*....|....
gi 157822719  426 RDPKQRPCFKDLCE 439
Cdd:pfam00069 200 KDPSKRLTATQALQ 213
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
197-431 1.42e-33

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: 126.90  E-value: 1.42e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKG-LVRVAVKVISRDNLLHQ--------------HTFQAEIQAMKKLRHKHILSLYAVAtaGDP-- 259
Cdd:cd14008    1 LGRGSFGKVKLALDTEtGQLYAIKIFNKSRLRKRregkndrgkiknalDDVRREIAIMKKLDHPNIVRLYEVI--DDPes 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 260 --VYIITELMPKGSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLV 337
Cdd:cd14008   79 dkLYLVLEYCEGGPVMELDSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGVSEMF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 338 -KEDIYLSRDHNVPYkWTAPEALSRGHYSI---KSDVWSFGVLLHeIFSRGQMPYPGMSNHETFLRVDAGYRM-PCPLEC 412
Cdd:cd14008  159 eDGNDTLQKTAGTPA-FLAPELCDGDSKTYsgkAADIWALGVTLY-CLVFGRLPFNGDNILELYEAIQNQNDEfPIPPEL 236
                        250
                 ....*....|....*....
gi 157822719 413 PPNIHKLMLSCWSRDPKQR 431
Cdd:cd14008  237 SPELKDLLRRMLEKDPEKR 255
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
195-432 1.98e-33

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: 127.03  E-value: 1.98e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEG-LWKGL--VRVAVKVI-SRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKG 270
Cdd:cd05087    3 KEIGHGWFGKVFLGeVNSGLssTQVVVKELkASASVQDQMQFLEEAQPYRALQHTNLLQCLAQCAEVTPYLLVMEFCPLG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 271 SL---LQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARL-VKEDIYLSRD 346
Cdd:cd05087   83 DLkgyLRSCRAAESMAPDPLTLQRMACEVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGLSHCkYKEDYFVTAD 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 347 HN-VPYKWTAPEALSRGHYSI-------KSDVWSFGVLLHEIFSRGQMPYPGMSNHE--TFLRVDAGYRMPCP---LECP 413
Cdd:cd05087  163 QLwVPLRWIAPELVDEVHGNLlvvdqtkQSNVWSLGVTIWELFELGNQPYRHYSDRQvlTYTVREQQLKLPKPqlkLSLA 242
                        250
                 ....*....|....*....
gi 157822719 414 PNIHKLMLSCWSRdPKQRP 432
Cdd:cd05087  243 ERWYEVMQFCWLQ-PEQRP 260
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
197-447 2.13e-33

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: 126.98  E-value: 2.13e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGLVRVAV-KVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSLLQL 275
Cdd:cd14222    1 LGKGFFGQAIKVTHKATGKVMVmKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTLKDF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 276 LRDSDEkdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSRDHNVPYK--- 352
Cdd:cd14222   81 LRADDP--FPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEEKKKPPPDKPTTKkrt 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 353 -----------------WTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETF-LRVDAGYRMPCPLECPP 414
Cdd:cd14222  159 lrkndrkkrytvvgnpyWMAPEMLNGKSYDEKVDIFSFGIVLCEIIGQVYADPDCLPRTLDFgLNVRLFWEKFVPKDCPP 238
                        250       260       270
                 ....*....|....*....|....*....|...
gi 157822719 415 NIHKLMLSCWSRDPKQRPCFKDLCEKLSGITRY 447
Cdd:cd14222  239 AFFPLAAICCRLEPDSRPAFSKLEDSFEALSLY 271
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
180-382 2.30e-33

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: 127.23  E-value: 2.30e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 180 HWDDwerpREEFTLCKKLGSGYFGEVFEGLWKGLVrVAVK------VISRDNLLHQhtFQAEIQAMKKLRHKHILSLYAV 253
Cdd:cd14158   10 NFDE----RPISVGGNKLGEGGFGVVFKGYINDKN-VAVKklaamvDISTEDLTKQ--FEQEIQVMAKCQHENLVELLGY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 254 ATAGDPVYIITELMPKGSLLQLLRDSDEK-DLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFG 332
Cdd:cd14158   83 SCDGPQLCLVYTYMPNGSLLDRLACLNDTpPLSWHMRCKIAQGTANGINYLHENNHIHRDIKSANILLDETFVPKISDFG 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 157822719 333 LARLVKED---IYLSRDHNVPyKWTAPEALsRGHYSIKSDVWSFGVLLHEIFS 382
Cdd:cd14158  163 LARASEKFsqtIMTERIVGTT-AYMAPEAL-RGEITPKSDIFSFGVVLLEIIT 213
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
197-446 2.93e-33

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: 126.05  E-value: 2.93e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFeglwKGLVRVAVKVI---------SRDNLLHqhtfqaEIQAMKKLRHKHILSLYAVATAGDPVYIITELM 267
Cdd:cd14155    1 IGSGFFSEVY----KVRHRTSGQVMalkmntlssNRANMLR------EVQLMNRLSHPNILRFMGVCVHQGQLHALTEYI 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 268 PKGSLLQLLrDSDEKdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLV--TENNLCK-VGDFGLArlvkEDIYLS 344
Cdd:cd14155   71 NGGNLEQLL-DSNEP-LSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIkrDENGYTAvVGDFGLA----EKIPDY 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 345 RDHNV-------PYkWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETF-LRVDAgYRMPCPlECPPNI 416
Cdd:cd14155  145 SDGKEklavvgsPY-WMAPEVLRGEPYNEKADVFSYGIILCEIIARIQADPDYLPRTEDFgLDYDA-FQHMVG-DCPPDF 221
                        250       260       270
                 ....*....|....*....|....*....|
gi 157822719 417 HKLMLSCWSRDPKQRPCFKDLCEKLSGITR 446
Cdd:cd14155  222 LQLAFNCCNMDPKSRPSFHDIVKTLEEILE 251
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
197-441 3.28e-33

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: 126.06  E-value: 3.28e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKG-------LVRVAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAgDPVYIITELMPK 269
Cdd:cd05037    7 LGQGTFTNIYDGILREvgdgrvqEVEVLLKVLDSDHRDISESFFETASLMSQISHKHLVKLYGVCVA-DENIMVQEYVRY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 270 GSLLQLLRdSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNL------CKVGDFGLARLVkediyL 343
Cdd:cd05037   86 GPLDKYLR-RMGNNVPLSWKLQVAKQLASALHYLEDKKLIHGNVRGRNILLAREGLdgyppfIKLSDPGVPITV-----L 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 344 SRDHNV-PYKWTAPEALSRGH--YSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPlECPPnIHKLM 420
Cdd:cd05037  160 SREERVdRIPWIAPECLRNLQanLTIAADKWSFGTTLWEICSGGEEPLSALSSQEKLQFYEDQHQLPAP-DCAE-LAELI 237
                        250       260
                 ....*....|....*....|.
gi 157822719 421 LSCWSRDPKQRPCFKDLCEKL 441
Cdd:cd05037  238 MQCWTYEPTKRPSFRAILRDL 258
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
184-434 8.18e-33

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: 125.53  E-value: 8.18e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 184 WERPREEFTLCKKLGSGYFGEVFEGLWKGLVRVAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDpVYII 263
Cdd:cd14149    7 WEIEASEVMLSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTKDN-LAIV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 264 TELMPKGSLLQLLRDSDEKdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARlVKEDIYL 343
Cdd:cd14149   86 TQWCEGSSLYKHLHVQETK-FQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAT-VKSRWSG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 344 SRDHNVPYK---WTAPEAL---SRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFL-RVDAGYRMP----CPLEC 412
Cdd:cd14149  164 SQQVEQPTGsilWMAPEVIrmqDNNPFSFQSDVYSYGIVLYELMT-GELPYSHINNRDQIIfMVGRGYASPdlskLYKNC 242
                        250       260
                 ....*....|....*....|..
gi 157822719 413 PPNIHKLMLSCWSRDPKQRPCF 434
Cdd:cd14149  243 PKAMKRLVADCIKKVKEERPLF 264
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
196-436 1.18e-32

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: 124.32  E-value: 1.18e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 196 KLGSGYFGEVFEGLWKGLVR--VAVKVISR--------DNLLHqhtfqaEIQAMKKLRHKHILSLYAVATAGDPVYIITE 265
Cdd:cd14121    2 KLGSGTYATVYKAYRKSGARevVAVKCVSKsslnkastENLLT------EIELLKKLKHPHIVELKDFQWDEEHIYLIME 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMPKGSLLQLLRDsdEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVT--ENNLCKVGDFGLARLVKEDiyl 343
Cdd:cd14121   76 YCSGGDLSRFIRS--RRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSsrYNPVLKLADFGFAQHLKPN--- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 344 srDHNVPYK----WTAPEALSRGHYSIKSDVWSFGVLLHEI-FsrGQMPYPGMSNHETFLRVdagyRMPCPLECPPNI-- 416
Cdd:cd14121  151 --DEAHSLRgsplYMAPEMILKKKYDARVDLWSVGVILYEClF--GRAPFASRSFEELEEKI----RSSKPIEIPTRPel 222
                        250       260
                 ....*....|....*....|....
gi 157822719 417 ----HKLMLSCWSRDPKQRPCFKD 436
Cdd:cd14121  223 sadcRDLLLRLLQRDPDRRISFEE 246
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
197-439 1.52e-32

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: 124.05  E-value: 1.52e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGL--WKGLVrVAVKVISRDNL----------LHQhtfqaEIQAMKKLRHKHILSLYAVATAGDPVYIIT 264
Cdd:cd06632    8 LGSGSFGSVYEGFngDTGDF-FAVKEVSLVDDdkksresvkqLEQ-----EIALLSKLRHPNIVQYYGTEREEDNLYIFL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 265 ELMPKGSLLQLLRDSDEKDLPILELvdFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLS 344
Cdd:cd06632   82 EYVPGGSIHKLLQRYGAFEEPVIRL--YTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVEAFSFAK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 345 RDHNVPYkWTAPEALSRGH--YSIKSDVWSFGVLLHEIfSRGQMPYPGMSNHETFLRVDAGYRMP-CPLECPPNIHKLML 421
Cdd:cd06632  160 SFKGSPY-WMAPEVIMQKNsgYGLAVDIWSLGCTVLEM-ATGKPPWSQYEGVAAIFKIGNSGELPpIPDHLSPDAKDFIR 237
                        250
                 ....*....|....*...
gi 157822719 422 SCWSRDPKQRPCFKDLCE 439
Cdd:cd06632  238 LCLQRDPEDRPTASQLLE 255
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
194-442 7.65e-32

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: 122.50  E-value: 7.65e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 194 CKKLGSGYFGE----VFEGLWKGLVrVAVKVISRdNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPK 269
Cdd:cd13992    3 CGSGASSHTGEpkyvKKVGVYGGRT-VAIKHITF-SRTEKRTILQELNQLKELVHDNLNKFIGICINPPNIAVVTEYCTR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 270 GSLLQLLRDSDEKdlpilelVD------FASQVAEGMCYLESQNYI-HRDLAARNVLVTENNLCKVGDFGLARLVKEDIY 342
Cdd:cd13992   81 GSLQDVLLNREIK-------MDwmfkssFIKDIVKGMNYLHSSSIGyHGRLKSSNCLVDSRWVVKLTDFGLRNLLEEQTN 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 343 LSRDHNVPYK---WTAPEALS------RGhySIKSDVWSFGVLLHEIFSRgQMPYPGMSNHETFLRV-DAGYRMPCP--- 409
Cdd:cd13992  154 HQLDEDAQHKkllWTAPELLRgsllevRG--TQKGDVYSFAIILYEILFR-SDPFALEREVAIVEKViSGGNKPFRPela 230
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 157822719 410 ---LECPPNIHKLMLSCWSRDPKQRPCFKDLCEKLS 442
Cdd:cd13992  231 vllDEFPPRLVLLVKQCWAENPEKRPSFKQIKKTLT 266
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
195-442 2.97e-31

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: 121.21  E-value: 2.97e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEG-LWKGLV--RVAVKVISRD-NLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKG 270
Cdd:cd14206    3 QEIGNGWFGKVILGeIFSDYTpaQVVVKELRVSaGPLEQRKFISEAQPYRSLQHPNILQCLGLCTETIPFLLIMEFCQLG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 271 SLLQLLR-----DSDEKDLP---ILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARL-VKEDI 341
Cdd:cd14206   83 DLKRYLRaqrkaDGMTPDLPtrdLRTLQRMAYEITLGLLHLHKNNYIHSDLALRNCLLTSDLTVRIGDYGLSHNnYKEDY 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 342 YLSRDHN-VPYKWTAPEALSRGHYSI-------KSDVWSFGVLLHEIFSRGQMPYPGMSNHE--TFLRVDAGYRMPCP-L 410
Cdd:cd14206  163 YLTPDRLwIPLRWVAPELLDELHGNLivvdqskESNVWSLGVTIWELFEFGAQPYRHLSDEEvlTFVVREQQMKLAKPrL 242
                        250       260       270
                 ....*....|....*....|....*....|....
gi 157822719 411 ECPPN--IHKLMLSCWsRDPKQRPCFKDLCEKLS 442
Cdd:cd14206  243 KLPYAdyWYEIMQSCW-LPPSQRPSVEELHLQLS 275
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
189-437 6.94e-31

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: 120.04  E-value: 6.94e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFEGLWKGLVR-VAVKVIsrdNLLHQHT----FQAEIQAMKKLRHKHILSLYAVATAGDPVYII 263
Cdd:cd06609    1 ELFTLLERIGKGSFGEVYKGIDKRTNQvVAIKVI---DLEEAEDeiedIQQEIQFLSQCDSPYITKYYGSFLKGSKLWII 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 264 TELMPKGSLLQLLRDS--DEKDLPILelvdfASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDI 341
Cdd:cd06609   78 MEYCGGGSVLDLLKPGplDETYIAFI-----LREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGQLTSTM 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 342 yLSRDHNV--PYkWTAPEALSRGHYSIKSDVWSFGVLLHEIFsRGQMPYPGMSNHETFLRVdagyrmpcPLECPPNIHKL 419
Cdd:cd06609  153 -SKRNTFVgtPF-WMAPEVIKQSGYDEKADIWSLGITAIELA-KGEPPLSDLHPMRVLFLI--------PKNNPPSLEGN 221
                        250       260
                 ....*....|....*....|....*..
gi 157822719 420 MLS---------CWSRDPKQRPCFKDL 437
Cdd:cd06609  222 KFSkpfkdfvelCLNKDPKERPSAKEL 248
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
187-439 5.87e-30

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


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 116.98  E-value: 5.87e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 187 PREEFTLCKKLGSGYFGEVFEGLWK--GLVrVAVKVISRDNLLHQhtFQAEIQAMKKLRHKHILSLYAVATAGDPVYIIT 264
Cdd:cd06612    1 PEEVFDILEKLGEGSYGSVYKAIHKetGQV-VAIKVVPVEEDLQE--IIKEISILKQCDSPYIVKYYGSYFKNTDLWIVM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 265 ELMPKGSLLQLLRdSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLArlvKEDIYLS 344
Cdd:cd06612   78 EYCGAGSVSDIMK-ITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVS---GQLTDTM 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 345 RDHNV----PYkWTAPEALSRGHYSIKSDVWSFGVLLHE----------------IFSRGQMPYPGMSNhetflrvdagy 404
Cdd:cd06612  154 AKRNTvigtPF-WMAPEVIQEIGYNNKADIWSLGITAIEmaegkppysdihpmraIFMIPNKPPPTLSD----------- 221
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 157822719 405 rmpcPLECPPNIHKLMLSCWSRDPKQRPCFKDLCE 439
Cdd:cd06612  222 ----PEKWSPEFNDFVKKCLVKDPEERPSAIQLLQ 252
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
191-437 7.14e-30

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: 116.72  E-value: 7.14e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEGLWKGLVRV-AVKVISRDNLLHQHTFQA--EIQAMKKLRHKHILSLYAVATAGDPVYIITELM 267
Cdd:cd08530    2 FKVLKKLGKGSYGSVYKVKRLSDNQVyALKEVNLGSLSQKEREDSvnEIRLLASVNHPNIIRYKEAFLDGNRLCIVMEYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 268 PKGSLLQLLRDSDEKDLPILE--LVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIyLSR 345
Cdd:cd08530   82 PFGDLSKLISKRKKKRRLFPEddIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISKVLKKNL-AKT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 346 DHNVPYkWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLSCWS 425
Cdd:cd08530  161 QIGTPL-YAAPEVWKGRPYDYKSDIWSLGCLLYEMAT-FRPPFEARTMQELRYKVCRGKFPPIPPVYSQDLQQIIRSLLQ 238
                        250
                 ....*....|..
gi 157822719 426 RDPKQRPCFKDL 437
Cdd:cd08530  239 VNPKKRPSCDKL 250
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
208-441 1.38e-29

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: 116.54  E-value: 1.38e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 208 GLWKGLVrVAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATagDP--VYIITELMPKGSLLQLLRDSDEK--D 283
Cdd:cd14042   26 GYYKGNL-VAIKKVNKKRIDLTREVLKELKHMRDLQHDNLTRFIGACV--DPpnICILTEYCPKGSLQDILENEDIKldW 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 284 LPILELVDfasQVAEGMCYL-ESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSRDHNVPYK--WTAPEALS 360
Cdd:cd14042  103 MFRYSLIH---DIVKGMHYLhDSEIKSHGNLKSSNCVVDSRFVLKITDFGLHSFRSGQEPPDDSHAYYAKllWTAPELLR 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 361 RGHYSI----KSDVWSFGVLLHEIFSRgQMPY----PGMSNHETFL-RVDAGYRMP-----CPLECPPNIHKLMLSCWSR 426
Cdd:cd14042  180 DPNPPPpgtqKGDVYSFGIILQEIATR-QGPFyeegPDLSPKEIIKkKVRNGEKPPfrpslDELECPDEVLSLMQRCWAE 258
                        250
                 ....*....|....*
gi 157822719 427 DPKQRPCFKDLCEKL 441
Cdd:cd14042  259 DPEERPDFSTLRNKL 273
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
190-432 2.23e-29

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: 115.20  E-value: 2.23e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLCKKLGSGYFGEVFEGLWKGLVRV-AVKVI--SRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITEL 266
Cdd:cd08529    1 DFEILNKLGKGSFGVVYKVVRKVDGRVyALKQIdiSRMSRKMREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 267 MPKGSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSRD 346
Cdd:cd08529   81 AENGDLHSLIKSQRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKILSDTTNFAQT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 347 H-NVPYkWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLSCWS 425
Cdd:cd08529  161 IvGTPY-YLSPELCEDKPYNEKSDVWALGCVLYELCT-GKHPFEAQNQGALILKIVRGKYPPISASYSQDLSQLIDSCLT 238

                 ....*..
gi 157822719 426 RDPKQRP 432
Cdd:cd08529  239 KDYRQRP 245
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
186-437 3.23e-29

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: 115.47  E-value: 3.23e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 186 RPREEFTLCKKLGSGYFGEVFEGLWK-GLVRVAVKVI-SRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYII 263
Cdd:cd13996    3 RYLNDFEEIELLGSGGFGSVYKVRNKvDGVTYAIKKIrLTEKSSASEKVLREVKALAKLNHPNIVRYYTAWVEEPPLYIQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 264 TELMPKGSLLQLLRDSD-EKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTEN-NLCKVGDFGLARLVKEDI 341
Cdd:cd13996   83 MELCEGGTLRDWIDRRNsSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDdLQVKIGDFGLATSIGNQK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 342 YLSRDHNVP--------------YKWTAPEALSRGHYSIKSDVWSFGVLLHEifsrgqMPYPGMSNHETFLRVDAGYRMP 407
Cdd:cd13996  163 RELNNLNNNnngntsnnsvgigtPLYASPEQLDGENYNEKADIYSLGIILFE------MLHPFKTAMERSTILTDLRNGI 236
                        250       260       270
                 ....*....|....*....|....*....|...
gi 157822719 408 CPLEC---PPNIHKLMLSCWSRDPKQRPCFKDL 437
Cdd:cd13996  237 LPESFkakHPKEADLIQSLLSKNPEERPSAEQL 269
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
197-387 9.91e-29

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: 114.13  E-value: 9.91e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGLVRVAVKVISRDNLL-HQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSLLQL 275
Cdd:cd14664    1 IGRGGAGTVYKGVMPNGTLVAVKRLKGEGTQgGDHGFQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPNGSLGEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 276 LRDSDEKDLPIlelvDF------ASQVAEGMCYLE---SQNYIHRDLAARNVLVTENNLCKVGDFGLARL-VKEDIYLSR 345
Cdd:cd14664   81 LHSRPESQPPL----DWetrqriALGSARGLAYLHhdcSPLIIHRDVKSNNILLDEEFEAHVADFGLAKLmDDKDSHVMS 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 157822719 346 DHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMP 387
Cdd:cd14664  157 SVAGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELIT-GKRP 197
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
191-388 1.69e-28

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: 113.05  E-value: 1.69e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEGLWKGL---VRVAVKVISR----DNLLHQHtFQAEIQAMKKLRHKHILSLYAVATAGDPVYII 263
Cdd:cd14080    2 YRLGKTIGEGSYSKVKLAEYTKSglkEKVACKIIDKkkapKDFLEKF-LPRELEILRKLRHPNIIQVYSIFERGSKVFIF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 264 TELMPKGSLLQLLRDSdeKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKED--I 341
Cdd:cd14080   81 MEYAEHGDLLEYIQKR--GALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFARLCPDDdgD 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 157822719 342 YLSRDHNVPYKWTAPEALsRGH-YSIK-SDVWSFGVLLHeIFSRGQMPY 388
Cdd:cd14080  159 VLSKTFCGSAAYAAPEIL-QGIpYDPKkYDIWSLGVILY-IMLCGSMPF 205
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
195-437 2.86e-28

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: 112.30  E-value: 2.86e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWKGL-VRVAVKVIS----RDNLLHQhtfqaEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPK 269
Cdd:cd06614    6 EKIGEGASGEVYKATDRATgKEVAIKKMRlrkqNKELIIN-----EILIMKECKHPNIVDYYDSYLVGDELWVVMEYMDG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 270 GSLLQLLrdsDEKDLPILElvdfaSQVA-------EGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGL-ARLVKEDi 341
Cdd:cd06614   81 GSLTDII---TQNPVRMNE-----SQIAyvcrevlQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFaAQLTKEK- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 342 ylSRDHNV---PYkWTAPEALSRGHYSIKSDVWSFGVLLHEIfSRGQMPY---PGMsnHETFLRVDAGyrmPCPLECP-- 413
Cdd:cd06614  152 --SKRNSVvgtPY-WMAPEVIKRKDYGPKVDIWSLGIMCIEM-AEGEPPYleePPL--RALFLITTKG---IPPLKNPek 222
                        250       260
                 ....*....|....*....|....*.
gi 157822719 414 --PNIHKLMLSCWSRDPKQRPCFKDL 437
Cdd:cd06614  223 wsPEFKDFLNKCLVKDPEKRPSAEEL 248
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
191-399 4.11e-28

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: 112.01  E-value: 4.11e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEGLWKGL-VRVAVKVISR----DNLLhQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITE 265
Cdd:cd14162    2 YIVGKTLGHGSYAVVKKAYSTKHkCKVAIKIVSKkkapEDYL-QKFLPREIEVIKGLKHPNLICFYEAIETTSRVYIIME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMPKGSLLQLLRDsdEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLAR----LVKEDI 341
Cdd:cd14162   81 LAENGDLLDYIRK--NGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFARgvmkTKDGKP 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 342 YLSRDHNVPYKWTAPEALsRG--HYSIKSDVWSFGVLLHEIFSrGQMPYPGmSNHETFLR 399
Cdd:cd14162  159 KLSETYCGSYAYASPEIL-RGipYDPFLSDIWSMGVVLYTMVY-GRLPFDD-SNLKVLLK 215
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
197-437 1.42e-27

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: 110.39  E-value: 1.42e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWK--GLVrVAVKVISRDNLLH--QHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSL 272
Cdd:cd14009    1 IGRGSFATVWKGRHKqtGEV-VAIKEISRKKLNKklQENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGGDL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 273 LQLLRdsDEKDLPilELV--DFASQVAEGMCYLESQNYIHRDLAARNVLVTENNL---CKVGDFGLARLVKEDIYLSRDH 347
Cdd:cd14009   80 SQYIR--KRGRLP--EAVarHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDdpvLKIADFGFARSLQPASMAETLC 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 348 NVPYkWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGmSNHETFL----RVDAGYRMPCPLECPPNIHKLMLSC 423
Cdd:cd14009  156 GSPL-YMAPEILQFQKYDAKADLWSVGAILFEMLV-GKPPFRG-SNHVQLLrnieRSDAVIPFPIAAQLSPDCKDLLRRL 232
                        250
                 ....*....|....
gi 157822719 424 WSRDPKQRPCFKDL 437
Cdd:cd14009  233 LRRDPAERISFEEF 246
SH3_Brk cd11847
Src homology 3 domain of Brk (Breast tumor kinase) Protein Tyrosine Kinase (PTK), also called ...
12-69 1.43e-27

Src homology 3 domain of Brk (Breast tumor kinase) Protein Tyrosine Kinase (PTK), also called PTK6; Brk is a cytoplasmic (or non-receptor) PTK with limited homology to Src kinases. It has been found to be overexpressed in a majority of breast tumors. It plays roles in normal cell differentiation, proliferation, survival, migration, and cell cycle progression. Brk substrates include RNA-binding proteins (SLM-1/2, Sam68), transcription factors (STAT3/5), and signaling molecules (Akt, paxillin, IRS-4). 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). However, Brk lacks the N-terminal myristoylation site. The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212781 [Multi-domain]  Cd Length: 58  Bit Score: 104.18  E-value: 1.43e-27
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 157822719  12 KYVGLWDFKARTDEELSFQAGDLLHVTRKEEQWWWATLLDAEGKALAEGYVPHNYLAE 69
Cdd:cd11847    1 IYKALWDFKARGDEELSFQAGDQFRIAERSGDWWTALKLDRAGGVVAQGFVPNNYLAR 58
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
190-437 1.52e-27

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: 110.49  E-value: 1.52e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLCKKLGSGYFGEVFEGLWKGL--VRVAVKVISRDNLLHQHTFQA-EIQAMKKLRHKHILSLYAVATAGDPVYIITEL 266
Cdd:cd14202    3 EFSRKDLIGHGAFAVVFKGRHKEKhdLEVAVKCINKKNLAKSQTLLGkEIKILKELKHENIVALYDFQEIANSVYLVMEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 267 MPKGSL---LQLLRDSDEKDLPIlelvdFASQVAEGMCYLESQNYIHRDLAARNVLVT--------ENNLC-KVGDFGLA 334
Cdd:cd14202   83 CNGGDLadyLHTMRTLSEDTIRL-----FLQQIAGAMKMLHSKGIIHRDLKPQNILLSysggrksnPNNIRiKIADFGFA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 335 RLVKEDIYLSRDHNVPYkWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHE--TFLRVDAGYRMPCPLEC 412
Cdd:cd14202  158 RYLQNNMMAATLCGSPM-YMAPEVIMSQHYDAKADLWSIGTIIYQCLT-GKAPFQASSPQDlrLFYEKNKSLSPNIPRET 235
                        250       260
                 ....*....|....*....|....*
gi 157822719 413 PPNIHKLMLSCWSRDPKQRPCFKDL 437
Cdd:cd14202  236 SSHLRQLLLGLLQRNQKDRMDFDEF 260
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
191-396 2.05e-27

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: 109.63  E-value: 2.05e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEGlwKGLV---RVAVKVISRDNLlHQHTFQAEIQAMKKLR----HKHILSLYAVAT--AGDPVY 261
Cdd:cd05118    1 YEVLRKIGEGAFGTVWLA--RDKVtgeKVAIKKIKNDFR-HPKAALREIKLLKHLNdvegHPNIVKLLDVFEhrGGNHLC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 262 IITELMPKgSLLQLLRDSdEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENN-LCKVGDFGLARLVKED 340
Cdd:cd05118   78 LVFELMGM-NLYELIKDY-PRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELgQLKLADFGLARSFTSP 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 157822719 341 IYlsrDHNV-PYKWTAPEALSR-GHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHET 396
Cdd:cd05118  156 PY---TPYVaTRWYRAPEVLLGaKPYGSSIDIWSLGCILAELLT-GRPLFPGDSEVDQ 209
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
187-437 5.45e-27

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: 109.37  E-value: 5.45e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 187 PREEFTLCKKLGSGYFGEVFEGL-WKGLVRVAVKVISRDNLLHQ-HTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIIT 264
Cdd:cd06640    2 PEELFTKLERIGKGSFGEVFKGIdNRTQQVVAIKIIDLEEAEDEiEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 265 ELMPKGSLLQLLRDSDEKDLPILELVdfaSQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLA-RLVKEDIYL 343
Cdd:cd06640   82 EYLGGGSALDLLRAGPFDEFQIATML---KEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAgQLTDTQIKR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 344 SRDHNVPYkWTAPEALSRGHYSIKSDVWSFGVLLHEIfSRGQMPYPGMSNHETFLRVDagyRMPCPL---ECPPNIHKLM 420
Cdd:cd06640  159 NTFVGTPF-WMAPEVIQQSAYDSKADIWSLGITAIEL-AKGEPPNSDMHPMRVLFLIP---KNNPPTlvgDFSKPFKEFI 233
                        250
                 ....*....|....*..
gi 157822719 421 LSCWSRDPKQRPCFKDL 437
Cdd:cd06640  234 DACLNKDPSFRPTAKEL 250
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
197-437 7.81e-27

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: 108.11  E-value: 7.81e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGL-WKGLVRVAVKVISRDNLLH----QHTFQAEIQAMKKLRHKHILSLYAVATAGDP--VYIITELMpK 269
Cdd:cd14119    1 LGEGSYGKVKEVLdTETLCRRAVKILKKRKLRRipngEANVKREIQILRRLNHRNVIKLVDVLYNEEKqkLYMVMEYC-V 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 270 GSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLAR---LVKEDIYLSRD 346
Cdd:cd14119   80 GGLQEMLDSAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAEaldLFAEDDTCTTS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 347 HNVPyKWTAPEaLSRGHYS---IKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRVDAG-YRMpcPLECPPNIHKLMLS 422
Cdd:cd14119  160 QGSP-AFQPPE-IANGQDSfsgFKVDIWSAGVTLYNMTT-GKYPFEGDNIYKLFENIGKGeYTI--PDDVDPDLQDLLRG 234
                        250
                 ....*....|....*
gi 157822719 423 CWSRDPKQRPCFKDL 437
Cdd:cd14119  235 MLEKDPEKRFTIEQI 249
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
197-440 8.80e-27

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: 108.36  E-value: 8.80e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGLVRVAVKVISR--DNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSLLQ 274
Cdd:cd14027    1 LDSGGFGKVSLCFHRTQGLVVLKTVYTgpNCIEHNEALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNLMH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 275 LLRdsdEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLA------RLVKEDIYLSRDHN 348
Cdd:cd14027   81 VLK---KVSVPLSVKGRIILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsKLTKEEHNEQREVD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 349 VPYK-------WTAPEALSRGHY--SIKSDVWSFGVLLHEIFSrGQMPYP-GMSNHETFLRVDAGYR---MPCPLECPPN 415
Cdd:cd14027  158 GTAKknagtlyYMAPEHLNDVNAkpTEKSDVYSFAIVLWAIFA-NKEPYEnAINEDQIIMCIKSGNRpdvDDITEYCPRE 236
                        250       260
                 ....*....|....*....|....*
gi 157822719 416 IHKLMLSCWSRDPKQRPCFKDLCEK 440
Cdd:cd14027  237 IIDLMKLCWEANPEARPTFPGIEEK 261
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
197-444 9.64e-27

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: 107.99  E-value: 9.64e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGLVRVAVKVISRdNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSLLQLL 276
Cdd:cd14156    1 IGSGFFSKVYKVTHGATGKVMVVKIYK-NDVDQHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCLEELL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 277 RDsdeKDLPIL--ELVDFASQVAEGMCYLESQNYIHRDLAARNVLV--TENNL-CKVGDFGLARLVKEDIYLSRDHNVPY 351
Cdd:cd14156   80 AR---EELPLSwrEKVELACDISRGMVYLHSKNIYHRDLNSKNCLIrvTPRGReAVVTDFGLAREVGEMPANDPERKLSL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 352 K----WTAPEALSRGHYSIKSDVWSFGVLLHEIFSRgqMPypgmSNHETFLRVD------AGYRMPCPlECPPNIHKLML 421
Cdd:cd14156  157 VgsafWMAPEMLRGEPYDRKVDVFSFGIVLCEILAR--IP----ADPEVLPRTGdfgldvQAFKEMVP-GCPEPFLDLAA 229
                        250       260
                 ....*....|....*....|...
gi 157822719 422 SCWSRDPKQRPCFKDLCEKLSGI 444
Cdd:cd14156  230 SCCRMDAFKRPSFAELLDELEDI 252
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
187-447 9.87e-27

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: 108.61  E-value: 9.87e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 187 PREEFTLCKKLGSGYFGEVFEGLWKGLVRV-AVKVISRDNLLHQ-HTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIIT 264
Cdd:cd06642    2 PEELFTKLERIGKGSFGEVYKGIDNRTKEVvAIKIIDLEEAEDEiEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 265 ELMPKGSLLQLLRDSDEKDLPILELVdfaSQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLA-RLVKEDIYL 343
Cdd:cd06642   82 EYLGGGSALDLLKPGPLEETYIATIL---REILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAgQLTDTQIKR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 344 SRDHNVPYkWTAPEALSRGHYSIKSDVWSFGVLLHEIfSRGQMPYPGMSNHETFLRVdagyrmpcPLECPPNIH------ 417
Cdd:cd06642  159 NTFVGTPF-WMAPEVIKQSAYDFKADIWSLGITAIEL-AKGEPPNSDLHPMRVLFLI--------PKNSPPTLEgqhskp 228
                        250       260       270
                 ....*....|....*....|....*....|..
gi 157822719 418 --KLMLSCWSRDPKQRPCFKDLCeKLSGITRY 447
Cdd:cd06642  229 fkEFVEACLNKDPRFRPTAKELL-KHKFITRY 259
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
191-388 1.05e-26

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: 107.81  E-value: 1.05e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEG---LWKGlvRVAVKVISRDNLLH--QHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITE 265
Cdd:cd14075    4 YRIRGELGSGNFSQVKLGihqLTKE--KVAIKILDKTKLDQktQRLLSREISSMEKLHHPNIIRLYEVVETLSKLHLVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMPKGSLLQL------LRDSDEKDLpilelvdFAsQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKE 339
Cdd:cd14075   82 YASGGELYTKistegkLSESEAKPL-------FA-QIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFSTHAKR 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 157822719 340 DIYLsrdhNV-----PYkwTAPEALSRGHY-SIKSDVWSFGVLLHEIFSrGQMPY 388
Cdd:cd14075  154 GETL----NTfcgspPY--AAPELFKDEHYiGIYVDIWALGVLLYFMVT-GVMPF 201
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
189-388 2.21e-26

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: 106.95  E-value: 2.21e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFEGLWKGLVR-VAVKVISR--------DNLlhqhtfQAEIQAMKKLRHKHILSLYAVATAGDP 259
Cdd:cd14002    1 ENYHVLELIGEGSFGKVYKGRRKYTGQvVALKFIPKrgksekelRNL------RQEIEILRKLNHPNIIEMLDSFETKKE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 260 VYIITELMpKGSLLQLLrdSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKE 339
Cdd:cd14002   75 FVVVTEYA-QGELFQIL--EDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARAMSC 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 157822719 340 DIYLSRDhnvpYKWT----APEALSRGHYSIKSDVWSFGVLLHEIFsRGQMPY 388
Cdd:cd14002  152 NTLVLTS----IKGTplymAPELVQEQPYDHTADLWSLGCILYELF-VGQPPF 199
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
188-401 2.85e-26

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: 107.09  E-value: 2.85e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 188 REEFTLCKKLGSGYFGEVFEGLWKGLV-RVAVKVISRDNL------LHQHTFQA--EIQAMKKLRHKHILSLYAVATAGD 258
Cdd:cd14084    5 RKKYIMSRTLGSGACGEVKLAYDKSTCkKVAIKIINKRKFtigsrrEINKPRNIetEIEILKKLSHPCIIKIEDFFDAED 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 259 PVYIITELMPKGSLLQLLRDSDEKDLPILELvdFASQVAEGMCYLESQNYIHRDLAARNVLVTENN---LCKVGDFGLAR 335
Cdd:cd14084   85 DYYIVLELMEGGELFDRVVSNKRLKEAICKL--YFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEeecLIKITDFGLSK 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157822719 336 LVKEDIYLSRDHNVPyKWTAPEAL---SRGHYSIKSDVWSFGVLLHEIFSRgqmpYPGMSNHETFLRVD 401
Cdd:cd14084  163 ILGETSLMKTLCGTP-TYLAPEVLrsfGTEGYTRAVDCWSLGVILFICLSG----YPPFSEEYTQMSLK 226
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
197-437 3.04e-26

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: 107.14  E-value: 3.04e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGLVRVAVKVI---SRDNLLHQHTF---QAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKG 270
Cdd:cd06631    9 LGKGAYGTVYCGLTSTGQLIAVKQVeldTSDKEKAEKEYeklQEEVDLLKTLKHVNIVGYLGTCLEDNVVSIFMEFVPGG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 271 SLLQLLRDSDEKDLPILelVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLV--------KEDIy 342
Cdd:cd06631   89 SIASILARFGALEEPVF--CRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAKRLcinlssgsQSQL- 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 343 LSRDHNVPYkWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRVDAGYR-MP-CPLECPPNIHKLM 420
Cdd:cd06631  166 LKSMRGTPY-WMAPEVINETGHGRKSDIWSIGCTVFEMAT-GKPPWADMNPMAAIFAIGSGRKpVPrLPDKFSPEARDFV 243
                        250
                 ....*....|....*..
gi 157822719 421 LSCWSRDPKQRPCFKDL 437
Cdd:cd06631  244 HACLTRDQDERPSAEQL 260
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
189-432 3.30e-26

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: 107.30  E-value: 3.30e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFEGLWKGLVR-VAVKVISRDNLLH---QHTFQAEIQAMKKLRHKHILSLYAvaTAGDP--VYI 262
Cdd:cd05581    1 NDFKFGKPLGEGSYSTVVLAKEKETGKeYAIKVLDKRHIIKekkVKYVTIEKEVLSRLAHPGIVKLYY--TFQDEskLYF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 263 ITELMPKGSLLQLLRDSdeKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKED-- 340
Cdd:cd05581   79 VLEYAPNGDLLEYIRKY--GSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGTAKVLGPDss 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 341 ---IYLSRDHNVPYKW--------TA----PEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRV-DAGY 404
Cdd:cd05581  157 pesTKGDADSQIAYNQaraasfvgTAeyvsPELLNEKPAGKSSDLWALGCIIYQMLT-GKPPFRGSNEYLTFQKIvKLEY 235
                        250       260       270
                 ....*....|....*....|....*....|
gi 157822719 405 RMPC--PLECPPNIHKLMLscwsRDPKQRP 432
Cdd:cd05581  236 EFPEnfPPDAKDLIQKLLV----LDPSKRL 261
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
191-431 3.57e-26

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: 106.57  E-value: 3.57e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEGLWK--GlVRVAVKVISRDNLLH---QHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITE 265
Cdd:cd14081    3 YRLGKTLGKGQTGLVKLAKHCvtG-QKVAIKIVNKEKLSKesvLMKVEREIAIMKLIEHPNVLKLYDVYENKKYLYLVLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMPKGSLLQLLRDsdEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSR 345
Cdd:cd14081   82 YVSGGELFDYLVK--KGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMASLQPEGSLLET 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 346 DHNVPYkWTAPEALSRGHY-SIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRVDAG-YRMP--CPLECPPNIHKlML 421
Cdd:cd14081  160 SCGSPH-YACPEVIKGEKYdGRKADIWSCGVILYALLV-GALPFDDDNLRQLLEKVKRGvFHIPhfISPDAQDLLRR-ML 236
                        250
                 ....*....|
gi 157822719 422 scwSRDPKQR 431
Cdd:cd14081  237 ---EVNPEKR 243
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
191-439 3.93e-26

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: 106.85  E-value: 3.93e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEGLWK--GLVrVAVKVISRdnllhqhTFQA--------EIQAMKKL-RHKHILSLYAVATAGDP 259
Cdd:cd07830    1 YKVIKQLGDGTFGSVYLARNKetGEL-VAIKKMKK-------KFYSweecmnlrEVKSLRKLnEHPNIVKLKEVFRENDE 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 260 VYIITELMpKGSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKe 339
Cdd:cd07830   73 LYFVFEYM-EGNLYQLMKDRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLAREIR- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 340 diylSRDhnvPY------KW-TAPEALSR-GHYSIKSDVWSFGVLLHEIFSrgQMP-YPGMSNHETFLRV---------- 400
Cdd:cd07830  151 ----SRP---PYtdyvstRWyRAPEILLRsTSYSSPVDIWALGCIMAELYT--LRPlFPGSSEIDQLYKIcsvlgtptkq 221
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 157822719 401 --DAGYRM------------PCPLE-----CPPNIHKLMLSCWSRDPKQRPCFKDLCE 439
Cdd:cd07830  222 dwPEGYKLasklgfrfpqfaPTSLHqlipnASPEAIDLIKDMLRWDPKKRPTASQALQ 279
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
190-440 7.82e-26

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: 105.82  E-value: 7.82e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLCKKLGSGYFGEVFEG--LWKGLVrVAVKVISRDNLLHQHTFQA---EIQAMKKLRHKHILSLYAVATAGDPVYIIT 264
Cdd:cd08224    1 NYEIEKKIGKGQFSVVYRArcLLDGRL-VALKKVQIFEMMDAKARQDclkEIDLLQQLNHPNIIKYLASFIENNELNIVL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 265 ELMPKGSLLQLLRDSDEKDLPILE--LVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARlvkediY 342
Cdd:cd08224   80 ELADAGDLSRLIKHFKKQKRLIPErtIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGLGR------F 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 343 LSRDHNV-------PYkWTAPEALSRGHYSIKSDVWSFGVLLHEiFSRGQMPY--PGMSNHETFLRVDAGYRMPCPLEC- 412
Cdd:cd08224  154 FSSKTTAahslvgtPY-YMSPERIREQGYDFKSDIWSLGCLLYE-MAALQSPFygEKMNLYSLCKKIEKCEYPPLPADLy 231
                        250       260
                 ....*....|....*....|....*...
gi 157822719 413 PPNIHKLMLSCWSRDPKQRPCFKDLCEK 440
Cdd:cd08224  232 SQELRDLVAACIQPDPEKRPDISYVLDV 259
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
197-416 1.30e-25

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: 105.31  E-value: 1.30e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGL--WKGLVrVAVKVI------SRDNLLHQHTFQA---EIQAMKKLRHKHILSLYAVATAGDPVYIITE 265
Cdd:cd06628    8 IGSGSFGSVYLGMnaSSGEL-MAVKQVelpsvsAENKDRKKSMLDAlqrEIALLRELQHENIVQYLGSSSDANHLNIFLE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMPKGSLLQLLRDSDEKDLPILElvDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLS- 344
Cdd:cd06628   87 YVPGGSVATLLNNYGAFEESLVR--NFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKKLEANSLSTk 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157822719 345 -RDHNVPYK----WTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRVdAGYRMPCPlecPPNI 416
Cdd:cd06628  165 nNGARPSLQgsvfWMAPEVVKQTSYTRKADIWSLGCLVVEMLT-GTHPFPDCTQMQAIFKI-GENASPTI---PSNI 236
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
189-432 1.84e-25

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: 104.75  E-value: 1.84e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFEGLWKGL-VRVAVKVI-------SRDNLLHqhtfqaEIQAMKKLRHKHILSLYAVATAGDPV 260
Cdd:cd06610    1 DDYELIEVIGSGATAVVYAAYCLPKkEKVAIKRIdlekcqtSMDELRK------EIQAMSQCNHPNVVSYYTSFVVGDEL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 261 YIITELMPKGSLLQLLRDSDEKD-LPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGL-ARLVK 338
Cdd:cd06610   75 WLVMPLLSGGSLLDIMKSSYPRGgLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVsASLAT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 339 EDIYLSRDHN----VPYkWTAPEALSRGH-YSIKSDVWSFGVLLHEIfSRGQMPY---PGM-------SNHETFLRVDAG 403
Cdd:cd06610  155 GGDRTRKVRKtfvgTPC-WMAPEVMEQVRgYDFKADIWSFGITAIEL-ATGAAPYskyPPMkvlmltlQNDPPSLETGAD 232
                        250       260
                 ....*....|....*....|....*....
gi 157822719 404 YRmpcplECPPNIHKLMLSCWSRDPKQRP 432
Cdd:cd06610  233 YK-----KYSKSFRKMISLCLQKDPSKRP 256
SH2 smart00252
Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides ...
76-161 2.73e-25

Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides via 2 surface pockets. Specificity is provided via interaction with residues that are distinct from the phosphotyrosine. Only a single occurrence of a SH2 domain has been found in S. cerevisiae.


Pssm-ID: 214585 [Multi-domain]  Cd Length: 84  Bit Score: 98.84  E-value: 2.73e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719    76 EPWFFGCISRSEAMHRLQSEdyPKGTFLIRVSQKPGADYVLSVWDAEAVRHYRIWRNSAGRLHLNEVVSFSSLSELVNYH 155
Cdd:smart00252   1 QPWYHGFISREEAEKLLKNE--GDGDFLVRDSESSPGDYVLSVRVKGKVKHYRIRRNEDGKFYLEGGRKFPSLVELVEHY 78

                   ....*.
gi 157822719   156 KTHNLS 161
Cdd:smart00252  79 QKNSLG 84
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
191-431 8.22e-25

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: 102.87  E-value: 8.22e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEGlwKGLV---RVAVKVISRDNLLhQHTF----QAEIQAMKKLRHKHILSLYAVATAGDPVYII 263
Cdd:cd14663    2 YELGRTLGEGTFAKVKFA--RNTKtgeSVAIKIIDKEQVA-REGMveqiKREIAIMKLLRHPNIVELHEVMATKTKIFFV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 264 TELMPKGSLLQllRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARL---VKED 340
Cdd:cd14663   79 MELVTGGELFS--KIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSALseqFRQD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 341 IYLSRDHNVPyKWTAPEALS-RGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRVDAGyRMPCPLECPPNIHKL 419
Cdd:cd14663  157 GLLHTTCGTP-NYVAPEVLArRGYDGAKADIWSCGVILFVLLA-GYLPFDDENLMALYRKIMKG-EFEYPRWFSPGAKSL 233
                        250
                 ....*....|..
gi 157822719 420 MLSCWSRDPKQR 431
Cdd:cd14663  234 IKRILDPNPSTR 245
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
191-432 1.03e-24

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: 102.50  E-value: 1.03e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVF---------EGLWKGLvrvavKVISRDNLLHQHTFQA--EIQAMKKLRHKHILSLYAVATAGDP 259
Cdd:cd08222    2 YRVVRKLGSGNFGTVYlvsdlkataDEELKVL-----KEISVGELQPDETVDAnrEAKLLSKLDHPAIVKFHDSFVEKES 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 260 VYIITELMPKGSL---LQLLRDSDEKdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVtENNLCKVGDFGLARL 336
Cdd:cd08222   77 FCIVTEYCEGGDLddkISEYKKSGTT-IDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFL-KNNVIKVGDFGISRI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 337 VKEDIYLSRDHN-VPYkWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRgQMPYPGMSNHETFLRVDAGYRMPCPLECPPN 415
Cdd:cd08222  155 LMGTSDLATTFTgTPY-YMSPEVLKHEGYNSKSDIWSLGCILYEMCCL-KHAFDGQNLLSVMYKIVEGETPSLPDKYSKE 232
                        250
                 ....*....|....*..
gi 157822719 416 IHKLMLSCWSRDPKQRP 432
Cdd:cd08222  233 LNAIYSRMLNKDPALRP 249
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
187-437 1.11e-24

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: 102.84  E-value: 1.11e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 187 PREEFTLCKKLGSGYFGEVFEGL-WKGLVRVAVKVISRDNLLHQ-HTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIIT 264
Cdd:cd06641    2 PEELFTKLEKIGKGSFGEVFKGIdNRTQKVVAIKIIDLEEAEDEiEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 265 ELMPKGSLLQLLRDSDEKDLPILELVdfaSQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLA-RLVKEDIYL 343
Cdd:cd06641   82 EYLGGGSALDLLEPGPLDETQIATIL---REILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAgQLTDTQIKR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 344 SRDHNVPYkWTAPEALSRGHYSIKSDVWSFGVLLHEIfSRGQMPYPGMSNHETFLRVdagyrmpcPLECPP--------N 415
Cdd:cd06641  159 N*FVGTPF-WMAPEVIKQSAYDSKADIWSLGITAIEL-ARGEPPHSELHPMKVLFLI--------PKNNPPtlegnyskP 228
                        250       260
                 ....*....|....*....|..
gi 157822719 416 IHKLMLSCWSRDPKQRPCFKDL 437
Cdd:cd06641  229 LKEFVEACLNKEPSFRPTAKEL 250
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
197-432 1.37e-24

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: 101.95  E-value: 1.37e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGlVRVAVKVISRD---NLLHQhtfqaEIQAMKKLRHKHILSLYAVATAgdPVYIITELMPKGSLL 273
Cdd:cd14068    2 LGDGGFGSVYRAVYRG-EDVAVKIFNKHtsfRLLRQ-----ELVVLSHLHHPSLVALLAAGTA--PRMLVMELAPKGSLD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 274 QLLRdSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLV-----TENNLCKVGDFGLARLVKEDIYLSRDHN 348
Cdd:cd14068   74 ALLQ-QDNASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLftlypNCAIIAKIADYGIAQYCCRMGIKTSEGT 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 349 VPYKwtAPEaLSRGH--YSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLE---CP--PNIHKLML 421
Cdd:cd14068  153 PGFR--APE-VARGNviYNQQADVYSFGLLLYDILTCGERIVEGLKFPNEFDELAIQGKLPDPVKeygCApwPGVEALIK 229
                        250
                 ....*....|.
gi 157822719 422 SCWSRDPKQRP 432
Cdd:cd14068  230 DCLKENPQCRP 240
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
197-441 1.52e-24

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: 101.84  E-value: 1.52e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGLVrVAVKVIsRDNLLHQHT----FQAEIQAMKKLRHKHILSlYAVATAGDPVY--IITELMPKG 270
Cdd:cd14064    1 IGSGSFGKVYKGRCRNKI-VAIKRY-RANTYCSKSdvdmFCREVSILCRLNHPCVIQ-FVGACLDDPSQfaIVTQYVSGG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 271 SLLQLLRDsDEKDLPILELVDFASQVAEGMCYLE--SQNYIHRDLAARNVLVTENNLCKVGDFGLARLVK---EDIYLSR 345
Cdd:cd14064   78 SLFSLLHE-QKRVIDLQSKLIIAVDVAKGMEYLHnlTQPIIHRDLNSHNILLYEDGHAVVADFGESRFLQsldEDNMTKQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 346 DHNVpyKWTAPEALSR-GHYSIKSDVWSFGVLLHEIFSrGQMPY----PG-----MSNHETflrvdagyRMPCPLECPPN 415
Cdd:cd14064  157 PGNL--RWMAPEVFTQcTRYSIKADVFSYALCLWELLT-GEIPFahlkPAaaaadMAYHHI--------RPPIGYSIPKP 225
                        250       260
                 ....*....|....*....|....*.
gi 157822719 416 IHKLMLSCWSRDPKQRPCFKDLCEKL 441
Cdd:cd14064  226 ISSLLMRGWNAEPESRPSFVEIVALL 251
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
186-437 1.66e-24

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: 101.95  E-value: 1.66e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 186 RPREEFTlcKKLGSGYFGEVFEGLWKGLVRVAVKVISRD------NLLHqhtFQAEIQAMKKLRHKHILSLYAVATAGDP 259
Cdd:cd14161    2 KHRYEFL--ETLGKGTYGRVKKARDSSGRLVAIKSIRKDrikdeqDLLH---IRREIEIMSSLNHPHIISVYEVFENSSK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 260 VYIITELMPKGSLLQLLrdSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKE 339
Cdd:cd14161   77 IVIVMEYASRGDLYDYI--SERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSNLYNQ 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 340 DIYLSRDHNVPYkWTAPEALS-RGHYSIKSDVWSFGVLLHeIFSRGQMPYPGMSNHETFLRVDAG-YRMPCPLECPPNIH 417
Cdd:cd14161  155 DKFLQTYCGSPL-YASPEIVNgRPYIGPEVDSWSLGVLLY-ILVHGTMPFDGHDYKILVKQISSGaYREPTKPSDACGLI 232
                        250       260
                 ....*....|....*....|
gi 157822719 418 KLMLSCwsrDPKQRPCFKDL 437
Cdd:cd14161  233 RWLLMV---NPERRATLEDV 249
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
195-437 1.74e-24

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: 102.25  E-value: 1.74e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEG-LWKG--LVRVAVKVI-SRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKG 270
Cdd:cd05086    3 QEIGNGWFGKVLLGeIYTGtsVARVVVKELkASANPKEQDDFLQQGEPYYILQHPNILQCVGQCVEAIPYLLVFEFCDLG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 271 SLLQLLRDSDEK---DLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLA-RLVKED-IYLSR 345
Cdd:cd05086   83 DLKTYLANQQEKlrgDSQIMLLQRMACEIAAGLAHMHKHNFLHSDLALRNCYLTSDLTVKVGDYGIGfSRYKEDyIETDD 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 346 DHNVPYKWTAPEALSRGHYSI-------KSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRV--DAGYRMPCP-LECP-- 413
Cdd:cd05086  163 KKYAPLRWTAPELVTSFQDGLlaaeqtkYSNIWSLGVTLWELFENAAQPYSDLSDREVLNHVikERQVKLFKPhLEQPys 242
                        250       260
                 ....*....|....*....|....
gi 157822719 414 PNIHKLMLSCWsRDPKQRPCFKDL 437
Cdd:cd05086  243 DRWYEVLQFCW-LSPEKRPTAEEV 265
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
195-449 3.02e-24

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


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 101.27  E-value: 3.02e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGL--WKGLVrVAVKVISRD-NLLHQHTFQAEIQAMKKLRHKHILSLY-AVATAGDpVYIITELMPKG 270
Cdd:cd06605    7 GELGEGNGGVVSKVRhrPSGQI-MAVKVIRLEiDEALQKQILRELDVLHKCNSPYIVGFYgAFYSEGD-ISICMEYMDGG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 271 SLLQLLRDSDEKDLPILELVDFAsqVAEGMCYLESQ-NYIHRDLAARNVLVTENNLCKVGDFGLA-RLVKEdiyLSRDHN 348
Cdd:cd06605   85 SLDKILKEVGRIPERILGKIAVA--VVKGLIYLHEKhKIIHRDVKPSNILVNSRGQVKLCDFGVSgQLVDS---LAKTFV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 349 VPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIfSRGQMPYPgMSNHET----FLRVDAGYRMPCPL----ECPPNIHKLM 420
Cdd:cd06605  160 GTRSYMAPERISGGKYTVKSDIWSLGLSLVEL-ATGRFPYP-PPNAKPsmmiFELLSYIVDEPPPLlpsgKFSPDFQDFV 237
                        250       260
                 ....*....|....*....|....*....
gi 157822719 421 LSCWSRDPKQRPCFKDLCEKlSGITRYEN 449
Cdd:cd06605  238 SQCLQKDPTERPSYKELMEH-PFIKRYEY 265
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
191-395 4.06e-24

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: 101.40  E-value: 4.06e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEGlwKGLVR---VAVKVISRDNLLHQHTFQA--EIQAMKKLRHKHILSLYAVATAGDPVYIITE 265
Cdd:cd07829    1 YEKLEKLGEGTYGVVYKA--KDKKTgeiVALKKIRLDNEEEGIPSTAlrEISLLKELKHPNIVKLLDVIHTENKLYLVFE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMPKgSLLQLLrDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDI--Yl 343
Cdd:cd07829   79 YCDQ-DLKKYL-DKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLARAFGIPLrtY- 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 157822719 344 srDHNVPYKW-TAPEAL--SRgHYSIKSDVWSFGVLLHEIFsRGQMPYPGMSNHE 395
Cdd:cd07829  156 --THEVVTLWyRAPEILlgSK-HYSTAVDIWSVGCIFAELI-TGKPLFPGDSEID 206
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
196-434 7.73e-24

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: 99.87  E-value: 7.73e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 196 KLGSGYFGEVFEGLWKGLVRVA--VKV------ISRDnllhqhtFQAEIQAMKKLRHKHILS-LYAVATAGDPVyIITEL 266
Cdd:cd14057    2 KINETHSGELWKGRWQGNDIVAkiLKVrdvttrISRD-------FNEEYPRLRIFSHPNVLPvLGACNSPPNLV-VISQY 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 267 MPKGSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLES-QNYIHR-DLAARNVLVTENNLCKV--GDFGLARLVKEDIY 342
Cdd:cd14057   74 MPYGSLYNVLHEGTGVVVDQSQAVKFALDIARGMAFLHTlEPLIPRhHLNSKHVMIDEDMTARInmADVKFSFQEPGKMY 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 343 LSrdhnvpyKWTAPEALSRGHYSIK---SDVWSFGVLLHEIFSRgQMPYPGMSNHETFLRVD-AGYRMPCPLECPPNIHK 418
Cdd:cd14057  154 NP-------AWMAPEALQKKPEDINrrsADMWSFAILLWELVTR-EVPFADLSNMEIGMKIAlEGLRVTIPPGISPHMCK 225
                        250
                 ....*....|....*.
gi 157822719 419 LMLSCWSRDPKQRPCF 434
Cdd:cd14057  226 LMKICMNEDPGKRPKF 241
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
197-437 9.52e-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: 100.15  E-value: 9.52e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGL--WKGLVrVAVKVIS-------RDNLLHQHTFQA---EIQAMKKLRHKHILSLYAVATAGDPVYIIT 264
Cdd:cd06629    9 IGKGTYGRVYLAMnaTTGEM-LAVKQVElpktssdRADSRQKTVVDAlksEIDTLKDLDHPNIVQYLGFEETEDYFSIFL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 265 ELMPKGSLLQLLRDSD--EKDLpileLVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARlVKEDIY 342
Cdd:cd06629   88 EYVPGGSIGSCLRKYGkfEEDL----VRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISK-KSDDIY 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 343 lSRDHNVPYK----WTAPEALSRGH--YSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRVDAGYRMPcPLecPPNI 416
Cdd:cd06629  163 -GNNGATSMQgsvfWMAPEVIHSQGqgYSAKVDIWSLGCVVLEMLA-GRRPWSDDEAIAAMFKLGNKRSAP-PV--PEDV 237
                        250       260
                 ....*....|....*....|....*..
gi 157822719 417 H------KLMLSCWSRDPKQRPCFKDL 437
Cdd:cd06629  238 NlspealDFLNACFAIDPRDRPTAAEL 264
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
197-439 1.10e-23

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: 99.51  E-value: 1.10e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFeglwkgLVRV-------AVKVISRDNLLH----QHTFqAEIQAMKKLRHKHILSLYAVATAGDPVYIITE 265
Cdd:cd05123    1 LGKGSFGKVL------LVRKkdtgklyAMKVLRKKEIIKrkevEHTL-NERNILERVNHPFIVKLHYAFQTEEKLYLVLD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMPKGSLLQLLrdSDEKDLPIlELVDF-ASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDI--- 341
Cdd:cd05123   74 YVPGGELFSHL--SKEGRFPE-ERARFyAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSDGdrt 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 342 --------YLsrdhnvpykwtAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRVDAG-YRMPCPLec 412
Cdd:cd05123  151 ytfcgtpeYL-----------APEVLLGKGYGKAVDWWSLGVLLYEMLT-GKPPFYAENRKEIYEKILKSpLKFPEYV-- 216
                        250       260
                 ....*....|....*....|....*..
gi 157822719 413 PPNIHKLMLSCWSRDPKQRPCFKDLCE 439
Cdd:cd05123  217 SPEAKSLISGLLQKDPTKRLGSGGAEE 243
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
191-438 1.14e-23

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: 99.38  E-value: 1.14e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEGLWKGLVR-VAVKVISRD------NLLHqhtFQAEIQAMKKLRHKHILSLYAVATAGDPVYII 263
Cdd:cd14073    3 YELLETLGKGTYGKVKLAIERATGReVAIKSIKKDkiedeqDMVR---IRREIEIMSSLNHPHIIRIYEVFENKDKIVIV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 264 TELMPKGSLLQLLrdSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYL 343
Cdd:cd14073   80 MEYASGGELYDYI--SERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSNLYSKDKLL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 344 SRDHNVPYkWTAPEALS-RGHYSIKSDVWSFGVLLHeIFSRGQMPYPGmSNHETFLR--VDAGYRMPCPlecPPNIHKLM 420
Cdd:cd14073  158 QTFCGSPL-YASPEIVNgTPYQGPEVDCWSLGVLLY-TLVYGTMPFDG-SDFKRLVKqiSSGDYREPTQ---PSDASGLI 231
                        250
                 ....*....|....*...
gi 157822719 421 LSCWSRDPKQRPCFKDLC 438
Cdd:cd14073  232 RWMLTVNPKRRATIEDIA 249
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
191-393 1.45e-23

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: 100.68  E-value: 1.45e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEGLWKGL-VRVAVKVISR--DNLLH-QHTFQaEIQAMKKLRHKHILSLYAVATAGDP-----VY 261
Cdd:cd07834    2 YELLKPIGSGAYGVVCSAYDKRTgRKVAIKKISNvfDDLIDaKRILR-EIKILRHLKHENIIGLLDILRPPSPeefndVY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 262 IITELMPKgSLLQLLRDsdEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDi 341
Cdd:cd07834   81 IVTELMET-DLHKVIKS--PQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGLARGVDPD- 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 157822719 342 yLSRDHNVPY---KW-TAPEA-LSRGHYSIKSDVWSFGVLLHEIFSRGQMpYPGMSN 393
Cdd:cd07834  157 -EDKGFLTEYvvtRWyRAPELlLSSKKYTKAIDIWSVGCIFAELLTRKPL-FPGRDY 211
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
186-437 1.63e-23

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: 99.24  E-value: 1.63e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 186 RPREEFTLCKKLGSGYFGEVFEGLWKGLVRV-AVKVISRDNLLHQHT---FQAEIQAMKKLRHKHILSLYAVATAGDPVY 261
Cdd:cd14187    4 RTRRRYVRGRFLGKGGFAKCYEITDADTKEVfAGKIVPKSLLLKPHQkekMSMEIAIHRSLAHQHVVGFHGFFEDNDFVY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 262 IITELMPKGSLLQLLRDsdEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDI 341
Cdd:cd14187   84 VVLELCRRRSLLELHKR--RKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKVEYDG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 342 YLSRDHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRVDAG-YRMPCPLEcpPNIHKLM 420
Cdd:cd14187  162 ERKKTLCGTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLV-GKPPFETSCLKETYLRIKKNeYSIPKHIN--PVAASLI 238
                        250
                 ....*....|....*..
gi 157822719 421 LSCWSRDPKQRPCFKDL 437
Cdd:cd14187  239 QKMLQTDPTARPTINEL 255
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
195-437 2.24e-23

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: 98.58  E-value: 2.24e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWKGLVR-VAVKVISRDNLlHQHT------FQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELM 267
Cdd:cd06625    6 KLLGQGAFGQVYLCYDADTGReLAVKQVEIDPI-NTEAskevkaLECEIQLLKNLQHERIVQYYGCLQDEKSLSIFMEYM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 268 PKGSLLQLLRdsdeKDLPILELV--DFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLA-RL--VKEDIY 342
Cdd:cd06625   85 PGGSVKDEIK----AYGALTENVtrKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASkRLqtICSSTG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 343 LSRDHNVPYkWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGqmpyPGMSNHET----FLRVDAGYRMPCPLECPPNIHK 418
Cdd:cd06625  161 MKSVTGTPY-WMSPEVINGEGYGRKADIWSVGCTVVEMLTTK----PPWAEFEPmaaiFKIATQPTNPQLPPHVSEDARD 235
                        250
                 ....*....|....*....
gi 157822719 419 LMLSCWSRDPKQRPCFKDL 437
Cdd:cd06625  236 FLSLIFVRNKKQRPSAEEL 254
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
196-437 7.50e-23

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: 97.30  E-value: 7.50e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 196 KLGSGYFGEVFeglwKGL-----VRVAVKVISRDNLLHQHT--FQAEIQAMKKLRHKHILSLYA--VATAGDPVYIITEL 266
Cdd:cd13983    8 VLGRGSFKTVY----RAFdteegIEVAWNEIKLRKLPKAERqrFKQEIEILKSLKHPNIIKFYDswESKSKKEVIFITEL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 267 MPKGSLLQLLRDSDEKDLPILElvDFASQVAEGMCYLESQNY--IHRDLAARNVLVTENN-LCKVGDFGLARLVKediyL 343
Cdd:cd13983   84 MTSGTLKQYLKRFKRLKLKVIK--SWCRQILEGLNYLHTRDPpiIHRDLKCDNIFINGNTgEVKIGDLGLATLLR----Q 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 344 SRDHNV---PyKWTAPEaLSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSN-HETFLRVDAGYrMPCPLE--CPPNIH 417
Cdd:cd13983  158 SFAKSVigtP-EFMAPE-MYEEHYDEKVDIYAFGMCLLEMAT-GEYPYSECTNaAQIYKKVTSGI-KPESLSkvKDPELK 233
                        250       260
                 ....*....|....*....|
gi 157822719 418 KLMLSCwSRDPKQRPCFKDL 437
Cdd:cd13983  234 DFIEKC-LKPPDERPSAREL 252
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
191-440 1.03e-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: 96.95  E-value: 1.03e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFegLWKGLVRVAVKVISRDNLL-----HQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITE 265
Cdd:cd08225    2 YEIIKKIGEGSFGKIY--LAKAKSDSEHCVIKEIDLTkmpvkEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMPKGSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNL-CKVGDFGLARLVKEDIYLS 344
Cdd:cd08225   80 YCDGGDLMKRINRQRGVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMvAKLGDFGIARQLNDSMELA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 345 RD-HNVPYkWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRgQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLSC 423
Cdd:cd08225  160 YTcVGTPY-YLSPEICQNRPYNNKTDIWSLGCVLYELCTL-KHPFEGNNLHQLVLKICQGYFAPISPNFSRDLRSLISQL 237
                        250
                 ....*....|....*..
gi 157822719 424 WSRDPKQRPCFKDLCEK 440
Cdd:cd08225  238 FKVSPRDRPSITSILKR 254
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
191-437 1.17e-22

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: 97.57  E-value: 1.17e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEG-LWKGLVRVAVK-------VISRdnllhqhtfqaEIQAMKKLRHKHILSL----YAVATAGD 258
Cdd:cd14137    6 YTIEKVIGSGSFGVVYQAkLLETGEVVAIKkvlqdkrYKNR-----------ELQIMRRLKHPNIVKLkyffYSSGEKKD 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 259 PVY--IITELMPKgSLLQLLRDS--DEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLV-TENNLCKVGDFGL 333
Cdd:cd14137   75 EVYlnLVMEYMPE-TLYRVIRHYskNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVdPETGVLKLCDFGS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 334 ARLVKEDiylsrDHNVPYKWT----APEAL--SRgHYSIKSDVWSFG-VL------------------LHEIF------S 382
Cdd:cd14137  154 AKRLVPG-----EPNVSYICSryyrAPELIfgAT-DYTTAIDIWSAGcVLaelllgqplfpgessvdqLVEIIkvlgtpT 227
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 383 RGQMPYpgMSNHETFLRVDAGYrmPCPLE------CPPNIHKLMLSCWSRDPKQR---------PCFKDL 437
Cdd:cd14137  228 REQIKA--MNPNYTEFKFPQIK--PHPWEkvfpkrTPPDAIDLLSKILVYNPSKRltalealahPFFDEL 293
PTK_Jak2_rpt1 cd05078
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely ...
197-442 1.18e-22

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: 96.94  E-value: 1.18e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGL--------VRVAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMP 268
Cdd:cd05078    7 LGQGTFTKIFKGIRREVgdygqlheTEVLLKVLDKAHRNYSESFFEAASMMSQLSHKHLVLNYGVCVCGDENILVQEYVK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 269 KGSLLQLLRdSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENN--------LCKVGDFGLARLVK-E 339
Cdd:cd05078   87 FGSLDTYLK-KNKNCINILWKLEVAKQLAWAMHFLEEKTLVHGNVCAKNILLIREEdrktgnppFIKLSDPGISITVLpK 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 340 DIYLSRdhnVPykWTAPEALSRG-HYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECppNIHK 418
Cdd:cd05078  166 DILLER---IP--WVPPECIENPkNLSLATDKWSFGTTLWEICSGGDKPLSALDSQRKLQFYEDRHQLPAPKWT--ELAN 238
                        250       260
                 ....*....|....*....|....
gi 157822719 419 LMLSCWSRDPKQRPCFKDLCEKLS 442
Cdd:cd05078  239 LINNCMDYEPDHRPSFRAIIRDLN 262
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
197-436 1.59e-22

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: 96.28  E-value: 1.59e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGL--VRVAVKVISRDNLLHQHTFQA-EIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSLL 273
Cdd:cd14120    1 IGHGAFAVVFKGRHRKKpdLPVAIKCITKKNLSKSQNLLGkEIKILKELSHENVVALLDCQETSSSVYLVMEYCNGGDLA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 274 QLLrdSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLC---------KVGDFGLARLVKEDIYLS 344
Cdd:cd14120   81 DYL--QAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSGRkpspndirlKIADFGFARFLQDGMMAA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 345 RDHNVPYkWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHE--TFLRVDAGYRMPCPLECPPNIHKLMLS 422
Cdd:cd14120  159 TLCGSPM-YMAPEVIMSLQYDAKADLWSIGTIVYQCLT-GKAPFQAQTPQElkAFYEKNANLRPNIPSGTSPALKDLLLG 236
                        250
                 ....*....|....
gi 157822719 423 CWSRDPKQRPCFKD 436
Cdd:cd14120  237 LLKRNPKDRIDFED 250
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
187-439 2.19e-22

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: 96.64  E-value: 2.19e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 187 PREEFTLCKKLGSGYFGEVFEGLWKGL-VRVAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITE 265
Cdd:cd06644   10 PNEVWEIIGELGDGAFGKVYKAKNKETgALAAAKVIETKSEEELEDYMVEIEILATCNHPYIVKLLGAFYWDGKLWIMIE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMPKGS----LLQLLRDSDEKDLPILelvdfASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLA-----RL 336
Cdd:cd06644   90 FCPGGAvdaiMLELDRGLTEPQIQVI-----CRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSaknvkTL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 337 VKEDIYLSrdhnVPYkWTAP-----EALSRGHYSIKSDVWSFGVLLHEIfSRGQMPYPGMSNHETFLRVdaGYRMPCPLE 411
Cdd:cd06644  165 QRRDSFIG----TPY-WMAPevvmcETMKDTPYDYKADIWSLGITLIEM-AQIEPPHHELNPMRVLLKI--AKSEPPTLS 236
                        250       260       270
                 ....*....|....*....|....*....|..
gi 157822719 412 CP----PNIHKLMLSCWSRDPKQRPCFKDLCE 439
Cdd:cd06644  237 QPskwsMEFRDFLKTALDKHPETRPSAAQLLE 268
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
188-404 2.42e-22

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: 96.60  E-value: 2.42e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 188 REEFTLCKKLGSGYFGEVFeglwkgLVR-------VAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPV 260
Cdd:cd14166    2 RETFIFMEVLGSGAFSEVY------LVKqrstgklYALKCIKKSPLSRDSSLENEIAVLKRIKHENIVTLEDIYESTTHY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 261 YIITELMPKGSLLQLLRDS---DEKDLPILelvdfASQVAEGMCYLESQNYIHRDLAARNVLV---TENNLCKVGDFGLA 334
Cdd:cd14166   76 YLVMQLVSGGELFDRILERgvyTEKDASRV-----INQVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFGLS 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 335 RLVKEDIyLSRDHNVPyKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRVDAGY 404
Cdd:cd14166  151 KMEQNGI-MSTACGTP-GYVAPEVLAQKPYSKAVDCWSIGVITYILLC-GYPPFYEETESRLFEKIKEGY 217
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
195-431 2.73e-22

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: 96.39  E-value: 2.73e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWKGlVRVAVKVIsrdnLLHQHTF---QAEIQAMKKLRHKHILSLYAVATAGD----PVYIITELM 267
Cdd:cd14144    1 RSVGKGRYGEVWKGKWRG-EKVAVKIF----FTTEEASwfrETEIYQTVLMRHENILGFIAADIKGTgswtQLYLITDYH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 268 PKGSLLQLLRDS--DEKDLPILelvdfASQVAEGMCYLESQNY--------IHRDLAARNVLVTENNLCKVGDFGLA-RL 336
Cdd:cd14144   76 ENGSLYDFLRGNtlDTQSMLKL-----AYSAACGLAHLHTEIFgtqgkpaiAHRDIKSKNILVKKNGTCCIADLGLAvKF 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 337 VKE--DIYLSRDHNVPYK-WTAPEALS----RGHYS--IKSDVWSFGVLLHEI----FSRG-----QMPY----PGMSNH 394
Cdd:cd14144  151 ISEtnEVDLPPNTRVGTKrYMAPEVLDeslnRNHFDayKMADMYSFGLVLWEIarrcISGGiveeyQLPYydavPSDPSY 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 157822719 395 ETFLRVDAGYRMPCPL-------ECPPNIHKLMLSCWSRDPKQR 431
Cdd:cd14144  231 EDMRRVVCVERRRPSIpnrwssdEVLRTMSKLMSECWAHNPAAR 274
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
183-435 3.30e-22

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: 95.85  E-value: 3.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 183 DWERPREEFtlckkLGSGYFGEVFEGLWKGLV--RVAVKVISRDNLLH-QHTFQAEIQAMKKLRHKHILSLYAVATAGDP 259
Cdd:cd14201    5 DFEYSRKDL-----VGHGAFAVVFKGRHRKKTdwEVAIKSINKKNLSKsQILLGKEIKILKELQHENIVALYDVQEMPNS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 260 VYIITELMPKGSLLQLLRDSDEKDLPILELvdFASQVAEGMCYLESQNYIHRDLAARNVLVTENN---------LCKVGD 330
Cdd:cd14201   80 VFLVMEYCNGGDLADYLQAKGTLSEDTIRV--FLQQIAAAMRILHSKGIIHRDLKPQNILLSYASrkkssvsgiRIKIAD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 331 FGLARLVKEDIYLSRDHNVPYkWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHE--TFLRVDAGYRMPC 408
Cdd:cd14201  158 FGFARYLQSNMMAATLCGSPM-YMAPEVIMSQHYDAKADLWSIGTVIYQCLV-GKPPFQANSPQDlrMFYEKNKNLQPSI 235
                        250       260
                 ....*....|....*....|....*..
gi 157822719 409 PLECPPNIHKLMLSCWSRDPKQRPCFK 435
Cdd:cd14201  236 PRETSPYLADLLLGLLQRNQKDRMDFE 262
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
190-432 8.28e-22

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


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 94.29  E-value: 8.28e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLCKKLGSGYFGEVFeglwKGLVR-----VAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIIT 264
Cdd:cd06613    1 DYELIQRIGSGTYGDVY----KARNIatgelAAVKVIKLEPGDDFEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVM 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 265 ELMPKGSLLQLLRDSDekdlPILEL-VDFAS-QVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIy 342
Cdd:cd06613   77 EYCGGGSLQDIYQVTG----PLSELqIAYVCrETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQLTATI- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 343 lSRDHN---VPYkWTAPEALS---RGHYSIKSDVWSFGVLLHEIfSRGQMPYPGMsnHEtfLRvdAGYRMPCPLECPPNI 416
Cdd:cd06613  152 -AKRKSfigTPY-WMAPEVAAverKGGYDGKCDIWALGITAIEL-AELQPPMFDL--HP--MR--ALFLIPKSNFDPPKL 222
                        250       260
                 ....*....|....*....|....*.
gi 157822719 417 ----------HKLMLSCWSRDPKQRP 432
Cdd:cd06613  223 kdkekwspdfHDFIKKCLTKNPKKRP 248
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
195-432 8.50e-22

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: 94.29  E-value: 8.50e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEG--LWKGLVrVAVKVIS-RDNllHQHTFQA---EIQAMKKLRHKHILSLYAVATAGDPVYIITELMP 268
Cdd:cd06626    6 NKIGEGTFGKVYTAvnLDTGEL-MAMKEIRfQDN--DPKTIKEiadEMKVLEGLDHPNLVRYYGVEVHREEVYIFMEYCQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 269 KGSLLQLLRDSdeKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKeDIYLSRDHN 348
Cdd:cd06626   83 EGTLEELLRHG--RILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVKLK-NNTTTMAPG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 349 VPYKWT------APEALSRG---HYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNH-ETFLRVDAGYRMPCP--LECPPNI 416
Cdd:cd06626  160 EVNSLVgtpaymAPEVITGNkgeGHGRAADIWSLGCVVLEMAT-GKRPWSELDNEwAIMYHVGMGHKPPIPdsLQLSPEG 238
                        250
                 ....*....|....*.
gi 157822719 417 HKLMLSCWSRDPKQRP 432
Cdd:cd06626  239 KDFLSRCLESDPKKRP 254
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
197-432 9.89e-22

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: 94.60  E-value: 9.89e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGlVRVAVKVISR---------------DNLLHQH------TFQAEIQAMKKLRHKHILSLYAVAT 255
Cdd:cd14000    2 LGDGGFGSVYRASYKG-EPVAVKIFNKhtssnfanvpadtmlRHLRATDamknfrLLRQELTVLSHLHHPSIVYLLGIGI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 256 agDPVYIITELMPKGSLLQLLRDSDEKDLPILELV--DFASQVAEGMCYLESQNYIHRDLAARNVLVTE---NNL--CKV 328
Cdd:cd14000   81 --HPLMLVLELAPLGSLDHLLQQDSRSFASLGRTLqqRIALQVADGLRYLHSAMIIYRDLKSHNVLVWTlypNSAiiIKI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 329 GDFGLARLVKEDIYLSRDHNVPYKwtAPEALSRG-HYSIKSDVWSFGVLLHEIFSrGQMPYPGmsnHETF-LRVDAGYRM 406
Cdd:cd14000  159 ADYGISRQCCRMGAKGSEGTPGFR--APEIARGNvIYNEKVDVFSFGMLLYEILS-GGAPMVG---HLKFpNEFDIHGGL 232
                        250       260       270
                 ....*....|....*....|....*....|.
gi 157822719 407 PCPL---EC--PPNIHKLMLSCWSRDPKQRP 432
Cdd:cd14000  233 RPPLkqyECapWPEVEVLMKKCWKENPQQRP 263
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
185-437 1.15e-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: 1.15e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 185 ERPREEFTLCKKLGSGYFGEVFEGLWKGL-VRVAVKVI---SRDNLlhqHTFQAEIQAMKKLRHKHILSLYAVATAGDPV 260
Cdd:cd06611    1 VNPNDIWEIIGELGDGAFGKVYKAQHKETgLFAAAKIIqieSEEEL---EDFMVEIDILSECKHPNIVGLYEAYFYENKL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 261 YIITELMPKGSLLQLLrDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGL-ARLVKE 339
Cdd:cd06611   78 WILIEFCDGGALDSIM-LELERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVsAKNKST 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 340 DIYLSRDHNVPYkWTAPEAL-----SRGHYSIKSDVWSFGVLLHEIfSRGQMPYPGMSNHETFLRVDAGyrMPCPLECP- 413
Cdd:cd06611  157 LQKRDTFIGTPY-WMAPEVVacetfKDNPYDYKADIWSLGITLIEL-AQMEPPHHELNPMRVLLKILKS--EPPTLDQPs 232
                        250       260
                 ....*....|....*....|....*..
gi 157822719 414 ---PNIHKLMLSCWSRDPKQRPCFKDL 437
Cdd:cd06611  233 kwsSSFNDFLKSCLVKDPDDRPTAAEL 259
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
189-403 1.35e-21

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: 93.83  E-value: 1.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKK--LGSGYFGEVFEGLWKGL-VRVAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITE 265
Cdd:cd14190    2 STFSIHSKevLGGGKFGKVHTCTEKRTgLKLAAKVINKQNSKDKEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIVLFME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMPKGSLLQLLRDSDEKdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLV--TENNLCKVGDFGLARLVKEDIYL 343
Cdd:cd14190   82 YVEGGELFERIVDEDYH-LTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCvnRTGHQVKIIDFGLARRYNPREKL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 344 SRDHNVPyKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRVDAG 403
Cdd:cd14190  161 KVNFGTP-EFLSPEVVNYDQVSFPTDMWSMGVITYMLLS-GLSPFLGDDDTETLNNVLMG 218
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
239-432 1.66e-21

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: 93.50  E-value: 1.66e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 239 MKKLRHKHILSLYAVATAGDPVYIITELMPKGSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNV 318
Cdd:cd08219   52 LAKMKHPNIVAFKESFEADGHLYIVMEYCDGGDLMQKIKLQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNI 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 319 LVTENNLCKVGDFGLARLVKEDI-YLSRDHNVPYkWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRgQMPYPGMSNHETF 397
Cdd:cd08219  132 FLTQNGKVKLGDFGSARLLTSPGaYACTYVGTPY-YVPPEIWENMPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLI 209
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 157822719 398 LRVDAGYRMPCPLECPPNIHKLMLSCWSRDPKQRP 432
Cdd:cd08219  210 LKVCQGSYKPLPSHYSYELRSLIKQMFKRNPRSRP 244
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
195-440 1.77e-21

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: 93.34  E-value: 1.77e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFeglwkgLVR-------VAVKVI--SRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITE 265
Cdd:cd08218    6 KKIGEGSFGKAL------LVKskedgkqYVIKEIniSKMSPKEREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMPKGSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSR 345
Cdd:cd08218   80 YCDGGDLYKRINAQRGVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVLNSTVELAR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 346 DH-NVPYkWTAPEALSRGHYSIKSDVWSFGVLLHEI------FSRGQMpypgmsnHETFLRVDAGYRMPCPLECPPNIHK 418
Cdd:cd08218  160 TCiGTPY-YLSPEICENKPYNNKSDIWALGCVLYEMctlkhaFEAGNM-------KNLVLKIIRGSYPPVPSRYSYDLRS 231
                        250       260
                 ....*....|....*....|..
gi 157822719 419 LMLSCWSRDPKQRPCFKDLCEK 440
Cdd:cd08218  232 LVSQLFKRNPRDRPSINSILEK 253
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
195-437 2.28e-21

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: 93.15  E-value: 2.28e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWKGLVRV-AVKVI--SRDNLLHQ-HTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKG 270
Cdd:cd14188    7 KVLGKGGFAKCYEMTDLTTNKVyAAKIIphSRVSKPHQrEKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRR 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 271 SLLQLLRDsdEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSRDHNVP 350
Cdd:cd14188   87 SMAHILKA--RKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEPLEHRRRTICGT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 351 YKWTAPEALSRGHYSIKSDVWSFGVLLHEIFsRGQMPYPGMSNHETFLRV-DAGYRMPCPLECPPNihKLMLSCWSRDPK 429
Cdd:cd14188  165 PNYLSPEVLNKQGHGCESDIWALGCVMYTML-LGRPPFETTNLKETYRCIrEARYSLPSSLLAPAK--HLIASMLSKNPE 241

                 ....*...
gi 157822719 430 QRPCFKDL 437
Cdd:cd14188  242 DRPSLDEI 249
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
197-437 2.71e-21

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: 93.24  E-value: 2.71e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGL-WKGLVRVAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSLLQL 275
Cdd:cd06624   16 LGKGTFGVVYAARdLSTQVRIAIKEIPERDSREVQPLHEEIALHSRLSHKNIVQYLGSVSEDGFFKIFMEQVPGGSLSAL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 276 LRDsdeKDLPILE----LVDFASQVAEGMCYLESQNYIHRDLAARNVLV-TENNLCKVGDFGLA-RLVKEDIYLSrdhnv 349
Cdd:cd06624   96 LRS---KWGPLKDnentIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVnTYSGVVKISDFGTSkRLAGINPCTE----- 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 350 PYKWT----APEALSRGH--YSIKSDVWSFGVLLHEIfSRGQMPYPGMSN-HETFLRVDAgYRM--PCPLECPPNIHKLM 420
Cdd:cd06624  168 TFTGTlqymAPEVIDKGQrgYGPPADIWSLGCTIIEM-ATGKPPFIELGEpQAAMFKVGM-FKIhpEIPESLSEEAKSFI 245
                        250
                 ....*....|....*..
gi 157822719 421 LSCWSRDPKQRPCFKDL 437
Cdd:cd06624  246 LRCFEPDPDKRATASDL 262
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
190-432 3.38e-21

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: 92.54  E-value: 3.38e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLCKKLGSGYFGEVFEGLWK--GLVRvAVKVISRDNLLHQHT----FQAEIQAMKKLRHKHILSLYAVATAGDPVYII 263
Cdd:cd14098    1 KYQIIDRLGSGTFAEVKKAVEVetGKMR-AIKQIVKRKVAGNDKnlqlFQREINILKSLEHPGIVRLIDWYEDDQHIYLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 264 TELMPKGSLLQLLrdSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENN--LCKVGDFGLARLVKEDI 341
Cdd:cd14098   80 MEYVEGGDLMDFI--MAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDpvIVKISDFGLAKVIHTGT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 342 YLSRDHNVPyKWTAPEAL------SRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRVDAGYRMPCPL---EC 412
Cdd:cd14098  158 FLVTFCGTM-AYLAPEILmskeqnLQGGYSNLVDMWSVGCLVYVMLT-GALPFDGSSQLPVEKRIRKGRYTQPPLvdfNI 235
                        250       260
                 ....*....|....*....|
gi 157822719 413 PPNIHKLMLSCWSRDPKQRP 432
Cdd:cd14098  236 SEEAIDFILRLLDVDPEKRM 255
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
196-390 3.43e-21

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: 93.40  E-value: 3.43e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 196 KLGSGYFGEVFEGLWKGL-VRVAVKVISRDNllhQH-----TFQAEIQAMKKLRHKHILSLYAVATAGDP------VYII 263
Cdd:cd07840    6 QIGEGTYGQVYKARNKKTgELVALKKIRMEN---EKegfpiTAIREIKLLQKLDHPNVVRLKEIVTSKGSakykgsIYMV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 264 TELMPKGslLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARlvkediYL 343
Cdd:cd07840   83 FEYMDHD--LTGLLDNPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLAR------PY 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 157822719 344 SRDHNVPYK------W-TAPEALsRG--HYSIKSDVWSFGVLLHEIFSrGQMPYPG 390
Cdd:cd07840  155 TKENNADYTnrvitlWyRPPELL-LGatRYGPEVDMWSVGCILAELFT-GKPIFQG 208
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
195-432 3.99e-21

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: 92.78  E-value: 3.99e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWKGL-VRVAVKVISRDNLLHQHTFQAEIQAMKKL-RHKHILSLYAVATAGDP----VYIITELMP 268
Cdd:cd13985    6 KQLGEGGFSYVYLAHDVNTgRRYALKRMYFNDEEQLRVAIKEIEIMKRLcGHPNIVQYYDSAILSSEgrkeVLLLMEYCP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 269 kGSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQN--YIHRDLAARNVLVTENNLCKVGDFGLA------------ 334
Cdd:cd13985   86 -GSLVDILEKSPPSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFGSAttehypleraee 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 335 -RLVKEDIylsRDHNVP-YKwtAPEAL---SRGHYSIKSDVWSFGVLLHEIFSRgQMPYPGmsnhETFLRVDAG-YRMPC 408
Cdd:cd13985  165 vNIIEEEI---QKNTTPmYR--APEMIdlySKKPIGEKADIWALGCLLYKLCFF-KLPFDE----SSKLAIVAGkYSIPE 234
                        250       260
                 ....*....|....*....|....
gi 157822719 409 PLECPPNIHKLMLSCWSRDPKQRP 432
Cdd:cd13985  235 QPRYSPELHDLIRHMLTPDPAERP 258
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
216-444 4.70e-21

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: 92.23  E-value: 4.70e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 216 VAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSLLQLLRDsdeKDLPILE--LVDFA 293
Cdd:cd14045   33 VAIKKIAKKSFTLSKRIRKEVKQVRELDHPNLCKFIGGCIEVPNVAIITEYCPKGSLNDVLLN---EDIPLNWgfRFSFA 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 294 SQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDI------YLSRDHNVpykWTAPEALSRGHY--S 365
Cdd:cd14045  110 TDIARGMAYLHQHKIYHGRLKSSNCVIDDRWVCKIADYGLTTYRKEDGsenasgYQQRLMQV---YLPPENHSNTDTepT 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 366 IKSDVWSFGVLLHEIFSRGQmPYPgmsnhETFLRVDAGYRMP------------CPleCPPNIHKLMLSCWSRDPKQRPC 433
Cdd:cd14045  187 QATDVYSYAIILLEIATRND-PVP-----EDDYSLDEAWCPPlpelisgktensCP--CPADYVELIRRCRKNNPAQRPT 258
                        250
                 ....*....|.
gi 157822719 434 FKDLCEKLSGI 444
Cdd:cd14045  259 FEQIKKTLHKI 269
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
197-439 5.62e-21

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: 92.06  E-value: 5.62e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVfeGLWKGLV---RVAVKVISRDNLLHQ-HTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSL 272
Cdd:cd14078   11 IGSGGFAKV--KLATHILtgeKVAIKIMDKKALGDDlPRVKTEIEALKNLSHQHICRLYHVIETDNKIFMVLEYCPGGEL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 273 LQLLRDSDEkdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIylsrDHNV--- 349
Cdd:cd14078   89 FDYIVAKDR--LSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCAKPKGGM----DHHLetc 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 350 ---PyKWTAPEALSRGHY-SIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRVDAG-YRMPCPLEcpPNIHKLMLSCW 424
Cdd:cd14078  163 cgsP-AYAAPELIQGKPYiGSEADVWSMGVLLYALLC-GFLPFDDDNVMALYRKIQSGkYEEPEWLS--PSSKLLLDQML 238
                        250
                 ....*....|....*
gi 157822719 425 SRDPKQRPCFKDLCE 439
Cdd:cd14078  239 QVDPKKRITVKELLN 253
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
195-392 5.62e-21

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: 92.63  E-value: 5.62e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWKGLVR-VAVK---VISRDNLLHQHTFQA--EIQAMKKLRHKHILSLYAVATAGDPVYIITELMP 268
Cdd:cd07841    6 KKLGEGTYAVVYKARDKETGRiVAIKkikLGERKEAKDGINFTAlrEIKLLQELKHPNIIGLLDVFGHKSNINLVFEFME 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 269 kGSLLQLLRDsdeKDLpILELVD---FASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARlvkedIYLSR 345
Cdd:cd07841   86 -TDLEKVIKD---KSI-VLTPADiksYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLAR-----SFGSP 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 157822719 346 D----HNVPYKW-TAPEAL--SRgHYSIKSDVWSFGVLLHEIFSRgqMPY-PGMS 392
Cdd:cd07841  156 NrkmtHQVVTRWyRAPELLfgAR-HYGVGVDMWSVGCIFAELLLR--VPFlPGDS 207
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
190-439 6.65e-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: 91.83  E-value: 6.65e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLCKKLGSGYFGEVFeglwkgLVR-------VAVKVISRDNLLHQHTFQ--AEIQAMKKLRHKHILSLY--AVATAGD 258
Cdd:cd08217    1 DYEVLETIGKGSFGTVR------KVRrksdgkiLVWKEIDYGKMSEKEKQQlvSEVNILRELKHPNIVRYYdrIVDRANT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 259 PVYIITELMPKGSLLQLLRDSDEKDLPILE--LVDFASQVAEGMCYLESQNY-----IHRDLAARNVLVTENNLCKVGDF 331
Cdd:cd08217   75 TLYIVMEYCEGGDLAQLIKKCKKENQYIPEefIWKIFTQLLLALYECHNRSVgggkiLHRDLKPANIFLDSDNNVKLGDF 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 332 GLARLVKEDIYLSRDH-NVPYKWtAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRVDAGYRMPCPL 410
Cdd:cd08217  155 GLARVLSHDSSFAKTYvGTPYYM-SPELLNEQSYDEKSDIWSLGCLIYELCA-LHPPFQAANQLELAKKIKEGKFPRIPS 232
                        250       260
                 ....*....|....*....|....*....
gi 157822719 411 ECPPNIHKLMLSCWSRDPKQRPCFKDLCE 439
Cdd:cd08217  233 RYSSELNEVIKSMLNVDPDKRPSVEELLQ 261
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
197-385 7.49e-21

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


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 91.60  E-value: 7.49e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEV---FEGLWKGLVRVAVKVISRD-----NLLHQHTFQAEIQAMKKLRHKHIL-SLYAVATAGDPVYIITELM 267
Cdd:cd13994    1 IGKGATSVVrivTKKNPRSGVLYAVKEYRRRddeskRKDYVKRLTSEYIISSKLHHPNIVkVLDLCQDLHGKWCLVMEYC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 268 PKGSLLQLLRDSDEkdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDI-YLSRD 346
Cdd:cd13994   81 PGGDLFTLIEKADS--LSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAEVFGMPAeKESPM 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 157822719 347 HN-----VPYkwTAPEALSRGHYSIKS-DVWSFGVLLHEIFSRGQ 385
Cdd:cd13994  159 SAglcgsEPY--MAPEVFTSGSYDGRAvDVWSCGIVLFALFTGRF 201
PTK_Jak3_rpt1 cd14208
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is ...
197-442 8.58e-21

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: 91.50  E-value: 8.58e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGLVR-------VAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVyIITELMPK 269
Cdd:cd14208    7 LGKGSFTKIYRGLRTDEEDderceteVLLKVMDPTHGNCQESFLEAASIMSQISHKHLVLLHGVCVGKDSI-MVQEFVCH 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 270 GSL-LQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENN------LCKVGDFGLARLVKEDIY 342
Cdd:cd14208   86 GALdLYLKKQQQKGPVAISWKLQVVKQLAYALNYLEDKQLVHGNVSAKKVLLSREGdkgsppFIKLSDPGVSIKVLDEEL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 343 LSrdHNVPykWTAPEALSRGH-YSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPLECppNIHKLML 421
Cdd:cd14208  166 LA--ERIP--WVAPECLSDPQnLALEADKWGFGATLWEIFSGGHMPLSALDPSKKLQFYNDRKQLPAPHWI--ELASLIQ 239
                        250       260
                 ....*....|....*....|.
gi 157822719 422 SCWSRDPKQRPCFKDLCEKLS 442
Cdd:cd14208  240 QCMSYNPLLRPSFRAIIRDLN 260
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
190-437 9.06e-21

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: 91.34  E-value: 9.06e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLCKKLGSGYFGEVFeglwkgLVRVAVK----VISRDNLLH-----QHTFQAEIQAMKKLRHKHILSlYAVATAGDP- 259
Cdd:cd08223    1 EYQFLRVIGKGSYGEVW------LVRHKRDrkqyVIKKLNLKNaskreRKAAEQEAKLLSKLKHPNIVS-YKESFEGEDg 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 260 -VYIITELMPKGSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVK 338
Cdd:cd08223   74 fLYIVMGFCEGGDLYTRLKEQKGVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 339 EDIYLSRDH-NVPYkWTAPEALSRGHYSIKSDVWSFGVLLHEI------FSRGQMpypgmsnHETFLRVDAGYRMPCPLE 411
Cdd:cd08223  154 SSSDMATTLiGTPY-YMSPELFSNKPYNHKSDVWALGCCVYEMatlkhaFNAKDM-------NSLVYKILEGKLPPMPKQ 225
                        250       260
                 ....*....|....*....|....*.
gi 157822719 412 CPPNIHKLMLSCWSRDPKQRPCFKDL 437
Cdd:cd08223  226 YSPELGELIKAMLHQDPEKRPSVKRI 251
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
197-446 1.30e-20

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: 91.22  E-value: 1.30e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGLVRVAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSLLQLL 276
Cdd:cd14153    8 IGKGRFGQVYHGRWHGEVAIRLIDIERDNEEQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLYSVV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 277 RDSdEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVtENNLCKVGDFGLARLVKEDIYLSRDHN--VPYKW- 353
Cdd:cd14153   88 RDA-KVVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGLFTISGVLQAGRREDKlrIQSGWl 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 354 --TAPEAL---------SRGHYSIKSDVWSFGVLLHEIFSRgQMPYPGMSNHETFLRVDAGYR-MPCPLECPPNIHKLML 421
Cdd:cd14153  166 chLAPEIIrqlspeteeDKLPFSKHSDVFAFGTIWYELHAR-EWPFKTQPAEAIIWQVGSGMKpNLSQIGMGKEISDILL 244
                        250       260
                 ....*....|....*....|....*
gi 157822719 422 SCWSRDPKQRPCFKDLCEKLSGITR 446
Cdd:cd14153  245 FCWAYEQEERPTFSKLMEMLEKLPK 269
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
195-432 1.31e-20

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: 91.56  E-value: 1.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWKGlVRVAVKVI-SRDNLLHQHtfQAEIQAMKKLRHKHILSLYAVATAGD----PVYIITELMPK 269
Cdd:cd14056    1 KTIGKGRYGEVWLGKYRG-EKVAVKIFsSRDEDSWFR--ETEIYQTVMLRHENILGFIAADIKSTgswtQLWLITEYHEH 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 270 GSLLQLLRdsdEKDLPILELVDFASQVAEGMCYLESQnyI----------HRDLAARNVLVTENNLCKVGDFGLA---RL 336
Cdd:cd14056   78 GSLYDYLQ---RNTLDTEEALRLAYSAASGLAHLHTE--IvgtqgkpaiaHRDLKSKNILVKRDGTCCIADLGLAvryDS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 337 VKEDIYLSRDHNVPYK-WTAPEALS----RGHYS--IKSDVWSFGVLLHEIFSRG---------QMPYPGMSNHE-TF-- 397
Cdd:cd14056  153 DTNTIDIPPNPRVGTKrYMAPEVLDdsinPKSFEsfKMADIYSFGLVLWEIARRCeiggiaeeyQLPYFGMVPSDpSFee 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 157822719 398 ---LRVDAGYRMPCPL-----ECPPNIHKLMLSCWSRDPKQRP 432
Cdd:cd14056  233 mrkVVCVEKLRPPIPNrwksdPVLRSMVKLMQECWSENPHARL 275
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
197-446 1.31e-20

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: 91.18  E-value: 1.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGLVRVAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILsLYAVATAGDP-VYIITELMPKGSLLQL 275
Cdd:cd14152    8 IGQGRWGKVHRGRWHGEVAIRLLEIDGNNQDHLKLFKKEVMNYRQTRHENVV-LFMGACMHPPhLAIITSFCKGRTLYSF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 276 LRDSdEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVtENNLCKVGDFGL---ARLVKEDiylsRDHN---V 349
Cdd:cd14152   87 VRDP-KTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLfgiSGVVQEG----RRENelkL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 350 PYKWT---APE---ALSRGH------YSIKSDVWSFGVLLHEIFSRgQMPYPGMSNHETFLRVDAGYRMPCPLECPP--- 414
Cdd:cd14152  161 PHDWLcylAPEivrEMTPGKdedclpFSKAADVYAFGTIWYELQAR-DWPLKNQPAEALIWQIGSGEGMKQVLTTISlgk 239
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 157822719 415 NIHKLMLSCWSRDPKQRPCFK---DLCEKLSGITR 446
Cdd:cd14152  240 EVTEILSACWAFDLEERPSFTllmDMLEKLPKLNR 274
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
189-432 1.35e-20

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: 91.33  E-value: 1.35e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFEGLWKGLVRV-AVKVISRDN--LLHQHTFQaEIQAMKKLRHKHILSLYA--VATAGDPVYII 263
Cdd:cd06621    1 DKIVELSSLGEGAGGSVTKCRLRNTKTIfALKTITTDPnpDVQKQILR-ELEINKSCASPYIVKYYGafLDEQDSSIGIA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 264 TELMPKGSLLQLLRDSDEKDLPILELV--DFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLA-RLVKEd 340
Cdd:cd06621   80 MEYCEGGSLDSIYKKVKKKGGRIGEKVlgKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVSgELVNS- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 341 iyLSRDHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIfSRGQMPYP--GMSNHETFLRVDAGYRMPCPL--ECPPN- 415
Cdd:cd06621  159 --LAGTFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEV-AQNRFPFPpeGEPPLGPIELLSYIVNMPNPElkDEPENg 235
                        250       260
                 ....*....|....*....|...
gi 157822719 416 ------IHKLMLSCWSRDPKQRP 432
Cdd:cd06621  236 ikwsesFKDFIEKCLEKDGTRRP 258
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
195-431 1.51e-20

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: 91.26  E-value: 1.51e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWKGlVRVAVKVI--SRDNLLHQHTfqaEIQAMKKLRHKHILSLYAVATAGD----PVYIITELMP 268
Cdd:cd14220    1 RQIGKGRYGEVWMGKWRG-EKVAVKVFftTEEASWFRET---EIYQTVLMRHENILGFIAADIKGTgswtQLYLITDYHE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 269 KGSLLQLLRDSDekdLPILELVDFASQVAEGMCYLESQNY--------IHRDLAARNVLVTENNLCKVGDFGLARLVKED 340
Cdd:cd14220   77 NGSLYDFLKCTT---LDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGTCCIADLGLAVKFNSD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 341 iylSRDHNVPY-------KWTAP----EALSRGHYS--IKSDVWSFGVLLHEIFSRG---------QMPY----PGMSNH 394
Cdd:cd14220  154 ---TNEVDVPLntrvgtkRYMAPevldESLNKNHFQayIMADIYSFGLIIWEMARRCvtggiveeyQLPYydmvPSDPSY 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 157822719 395 ETFLRVDAGYRMPCPL-------ECPPNIHKLMLSCWSRDPKQR 431
Cdd:cd14220  231 EDMREVVCVKRLRPTVsnrwnsdECLRAVLKLMSECWAHNPASR 274
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
239-446 1.51e-20

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: 90.93  E-value: 1.51e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 239 MKKLRHKHILSLYAVATAGDPVYIITELMPKGSLLQLLRDSDEK-------DLpILELVdfasqvaEGMCYLESQNYIHR 311
Cdd:cd14043   50 LRELRHENVNLFLGLFVDCGILAIVSEHCSRGSLEDLLRNDDMKldwmfksSL-LLDLI-------KGMRYLHHRGIVHG 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 312 DLAARNVLVTENNLCKVGDFGLARLVkEDIYLSRDHNVPYK--WTAPE-----ALSRGHySIKSDVWSFGVLLHEIFSRG 384
Cdd:cd14043  122 RLKSRNCVVDGRFVLKITDYGYNEIL-EAQNLPLPEPAPEEllWTAPEllrdpRLERRG-TFPGDVFSFAIIMQEVIVRG 199
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157822719 385 QmPYP--GMSNHETFLRVdagyRMPCPL--------ECPPNIHKLMLSCWSRDPKQRPCFKDLCEKLSGITR 446
Cdd:cd14043  200 A-PYCmlGLSPEEIIEKV----RSPPPLcrpsvsmdQAPLECIQLMKQCWSEAPERRPTFDQIFDQFKSINK 266
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
235-437 1.53e-20

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: 90.50  E-value: 1.53e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 235 EIQAMKKLRHKHILSLYAVA------TAGDPVYIITELMPKGSLLQLLrdSDEKDLPILELVDFASQVAEGMCYLESQNY 308
Cdd:cd14012   48 ELESLKKLRHPNLVSYLAFSierrgrSDGWKVYLLTEYAPGGSLSELL--DSVGSVPLDTARRWTLQLLEALEYLHRNGV 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 309 IHRDLAARNVLV---TENNLCKVGDFGL-ARLVKEDIYLSRDHNVPYKWTAPE-ALSRGHYSIKSDVWSFGVLLHeifsr 383
Cdd:cd14012  126 VHKSLHAGNVLLdrdAGTGIVKLTDYSLgKTLLDMCSRGSLDEFKQTYWLPPElAQGSKSPTRKTDVWDLGLLFL----- 200
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 157822719 384 gQMpypgMSNHETFLRVDAGYRMPCPLECPPNIHKLMLSCWSRDPKQRPCFKDL 437
Cdd:cd14012  201 -QM----LFGLDVLEKYTSPNPVLVSLDLSASLQDFLSKCLSLDPKKRPTALEL 249
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
196-432 1.61e-20

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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: 91.22  E-value: 1.61e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 196 KLGSGYFGEVfeglWKGLVR-----VAVK--VISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMP 268
Cdd:cd07833    8 VVGEGAYGVV----LKCRNKatgeiVAIKkfKESEDDEDVKKTALREVKVLRQLRHENIVNLKEAFRRKGRLYLVFEYVE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 269 KgSLLQLLrDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSRDHN 348
Cdd:cd07833   84 R-TLLELL-EASPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARALTARPASPLTDY 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 349 VPYKW-TAPEAL-SRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNH------------------ETFLR--VDAGYRM 406
Cdd:cd07833  162 VATRWyRAPELLvGDTNYGKPVDVWAIGCIMAELLD-GEPLFPGDSDIdqlyliqkclgplppshqELFSSnpRFAGVAF 240
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 157822719 407 PCPLE-----------CPPNIHKLMLSCWSRDPKQRP 432
Cdd:cd07833  241 PEPSQpeslerrypgkVSSPALDFLKACLRMDPKERL 277
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
189-389 1.63e-20

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: 90.73  E-value: 1.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFEGLWKGLVR-VAVKVI-SRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITEL 266
Cdd:cd06623    1 SDLERVKVLGQGSSGVVYKVRHKPTGKiYALKKIhVDGDEEFRKQLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 267 MPKGSLLQLLRdsdeKDLPILE--LVDFASQVAEGMCYLESQ-NYIHRDLAARNVLVTENNLCKVGDFGLARLVkEDiyl 343
Cdd:cd06623   81 MDGGSLADLLK----KVGKIPEpvLAYIARQILKGLDYLHTKrHIIHRDIKPSNLLINSKGEVKIADFGISKVL-EN--- 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 157822719 344 SRDHNVPYKWTA----PEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYP 389
Cdd:cd06623  153 TLDQCNTFVGTVtymsPERIQGESYSYAADIWSLGLTLLECAL-GKFPFL 201
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
190-400 1.98e-20

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: 90.85  E-value: 1.98e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLCKKLGSGYFGEVFEGlwKGLVR---VAVKVISRDNLLHQHTFQA--EIQAMKKLR-HKHILSLYAVATAGDPVYII 263
Cdd:cd07832    1 RYKILGRIGEGAHGIVFKA--KDRETgetVALKKVALRKLEGGIPNQAlrEIKALQACQgHPYVVKLRDVFPHGTGFVLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 264 TELMPkGSLLQLLRDSdEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYL 343
Cdd:cd07832   79 FEYML-SSLSEVLRDE-ERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLARLFSEEDPR 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 344 SRDHNVPYKW-TAPEAL--SRgHYSIKSDVWSFGVLLHEIFsRGQMPYPGMSNHETFLRV 400
Cdd:cd07832  157 LYSHQVATRWyRAPELLygSR-KYDEGVDLWAVGCIFAELL-NGSPLFPGENDIEQLAIV 214
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
184-390 2.10e-20

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: 92.02  E-value: 2.10e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 184 WERPrEEFTLCKKLGSGYFGEVFEGL-WKGLVRVAVKVISR--DNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAG--- 257
Cdd:cd07877   13 WEVP-ERYQNLSPVGSGAYGSVCAAFdTKTGLRVAVKKLSRpfQSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPArsl 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 258 ---DPVYIITELMpKGSLLQLLRDSDEKDLPILELVdfaSQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLA 334
Cdd:cd07877   92 eefNDVYLVTHLM-GADLNNIVKCQKLTDDHVQFLI---YQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLA 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 157822719 335 RLVKEDIylsrDHNVPYKW-TAPE-ALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPG 390
Cdd:cd07877  168 RHTDDEM----TGYVATRWyRAPEiMLNWMHYNQTVDIWSVGCIMAELLT-GRTLFPG 220
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
190-409 2.84e-20

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: 90.08  E-value: 2.84e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLCKKLGSGYFGEVFEGLWKGLV-RVAVKVISRDNLL-HQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELM 267
Cdd:cd14095    1 KYDIGRVIGDGNFAVVKECRDKATDkEYALKIIDKAKCKgKEHMIENEVAILRRVKHPNIVQLIEEYDTDTELYLVMELV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 268 PKGSLLQLLRDSdekdlpilelVDFASQVAEGMC--------YLESQNYIHRDLAARNVLVTENNL----CKVGDFGLAR 335
Cdd:cd14095   81 KGGDLFDAITSS----------TKFTERDASRMVtdlaqalkYLHSLSIVHRDIKPENLLVVEHEDgsksLKLADFGLAT 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 336 LVKEDIYlsrdhNV---PyKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPY--PGMSNHETFLRVDAG-YRMPCP 409
Cdd:cd14095  151 EVKEPLF-----TVcgtP-TYVAPEILAETGYGLKVDIWAAGVITYILLC-GFPPFrsPDRDQEELFDLILAGeFEFLSP 223
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
190-432 2.97e-20

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


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 89.75  E-value: 2.97e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLCKKLGSGYFGEVFeglwkglvrvavKVISR-DNLLH-----QHTFQ---------AEIQAMKKL-RHKHILSLYAV 253
Cdd:cd13997    1 HFHELEQIGSGSFSEVF------------KVRSKvDGCLYavkksKKPFRgpkeraralREVEAHAALgQHPNIVRYYSS 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 254 ATAGDPVYIITELMPKGSLLQLL-RDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFG 332
Cdd:cd13997   69 WEEGGHLYIQMELCENGSLQDALeELSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFG 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 333 LA-RLVKEDIYLSRDHnvpyKWTAPEALS-RGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHEtfLRVDagyRMPCPL 410
Cdd:cd13997  149 LAtRLETSGDVEEGDS----RYLAPELLNeNYTHLPKADIFSLGVTVYEAATGEPLPRNGQQWQQ--LRQG---KLPLPP 219
                        250       260
                 ....*....|....*....|....
gi 157822719 411 ECP--PNIHKLMLSCWSRDPKQRP 432
Cdd:cd13997  220 GLVlsQELTRLLKVMLDPDPTRRP 243
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
189-439 3.04e-20

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: 90.02  E-value: 3.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFeglwkgLVR-------VAVKVISRDNLLH---QHTFQAEIQAMKKLRHKHILSLYAVATAGD 258
Cdd:cd14116    5 EDFEIGRPLGKGKFGNVY------LARekqskfiLALKVLFKAQLEKagvEHQLRREVEIQSHLRHPNILRLYGYFHDAT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 259 PVYIITELMPKGSL---LQLLRDSDEKdlpilELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLAR 335
Cdd:cd14116   79 RVYLILEYAPLGTVyreLQKLSKFDEQ-----RTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 336 LVKEdiylSRDHNV--PYKWTAPEALSRGHYSIKSDVWSFGVLLHEiFSRGQMPYPGMSNHETFLRVdAGYRMPCPLECP 413
Cdd:cd14116  154 HAPS----SRRTTLcgTLDYLPPEMIEGRMHDEKVDLWSLGVLCYE-FLVGKPPFEANTYQETYKRI-SRVEFTFPDFVT 227
                        250       260
                 ....*....|....*....|....*.
gi 157822719 414 PNIHKLMLSCWSRDPKQRPCFKDLCE 439
Cdd:cd14116  228 EGARDLISRLLKHNPSQRPMLREVLE 253
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
189-388 3.29e-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: 89.70  E-value: 3.29e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFEG-LWKGLVRVAVKVIS--------RDNLlhqhtfQAEIQAMKKLRHKHILSLYAVATAGDP 259
Cdd:cd14069    1 EDWDLVQTLGEGAFGEVFLAvNRNTEEAVAVKFVDmkrapgdcPENI------KKEVCIQKMLSHKNVVRFYGHRREGEF 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 260 VYIITELMPKGSLLqllrDSDEKDLPILElvDFA----SQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLAR 335
Cdd:cd14069   75 QYLFLEYASGGELF----DKIEPDVGMPE--DVAqfyfQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLAT 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 157822719 336 LV----KEDIYLSRDHNVPYkwTAPEAL-SRGHYSIKSDVWSFGVLLHEIFSrGQMPY 388
Cdd:cd14069  149 VFrykgKERLLNKMCGTLPY--VAPELLaKKKYRAEPVDVWSCGIVLFAMLA-GELPW 203
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
197-433 3.34e-20

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


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 89.84  E-value: 3.34e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGLVR-VAVKVISRDNL---LHQHTFQAEIQAMKKLRHKHILSLYAV-ATAGDPVYIITELMPKGS 271
Cdd:cd14165    9 LGEGSYAKVKSAYSERLKCnVAIKIIDKKKApddFVEKFLPRELEILARLNHKSIIKTYEIfETSDGKVYIVMELGVQGD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 272 LLQLLRDSDEkdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKED----IYLSRDH 347
Cdd:cd14165   89 LLEFIKLRGA--LPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCLRDengrIVLSKTF 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 348 NVPYKWTAPEALSRGHYSIK-SDVWSFGVLLHeIFSRGQMPYPGmSNHETFLRVDAGYRMPCP------LECPPNIHKLM 420
Cdd:cd14165  167 CGSAAYAAPEVLQGIPYDPRiYDIWSLGVILY-IMVCGSMPYDD-SNVKKMLKIQKEHRVRFPrsknltSECKDLIYRLL 244
                        250
                 ....*....|...
gi 157822719 421 lscwSRDPKQRPC 433
Cdd:cd14165  245 ----QPDVSQRLC 253
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
197-397 4.35e-20

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: 89.21  E-value: 4.35e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWK--GLVRVA--VKVIS---RDNLLHqhtfqaEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPK 269
Cdd:cd14103    1 LGRGKFGTVYRCVEKatGKELAAkfIKCRKakdREDVRN------EIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 270 GSLLQLLRDsDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLV--TENNLCKVGDFGLARLVKEDIYLSRDH 347
Cdd:cd14103   75 GELFERVVD-DDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILCvsRTGNQIKIIDFGLARKYDPDKKLKVLF 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 157822719 348 NVPyKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETF 397
Cdd:cd14103  154 GTP-EFVAPEVVNYEPISYATDMWSVGVICYVLLS-GLSPFMGDNDAETL 201
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
189-432 4.39e-20

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: 89.53  E-value: 4.39e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVF--EGLWKGLvRVAVKVISRdNLLHQ----HTFQAEIQAMKKLRHKHILSLYAVATAGDPVYI 262
Cdd:cd14186    1 EDFKVLNLLGKGSFACVYraRSLHTGL-EVAIKMIDK-KAMQKagmvQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 263 ITELMPKGSLLQLLRDSdEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKediy 342
Cdd:cd14186   79 VLEMCHNGEMSRYLKNR-KKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLK---- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 343 lsRDHNVPY------KWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRVD-AGYRMPCPL--ECP 413
Cdd:cd14186  154 --MPHEKHFtmcgtpNYISPEIATRSAHGLESDVWSLGCMFYTLLV-GRPPFDTDTVKNTLNKVVlADYEMPAFLsrEAQ 230
                        250
                 ....*....|....*....
gi 157822719 414 PNIHKLMlscwSRDPKQRP 432
Cdd:cd14186  231 DLIHQLL----RKNPADRL 245
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
191-378 4.76e-20

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: 89.25  E-value: 4.76e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEGLWK--GlVRVAVKVISRDNLLH---QHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITE 265
Cdd:cd14079    4 YILGKTLGVGSFGKVKLAEHEltG-HKVAVKILNRQKIKSldmEEKIRREIQILKLFRHPHIIRLYEVIETPTDIFMVME 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMPKGSLLQLLrdSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSR 345
Cdd:cd14079   83 YVSGGELFDYI--VQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSNIMRDGEFLKT 160
                        170       180       190
                 ....*....|....*....|....*....|....
gi 157822719 346 DHNVPyKWTAPEALSRGHYS-IKSDVWSFGVLLH 378
Cdd:cd14079  161 SCGSP-NYAAPEVISGKLYAgPEVDVWSCGVILY 193
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
197-396 6.10e-20

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: 89.25  E-value: 6.10e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFE--GLWKGLvRVAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSLLQ 274
Cdd:cd14192   12 LGGGRFGQVHKctELSTGL-TLAAKIIKVKGAKEREEVKNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGGELFD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 275 llRDSDEK-DLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTEN--NLCKVGDFGLARLVKEDIYLSRDHNVPy 351
Cdd:cd14192   91 --RITDESyQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCVNStgNQIKIIDFGLARRYKPREKLKVNFGTP- 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 157822719 352 KWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHET 396
Cdd:cd14192  168 EFLAPEVVNYDFVSFPTDMWSVGVITYMLLS-GLSPFLGETDAET 211
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
184-390 7.53e-20

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: 90.49  E-value: 7.53e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 184 WERPrEEFTLCKKLGSGYFGEVFEGL-WKGLVRVAVKVISR--DNLLHQHTFQAEIQAMKKLRHKHILSLYAV---ATAG 257
Cdd:cd07878   11 WEVP-ERYQNLTPVGSGAYGSVCSAYdTRLRQKVAVKKLSRpfQSLIHARRTYRELRLLKHMKHENVIGLLDVftpATSI 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 258 D---PVYIITELMPK--GSLLQLLRDSDEKdlpilelVDF-ASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDF 331
Cdd:cd07878   90 EnfnEVYLVTNLMGAdlNNIVKCQKLSDEH-------VQFlIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDF 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157822719 332 GLARLVKEDIylsrDHNVPYKW-TAPE-ALSRGHYSIKSDVWSFGVLLHEIFsRGQMPYPG 390
Cdd:cd07878  163 GLARQADDEM----TGYVATRWyRAPEiMLNWMHYNQTVDIWSVGCIMAELL-KGKALFPG 218
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
195-442 1.02e-19

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: 88.71  E-value: 1.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGlwKGLVRVAVKVISRDNLLH-----QHTFQAEIQAMKKLRHKHILSLYAVATagDPVYIITELMPK 269
Cdd:cd14025    2 EKVGSGGFGQVYKV--RHKHWKTWLAIKCPPSLHvddseRMELLEEAKKMEMAKFRHILPVYGICS--EPVGLVMEYMET 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 270 GSLLQLLRdsdEKDLPILELVDFASQVAEGMCYLESQN--YIHRDLAARNVLVTENNLCKVGDFGLARL--VKEDIYLSR 345
Cdd:cd14025   78 GSLEKLLA---SEPLPWELRFRIIHETAVGMNFLHCMKppLLHLDLKPANILLDAHYHVKISDFGLAKWngLSHSHDLSR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 346 DH---NVPYkwTAPEAL--SRGHYSIKSDVWSFGVLLHEIFSRgQMPYPGMSNHETFL-RVDAGYRMPCPL-------EC 412
Cdd:cd14025  155 DGlrgTIAY--LPPERFkeKNRCPDTKHDVYSFAIVIWGILTQ-KKPFAGENNILHIMvKVVKGHRPSLSPiprqrpsEC 231
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 157822719 413 PpNIHKLMLSCWSRDPKQRPCFKD-------LCEKLS 442
Cdd:cd14025  232 Q-QMICLMKRCWDQDPRKRPTFQDitsetenLLSLLE 267
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
185-437 1.39e-19

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


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 88.32  E-value: 1.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 185 ERPREEFTLCKKLGSGYFGEVFeglwKGLVRVAVK--VISRDNLlHQHTFQAEIQAMKKLRHKHILSLYAVATAGDP--- 259
Cdd:cd14047    2 ERFRQDFKEIELIGSGGFGQVF----KAKHRIDGKtyAIKRVKL-NNEKAEREVKALAKLDHPNIVRYNGCWDGFDYdpe 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 260 -------------VYIITELMPKGSLLQLL-RDSDEKDLPILELVDFaSQVAEGMCYLESQNYIHRDLAARNVLVTENNL 325
Cdd:cd14047   77 tsssnssrsktkcLFIQMEFCEKGTLESWIeKRNGEKLDKVLALEIF-EQITKGVEYIHSKKLIHRDLKPSNIFLVDTGK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 326 CKVGDFGLARLVKEDIYLSRDHNVPyKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQmpyPGMSNHETFLRVDAGYR 405
Cdd:cd14047  156 VKIGDFGLVTSLKNDGKRTKSKGTL-SYMSPEQISSQDYGKEVDIYALGLILFELLHVCD---SAFEKSKFWTDLRNGIL 231
                        250       260       270
                 ....*....|....*....|....*....|..
gi 157822719 406 MPCPLECPPNIHKLMLSCWSRDPKQRPCFKDL 437
Cdd:cd14047  232 PDIFDKRYKIEKTIIKKMLSKKPEDRPNASEI 263
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
187-439 1.43e-19

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: 88.63  E-value: 1.43e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 187 PREEFTLCKKLGSGYFGEVFEGLWKGLVR-VAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITE 265
Cdd:cd06655   17 PKKKYTRYEKIGQGASGTVFTAIDVATGQeVAIKQINLQKQPKKELIINEILVMKELKNPNIVNFLDSFLVGDELFVVME 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMPKGSLLQLLRDS--DEKdlpilELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGL-ARLVKEDIY 342
Cdd:cd06655   97 YLAGGSLTDVVTETcmDEA-----QIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFcAQITPEQSK 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 343 LSRDHNVPYkWTAPEALSRGHYSIKSDVWSFGVLLHEIFsRGQMPYPgmsnHETFLR------VDAGYRMPCPLECPPNI 416
Cdd:cd06655  172 RSTMVGTPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMV-EGEPPYL----NENPLRalyliaTNGTPELQNPEKLSPIF 245
                        250       260
                 ....*....|....*....|...
gi 157822719 417 HKLMLSCWSRDPKQRPCFKDLCE 439
Cdd:cd06655  246 RDFLNRCLEMDVEKRGSAKELLQ 268
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
195-438 2.16e-19

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


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 87.57  E-value: 2.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWKGL-VRVAVKVI----SRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPK 269
Cdd:cd14070    8 RKLGEGSFAKVREGLHAVTgEKVAIKVIdkkkAKKDSYVTKNLRREGRIQQMIRHPNITQLLDILETENSYYLVMELCPG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 270 GSLLQllRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIY---LSRD 346
Cdd:cd14070   88 GNLMH--RIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNCAGILGYsdpFSTQ 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 347 HNVPyKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYP--GMSNHETFLRVDAGYRMPCPLECPPNIHKLMLSCW 424
Cdd:cd14070  166 CGSP-AYAAPELLARKKYGPKVDVWSIGVNMYAMLT-GTLPFTvePFSLRALHQKMVDKEMNPLPTDLSPGAISFLRSLL 243
                        250
                 ....*....|....
gi 157822719 425 SRDPKQRPCFKDLC 438
Cdd:cd14070  244 EPDPLKRPNIKQAL 257
SH2 cd00173
Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they ...
77-155 2.30e-19

Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they bind pTyr-containing polypeptide ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. They are present in a wide array of proteins including: adaptor proteins (Nck1, Crk, Grb2), scaffolds (Slp76, Shc, Dapp1), kinases (Src, Syk, Fps, Tec), phosphatases (Shp-1, Shp-2), transcription factors (STAT1), Ras signaling molecules (Ras-Gap), ubiquitination factors (c-Cbl), cytoskeleton regulators (Tensin), signal regulators (SAP), and phospholipid second messengers (PLCgamma), amongst others.


Pssm-ID: 198173 [Multi-domain]  Cd Length: 79  Bit Score: 82.12  E-value: 2.30e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719  77 PWFFGCISRSEAMHRLQSEdyPKGTFLIRVSQKPGADYVLSVW-DAEAVRHYRIWRNSAG-RLHLNEVVSFSSLSELVNY 154
Cdd:cd00173    1 PWFHGSISREEAERLLRGK--PDGTFLVRESSSEPGDYVLSVRsGDGKVKHYLIERNEGGyYLLGGSGRTFPSLPELVEH 78

                 .
gi 157822719 155 H 155
Cdd:cd00173   79 Y 79
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
191-388 2.60e-19

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: 87.35  E-value: 2.60e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEGLWKGLVR-VAVKVI--SRDNLLHQHtfqaeIQAMKKLRHKHILSLYAVATAGDPVYIITELM 267
Cdd:cd14010    2 YVLYDEIGRGKHSVVYKGRRKGTIEfVAIKCVdkSKRPEVLNE-----VRLTHELKHPNVLKFYEWYETSNHLWLVVEYC 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 268 PKGSLLQLLRdSDEKdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKE-------- 339
Cdd:cd14010   77 TGGDLETLLR-QDGN-LPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLARREGEilkelfgq 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 157822719 340 --DIYLSRDHNVPYK------WTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPY 388
Cdd:cd14010  155 fsDEGNVNKVSKKQAkrgtpyYMAPELFQGGVHSFASDLWALGCVLYEMFT-GKPPF 210
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
186-437 3.12e-19

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: 87.11  E-value: 3.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 186 RPREEFTLCKKLGSGYFGEVFEGLWKGLVR-VAVKvisRDNLLHQHTFQA---EIQAMKKLRHKHILSLYAVATAGDPVY 261
Cdd:cd06648    4 DPRSDLDNFVKIGEGSTGIVCIATDKSTGRqVAVK---KMDLRKQQRRELlfnEVVIMRDYQHPNIVEMYSSYLVGDELW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 262 IITELMPKGSLLQLL---RDSDEKDLPILElvdfasQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVK 338
Cdd:cd06648   81 VVMEFLEGGALTDIVthtRMNEEQIATVCR------AVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQVS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 339 EDIYLSRDH-NVPYkWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHE--TFLRVDAGYRMPCPLECPPN 415
Cdd:cd06648  155 KEVPRRKSLvGTPY-WMAPEVISRLPYGTEVDIWSLGIMVIEMVD-GEPPYFNEPPLQamKRIRDNEPPKLKNLHKVSPR 232
                        250       260
                 ....*....|....*....|..
gi 157822719 416 IHKLMLSCWSRDPKQRPCFKDL 437
Cdd:cd06648  233 LRSFLDRMLVRDPAQRATAAEL 254
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
189-383 4.21e-19

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: 88.13  E-value: 4.21e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFEGLWKGL-VRVAVKVIS--RDNLLHQHTFQaEIQAMKKLRHKHILSLYAVATAGD-----PV 260
Cdd:cd07849    5 PRYQNLSYIGEGAYGMVCSAVHKPTgQKVAIKKISpfEHQTYCLRTLR-EIKILLRFKHENIIGILDIQRPPTfesfkDV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 261 YIITELMPKgSLLQLLRDSDEKDLPILElvdFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKED 340
Cdd:cd07849   84 YIVQELMET-DLYKLIKTQHLSNDHIQY---FLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLARIADPE 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157822719 341 iylsRDHN------VPYKW-TAPE-ALSRGHYSIKSDVWSFGVLLHEIFSR 383
Cdd:cd07849  160 ----HDHTgflteyVATRWyRAPEiMLNSKGYTKAIDIWSVGCILAEMLSN 206
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
200-437 4.65e-19

Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K8 is also called Tumor progression locus 2 (Tpl2) or Cancer Osaka thyroid (Cot), and was first identified as a proto-oncogene in T-cell lymphoma induced by MoMuL virus and in breast carcinoma induced by MMTV. Activated MAP3K8 induces various MAPK pathways including Extracellular Regulated Kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38. It plays a pivotal role in innate immunity, linking Toll-like receptors to the production of TNF and the activation of ERK in macrophages. It is also required in interleukin-1beta production and is critical in host defense against Gram-positive bacteria. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K8 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 86.60  E-value: 4.65e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 200 GYFGEVFEGL-WKGLVRVAVKVISRDnllHQHTFQAEIQAmkKLRHKHILSLYAVATAGDPVYIITELMPKGSLLQLLrd 278
Cdd:cd13995   15 GAFGKVYLAQdTKTKKRMACKLIPVE---QFKPSDVEIQA--CFRHENIAELYGALLWEETVHLFMEAGEGGSVLEKL-- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 279 sdEKDLPI--LELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVgDFGLARLVKEDIYLSRDHNVPYKWTAP 356
Cdd:cd13995   88 --ESCGPMreFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAVLV-DFGLSVQMTEDVYVPKDLRGTEIYMSP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 357 EA-LSRGHySIKSDVWSFGVLLHEIFSrGQMP----YPgMSNHETFLRVDagYRMPCPLE-----CPPNIHKLMLSCWSR 426
Cdd:cd13995  165 EViLCRGH-NTKADIYSLGATIIHMQT-GSPPwvrrYP-RSAYPSYLYII--HKQAPPLEdiaqdCSPAMRELLEAALER 239
                        250
                 ....*....|.
gi 157822719 427 DPKQRPCFKDL 437
Cdd:cd13995  240 NPNHRSSAAEL 250
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
195-439 4.69e-19

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: 86.52  E-value: 4.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWKGLVRV-AVKVISRDNLLHQHTFQA---EIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKG 270
Cdd:cd14189    7 RLLGKGGFARCYEMTDLATNKTyAVKVIPHSRVAKPHQREKivnEIELHRDLHHKHVVKFSHHFEDAENIYIFLELCSRK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 271 SLLQLLRDSDEKDLPilELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGL-ARLVKEDIYLSRDHNV 349
Cdd:cd14189   87 SLAHIWKARHTLLEP--EVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLaARLEPPEQRKKTICGT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 350 PyKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRV-DAGYRMPCPLECPPniHKLMLSCWSRDP 428
Cdd:cd14189  165 P-NYLAPEVLLRQGHGPESDVWSLGCVMYTLLC-GNPPFETLDLKETYRCIkQVKYTLPASLSLPA--RHLLAGILKRNP 240
                        250
                 ....*....|.
gi 157822719 429 KQRPCFKDLCE 439
Cdd:cd14189  241 GDRLTLDQILE 251
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
184-394 5.72e-19

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: 87.73  E-value: 5.72e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 184 WERPrEEFTLCKKLGSGYFGEVFEGLWKGL-VRVAVKVISR--DNLLH-QHTFQaEIQAMKKLRHKHILSLYAVATAGDP 259
Cdd:cd07851   11 WEVP-DRYQNLSPVGSGAYGQVCSAFDTKTgRKVAIKKLSRpfQSAIHaKRTYR-ELRLLKHMKHENVIGLLDVFTPASS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 260 ------VYIITELMPK--GSLLQLLRDSDEKdlpILELVdfaSQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDF 331
Cdd:cd07851   89 ledfqdVYLVTHLMGAdlNNIVKCQKLSDDH---IQFLV---YQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDF 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157822719 332 GLARLVKEDI--YlsrdhnVPYKW-TAPEA-LSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGmSNH 394
Cdd:cd07851  163 GLARHTDDEMtgY------VATRWyRAPEImLNWMHYNQTVDIWSVGCIMAELLT-GKTLFPG-SDH 221
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
198-431 5.97e-19

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: 86.72  E-value: 5.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 198 GSGYFGEVFEGLWKGLVrVAVKVISRDNllHQHTF-QAEIQAMKKLRHKHILSLYA----VATAGDPVYIITELMPKGSL 272
Cdd:cd13998    4 GKGRFGEVWKASLKNEP-VAVKIFSSRD--KQSWFrEKEIYRTPMLKHENILQFIAaderDTALRTELWLVTAFHPNGSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 273 LQLLRdsdEKDLPILELVDFASQVAEGMCYLESQNYI---------HRDLAARNVLVTENNLCKVGDFGLArlVKEDIYL 343
Cdd:cd13998   81 *DYLS---LHTIDWVSLCRLALSVARGLAHLHSEIPGctqgkpaiaHRDLKSKNILVKNDGTCCIADFGLA--VRLSPST 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 344 SRDHNVPY------KWTAPEAL------SRGHYSIKSDVWSFGVLLHEIFSRG----------QMPYPG-MSNHETF--- 397
Cdd:cd13998  156 GEEDNANNgqvgtkRYMAPEVLegainlRDFESFKRVDIYAMGLVLWEMASRCtdlfgiveeyKPPFYSeVPNHPSFedm 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 157822719 398 --LRVDAGYRMPCP---LECPP--NIHKLMLSCWSRDPKQR 431
Cdd:cd13998  236 qeVVVRDKQRPNIPnrwLSHPGlqSLAETIEECWDHDAEAR 276
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
187-432 6.31e-19

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


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 86.24  E-value: 6.31e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 187 PREEFTLCKKLGSGYFGEVFEG--LWKGLVrVAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIIT 264
Cdd:cd06646    7 PQHDYELIQRVGSGTYGDVYKArnLHTGEL-AAVKIIKLEPGDDFSLIQQEIFMVKECKHCNIVAYFGSYLSREKLWICM 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 265 ELMPKGSLLQLLRDSDEkdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLS 344
Cdd:cd06646   86 EYCGGGSLQDIYHVTGP--LSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAAKITATIAKR 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 345 RDH-NVPYkWTAPEALS---RGHYSIKSDVWSFGVLLHEIfsrGQMPYPGMSNHET---FLRVDAGYRMPC---PLECPP 414
Cdd:cd06646  164 KSFiGTPY-WMAPEVAAvekNGGYNQLCDIWAVGITAIEL---AELQPPMFDLHPMralFLMSKSNFQPPKlkdKTKWSS 239
                        250
                 ....*....|....*...
gi 157822719 415 NIHKLMLSCWSRDPKQRP 432
Cdd:cd06646  240 TFHNFVKISLTKNPKKRP 257
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
190-432 6.75e-19

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: 86.23  E-value: 6.75e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLCKKLGSGYFGEVFEGLWK-GLVRVAVKVISRDNLLHQHTFQ---AEIQAMKKLRHKHILSLYAVATAGDPVYIITE 265
Cdd:cd08228    3 NFQIEKKIGRGQFSEVYRATCLlDRKPVALKKVQIFEMMDAKARQdcvKEIDLLKQLNHPNVIKYLDSFIEDNELNIVLE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMPKGSLLQLLR--DSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYL 343
Cdd:cd08228   83 LADAGDLSQMIKyfKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 344 SRDH-NVPYkWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRgQMPYPG--MSNHETFLRVDAGYRMPCPLE-CPPNIHKL 419
Cdd:cd08228  163 AHSLvGTPY-YMSPERIHENGYNFKSDIWSLGCLLYEMAAL-QSPFYGdkMNLFSLCQKIEQCDYPPLPTEhYSEKLREL 240
                        250
                 ....*....|...
gi 157822719 420 MLSCWSRDPKQRP 432
Cdd:cd08228  241 VSMCIYPDPDQRP 253
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
215-431 6.95e-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: 85.91  E-value: 6.95e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 215 RVAVKVISRDNLLHQH--TFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSLLQLLrdSDEKDLPILELVDF 292
Cdd:cd14071   27 EVAIKIIDKSQLDEENlkKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEYASNGEIFDYL--AQHGRMSEKEARKK 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 293 ASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSRDHNVPyKWTAPEALSRGHYS-IKSDVW 371
Cdd:cd14071  105 FWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSNFFKPGELLKTWCGSP-PYAAPEVFEGKEYEgPQLDIW 183
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157822719 372 SFGVLLHeIFSRGQMPYPGMSNHETFLRVDAG-YRMPCPL--ECPPNIHKLMLscwsRDPKQR 431
Cdd:cd14071  184 SLGVVLY-VLVCGALPFDGSTLQTLRDRVLSGrFRIPFFMstDCEHLIRRMLV----LDPSKR 241
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
191-432 7.50e-19

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: 86.62  E-value: 7.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEG--LWKGLVrVAVKVISRDNLLHQHTFQ---AEIQAMKKLRHKHILSLYAVATAGDPVYIITE 265
Cdd:cd08229   26 FRIEKKIGRGQFSEVYRAtcLLDGVP-VALKKVQIFDLMDAKARAdciKEIDLLKQLNHPNVIKYYASFIEDNELNIVLE 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMPKGSLLQLLR--DSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYL 343
Cdd:cd08229  105 LADAGDLSRMIKhfKKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTA 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 344 SRDH-NVPYkWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRgQMPYPG--MSNHETFLRVDAGYRMPCPLE-CPPNIHKL 419
Cdd:cd08229  185 AHSLvGTPY-YMSPERIHENGYNFKSDIWSLGCLLYEMAAL-QSPFYGdkMNLYSLCKKIEQCDYPPLPSDhYSEELRQL 262
                        250
                 ....*....|...
gi 157822719 420 MLSCWSRDPKQRP 432
Cdd:cd08229  263 VNMCINPDPEKRP 275
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
191-437 7.62e-19

Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 85.44  E-value: 7.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFeglwkglvrvavKVISR-DNLLH-----QHTFQAEIQAMKKLR----------HKHILSLYAVA 254
Cdd:cd14050    3 FTILSKLGEGSFGEVF------------KVRSReDGKLYavkrsRSRFRGEKDRKRKLEeverheklgeHPNCVRFIKAW 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 255 TAGDPVYIITELMPKgSLLQLLRDSDekDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGL- 333
Cdd:cd14050   71 EEKGILYIQTELCDT-SLQQYCEETH--SLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLv 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 334 ARLVKEDI-YLSRDHNvpyKWTAPEALsRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHEtfLRvdAGYrmpCPLEC 412
Cdd:cd14050  148 VELDKEDIhDAQEGDP---RYMAPELL-QGSFTKAADIFSLGITILELACNLELPSGGDGWHQ--LR--QGY---LPEEF 216
                        250       260
                 ....*....|....*....|....*....
gi 157822719 413 ----PPNIHKLMLSCWSRDPKQRPCFKDL 437
Cdd:cd14050  217 taglSPELRSIIKLMMDPDPERRPTAEDL 245
SH2 pfam00017
SH2 domain;
78-155 7.64e-19

SH2 domain;


Pssm-ID: 425423 [Multi-domain]  Cd Length: 77  Bit Score: 80.72  E-value: 7.64e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157822719   78 WFFGCISRSEAMHRLQSEDyPKGTFLIRVSQ-KPGaDYVLSVWDAEAVRHYRIWRNSAGRLHLNEVVSFSSLSELVNYH 155
Cdd:pfam00017   1 WYHGKISRQEAERLLLNGK-PDGTFLVRESEsTPG-GYTLSVRDDGKVKHYKIQSTDNGGYYISGGVKFSSLAELVEHY 77
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
191-431 8.39e-19

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: 85.54  E-value: 8.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFG------EVFEGLwkglvRVAVKVISR---DNLLHQHTFQaEIQAMKKLRHKHILSLYAVATAGDPVY 261
Cdd:cd14074    5 YDLEETLGRGHFAvvklarHVFTGE-----KVAVKVIDKtklDDVSKAHLFQ-EVRCMKLVQHPNVVRLYEVIDTQTKLY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 262 IITELMPKGSLLQLLRdSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENN-LCKVGDFGLARLVKED 340
Cdd:cd14074   79 LILELGDGGDMYDYIM-KHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQgLVKLTDFGFSNKFQPG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 341 IYLSRDHNvPYKWTAPEALSRGHYSI-KSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRV-DAGYRMPCPL--ECPPNI 416
Cdd:cd14074  158 EKLETSCG-SLAYSAPEILLGDEYDApAVDIWSLGVILYMLVC-GQPPFQEANDSETLTMImDCKYTVPAHVspECKDLI 235
                        250
                 ....*....|....*
gi 157822719 417 HKLMLscwsRDPKQR 431
Cdd:cd14074  236 RRMLI----RDPKKR 246
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
187-439 8.55e-19

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: 85.87  E-value: 8.55e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 187 PREEFTLCKKLGSGYFGEVFEG--LWKGLVrVAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIIT 264
Cdd:cd06645    9 PQEDFELIQRIGSGTYGDVYKArnVNTGEL-AAIKVIKLEPGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICM 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 265 ELMPKGSLLQLLRDSDEkdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLS 344
Cdd:cd06645   88 EFCGGGSLQDIYHVTGP--LSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITATIAKR 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 345 RDH-NVPYkWTAPEALS---RGHYSIKSDVWSFGVLLHEIfsrGQMPYPGMSNHET---FLRVDAGYRMPC---PLECPP 414
Cdd:cd06645  166 KSFiGTPY-WMAPEVAAverKGGYNQLCDIWAVGITAIEL---AELQPPMFDLHPMralFLMTKSNFQPPKlkdKMKWSN 241
                        250       260
                 ....*....|....*....|....*
gi 157822719 415 NIHKLMLSCWSRDPKQRPCFKDLCE 439
Cdd:cd06645  242 SFHHFVKMALTKNPKKRPTAEKLLQ 266
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
187-388 8.75e-19

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


Pssm-ID: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 85.75  E-value: 8.75e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 187 PREEFTLCKKLGSGYFGEVFEGLWKGL-VRVAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITE 265
Cdd:cd06647    5 PKKKYTRFEKIGQGASGTVYTAIDVATgQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVME 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMPKGSLLQLLRDSDEKDLPILELvdfASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGL-ARLVKEDIYLS 344
Cdd:cd06647   85 YLAGGSLTDVVTETCMDEGQIAAV---CRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQITPEQSKRS 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 157822719 345 RDHNVPYkWTAPEALSRGHYSIKSDVWSFGVLLHEIFsRGQMPY 388
Cdd:cd06647  162 TMVGTPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMV-EGEPPY 203
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
189-402 9.73e-19

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: 85.71  E-value: 9.73e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFEGLWKGLVRV-AVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELM 267
Cdd:cd14114    2 DHYDILEELGTGAFGVVHRCTERATGNNfAAKFIMTPHESDKETVRKEIQIMNQLHHPKLINLHDAFEDDNEMVLILEFL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 268 PKGSLLQLLRDSDEKdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVT--ENNLCKVGDFGLArlvkedIYLSR 345
Cdd:cd14114   82 SGGELFERIAAEHYK-MSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTtkRSNEVKLIDFGLA------THLDP 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157822719 346 DHNVPY-----KWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRVDA 402
Cdd:cd14114  155 KESVKVttgtaEFAAPEIVEREPVGFYTDMWAVGVLSYVLLS-GLSPFAGENDDETLRNVKS 215
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
189-392 9.79e-19

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: 87.04  E-value: 9.79e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFEGLWKGL-VRVAVKVISR--DNL-LHQHTFQaEIQAMKKLRHKHILSLYAVATA------GD 258
Cdd:cd07855    5 DRYEPIETIGSGAYGVVCSAIDTKSgQKVAIKKIPNafDVVtTAKRTLR-ELKILRHFKHDNIIAIRDILRPkvpyadFK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 259 PVYIITELMpKGSLLQLLRdSDEkdlPI-LELVD-FASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARL 336
Cdd:cd07855   84 DVYVVLDLM-ESDLHHIIH-SDQ---PLtLEHIRyFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMARG 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157822719 337 V----KEDIYLSRDHnVPYKW-TAPE-ALSRGHYSIKSDVWSFGVLLHEIFSRGQMpYPGMS 392
Cdd:cd07855  159 LctspEEHKYFMTEY-VATRWyRAPElMLSLPEYTQAIDMWSVGCIFAEMLGRRQL-FPGKN 218
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
197-397 1.05e-18

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: 85.35  E-value: 1.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWK--GLvRVAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSLLQ 274
Cdd:cd14193   12 LGGGRFGQVHKCEEKssGL-KLAAKIIKARSQKEKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVDGGELFD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 275 LLRDSDEKdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVT--ENNLCKVGDFGLARLVKEDIYLSRDHNVPyK 352
Cdd:cd14193   91 RIIDENYN-LTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVsrEANQVKIIDFGLARRYKPREKLRVNFGTP-E 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 157822719 353 WTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETF 397
Cdd:cd14193  169 FLAPEVVNYEFVSFPTDMWSLGVIAYMLLS-GLSPFLGEDDNETL 212
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
186-432 1.41e-18

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: 85.50  E-value: 1.41e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 186 RPREEFTLCKKLGSGYFGEVfeglwkglVRV---------AVKVIS-RDNLLHQHTFQAEIQAMKKLRHKHILSLYAVAT 255
Cdd:cd14046    3 RYLTDFEELQVLGKGAFGQV--------VKVrnkldgryyAIKKIKlRSESKNNSRILREVMLLSRLNHQHVVRYYQAWI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 256 AGDPVYIITELMPKGSLLQLLRDsdEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLAR 335
Cdd:cd14046   75 ERANLYIQMEYCEKSTLRDLIDS--GLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLAT 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 336 LVKEDI-YLSRDHNVPYK-----------------WTAPEALSR--GHYSIKSDVWSFGVLLHEifsrgqMPYPGMSNHE 395
Cdd:cd14046  153 SNKLNVeLATQDINKSTSaalgssgdltgnvgtalYVAPEVQSGtkSTYNEKVDMYSLGIIFFE------MCYPFSTGME 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 157822719 396 TFLRVDAgYRMPcPLECPP----NIH----KLMLSCWSRDPKQRP 432
Cdd:cd14046  227 RVQILTA-LRSV-SIEFPPdfddNKHskqaKLIRWLLNHDPAKRP 269
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
295-437 1.52e-18

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 88.00  E-value: 1.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 295 QVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARL----VKEDIylSRDH-NVPYkWTAPEALSRGHYSIKSD 369
Cdd:PTZ00283 151 QVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFGFSKMyaatVSDDV--GRTFcGTPY-YVAPEIWRRKPYSKKAD 227
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157822719 370 VWSFGVLLHEIFSRgQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLSCWSRDPKQRPCFKDL 437
Cdd:PTZ00283 228 MFSLGVLLYELLTL-KRPFDGENMEEVMHKTLAGRYDPLPPSISPEMQEIVTALLSSDPKRRPSSSKL 294
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
189-431 2.01e-18

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: 85.49  E-value: 2.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFEGLWKGlVRVAVKVISRDNLLHQHTfQAEIQAMKKLRHKHILSLYAVATAGD----PVYIIT 264
Cdd:cd14219    5 KQIQMVKQIGKGRYGEVWMGKWRG-EKVAVKVFFTTEEASWFR-ETEIYQTVLMRHENILGFIAADIKGTgswtQLYLIT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 265 ELMPKGSLLQLLRDSDEKDLPILELvdfASQVAEGMCYLESQNY--------IHRDLAARNVLVTENNLCKVGDFGLARL 336
Cdd:cd14219   83 DYHENGSLYDYLKSTTLDTKAMLKL---AYSSVSGLCHLHTEIFstqgkpaiAHRDLKSKNILVKKNGTCCIADLGLAVK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 337 VKEDiylSRDHNVP-------YKWTAP----EALSRGHYS--IKSDVWSFGVLLHEIFSRG---------QMPY----PG 390
Cdd:cd14219  160 FISD---TNEVDIPpntrvgtKRYMPPevldESLNRNHFQsyIMADMYSFGLILWEVARRCvsggiveeyQLPYhdlvPS 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 157822719 391 MSNHETFLRVDAGYRMPCPL-------ECPPNIHKLMLSCWSRDPKQR 431
Cdd:cd14219  237 DPSYEDMREIVCIKRLRPSFpnrwssdECLRQMGKLMTECWAHNPASR 284
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
192-437 2.27e-18

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: 85.42  E-value: 2.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 192 TLCKKLGSGYFGEVFEGLWKGLVR---VAVKVISRDNLLHQHT--FQAEIQAMKKLRHKHILSLYAVATAGDPVYIITEL 266
Cdd:cd08216    1 ELLYEIGKCFKGGGVVHLAKHKPTntlVAVKKINLESDSKEDLkfLQQEILTSRQLQHPNILPYVTSFVVDNDLYVVTPL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 267 MPKGSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLAR-LVKEDIYLSR 345
Cdd:cd08216   81 MAYGSCRDLLKTHFPEGLPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYAYsMVKHGKRQRV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 346 DHNVP------YKWTAPEALS---RGhYSIKSDVWSFGVLLHEIfSRGQMPYPGMsnHETFLRVDA--GYrMPCPLEC-- 412
Cdd:cd08216  161 VHDFPksseknLPWLSPEVLQqnlLG-YNEKSDIYSVGITACEL-ANGVVPFSDM--PATQMLLEKvrGT-TPQLLDCst 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 157822719 413 ---------------------------------PPNIHKLMLSCWSRDPKQRPCFKDL 437
Cdd:cd08216  236 ypleedsmsqsedsstehpnnrdtrdipyqrtfSEAFHQFVELCLQRDPELRPSASQL 293
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
199-435 2.35e-18

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: 84.58  E-value: 2.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 199 SGYFGEVFeglwkgLVR-------VAVKVISRDNLL---HQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMP 268
Cdd:cd05579    3 RGAYGRVY------LAKkkstgdlYAIKVIKKRDMIrknQVDSVLAERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 269 KGSLLQLLR-----DSDEKDLPILELVdfasqvaEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLAR--LVKEDI 341
Cdd:cd05579   77 GGDLYSLLEnvgalDEDVARIYIAEIV-------LALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKvgLVRRQI 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 342 YLSRDHNVPYKWT-------------APEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRVDAG-YRMP 407
Cdd:cd05579  150 KLSIQKKSNGAPEkedrrivgtpdylAPEILLGQGHGKTVDWWSLGVILYEFLV-GIPPFHAETPEEIFQNILNGkIEWP 228
                        250       260       270
                 ....*....|....*....|....*....|..
gi 157822719 408 CPLECPPN----IHKLMLScwsrDPKQRPCFK 435
Cdd:cd05579  229 EDPEVSDEakdlISKLLTP----DPEKRLGAK 256
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
187-437 3.95e-18

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: 84.65  E-value: 3.95e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 187 PREEFTLCKKLGSGYFGEVFEGLWKGLVR-VAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITE 265
Cdd:cd06659   19 PRQLLENYVKIGEGSTGVVCIAREKHSGRqVAVKMMDLRKQQRRELLFNEVVIMRDYQHPNVVEMYKSYLVGEELWVLME 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMPKGSLLQLL---RDSDEKDLPILElvdfasQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIY 342
Cdd:cd06659   99 YLQGGALTDIVsqtRLNEEQIATVCE------AVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQISKDVP 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 343 LSRDH-NVPYkWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRVDagyrmpcplECPP----NIH 417
Cdd:cd06659  173 KRKSLvGTPY-WMAPEVISRCPYGTEVDIWSLGIMVIEMVD-GEPPYFSDSPVQAMKRLR---------DSPPpklkNSH 241
                        250       260
                 ....*....|....*....|....*..
gi 157822719 418 K-------LMLSCWSRDPKQRPCFKDL 437
Cdd:cd06659  242 KaspvlrdFLERMLVRDPQERATAQEL 268
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
189-380 4.25e-18

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: 84.41  E-value: 4.25e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFEGLW-KGLVR-VAVKVISRDNLlHQHTFQA--------EIQAMKKLRHKHILSLYAVATAGD 258
Cdd:cd14096    1 ENYRLINKIGEGAFSNVYKAVPlRNTGKpVAIKVVRKADL-SSDNLKGssranilkEVQIMKRLSHPNIVKLLDFQESDE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 259 PVYIITELMPKGSLLQllrdsdekdlPILELVDFA--------SQVAEGMCYLESQNYIHRDLAARNVL----------- 319
Cdd:cd14096   80 YYYIVLELADGGEIFH----------QIVRLTYFSedlsrhviTQVASAVKYLHEIGVVHRDIKPENLLfepipfipsiv 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 320 -----------VTENN-----------LCKVGDFGLARLVKEDIYLSRDHNVPYkwTAPEALSRGHYSIKSDVWSFGVLL 377
Cdd:cd14096  150 klrkadddetkVDEGEfipgvggggigIVKLADFGLSKQVWDSNTKTPCGTVGY--TAPEVVKDERYSKKVDMWALGCVL 227

                 ...
gi 157822719 378 HEI 380
Cdd:cd14096  228 YTL 230
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
192-432 4.65e-18

Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 83.87  E-value: 4.65e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 192 TLCKKLGSGYFGEVFegLWKGL---VRVAVKVISRDNLLHQHTFQAEIQAMKKLR-HKHILSL---YAVATAGD--PVYI 262
Cdd:cd14037    6 TIEKYLAEGGFAHVY--LVKTSnggNRAALKRVYVNDEHDLNVCKREIEIMKRLSgHKNIVGYidsSANRSGNGvyEVLL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 263 ITELMPKGSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQN--YIHRDLAARNVLVTENNLCKVGDFGLA------ 334
Cdd:cd14037   84 LMEYCKGGGVIDLMNQRLQTGLTESEILKIFCDVCEAVAAMHYLKppLIHRDLKVENVLISDSGNYKLCDFGSAttkilp 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 335 -------RLVKEDIYlsRDHNVPYKwtAPEA--LSRGH-YSIKSDVWSFGVLLHEI--FSrgqMPYpGMSNheTFLRVDA 402
Cdd:cd14037  164 pqtkqgvTYVEEDIK--KYTTLQYR--APEMidLYRGKpITEKSDIWALGCLLYKLcfYT---TPF-EESG--QLAILNG 233
                        250       260       270
                 ....*....|....*....|....*....|
gi 157822719 403 GYRMPCPLECPPNIHKLMLSCWSRDPKQRP 432
Cdd:cd14037  234 NFTFPDNSRYSKRLHKLIRYMLEEDPEKRP 263
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
189-431 4.86e-18

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


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 84.98  E-value: 4.86e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFEGLWKGLVR-VAVKVISRDNLLHQHTFQAEIQAMKKL----RHKHILSLYAVATAGDPVYII 263
Cdd:cd05619    5 EDFVLHKMLGKGSFGKVFLAELKGTNQfFAIKALKKDVVLMDDDVECTMVEKRVLslawEHPFLTHLFCTFQTKENLFFV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 264 TELMPKGSLLQLLRDSDEKDLPILELvdFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLArlvKEDIYL 343
Cdd:cd05619   85 MEYLNGGDLMFHIQSCHKFDLPRATF--YAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMC---KENMLG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 344 SRDHN----VPyKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETF--LRVDAgyrmPC-PLECPPNI 416
Cdd:cd05619  160 DAKTStfcgTP-DYIAPEILLGQKYNTSVDWWSFGVLLYEMLI-GQSPFHGQDEEELFqsIRMDN----PFyPRWLEKEA 233
                        250
                 ....*....|....*
gi 157822719 417 HKLMLSCWSRDPKQR 431
Cdd:cd05619  234 KDILVKLFVREPERR 248
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
233-437 5.03e-18

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 86.22  E-value: 5.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 233 QAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSLLQLLRDSDEKDLPILE----LVDFasQVAEGMCYLESQNY 308
Cdd:PTZ00267 113 RSELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYGSGGDLNKQIKQRLKEHLPFQEyevgLLFY--QIVLALDEVHSRKM 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 309 IHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYL---SRDHNVPYkWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRgQ 385
Cdd:PTZ00267 191 MHRDLKSANIFLMPTGIIKLGDFGFSKQYSDSVSLdvaSSFCGTPY-YLAPELWERKRYSKKADMWSLGVILYELLTL-H 268
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 157822719 386 MPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLSCWSRDPKQRPCFKDL 437
Cdd:PTZ00267 269 RPFKGPSQREIMQQVLYGKYDPFPCPVSSGMKALLDPLLSKNPALRPTTQQL 320
SH2_Src_Frk cd10369
Src homology 2 (SH2) domain found in the Fyn-related kinase (Frk); Frk is a member of the Src ...
74-157 5.10e-18

Src homology 2 (SH2) domain found in the Fyn-related kinase (Frk); Frk is a member of the Src non-receptor type tyrosine kinase family of proteins. The Frk subfamily is composed of Frk/Rak and Iyk/Bsk/Gst. It is expressed primarily epithelial cells. Frk is a nuclear protein and may function during G1 and S phase of the cell cycle and suppress growth. Unlike the other Src members it lacks a glycine at position 2 of SH4 which is important for addition of a myristic acid moiety that is involved in targeting Src PTKs to cellular membranes. FRK and SHB exert similar effects when overexpressed in rat phaeochromocytoma (PC12) and beta-cells, where both induce PC12 cell differentiation and beta-cell proliferation. Under conditions that cause beta-cell degeneration these proteins augment beta-cell apoptosis. The FRK-SHB responses involve FAK and insulin receptor substrates (IRS) -1 and -2. Frk has been demonstrated to interact with retinoblastoma protein. Frk regulates PTEN protein stability by phosphorylating PTEN, which in turn prevents PTEN degradation. Frk also plays a role in regulation of embryonal pancreatic beta cell formation. Frk has a unique N-terminal domain, an SH3 domain, an SH2 domain, a kinase domain and a regulatory tail, as do the other members of the family. Like the other members of the Src family the SH2 domain in addition to binding the target, also plays an autoinhibitory role by binding to its activation loop. The tryosine involved is at the same site as the tyrosine involved in the autophosphorylation of Src. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 199831  Cd Length: 96  Bit Score: 78.77  E-value: 5.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719  74 ESEPWFFGCISRSEAMHRLQSEDYPKGTFLIRVSQKPGADYVLSVWDAEAVRHYRIWRNSAGRLHLNEVVSFSSLSELVN 153
Cdd:cd10369    1 QAEPWFFGAIKRADAEKQLLYSENQTGAFLIRESESQKGEFSLSVLDGGVVKHYRIRRLDEGGFFLTRRKTFSTLNEFVN 80

                 ....
gi 157822719 154 YHKT 157
Cdd:cd10369   81 YYTT 84
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
197-432 5.91e-18

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: 83.77  E-value: 5.91e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGLVRV-AVKVISRDNLLH-QHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSLlq 274
Cdd:cd06619    9 LGHGNGGTVYKAYHLLTRRIlAVKVIPLDITVElQKQIMSELEILYKCDSPYIIGFYGAFFVENRISICTEFMDGGSL-- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 275 llrdSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIylSRDHNVPYKWT 354
Cdd:cd06619   87 ----DVYRKIPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLVNSI--AKTYVGTNAYM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 355 APEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLR--------VD-AGYRMPCPLECPPNIHkLMLSCWS 425
Cdd:cd06619  161 APERISGEQYGIHSDVWSLGISFMELAL-GRFPYPQIQKNQGSLMplqllqciVDeDPPVLPVGQFSEKFVH-FITQCMR 238

                 ....*..
gi 157822719 426 RDPKQRP 432
Cdd:cd06619  239 KQPKERP 245
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
197-403 5.99e-18

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: 83.09  E-value: 5.99e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGLVR-VAVKVIS-----RDNLLHqhtfqaEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKG 270
Cdd:cd14006    1 LGRGRFGVVKRCIEKATGReFAAKFIPkrdkkKEAVLR------EISILNQLQHPRIIQLHEAYESPTELVLILELCSGG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 271 SLLQLLRDSDEkdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTEN--NLCKVGDFGLARLVKEDIYLSRDHN 348
Cdd:cd14006   75 ELLDRLAERGS--LSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRpsPQIKIIDFGLARKLNPGEELKEIFG 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 157822719 349 VPyKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRVDAG 403
Cdd:cd14006  153 TP-EFVAPEIVNGEPVSLATDMWSIGVLTYVLLS-GLSPFLGEDDQETLANISAC 205
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
244-439 6.89e-18

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: 83.17  E-value: 6.89e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 244 HKHILSLYAVATAGDPVYIITELMPKGSLLQLLrDSDEKdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVT-E 322
Cdd:cd14106   67 CPRVVNLHEVYETRSELILILELAAGGELQTLL-DEEEC-LTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTsE 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 323 NNLC--KVGDFGLARLVKEDIYLSRDHNVPyKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRV 400
Cdd:cd14106  145 FPLGdiKLCDFGISRVIGEGEEIREILGTP-DYVAPEILSYEPISLATDMWSIGVLTYVLLT-GHSPFGGDDKQETFLNI 222
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 157822719 401 DAgyrmpCPLECPPNIHK--------LMLSCWSRDPKQRPCFKDLCE 439
Cdd:cd14106  223 SQ-----CNLDFPEELFKdvsplaidFIKRLLVKDPEKRLTAKECLE 264
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
188-431 8.01e-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: 83.15  E-value: 8.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 188 REEFTLCKKLGSGYFGEVFEGLWKGLVR-VAVKVISRDNLLHQHT-FQAEIQAMKKLRHKHILSLYAVATAGDPVYIITE 265
Cdd:cd14167    2 RDIYDFREVLGTGAFSEVVLAEEKRTQKlVAIKCIAKKALEGKETsIENEIAVLHKIKHPNIVALDDIYESGGHLYLIMQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMPKGSLLQLLRDS---DEKDLPILelvdfASQVAEGMCYLESQNYIHRDLAARNVL---VTENNLCKVGDFGLARLVKE 339
Cdd:cd14167   82 LVSGGELFDRIVEKgfyTERDASKL-----IFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGLSKIEGS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 340 DIYLSRDHNVPyKWTAPEALSRGHYSIKSDVWSFGVLLHeIFSRGQMPYPGMSNHETFLRV-DAGYRMPCPL--ECPPNI 416
Cdd:cd14167  157 GSVMSTACGTP-GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDAKLFEQIlKAEYEFDSPYwdDISDSA 234
                        250
                 ....*....|....*
gi 157822719 417 HKLMLSCWSRDPKQR 431
Cdd:cd14167  235 KDFIQHLMEKDPEKR 249
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
195-390 8.72e-18

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 85.62  E-value: 8.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWKGLVR-VAVKVIsRDNLLHQHTFQA----EIQAMKKLRHKHILSLYAVATAGDPVYIITELMPK 269
Cdd:NF033483  13 ERIGRGGMAEVYLAKDTRLDRdVAVKVL-RPDLARDPEFVArfrrEAQSAASLSHPNIVSVYDVGEDGGIPYIVMEYVDG 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 270 GSLLQLLRDsdEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDI-------- 341
Cdd:NF033483  92 RTLKDYIRE--HGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIARALSSTTmtqtnsvl 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 157822719 342 ----YLSrdhnvpykwtaPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPG 390
Cdd:NF033483 170 gtvhYLS-----------PEQARGGTVDARSDIYSLGIVLYEMLT-GRPPFDG 210
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
195-390 1.08e-17

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: 84.06  E-value: 1.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGL-WKGLVRVAVKVIS-RDNLLHQHTFQaEIQAMKKLRHKHILSLYAVATAG--------------D 258
Cdd:cd07854   11 RPLGCGSNGLVFSAVdSDCDKRVAVKKIVlTDPQSVKHALR-EIKIIRRLDHDNIVKVYEVLGPSgsdltedvgsltelN 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 259 PVYIITELMpKGSLLQLLrdsDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLV-TENNLCKVGDFGLARLV 337
Cdd:cd07854   90 SVYIVQEYM-ETDLANVL---EQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFInTEDLVLKIGDFGLARIV 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 157822719 338 KEDI----YLSRdhNVPYKW-TAPE-ALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPG 390
Cdd:cd07854  166 DPHYshkgYLSE--GLVTKWyRSPRlLLSPNNYTKAIDMWAAGCIFAEMLT-GKPLFAG 221
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
189-380 1.34e-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: 82.63  E-value: 1.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFeglwkgLVR-------VAVKVISRDNLLHQ----HTFqAEIQAMKKLRHKHILSLYAvaTAG 257
Cdd:cd05580    1 DDFEFLKTLGTGSFGRVR------LVKhkdsgkyYALKILKKAKIIKLkqveHVL-NEKRILSEVRHPFIVNLLG--SFQ 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 258 DP--VYIITELMPKGSLLQLLRDSDEKDLPILELvdFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLAR 335
Cdd:cd05580   72 DDrnLYMVMEYVPGGELFSLLRRSGRFPNDVAKF--YAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAK 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 157822719 336 LVKEDiylsrdhnvpyKWT--------APEALSRGHYSIKSDVWSFGVLLHEI 380
Cdd:cd05580  150 RVKDR-----------TYTlcgtpeylAPEIILSKGHGKAVDWWALGILIYEM 191
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
197-434 1.38e-17

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: 82.66  E-value: 1.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGL---WKglVRVAVKVISRDNLL---HQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKG 270
Cdd:cd14026    5 LSRGAFGTVSRARhadWR--VTVAIKCLKLDSPVgdsERNCLLKEAEILHKARFSYILPILGICNEPEFLGIVTEYMTNG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 271 SLLQLLRDSDE-KDLPILELVDFASQVAEGMCYLESQN--YIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSRDH 347
Cdd:cd14026   83 SLNELLHEKDIyPDVAWPLRLRILYEIALGVNYLHNMSppLLHHDLKTQNILLDGEFHVKIADFGLSKWRQLSISQSRSS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 348 N----------VPYKWTAPEALSRGhySIKSDVWSFGVLLHEIFSRGQmPYPGMSNH-ETFLRVDAGYRMPCPLECPP-- 414
Cdd:cd14026  163 KsapeggtiiyMPPEEYEPSQKRRA--SVKHDIYSYAIIMWEVLSRKI-PFEEVTNPlQIMYSVSQGHRPDTGEDSLPvd 239
                        250       260
                 ....*....|....*....|....*
gi 157822719 415 -----NIHKLMLSCWSRDPKQRPCF 434
Cdd:cd14026  240 iphraTLINLIESGWAQNPDERPSF 264
SH2_Src_family cd09933
Src homology 2 (SH2) domain found in the Src family of non-receptor tyrosine kinases; The Src ...
74-169 1.39e-17

Src homology 2 (SH2) domain found in the Src family of non-receptor tyrosine kinases; The Src family kinases are nonreceptor tyrosine kinases that have been implicated in pathways regulating proliferation, angiogenesis, invasion and metastasis, and bone metabolism. It is thought that transforming ability of Src is linked to its ability to activate key signaling molecules in these pathways, rather than through direct activity. As such blocking Src activation has been a target for drug companies. Src family members can be divided into 3 groups based on their expression pattern: 1) Src, Fyn, and Yes; 2) Blk, Fgr, Hck, Lck, and Lyn; and 3) Frk-related kinases Frk/Rak and Iyk/Bsk Of these, cellular c-Src is the best studied and most frequently implicated in oncogenesis. The c-Src contains five distinct regions: a unique N-terminal domain, an SH3 domain, an SH2 domain, a kinase domain and a regulatory tail, as do the other members of the family. Src exists in both active and inactive conformations. Negative regulation occurs through phosphorylation of Tyr, resulting in an intramolecular association between phosphorylated Tyr and the SH2 domain of SRC, which locks the protein in a closed conformation. Further stabilization of the inactive state occurs through interactions between the SH3 domain and a proline-rich stretch of residues within the kinase domain. Conversely, dephosphorylation of Tyr allows SRC to assume an open conformation. Full activity requires additional autophosphorylation of a Tyr residue within the catalytic domain. Loss of the negative-regulatory C-terminal segment has been shown to result in increased activity and transforming potential. Phosphorylation of the C-terminal Tyr residue by C-terminal Src kinase (Csk) and Csk homology kinase results in increased intramolecular interactions and consequent Src inactivation. Specific phosphatases, protein tyrosine phosphatase a (PTPa) and the SH-containing phosphatases SHP1/SHP2, have also been shown to take a part in Src activation. Src is also activated by direct binding of focal adhesion kinase (Fak) and Crk-associated substrate (Cas) to the SH2 domain. SRC activity can also be regulated by numerous receptor tyrosine kinases (RTKs), such as Her2, epidermal growth factor receptor (EGFR), fibroblast growth factor receptor, platelet-derived growth factor receptor (PDGFR), and vascular endothelial growth factor receptor (VEGFR). In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 199827  Cd Length: 101  Bit Score: 77.62  E-value: 1.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719  74 ESEPWFFGCISRSEAMHRLQSEDYPKGTFLIRVSQ-KPGaDYVLSVWD-----AEAVRHYRIWRNSAGRLHLNEVVSFSS 147
Cdd:cd09933    1 EAEEWFFGKIKRKDAEKLLLAPGNPRGTFLIRESEtTPG-AYSLSVRDgddarGDTVKHYRIRKLDNGGYYITTRATFPT 79
                         90       100
                 ....*....|....*....|....
gi 157822719 148 LSELVNYHKTHnlSPGL--QLSMA 169
Cdd:cd09933   80 LQELVQHYSKD--ADGLccRLTVP 101
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
197-431 1.50e-17

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: 82.52  E-value: 1.50e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGLVR-VAVKVISRDNLLHQ-HTFQAEIQAMKKLRH---KHILSLYAVATAGDPVYIITELMPKGS 271
Cdd:cd06917    9 VGRGSYGAVYRGYHVKTGRvVALKVLNLDTDDDDvSDIQKEVALLSQLKLgqpKNIIKYYGSYLKGPSLWIIMDYCEGGS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 272 LLQLLRDSdekdlPILELvdFAS----QVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDiYLSRDH 347
Cdd:cd06917   89 IRTLMRAG-----PIAER--YIAvimrEVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQN-SSKRST 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 348 NV--PYkWTAPEALSRG-HYSIKSDVWSFGVLLHEIfSRGQMPYPGMSNHETFLRVdaGYRMPCPLE---CPPNIHKLML 421
Cdd:cd06917  161 FVgtPY-WMAPEVITEGkYYDTKADIWSLGITTYEM-ATGNPPYSDVDALRAVMLI--PKSKPPRLEgngYSPLLKEFVA 236
                        250
                 ....*....|
gi 157822719 422 SCWSRDPKQR 431
Cdd:cd06917  237 ACLDEEPKDR 246
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
191-437 1.64e-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: 82.11  E-value: 1.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEGLWKGLVR-VAVKVISRDNLLHQHTFQ---AEIQAMKKLRHKHILSLYAVATAGDPVYIITEL 266
Cdd:cd06607    3 FEDLREIGHGSFGAVYYARNKRTSEvVAIKKMSYSGKQSTEKWQdiiKEVKFLRQLRHPNTIEYKGCYLREHTAWLVMEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 267 MpKGSLLQLLrDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSrd 346
Cdd:cd06607   83 C-LGSASDIV-EVHKKPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFGSASLVCPANSFV-- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 347 hNVPYkWTAPE---ALSRGHYSIKSDVWSFGVLLHEIFSRgQMPYPGMsNHETFLRVDAGYRMPC--PLECPPNIHKLML 421
Cdd:cd06607  159 -GTPY-WMAPEvilAMDEGQYDGKVDVWSLGITCIELAER-KPPLFNM-NAMSALYHIAQNDSPTlsSGEWSDDFRNFVD 234
                        250
                 ....*....|....*.
gi 157822719 422 SCWSRDPKQRPCFKDL 437
Cdd:cd06607  235 SCLQKIPQDRPSAEDL 250
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
191-392 1.69e-17

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: 83.38  E-value: 1.69e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVfeglWKGLVR-----VAVKVI------SRDNllhQHTFQaEIQAMKKLR-HKHILSLYAV--ATA 256
Cdd:cd07852    9 YEILKKLGKGAYGIV----WKAIDKktgevVALKKIfdafrnATDA---QRTFR-EIMFLQELNdHPNIIKLLNVirAEN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 257 GDPVYIITELMpkgsllqllrdsdEKDL------PILELVD---FASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCK 327
Cdd:cd07852   81 DKDIYLVFEYM-------------ETDLhaviraNILEDIHkqyIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVK 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157822719 328 VGDFGLARLVKEdiyLSRDHNVP----Y---KW-TAPEAL--SRgHYSIKSDVWSFGVLLHEIFsRGQMPYPGMS 392
Cdd:cd07852  148 LADFGLARSLSQ---LEEDDENPvltdYvatRWyRAPEILlgST-RYTKGVDMWSVGCILGEML-LGKPLFPGTS 217
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
191-397 1.78e-17

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: 82.21  E-value: 1.78e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEGLWKGL-VRVAVKVISRDNL--LHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELM 267
Cdd:cd14097    3 YTFGRKLGQGSFGVVIEATHKETqTKWAIKKINREKAgsSAVKLLEREVDILKHVNHAHIIHLEEVFETPKRMYLVMELC 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 268 PKGSLLQLLrdSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVT----ENNL---CKVGDFGLARL---V 337
Cdd:cd14097   83 EDGELKELL--LRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKssiiDNNDklnIKVTDFGLSVQkygL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 338 KEDIYLSRDHNVPYkwTAPEALSRGHYSIKSDVWSFGVLLHeIFSRGQMPYPGMSNHETF 397
Cdd:cd14097  161 GEDMLQETCGTPIY--MAPEVISAHGYSQQCDIWSIGVIMY-MLLCGEPPFVAKSEEKLF 217
SH2_Grb2_like cd09941
Src homology 2 domain found in Growth factor receptor-bound protein 2 (Grb2) and similar ...
77-161 2.01e-17

Src homology 2 domain found in Growth factor receptor-bound protein 2 (Grb2) and similar proteins; The adaptor proteins here include homologs Grb2 in humans, Sex muscle abnormal protein 5 (Sem-5) in Caenorhabditis elegans, and Downstream of receptor kinase (drk) in Drosophila melanogaster. They are composed of one SH2 and two SH3 domains. Grb2/Sem-5/drk regulates the Ras pathway by linking the tyrosine kinases to the Ras guanine nucleotide releasing protein Sos, which converts Ras to the active GTP-bound state. The SH2 domain of Grb2/Sem-5/drk binds class II phosphotyrosyl peptides while its SH3 domain binds to Sos and Sos-derived, proline-rich peptides. Besides it function in Ras signaling, Grb2 is also thought to play a role in apoptosis. Unlike most SH2 structures in which the peptide binds in an extended conformation (such that the +3 peptide residue occupies a hydrophobic pocket in the protein, conferring a modest degree of selectivity), Grb2 forms several hydrogen bonds via main chain atoms with the side chain of +2 Asn. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 199828  Cd Length: 95  Bit Score: 77.31  E-value: 2.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719  77 PWFFGCISRSEAMHRLQsEDYPKGTFLIRVSQKPGADYVLSVWDAEAVRHYRIWRNSAGRLHLnEVVSFSSLSELVNYHK 156
Cdd:cd09941    4 PWFHGKISRAEAEEILM-NQRPDGAFLIRESESSPGDFSLSVKFGNDVQHFKVLRDGAGKYFL-WVVKFNSLNELVDYHR 81

                 ....*
gi 157822719 157 THNLS 161
Cdd:cd09941   82 TTSVS 86
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
189-439 2.32e-17

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


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 82.20  E-value: 2.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFEGLWKGL-VRVAVKVISRDnlLHQHTFQA---EIQAMKKLRHKHILSLYAVATAGDPVYIIT 264
Cdd:cd06622    1 DEIEVLDELGKGNYGSVYKVLHRPTgVTMAMKEIRLE--LDESKFNQiimELDILHKAVSPYIVDFYGAFFIEGAVYMCM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 265 ELMPKGSLLQLLRDSDE---KDLPILELVDFAsqVAEGM-CYLESQNYIHRDLAARNVLVTENNLCKVGDFGLA-RLVKE 339
Cdd:cd06622   79 EYMDAGSLDKLYAGGVAtegIPEDVLRRITYA--VVKGLkFLKEEHNIIHRDVKPTNVLVNGNGQVKLCDFGVSgNLVAS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 340 diyLSRDHNVPYKWTAPEALS------RGHYSIKSDVWSFGVLLHEIfSRGQMPYPGMSNHETFLRVDA---GYRMPCPL 410
Cdd:cd06622  157 ---LAKTNIGCQSYMAPERIKsggpnqNPTYTVQSDVWSLGLSILEM-ALGRYPYPPETYANIFAQLSAivdGDPPTLPS 232
                        250       260
                 ....*....|....*....|....*....
gi 157822719 411 ECPPNIHKLMLSCWSRDPKQRPCFKDLCE 439
Cdd:cd06622  233 GYSDDAQDFVAKCLNKIPNRRPTYAQLLE 261
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
195-378 2.73e-17

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: 81.53  E-value: 2.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGL-WKGLVRVAVKVISRDNLL-HQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSL 272
Cdd:cd14185    6 RTIGDGNFAVVKECRhWNENQEYAMKIIDKSKLKgKEDMIESEILIIKSLSHPNIVKLFEVYETEKEIYLILEYVRGGDL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 273 LQLLRDS---DEKDLPILeLVDfasqVAEGMCYLESQNYIHRDLAARNVLVTEN----NLCKVGDFGLARLVKEDIYLSr 345
Cdd:cd14185   86 FDAIIESvkfTEHDAALM-IID----LCEALVYIHSKHIVHRDLKPENLLVQHNpdksTTLKLADFGLAKYVTGPIFTV- 159
                        170       180       190
                 ....*....|....*....|....*....|...
gi 157822719 346 dHNVPyKWTAPEALSRGHYSIKSDVWSFGVLLH 378
Cdd:cd14185  160 -CGTP-TYVAPEILSEKGYGLEVDMWAAGVILY 190
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
187-388 2.96e-17

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: 82.08  E-value: 2.96e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 187 PREEFTLCKKLGSGYFGEVFEGLWKGLVR-VAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITE 265
Cdd:cd06656   17 PKKKYTRFEKIGQGASGTVYTAIDIATGQeVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVME 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMPKGSLLQLLRDS--DEKdlpilELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGL-ARLVKEDIY 342
Cdd:cd06656   97 YLAGGSLTDVVTETcmDEG-----QIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQITPEQSK 171
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 157822719 343 LSRDHNVPYkWTAPEALSRGHYSIKSDVWSFGVLLHEIFsRGQMPY 388
Cdd:cd06656  172 RSTMVGTPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMV-EGEPPY 215
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
191-403 2.98e-17

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: 81.38  E-value: 2.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEGLWKGLVRV-AVKVISRDNL------LHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYII 263
Cdd:cd14105    7 YDIGEELGSGQFAVVKKCREKSTGLEyAAKFIKKRRSkasrrgVSREDIEREVSILRQVLHPNIITLHDVFENKTDVVLI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 264 TELMPKGSLLQLLrdSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNL----CKVGDFGLARLVKE 339
Cdd:cd14105   87 LELVAGGELFDFL--AEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNVpiprIKLIDFGLAHKIED 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157822719 340 DIYLSRDHNVPyKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRVDAG 403
Cdd:cd14105  165 GNEFKNIFGTP-EFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGDTKQETLANITAV 226
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
191-403 3.18e-17

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: 81.61  E-value: 3.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEGLWKGL-VRVAVKVISRDnllhQHTFQAEIQAMKKL-RHKHILSLYAVATAGDPVYIITELMP 268
Cdd:cd14175    3 YVVKETIGVGSYSVCKRCVHKATnMEYAVKVIDKS----KRDPSEEIEILLRYgQHPNIITLKDVYDDGKHVYLVTELMR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 269 KGSLL-QLLRDS--DEKDlpilelvdfASQVAEGMC----YLESQNYIHRDLAARNVLVTENN----LCKVGDFGLARLV 337
Cdd:cd14175   79 GGELLdKILRQKffSERE---------ASSVLHTICktveYLHSQGVVHRDLKPSNILYVDESgnpeSLRICDFGFAKQL 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157822719 338 KEDIYLSRDHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPY---PGMSNHETFLRVDAG 403
Cdd:cd14175  150 RAENGLLMTPCYTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLA-GYTPFangPSDTPEEILTRIGSG 217
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
187-395 3.24e-17

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


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 81.61  E-value: 3.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 187 PREEFTLCKKLGSGYFGEVFEGLWKGL-VRVAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITE 265
Cdd:cd06643    3 PEDFWEIVGELGDGAFGKVYKAQNKETgILAAAKVIDTKSEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMPKGS----LLQLLRDSDEKDLPILelvdfASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLA-----RL 336
Cdd:cd06643   83 FCAGGAvdavMLELERPLTEPQIRVV-----CKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSakntrTL 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157822719 337 VKEDIYLSrdhnVPYkWTAPEAL----SRGH-YSIKSDVWSFGVLLHEIfsrGQMPYPgmsNHE 395
Cdd:cd06643  158 QRRDSFIG----TPY-WMAPEVVmcetSKDRpYDYKADVWSLGVTLIEM---AQIEPP---HHE 210
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
195-383 3.84e-17

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: 81.98  E-value: 3.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWKGLVR-VAVKVIsrdnLLHQH------TFQAEIQAMKKLRHKHILSL------YAVATAGDP-- 259
Cdd:cd07866   14 GKLGEGTFGEVYKARQIKTGRvVALKKI----LMHNEkdgfpiTALREIKILKKLKHPNVVPLidmaveRPDKSKRKRgs 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 260 VYIITELMpKGSLLQLLRDSDEKdlpiLELVD---FASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARL 336
Cdd:cd07866   90 VYMVTPYM-DHDLSGLLENPSVK----LTESQikcYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFGLARP 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 157822719 337 VKEDIY--------LSRDHN--VPYKWTAPEALSRG--HYSIKSDVWSFGVLLHEIFSR 383
Cdd:cd07866  165 YDGPPPnpkgggggGTRKYTnlVVTRWYRPPELLLGerRYTTAVDIWGIGCVFAEMFTR 223
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
195-400 3.92e-17

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: 81.37  E-value: 3.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWKGL-VRVAVKVISRDNLLHQ-HTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGsl 272
Cdd:cd07836    6 EKLGEGTYATVYKGRNRTTgEIVALKEIHLDAEEGTpSTAIREISLMKELKHENIVRLHDVIHTENKLMLVFEYMDKD-- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 273 LQLLRDS--DEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSRDHNVP 350
Cdd:cd07836   84 LKKYMDThgVRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARAFGIPVNTFSNEVVT 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 157822719 351 YKWTAPEAL--SRGhYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRV 400
Cdd:cd07836  164 LWYRAPDVLlgSRT-YSTSIDIWSVGCIMAEMIT-GRPLFPGTNNEDQLLKI 213
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
190-432 4.49e-17

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: 81.11  E-value: 4.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLCKKLGSGYFGEVFEGLWKGLVRVAVKVISRDNLLHQ--HTFQAEIQAMKKLRH-KHILSLYA--VATAGDPVYIit 264
Cdd:cd14131    2 PYEILKQLGKGGSSKVYKVLNPKKKIYALKRVDLEGADEQtlQSYKNEIELLKKLKGsDRIIQLYDyeVTDEDDYLYM-- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 265 eLMPKG--SLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLcKVGDFGLARLVKED-I 341
Cdd:cd14131   80 -VMECGeiDLATILKKKRPKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLVKGRL-KLIDFGIAKAIQNDtT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 342 YLSRDHNV-PYKWTAPEALSRGHYSI----------KSDVWSFGVLLHEiFSRGQMPYPGMSNhetFLR-----VDAGYR 405
Cdd:cd14131  158 SIVRDSQVgTLNYMSPEAIKDTSASGegkpkskigrPSDVWSLGCILYQ-MVYGKTPFQHITN---PIAklqaiIDPNHE 233
                        250       260
                 ....*....|....*....|....*..
gi 157822719 406 MPCPLECPPNIHKLMLSCWSRDPKQRP 432
Cdd:cd14131  234 IEFPDIPNPDLIDVMKRCLQRDPKKRP 260
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
188-376 4.98e-17

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: 80.49  E-value: 4.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 188 REEFTLCKKLGSGYFGEVFEGLWKGLVR-VAVKVISRDNLL-HQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITE 265
Cdd:cd14083    2 RDKYEFKEVLGTGAFSEVVLAEDKATGKlVAIKCIDKKALKgKEDSLENEIAVLRKIKHPNIVQLLDIYESKSHLYLVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMPKGSLLQ--LLRDS-DEKDLPILelvdfASQVAEGMCYLESQNYIHRDLAARNVLV---TENNLCKVGDFGLARLVKE 339
Cdd:cd14083   82 LVTGGELFDriVEKGSyTEKDASHL-----IRQVLEAVDYLHSLGIVHRDLKPENLLYyspDEDSKIMISDFGLSKMEDS 156
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 157822719 340 DIyLSRDHNVPyKWTAPEALSRGHYSIKSDVWSFGVL 376
Cdd:cd14083  157 GV-MSTACGTP-GYVAPEVLAQKPYGKAVDCWSIGVI 191
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
190-439 5.07e-17

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: 81.07  E-value: 5.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLCKKLGSGYFGEVFEGLWK--------GLVRVAVKVISRDNLLHqhtfqaEIQAMKKLRHKHILSLYAVATAGDP-- 259
Cdd:cd14048    7 DFEPIQCLGRGGFGVVFEAKNKvddcnyavKRIRLPNNELAREKVLR------EVRALAKLDHPGIVRYFNAWLERPPeg 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 260 ---------VYIITELMPKGSLLQLLRDSDE-KDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVG 329
Cdd:cd14048   81 wqekmdevyLYIQMQLCRKENLKDWMNRRCTmESRELFVCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 330 DFGLARLVKED-----------IYLSRDHNVPYK-WTAPEALSRGHYSIKSDVWSFGVLLHE-IFSRGQMpypgMSNHET 396
Cdd:cd14048  161 DFGLVTAMDQGepeqtvltpmpAYAKHTGQVGTRlYMSPEQIHGNQYSEKVDIFALGLILFElIYSFSTQ----MERIRT 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 157822719 397 FLRVDAGYRMPCPLECPPNIHKLMLSCWSRDPKQRPCFKDLCE 439
Cdd:cd14048  237 LTDVRKLKFPALFTNKYPEERDMVQQMLSPSPSERPEAHEVIE 279
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
215-390 5.54e-17

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: 81.65  E-value: 5.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 215 RVAVKVISR--DNLLHQHTFQAEIQAMKKLRHKHILSLYAVAT-----AGDPVYIITELMPKgSLLQLLRDSDEkdlpil 287
Cdd:cd07858   32 KVAIKKIANafDNRIDAKRTLREIKLLRHLDHENVIAIKDIMPpphreAFNDVYIVYELMDT-DLHQIIRSSQT------ 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 288 eLVD-----FASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSRDHNVPYKWTAPEA-LSR 361
Cdd:cd07858  105 -LSDdhcqyFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLARTTSEKGDFMTEYVVTRWYRAPELlLNC 183
                        170       180
                 ....*....|....*....|....*....
gi 157822719 362 GHYSIKSDVWSFGVLLHEIFSRGQMpYPG 390
Cdd:cd07858  184 SEYTTAIDVWSVGCIFAELLGRKPL-FPG 211
SH2_Src_Lck cd10362
Src homology 2 (SH2) domain in lymphocyte cell kinase (Lck); Lck is a member of the Src ...
74-164 5.58e-17

Src homology 2 (SH2) domain in lymphocyte cell kinase (Lck); Lck is a member of the Src non-receptor type tyrosine kinase family of proteins. It is expressed in the brain, T-cells, and NK cells. The unique domain of Lck mediates its interaction with two T-cell surface molecules, CD4 and CD8. It associates with their cytoplasmic tails on CD4 T helper cells and CD8 cytotoxic T cells to assist signaling from the T cell receptor (TCR) complex. When the T cell receptor is engaged by the specific antigen presented by MHC, Lck phosphorylase the intracellular chains of the CD3 and zeta-chains of the TCR complex, allowing ZAP-70 to bind them. Lck then phosphorylates and activates ZAP-70, which in turn phosphorylates Linker of Activated T cells (LAT), a transmembrane protein that serves as a docking site for proteins including: Shc-Grb2-SOS, PI3K, and phospholipase C (PLC). The tyrosine phosphorylation cascade culminates in the intracellular mobilization of a calcium ions and activation of important signaling cascades within the lymphocyte, including the Ras-MEK-ERK pathway, which goes on to activate certain transcription factors such as NFAT, NF-kappaB, and AP-1. These transcription factors regulate the production cytokines such as Interleukin-2 that promote long-term proliferation and differentiation of the activated lymphocytes. The N-terminal tail of Lck is myristoylated and palmitoylated and it tethers the protein to the plasma membrane of the cell. Lck also contains a SH3 domain, a SH2 domain, and a C-terminal tyrosine kinase domain. Lck has 2 phosphorylation sites, the first an autophosphorylation site that is linked to activation of the protein and the second which is phosphorylated by Csk, which inhibits it. Lck is also inhibited by SHP-1 dephosphorylation and by Cbl ubiquitin ligase, which is part of the ubiquitin-mediated pathway. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198225  Cd Length: 101  Bit Score: 76.06  E-value: 5.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719  74 ESEPWFFGCISRSEAMHRLQSEDYPKGTFLIRVSQKPGADYVLSVWD-----AEAVRHYRIWRNSAGRLHLNEVVSFSSL 148
Cdd:cd10362    1 EPEPWFFKNLSRNDAERQLLAPGNTHGSFLIRESETTAGSFSLSVRDfdqnqGEVVKHYKIRNLDNGGFYISPRITFPGL 80
                         90
                 ....*....|....*.
gi 157822719 149 SELVNYHKthNLSPGL 164
Cdd:cd10362   81 HELVRHYT--NASDGL 94
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
191-402 6.32e-17

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: 80.43  E-value: 6.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEGLWKGL-VRVAVKVISRDNL------LHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYII 263
Cdd:cd14195    7 YEMGEELGSGQFAIVRKCREKGTgKEYAAKFIKKRRLsssrrgVSREEIEREVNILREIQHPNIITLHDIFENKTDVVLI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 264 TELMPKGSLLQLLrdSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNL----CKVGDFGLARLVKE 339
Cdd:cd14195   87 LELVSGGELFDFL--AEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVpnprIKLIDFGIAHKIEA 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157822719 340 DIYLSRDHNVPyKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRVDA 402
Cdd:cd14195  165 GNEFKNIFGTP-EFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGETKQETLTNISA 225
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
185-402 6.60e-17

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: 80.45  E-value: 6.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 185 ERPREEFTLCKKLGSGYFGEVFEGLWKGL-VRVAVKVISRDNL------LHQHTFQAEIQAMKKLRHKHILSLYAVATAG 257
Cdd:cd14194    1 ENVDDYYDTGEELGSGQFAVVKKCREKSTgLQYAAKFIKKRRTkssrrgVSREDIEREVSILKEIQHPNVITLHEVYENK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 258 DPVYIITELMPKGSLLQLLrdSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNL----CKVGDFGL 333
Cdd:cd14194   81 TDVILILELVAGGELFDFL--AEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVpkprIKIIDFGL 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157822719 334 ARLVKEDIYLSRDHNVPyKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRVDA 402
Cdd:cd14194  159 AHKIDFGNEFKNIFGTP-EFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGDTKQETLANVSA 225
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
235-440 6.78e-17

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: 80.56  E-value: 6.78e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 235 EIQAMKKLRHKHILSLYAVATAGDP-VYIITELMPKGSLLQLLRDSdeKDLPILELVDFASQVAEGMCYLESQNYI-HRD 312
Cdd:cd06620   53 ELQILHECHSPYIVSFYGAFLNENNnIIICMEYMDCGSLDKILKKK--GPFPEEVLGKIAVAVLEGLTYLYNVHRIiHRD 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 313 LAARNVLVTENNLCKVGDFGLAR---------LVKEDIYLSrdhnvpykwtaPEALSRGHYSIKSDVWSFGVLLHEIFSr 383
Cdd:cd06620  131 IKPSNILVNSKGQIKLCDFGVSGelinsiadtFVGTSTYMS-----------PERIQGGKYSVKSDVWSLGLSIIELAL- 198
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157822719 384 GQMPYpGMSNHETFLRVD-AGY-------------RMPCPLECPPNIHKLMLSCWSRDPKQRPCFKDLCEK 440
Cdd:cd06620  199 GEFPF-AGSNDDDDGYNGpMGIldllqrivnepppRLPKDRIFPKDLRDFVDRCLLKDPRERPSPQLLLDH 268
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
191-431 7.51e-17

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: 79.99  E-value: 7.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFeglwkgLVR-------VAVKVISRDNLLHQHTFQA---EIQAMKKLRHKHILSLYAVATAGDPV 260
Cdd:cd05578    2 FQILRVIGKGSFGKVC------IVQkkdtkkmFAMKYMNKQKCIEKDSVRNvlnELEILQELEHPFLVNLWYSFQDEEDM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 261 YIITELMPKGSL---LQLLRDSDEkdlpilELVDF-ASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARL 336
Cdd:cd05578   76 YMVVDLLLGGDLryhLQQKVKFSE------ETVKFyICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATK 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 337 VKEDIYL-SRDHNVPYkwTAPEALSRGHYSIKSDVWSFGVLLHEiFSRGQMPYPGMSNH------ETFLRVDAGYRMPCP 409
Cdd:cd05578  150 LTDGTLAtSTSGTKPY--MAPEVFMRAGYSFAVDWWSLGVTAYE-MLRGKRPYEIHSRTsieeirAKFETASVLYPAGWS 226
                        250       260
                 ....*....|....*....|..
gi 157822719 410 LECPPNIHKLMlscwSRDPKQR 431
Cdd:cd05578  227 EEAIDLINKLL----ERDPQKR 244
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
187-388 7.93e-17

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: 80.54  E-value: 7.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 187 PREEFTLCKKLGSGYFGEVFEGLWKGLVR-VAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITE 265
Cdd:cd06654   18 PKKKYTRFEKIGQGASGTVYTAMDVATGQeVAIRQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVME 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMPKGSLLQLLRDS--DEKdlpilELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGL-ARLVKEDIY 342
Cdd:cd06654   98 YLAGGSLTDVVTETcmDEG-----QIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQITPEQSK 172
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 157822719 343 LSRDHNVPYkWTAPEALSRGHYSIKSDVWSFGVLLHEIFsRGQMPY 388
Cdd:cd06654  173 RSTMVGTPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMI-EGEPPY 216
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
197-380 8.55e-17

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: 79.96  E-value: 8.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGLVRV-AVKVISRDNL----LHQHTFQaEIQAMKKLRHKHILSLYAvaTAGDP--VYIITELMPK 269
Cdd:cd05572    1 LGVGGFGRVELVQLKSKGRTfALKCVKKRHIvqtrQQEHIFS-EKEILEECNSPFIVKLYR--TFKDKkyLYMLMEYCLG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 270 GSLLQLLRDSDekdlpileLVD------FASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKediyl 343
Cdd:cd05572   78 GELWTILRDRG--------LFDeytarfYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKKLG----- 144
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 157822719 344 srdhNVPYKWT--------APEALSRGHYSIKSDVWSFGVLLHEI 380
Cdd:cd05572  145 ----SGRKTWTfcgtpeyvAPEIILNKGYDFSVDYWSLGILLYEL 185
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
197-436 9.04e-17

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: 80.48  E-value: 9.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVfeglWKGLV---RVAVKVISRDnllHQHTFQAE--IQAMKKLRHKHILSLYA----VATAGDPVY-IITEL 266
Cdd:cd14054    3 IGQGRYGTV----WKGSLderPVAVKVFPAR---HRQNFQNEkdIYELPLMEHSNILRFIGaderPTADGRMEYlLVLEY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 267 MPKGSLLQLLRdsdEKDLPILELVDFASQVAEGMCYLESQNYI---------HRDLAARNVLVTENNLCKVGDFGLARLV 337
Cdd:cd14054   76 APKGSLCSYLR---ENTLDWMSSCRMALSLTRGLAYLHTDLRRgdqykpaiaHRDLNSRNVLVKADGSCVICDFGLAMVL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 338 KEDIYLSRDHNVPYKWT----------APEAL-------SRGHYSIKSDVWSFGVLLHEIFSRGQMPYPGMSNHEtflrv 400
Cdd:cd14054  153 RGSSLVRGRPGAAENASisevgtlrymAPEVLegavnlrDCESALKQVDVYALGLVLWEIAMRCSDLYPGESVPP----- 227
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 157822719 401 dagYRMPCPLECPPNIH-KLMLSCWSRDpKQRPCFKD 436
Cdd:cd14054  228 ---YQMPYEAELGNHPTfEDMQLLVSRE-KARPKFPD 260
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
189-383 1.50e-16

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: 79.30  E-value: 1.50e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVF------EGLWKGLVRVAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATagDP--- 259
Cdd:cd06653    2 VNWRLGKLLGRGAFGEVYlcydadTGRELAVKQVPFDPDSQETSKEVNALECEIQLLKNLRHDRIVQYYGCLR--DPeek 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 260 -VYIITELMPKGSLlqllRDSDEKDLPILELVD--FASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARL 336
Cdd:cd06653   80 kLSIFVEYMPGGSV----KDQLKAYGALTENVTrrYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKR 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 157822719 337 VkEDIYLSRD-----HNVPYkWTAPEALSRGHYSIKSDVWSFGVLLHEIFSR 383
Cdd:cd06653  156 I-QTICMSGTgiksvTGTPY-WMSPEVISGEGYGRKADVWSVACTVVEMLTE 205
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
185-383 1.53e-16

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: 79.85  E-value: 1.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 185 ERPREEFTLCKKLGSGYFGEVFEGLWKGLVR-VAVKVISRDNLLHQHTFQA--EIQAMKKLRHKHILSLYAVATagDPVY 261
Cdd:cd07864    3 KRCVDKFDIIGIIGEGTYGQVYKAKDKDTGElVALKKVRLDNEKEGFPITAirEIKILRQLNHRSVVNLKEIVT--DKQD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 262 IITELMPKGSLLQLLRDSDEKDLPILE--LVDFAS--------QVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDF 331
Cdd:cd07864   81 ALDFKKDKGAFYLVFEYMDHDLMGLLEsgLVHFSEdhiksfmkQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADF 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 157822719 332 GLARLVKEDIYLSRDHNVPYKWTAPEALSRGH--YSIKSDVWSFGVLLHEIFSR 383
Cdd:cd07864  161 GLARLYNSEESRPYTNKVITLWYRPPELLLGEerYGPAIDVWSCGCILGELFTK 214
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
197-388 1.74e-16

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: 78.99  E-value: 1.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGLVR-VAVKVISRDNLLHQHTFQ--AEIQAMKKLRHKHILSLYAVATAGDPVYIITELMpKGSLL 273
Cdd:cd14082   11 LGSGQFGIVYGGKHRKTGRdVAIKVIDKLRFPTKQESQlrNEVAILQQLSHPGVVNLECMFETPERVFVVMEKL-HGDML 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 274 QLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENN---LCKVGDFGLARLVKEDIYLSRDHNVP 350
Cdd:cd14082   90 EMILSSEKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEpfpQVKLCDFGFARIIGEKSFRRSVVGTP 169
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 157822719 351 yKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPY 388
Cdd:cd14082  170 -AYLAPEVLRNKGYNRSLDMWSVGVIIYVSLS-GTFPF 205
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
217-431 1.75e-16

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: 79.33  E-value: 1.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 217 AVKVISRDNLLHQHTF-----------------------QAEIQAMKKLRHKHILSLYAVA--TAGDPVYIITELMPKGS 271
Cdd:cd14118   23 AMKILSKKKLLKQAGFfrrppprrkpgalgkpldpldrvYREIAILKKLDHPNVVKLVEVLddPNEDNLYMVFELVDKGA 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 272 LLqllrdSDEKDLPILElvDFA----SQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVK-EDIYLSRD 346
Cdd:cd14118  103 VM-----EVPTDNPLSE--ETArsyfRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIADFGVSNEFEgDDALLSST 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 347 HNVPYkWTAPEAL--SRGHYSIKS-DVWSFGVLLHeIFSRGQMPYpgMSNHETFL----RVDAgYRMPCPLECPPNIHKL 419
Cdd:cd14118  176 AGTPA-FMAPEALseSRKKFSGKAlDIWAMGVTLY-CFVFGRCPF--EDDHILGLhekiKTDP-VVFPDDPVVSEQLKDL 250
                        250
                 ....*....|..
gi 157822719 420 MLSCWSRDPKQR 431
Cdd:cd14118  251 ILRMLDKNPSER 262
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
191-402 1.76e-16

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: 79.23  E-value: 1.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEGLWKGL-VRVAVKVI-------SRDNLLHQHtFQAEIQAMKKLRHKHILSLYAVATAGDPVYI 262
Cdd:cd14196    7 YDIGEELGSGQFAIVKKCREKSTgLEYAAKFIkkrqsraSRRGVSREE-IEREVSILRQVLHPNIITLHDVYENRTDVVL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 263 ITELMPKGSLLQLLrdSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNL----CKVGDFGLARLVK 338
Cdd:cd14196   86 ILELVSGGELFDFL--AQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIE 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157822719 339 EDIYLSRDHNVPyKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRVDA 402
Cdd:cd14196  164 DGVEFKNIFGTP-EFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGDTKQETLANITA 225
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
187-383 1.96e-16

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: 79.68  E-value: 1.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 187 PREEFTLCKKLGSGYFGEVFeglWKGLVR----VAVKVISRDNLLHQHTFQ---AEIQAMKKLRHKHILSLYAVATAGDP 259
Cdd:cd06634   13 PEKLFSDLREIGHGSFGAVY---FARDVRnnevVAIKKMSYSGKQSNEKWQdiiKEVKFLQKLRHPNTIEYRGCYLREHT 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 260 VYIITELMpKGSLLQLLrDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKE 339
Cdd:cd06634   90 AWLVMEYC-LGSASDLL-EVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGSASIMAP 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 157822719 340 DIYLSrdhNVPYkWTAPE---ALSRGHYSIKSDVWSFGVLLHEIFSR 383
Cdd:cd06634  168 ANSFV---GTPY-WMAPEvilAMDEGQYDGKVDVWSLGITCIELAER 210
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
217-437 2.18e-16

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: 79.01  E-value: 2.18e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 217 AVKVIS--RDNLLHQH----TFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSLLQLLrdsdEKDLPILE-- 288
Cdd:cd06630   29 AVKQVSfcRNSSSEQEevveAIREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWMAGGSVASLL----SKYGAFSEnv 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 289 LVDFASQVAEGMCYLESQNYIHRDLAARNVLV--TENNLcKVGDFGLARLVKEDIYLSRDHNVPYKWT----APEALSRG 362
Cdd:cd06630  105 IINYTLQILRGLAYLHDNQIIHRDLKGANLLVdsTGQRL-RIADFGAAARLASKGTGAGEFQGQLLGTiafmAPEVLRGE 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 363 HYSIKSDVWSFGVLLHEIFSrGQMPYPG--MSNHETFLrvdagYRMPCPLECP-------PNIHKLMLSCWSRDPKQRPC 433
Cdd:cd06630  184 QYGRSCDVWSVGCVIIEMAT-AKPPWNAekISNHLALI-----FKIASATTPPpipehlsPGLRDVTLRCLELQPEDRPP 257

                 ....
gi 157822719 434 FKDL 437
Cdd:cd06630  258 AREL 261
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
195-431 2.27e-16

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: 79.60  E-value: 2.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWKGLVR-VAVKVISRDNLLHQHTFQAEIQAMKKL----RHKHILSLYAVATAGDPVYIITELMPK 269
Cdd:cd05620    1 KVLGKGSFGKVLLAELKGKGEyFAVKALKKDVVLIDDDVECTMVEKRVLalawENPFLTHLYCTFQTKEHLFFVMEFLNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 270 GSLLQLLRDSDEKDLpiLELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLArlvKEDIY----LSR 345
Cdd:cd05620   81 GDLMFHIQDKGRFDL--YRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMC---KENVFgdnrAST 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 346 DHNVPyKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETF--LRVDAGYRmpcPLECPPNIHKLMLSC 423
Cdd:cd05620  156 FCGTP-DYIAPEILQGLKYTFSVDWWSFGVLLYEMLI-GQSPFHGDDEDELFesIRVDTPHY---PRWITKESKDILEKL 230

                 ....*...
gi 157822719 424 WSRDPKQR 431
Cdd:cd05620  231 FERDPTRR 238
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
187-388 2.47e-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: 79.31  E-value: 2.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 187 PREEFTLCKKLGSGYFGEVFEGLWKGLVR-VAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITE 265
Cdd:cd06658   20 PREYLDSFIKIGEGSTGIVCIATEKHTGKqVAVKKMDLRKQQRRELLFNEVVIMRDYHHENVVDMYNSYLVGDELWVVME 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMPKGSLLQLLRDS--DEKDLPILELvdfasQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYL 343
Cdd:cd06658  100 FLEGGALTDIVTHTrmNEEQIATVCL-----SVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKEVPK 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 157822719 344 SRDH-NVPYkWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPY 388
Cdd:cd06658  175 RKSLvGTPY-WMAPEVISRLPYGTEVDIWSLGIMVIEMID-GEPPY 218
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
191-390 2.53e-16

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: 78.36  E-value: 2.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEV-FEGLWKGLVRVAVKVISRDNL---LHQHTFQAEIQAMKKLRHKHILSLYA-VATAGDPVYIITE 265
Cdd:cd14164    2 YTLGTTIGEGSFSKVkLATSQKYCCKVAIKIVDRRRAspdFVQKFLPRELSILRRVNHPNIVQMFEcIEVANGRLYIVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMPKgSLLQLLRDSdeKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVT-ENNLCKVGDFGLARLVKEDIYLS 344
Cdd:cd14164   82 AAAT-DLLQKIQEV--HHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSaDDRKIKIADFGFARFVEDYPELS 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 157822719 345 RDHNVPYKWTAPEALSRGHYSIKS-DVWSFGVLLHEIFSrGQMPYPG 390
Cdd:cd14164  159 TTFCGSRAYTPPEVILGTPYDPKKyDVWSLGVVLYVMVT-GTMPFDE 204
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
185-383 2.74e-16

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


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 79.31  E-value: 2.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 185 ERPREEFTLCKKLGSGYFGEVF--EGLWKGLVrVAVKVISRDNLLHQHTFQ---AEIQAMKKLRHKHILSLYAVATAGDP 259
Cdd:cd06633   17 DDPEEIFVDLHEIGHGSFGAVYfaTNSHTNEV-VAIKKMSYSGKQTNEKWQdiiKEVKFLQQLKHPNTIEYKGCYLKDHT 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 260 VYIITELMpKGSLLQLLrDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKE 339
Cdd:cd06633   96 AWLVMEYC-LGSASDLL-EVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIASP 173
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 157822719 340 DIYLSrdhNVPYkWTAPE---ALSRGHYSIKSDVWSFGVLLHEIFSR 383
Cdd:cd06633  174 ANSFV---GTPY-WMAPEvilAMDEGQYDGKVDIWSLGITCIELAER 216
PHA02988 PHA02988
hypothetical protein; Provisional
232-442 3.22e-16

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 78.63  E-value: 3.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 232 FQAEIQAMKKLRHKHILSLYA-VATAGDP---VYIITELMPKGSLLQLLRDsdEKDLPILELVDFASQVAEGMCYL-ESQ 306
Cdd:PHA02988  65 TENEIKNLRRIDSNNILKIYGfIIDIVDDlprLSLILEYCTRGYLREVLDK--EKDLSFKTKLDMAIDCCKGLYNLyKYT 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 307 NYIHRDLAARNVLVTENNLCKVGDFGLARLVKediylsrdhNVPYK------WTAPEALSR--GHYSIKSDVWSFGVLLH 378
Cdd:PHA02988 143 NKPYKNLTSVSFLVTENYKLKIICHGLEKILS---------SPPFKnvnfmvYFSYKMLNDifSEYTIKDDIYSLGVVLW 213
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157822719 379 EIFSrGQMPYPGMSNHETF-LRVDAGYRMPCPLECPPNIHKLMLSCWSRDPKQRPCFKDLCEKLS 442
Cdd:PHA02988 214 EIFT-GKIPFENLTTKEIYdLIINKNNSLKLPLDCPLEIKCIVEACTSHDSIKRPNIKEILYNLS 277
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
190-397 3.82e-16

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: 79.27  E-value: 3.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLCKKLGSGYFGEVFEGLWKGLVRV-AVKVISRDNLLHQHTFQAEIQAMKKL----RHKHILSLYAVATAGDPVYIIT 264
Cdd:cd05616    1 DFNFLMVLGKGSFGKVMLAERKGTDELyAVKILKKDVVIQDDDVECTMVEKRVLalsgKPPFLTQLHSCFQTMDRLYFVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 265 ELMPKGSLLQLLRDSDEKDLPilELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLS 344
Cdd:cd05616   81 EYVNGGDLMYHIQQVGRFKEP--HAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTT 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 157822719 345 RDHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETF 397
Cdd:cd05616  159 KTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLA-GQAPFEGEDEDELF 210
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
191-380 4.42e-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: 78.23  E-value: 4.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVF---EGLWKGLVrVAVKVI--------SRDNLLHqhtfqaEIQAMKKLR---HKHILSLYAVATA 256
Cdd:cd14052    2 FANVELIGSGEFSQVYkvsERVPTGKV-YAVKKLkpnyagakDRLRRLE------EVSILRELTldgHDNIVQLIDSWEY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 257 GDPVYIITELMPKGSLLQLLRD-SDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLAR 335
Cdd:cd14052   75 HGHLYIQTELCENGSLDVFLSElGLLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMAT 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 157822719 336 LVKEDIYLSRDHNVPYkwTAPEALSRGHYSIKSDVWSFGVLLHEI 380
Cdd:cd14052  155 VWPLIRGIEREGDREY--IAPEILSEHMYDKPADIFSLGLILLEA 197
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
216-390 4.58e-16

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: 78.77  E-value: 4.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 216 VAVKVISR---DNLLHQHTFQaEIQAMKKLRHKHILSLYAV-ATAGDPVYIITELMpkGSLLQLLRDSDEKDLPILELvd 291
Cdd:cd07856   38 VAVKKIMKpfsTPVLAKRTYR-ELKLLKHLRHENIISLSDIfISPLEDIYFVTELL--GTDLHRLLTSRPLEKQFIQY-- 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 292 FASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDI--YLSRDHnvpykWTAPE-ALSRGHYSIKS 368
Cdd:cd07856  113 FLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLARIQDPQMtgYVSTRY-----YRAPEiMLTWQKYDVEV 187
                        170       180
                 ....*....|....*....|..
gi 157822719 369 DVWSFGVLLHEIFsRGQMPYPG 390
Cdd:cd07856  188 DIWSAGCIFAEML-EGKPLFPG 208
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
217-403 6.30e-16

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


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 78.13  E-value: 6.30e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 217 AVKVISRDNllHQHTFQAEIqAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSLL-QLLRdsdEKDLPILELVDFASQ 295
Cdd:cd14177   33 AVKIIDKSK--RDPSEEIEI-LMRYGQHPNIITLKDVYDDGRYVYLVTELMKGGELLdRILR---QKFFSEREASAVLYT 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 296 VAEGMCYLESQNYIHRDLAARNVLVTEN----NLCKVGDFGLARLVKEDIYLSRDHNVPYKWTAPEALSRGHYSIKSDVW 371
Cdd:cd14177  107 ITKTVDYLHCQGVVHRDLKPSNILYMDDsanaDSIRICDFGFAKQLRGENGLLLTPCYTANFVAPEVLMRQGYDAACDIW 186
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 157822719 372 SFGVLLHEIFSrGQMPY---PGMSNHETFLRVDAG 403
Cdd:cd14177  187 SLGVLLYTMLA-GYTPFangPNDTPEEILLRIGSG 220
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
187-437 6.47e-16

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


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 77.84  E-value: 6.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 187 PREEFTLCKKLGSGYFGEVFEG--LWKG-LVRVAVKVISRDnllHQHTFQAEIQAMKKL-RHKHILSLYAVATAGDP--- 259
Cdd:cd06637    4 PAGIFELVELVGNGTYGQVYKGrhVKTGqLAAIKVMDVTGD---EEEEIKQEINMLKKYsHHRNIATYYGAFIKKNPpgm 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 260 ---VYIITELMPKGSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLArl 336
Cdd:cd06637   81 ddqLWLVMEFCGAGSVTDLIKNTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVS-- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 337 VKEDIYLSRDHN---VPYkWTAPEALS-----RGHYSIKSDVWSFGVLLHEIfSRGQMPYPGMSNHETFLRVDagyRMPC 408
Cdd:cd06637  159 AQLDRTVGRRNTfigTPY-WMAPEVIAcdenpDATYDFKSDLWSLGITAIEM-AEGAPPLCDMHPMRALFLIP---RNPA 233
                        250       260       270
                 ....*....|....*....|....*....|...
gi 157822719 409 PL----ECPPNIHKLMLSCWSRDPKQRPCFKDL 437
Cdd:cd06637  234 PRlkskKWSKKFQSFIESCLVKNHSQRPSTEQL 266
SH3_Src_like cd11845
Src homology 3 domain of Src kinase-like Protein Tyrosine Kinases; Src subfamily members ...
13-66 6.74e-16

Src homology 3 domain of Src kinase-like Protein Tyrosine Kinases; Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, Yes, and Brk. 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). However, Brk lacks the N-terminal myristoylation sites. 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, Lyn, and Brk show a limited expression pattern. This subfamily also includes Drosophila Src42A, Src oncogene at 42A (also known as Dsrc41) which accumulates at sites of cell-cell or cell-matrix adhesion, and participates in Drosphila development and wound healing. It has been shown to promote tube elongation in the tracheal system, is essential for proper cell-cell matching during dorsal closure, and regulates cell-cell contacts in developing Drosophila eyes. The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212779 [Multi-domain]  Cd Length: 52  Bit Score: 71.46  E-value: 6.74e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 157822719  13 YVGLWDFKARTDEELSFQAGDLLHVTRK-EEQWWWATLLDaEGKalaEGYVPHNY 66
Cdd:cd11845    2 YVALYDYEARTDDDLSFKKGDRLQILDDsDGDWWLARHLS-TGK---EGYIPSNY 52
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
189-378 6.94e-16

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: 77.38  E-value: 6.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFEGLWKGLVR-VAVKVISRDNLL-HQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITEL 266
Cdd:cd14184    1 EKYKIGKVIGDGNFAVVKECVERSTGKeFALKIIDKAKCCgKEHLIENEVSILRRVKHPNIIMLIEEMDTPAELYLVMEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 267 MPKGSLLQLLRDSD---EKDLPILelvdfASQVAEGMCYLESQNYIHRDLAARNVLVTE----NNLCKVGDFGLARLVKE 339
Cdd:cd14184   81 VKGGDLFDAITSSTkytERDASAM-----VYNLASALKYLHGLCIVHRDIKPENLLVCEypdgTKSLKLGDFGLATVVEG 155
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 157822719 340 DIYLSrdHNVPyKWTAPEALSRGHYSIKSDVWSFGVLLH 378
Cdd:cd14184  156 PLYTV--CGTP-TYVAPEIIAETGYGLKVDIWAAGVITY 191
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
195-400 7.35e-16

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: 77.35  E-value: 7.35e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWKGLVRV-AVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSLL 273
Cdd:cd14191    8 ERLGSGKFGQVFRLVEKKTKKVwAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEMVSGGELF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 274 QLLRDSDeKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVG--DFGLARLVKEDIYLSRDHNVPy 351
Cdd:cd14191   88 ERIIDED-FELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTKIKliDFGLARRLENAGSLKVLFGTP- 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 157822719 352 KWTAPEALSRGHYSIKSDVWSFGVLLHeIFSRGQMPYPGMSNHETFLRV 400
Cdd:cd14191  166 EFVAPEVINYEPIGYATDMWSIGVICY-ILVSGLSPFMGDNDNETLANV 213
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
232-432 7.62e-16

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: 77.31  E-value: 7.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 232 FQAEIQAMKKLRHKHILSLYAVATagDPVYIITELMPKGSLLQLLRDS--DEKDLPILELVDF--ASQVAEGMCYLESQN 307
Cdd:cd14067   57 FRQEASMLHSLQHPCIVYLIGISI--HPLCFALELAPLGSLNTVLEENhkGSSFMPLGHMLTFkiAYQIAAGLAYLHKKN 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 308 YIHRDLAARNVLV-----TENNLCKVGDFGLARLVKEDIYLSRDHNVPYKwtAPEALSRGHYSIKSDVWSFGVLLHEIFS 382
Cdd:cd14067  135 IIFCDLKSDNILVwsldvQEHINIKLSDYGISRQSFHEGALGVEGTPGYQ--APEIRPRIVYDEKVDMFSYGMVLYELLS 212
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 157822719 383 rGQMPYPGMSNHETFLRVDAGYRmpcPLECPPN------IHKLMLSCWSRDPKQRP 432
Cdd:cd14067  213 -GQRPSLGHHQLQIAKKLSKGIR---PVLGQPEevqffrLQALMMECWDTKPEKRP 264
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
195-432 9.82e-16

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: 76.93  E-value: 9.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGE-VFEGLWKGLvRVAVKVIsrdnLLHQHTFQA-EIQAmkkLR----HKHILSLYAVATAGDPVYIITELMP 268
Cdd:cd13982    7 KVLGYGSEGTiVFRGTFDGR-PVAVKRL----LPEFFDFADrEVQL---LResdeHPNVIRYFCTEKDRQFLYIALELCA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 269 kGSLLQLLRDSDEKDL---PILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLC-----KVGDFGLARLVKED 340
Cdd:cd13982   79 -ASLQDLVESPRESKLflrPGLEPVRLLRQIASGLAHLHSLNIVHRDLKPQNILISTPNAHgnvraMISDFGLCKKLDVG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 341 IY-LSRDHNVP--YKWTAPEALSRGHY---SIKSDVWSFGVLLHEIFSRGQMPYPGMsnhetfLRVDAG-----YRMPCP 409
Cdd:cd13982  158 RSsFSRRSGVAgtSGWIAPEMLSGSTKrrqTRAVDIFSLGCVFYYVLSGGSHPFGDK------LEREANilkgkYSLDKL 231
                        250       260
                 ....*....|....*....|....*.
gi 157822719 410 L---ECPPNIHKLMLSCWSRDPKQRP 432
Cdd:cd13982  232 LslgEHGPEAQDLIERMIDFDPEKRP 257
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
193-447 9.84e-16

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: 76.76  E-value: 9.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 193 LCKKLGSGYFGEVFE-GLWKGLVRVAVKVISRDNLLHQHTFQAEIQAMKKL-RHKHILSLYAVAT-------AGDPVYII 263
Cdd:cd13975    4 LGRELGRGQYGVVYAcDSWGGHFPCALKSVVPPDDKHWNDLALEFHYTRSLpKHERIVSLHGSVIdysygggSSIAVLLI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 264 TELMPKgSLLQLLRdsdeKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLAR-------- 335
Cdd:cd13975   84 MERLHR-DLYTGIK----AGLSLEERLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFCKpeammsgs 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 336 LVKEDIYLsrdhnvpykwtAPEALSrGHYSIKSDVWSFGVLLHEIFSrGQMPYPgmSNHETFLRVD---AGYRMPCPLEC 412
Cdd:cd13975  159 IVGTPIHM-----------APELFS-GKYDNSVDVYAFGILFWYLCA-GHVKLP--EAFEQCASKDhlwNNVRKGVRPER 223
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 157822719 413 PPNIH----KLMLSCWSRDPKQRPCFKDLCEKLSGITRY 447
Cdd:cd13975  224 LPVFDeecwNLMEACWSGDPSQRPLLGIVQPKLQGIMDR 262
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
234-432 1.08e-15

Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 76.98  E-value: 1.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 234 AEIQAMKKLRHKHILSL----------YAVATagDPVYiitelmpkGSLLQLLRDSDEKDLPILELVDFA---------- 293
Cdd:cd14011   51 RGVKQLTRLRHPRILTVqhpleesresLAFAT--EPVF--------ASLANVLGERDNMPSPPPELQDYKlydveikygl 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 294 SQVAEGMCYL-ESQNYIHRDLAARNVLVTENNLCKVGDFGLA-----RLVKEDIYLSRDHNVP------YKWTAPE-ALS 360
Cdd:cd14011  121 LQISEALSFLhNDVKLVHGNICPESVVINSNGEWKLAGFDFCisseqATDQFPYFREYDPNLPplaqpnLNYLAPEyILS 200
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157822719 361 RGHySIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRV--DAGYRMPCPLECPP----NIHKLMLscwSRDPKQRP 432
Cdd:cd14011  201 KTC-DPASDMFSLGVLIYAIYNKGKPLFDCVNNLLSYKKNsnQLRQLSLSLLEKVPeelrDHVKTLL---NVTPEVRP 274
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
193-383 1.19e-15

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: 76.62  E-value: 1.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 193 LCKKLGSGYFGEVF------EGLWKGLVRVAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATagDP----VYI 262
Cdd:cd06652    6 LGKLLGQGAFGRVYlcydadTGRELAVKQVQFDPESPETSKEVNALECEIQLLKNLLHERIVQYYGCLR--DPqertLSI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 263 ITELMPKGSLlqllRDSDEKDLPILELV--DFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVkED 340
Cdd:cd06652   84 FMEYMPGGSI----KDQLKSYGALTENVtrKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGASKRL-QT 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 157822719 341 IYLSRD-----HNVPYkWTAPEALSRGHYSIKSDVWSFGVLLHEIFSR 383
Cdd:cd06652  159 ICLSGTgmksvTGTPY-WMSPEVISGEGYGRKADIWSVGCTVVEMLTE 205
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
189-398 1.27e-15

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: 76.57  E-value: 1.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFEGLWKGLVRV-AVKVISRDNLL-HQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITEL 266
Cdd:cd14183    6 ERYKVGRTIGDGNFAVVKECVERSTGREyALKIINKSKCRgKEHMIQNEVSILRRVKHPNIVLLIEEMDMPTELYLVMEL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 267 MPKGSLLQLLRDSD---EKDLPILeLVDFASQVAegmcYLESQNYIHRDLAARNVLVTENN----LCKVGDFGLARLVKE 339
Cdd:cd14183   86 VKGGDLFDAITSTNkytERDASGM-LYNLASAIK----YLHSLNIVHRDIKPENLLVYEHQdgskSLKLGDFGLATVVDG 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 157822719 340 DIYLSrdHNVPyKWTAPEALSRGHYSIKSDVWSFGVLLHeIFSRGQMPYPGMSNHETFL 398
Cdd:cd14183  161 PLYTV--CGTP-TYVAPEIIAETGYGLKVDIWAAGVITY-ILLCGFPPFRGSGDDQEVL 215
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
189-400 1.28e-15

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: 77.71  E-value: 1.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFeglwkgLVR-------VAVKVISRDNLLHQHT---FQAEIQAMKKLRHKHILSLYAVATAGD 258
Cdd:cd05573    1 DDFEVIKVIGRGAFGEVW------LVRdkdtgqvYAMKILRKSDMLKREQiahVRAERDILADADSPWIVRLHYAFQDED 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 259 PVYIITELMPKGSLLQLLRDSDekDLPIlELVDFasQVAEGMCYLES---QNYIHRDLAARNVLVTENNLCKVGDFGLAR 335
Cdd:cd05573   75 HLYLVMEYMPGGDLMNLLIKYD--VFPE-ETARF--YIAELVLALDSlhkLGFIHRDIKPDNILLDADGHIKLADFGLCT 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 336 LVKED----IYLSRDHNVPYK-------------------------WTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQM 386
Cdd:cd05573  150 KMNKSgdreSYLNDSVNTLFQdnvlarrrphkqrrvraysavgtpdYIAPEVLRGTGYGPECDWWSLGVILYEMLY-GFP 228
                        250
                 ....*....|....
gi 157822719 387 PYPGMSNHETFLRV 400
Cdd:cd05573  229 PFYSDSLVETYSKI 242
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
187-439 1.29e-15

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: 76.57  E-value: 1.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 187 PREEFTLCKKLGSGYFGEVFEGLWKGLVR-VAVKVIsrDNLL-HQHTFQAEIQAMKKL-RHKHILSLYAV------ATAG 257
Cdd:cd06608    4 PAGIFELVEVIGEGTYGKVYKARHKKTGQlAAIKIM--DIIEdEEEEIKLEINILRKFsNHPNIATFYGAfikkdpPGGD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 258 DPVYIITELMPKGSLLQLLRDSDEKDLPILE--LVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLAR 335
Cdd:cd06608   82 DQLWLVMEYCGGGSVTDLVKGLRKKGKRLKEewIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGVSA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 336 LVKEDiyLSRDHNV---PYkWTAPEALS-----RGHYSIKSDVWSFGVLLHEIfSRGQMPYPGMsnHET---FLRVdagy 404
Cdd:cd06608  162 QLDST--LGRRNTFigtPY-WMAPEVIAcdqqpDASYDARCDVWSLGITAIEL-ADGKPPLCDM--HPMralFKIP---- 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 157822719 405 RMPCPLECPP-----NIHKLMLSCWSRDPKQRPCFKDLCE 439
Cdd:cd06608  232 RNPPPTLKSPekwskEFNDFISECLIKNYEQRPFTEELLE 271
PTK_Jak1_rpt1 cd05077
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely ...
214-435 1.30e-15

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: 76.51  E-value: 1.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 214 VRVAVKVIS---RDNLLhqhTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSL-LQLLRDSDEKDLPILEL 289
Cdd:cd05077   37 IKVILKVLDpshRDISL---AFFETASMMRQVSHKHIVLLYGVCVRDVENIMVEEFVEFGPLdLFMHRKSDVLTTPWKFK 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 290 VdfASQVAEGMCYLESQNYIHRDLAARNVLVTENNL-------CKVGDFGLARLVkediyLSRDHNVP-YKWTAPEALS- 360
Cdd:cd05077  114 V--AKQLASALSYLEDKDLVHGNVCTKNILLAREGIdgecgpfIKLSDPGIPITV-----LSRQECVErIPWIAPECVEd 186
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157822719 361 RGHYSIKSDVWSFGVLLHEIFSRGQMPYPG--MSNHETFLrvdAGYRMPCPLECpPNIHKLMLSCWSRDPKQRPCFK 435
Cdd:cd05077  187 SKNLSIAADKWSFGTTLWEICYNGEIPLKDktLAEKERFY---EGQCMLVTPSC-KELADLMTHCMNYDPNQRPFFR 259
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
191-437 1.32e-15

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: 76.57  E-value: 1.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEGLWKGLVR-VAVKVISRD---NLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGD-PVYIITE 265
Cdd:cd14163    2 YQLGKTIGEGTYSKVKEAFSKKHQRkVAIKIIDKSggpEEFIQRFLPRELQIVERLDHKNIIHVYEMLESADgKIYLVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMPKGSLLQLLrdSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLcKVGDFGLARLV-KEDIYLS 344
Cdd:cd14163   82 LAEDGDVFDCV--LHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGFTL-KLTDFGFAKQLpKGGRELS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 345 RDHNVPYKWTAPEALSR-GHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLSC 423
Cdd:cd14163  159 QTFCGSTAYAAPEVLQGvPHDSRKGDIWSMGVVLYVMLC-AQLPFDDTDIPKMLCQQQKGVSLPGHLGVSRTCQDLLKRL 237
                        250
                 ....*....|....
gi 157822719 424 WSRDPKQRPCFKDL 437
Cdd:cd14163  238 LEPDMVLRPSIEEV 251
SH2_Vav_family cd09940
Src homology 2 (SH2) domain found in the Vav family; Vav proteins are involved in several ...
77-161 1.44e-15

Src homology 2 (SH2) domain found in the Vav family; Vav proteins are involved in several processes that require cytoskeletal reorganization, such as the formation of the immunological synapse (IS), phagocytosis, platelet aggregation, spreading, and transformation. Vavs function as guanine nucleotide exchange factors (GEFs) for the Rho/Rac family of GTPases. Vav family members have several conserved motifs/domains including: a leucine-rich region, a leucine-zipper, a calponin homology (CH) domain, an acidic domain, a Dbl-homology (DH) domain, a pleckstrin homology (PH) domain, a cysteine-rich domain, 2 SH3 domains, a proline-rich region, and a SH2 domain. Vavs are the only known Rho GEFs that have both the DH/PH motifs and SH2/SH3 domains in the same protein. The leucine-rich helix-loop-helix (HLH) domain is thought to be involved in protein heterodimerization with other HLH proteins and it may function as a negative regulator by forming inactive heterodimers. The CH domain is usually involved in the association with filamentous actin, but in Vav it controls NFAT stimulation, Ca2+ mobilization, and its transforming activity. Acidic domains are involved in protein-protein interactions and contain regulatory tyrosines. The DH domain is a GDP-GTP exchange factor on Rho/Rac GTPases. The PH domain in involved in interactions with GTP-binding proteins, lipids and/or phosphorylated serine/threonine residues. The SH3 domain is involved in localization of proteins to specific sites within the cell interacting with protein with proline-rich sequences. The SH2 domain mediates a high affinity interaction with tyrosine phosphorylated proteins. There are three Vav mammalian family members: Vav1 which is expressed in the hematopoietic system, Vav2 and Vav3 are more ubiquitously expressed. The members here include insect and amphibian Vavs. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198193  Cd Length: 102  Bit Score: 72.33  E-value: 1.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719  77 PWFFGCISRSEAMHRLQSEdyPKGTFLIRVSQKPGADYVLSVWDAEAVRHYRIWRNSAGRLHLNEVVSFSSLSELVNYHK 156
Cdd:cd09940    6 LWFVGEMERDTAENRLENR--PDGTYLVRVRPQGETQYALSIKYNGDVKHMKIEQRSDGLYYLSESRHFKSLVELVNYYE 83

                 ....*
gi 157822719 157 THNLS 161
Cdd:cd09940   84 RNSLG 88
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
197-437 1.68e-15

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: 75.92  E-value: 1.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFegLWKGLV---RVAVKVISRDNLLHQHTFQA--EIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGS 271
Cdd:cd08220    8 VGRGAYGTVY--LCRRKDdnkLVIIKQIPVEQMTKEERQAAlnEVKVLSMLHHPNIIEYYESFLEDKALMIVMEYAPGGT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 272 LLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTEN-NLCKVGDFGLARLVKEDiylSRDHNV- 349
Cdd:cd08220   86 LFEYIQQRKGSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKrTVVKIGDFGISKILSSK---SKAYTVv 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 350 --PyKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRgQMPYPGMSNHETFLRVDAGYRMPCPLECPPNIHKLMLSCWSRD 427
Cdd:cd08220  163 gtP-CYISPELCEGKPYNQKSDIWALGCVLYELASL-KRAFEAANLPALVLKIMRGTFAPISDRYSEELRHLILSMLHLD 240
                        250
                 ....*....|
gi 157822719 428 PKQRPCFKDL 437
Cdd:cd08220  241 PNKRPTLSEI 250
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
191-383 1.81e-15

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: 77.06  E-value: 1.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEGLWKGL---VRVAVKVISRdnllhqhTFQAEIQAMKKLR----------HKHILSLYAV---- 253
Cdd:cd07857    2 YELIKELGQGAYGIVCSARNAETseeETVAIKKITN-------VFSKKILAKRALRelkllrhfrgHKNITCLYDMdivf 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 254 ATAGDPVYIITELMpKGSLLQLLRDSdeKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGL 333
Cdd:cd07857   75 PGNFNELYLYEELM-EADLHQIIRSG--QPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGL 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 157822719 334 ARLVKEDIYLSRDHNVPY---KW-TAPE-ALSRGHYSIKSDVWSFGVLLHEIFSR 383
Cdd:cd07857  152 ARGFSENPGENAGFMTEYvatRWyRAPEiMLSFQSYTKAIDVWSVGCILAELLGR 206
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
191-407 1.85e-15

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: 76.02  E-value: 1.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVfeGLWKGL---VRVAVKVISRDNLLH---QHTFQaEIQAMKKLRHKHILSLYAVATAGDPVYIIT 264
Cdd:cd14072    2 YRLLKTIGKGNFAKV--KLARHVltgREVAIKIIDKTQLNPsslQKLFR-EVRIMKILNHPNIVKLFEVIETEKTLYLVM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 265 ELMPKGSLLQLLRDS---DEKDlpilELVDFaSQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLV---- 337
Cdd:cd14072   79 EYASGGEVFDYLVAHgrmKEKE----ARAKF-RQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFtpgn 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157822719 338 KEDIYLSrdhNVPYkwTAPEALSRGHYS-IKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRVDAG-YRMP 407
Cdd:cd14072  154 KLDTFCG---SPPY--AAPELFQGKKYDgPEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVLRGkYRIP 219
PTK_Tyk2_rpt1 cd05076
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Tyk2 is ...
214-442 1.91e-15

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: 76.10  E-value: 1.91e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 214 VRVAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSLLQLLRdSDEKDLPILELVDFA 293
Cdd:cd05076   44 LRVVLKVLDPSHHDIALAFFETASLMSQVSHTHLVFVHGVCVRGSENIMVEEFVEHGPLDVWLR-KEKGHVPMAWKFVVA 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 294 SQVAEGMCYLESQNYIHRDLAARNVLVTENNL-------CKVGDFGLARLVkediyLSRDHNVP-YKWTAPEALSRGH-Y 364
Cdd:cd05076  123 RQLASALSYLENKNLVHGNVCAKNILLARLGLeegtspfIKLSDPGVGLGV-----LSREERVErIPWIAPECVPGGNsL 197
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157822719 365 SIKSDVWSFGVLLHEIFSRGQMPYPGMSNHETFLRVDAGYRMPCPlECpPNIHKLMLSCWSRDPKQRPCFKDLCEKLS 442
Cdd:cd05076  198 STAADKWGFGATLLEICFNGEAPLQSRTPSEKERFYQRQHRLPEP-SC-PELATLISQCLTYEPTQRPSFRTILRDLT 273
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
189-400 1.99e-15

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: 76.06  E-value: 1.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFEGLWKGL-VRVAVKV-----ISRDNLLHQHTFQAEIQAmkKLRHKHILSLYAVATAGDPVYI 262
Cdd:cd14117    6 DDFDIGRPLGKGKFGNVYLAREKQSkFIVALKVlfksqIEKEGVEHQLRREIEIQS--HLRHPNILRLYNYFHDRKRIYL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 263 ITELMPKGSLLQLLRDS---DEKdlpilELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLArlVKE 339
Cdd:cd14117   84 ILEYAPRGELYKELQKHgrfDEQ-----RTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWS--VHA 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157822719 340 DIYLSRDHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRV 400
Cdd:cd14117  157 PSLRRRTMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLV-GMPPFESASHTETYRRI 216
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
191-400 2.00e-15

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: 76.39  E-value: 2.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEGLWKGLVR-VAVKVISRDNLLH--QHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELM 267
Cdd:cd07860    2 FQKVEKIGEGTYGVVYKARNKLTGEvVALKKIRLDTETEgvPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 268 PKgSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYlSRDH 347
Cdd:cd07860   82 HQ-DLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVR-TYTH 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 157822719 348 NVPYKW-TAPEAL--SRgHYSIKSDVWSFGVLLHEIFSRGQMpYPGMSNHETFLRV 400
Cdd:cd07860  160 EVVTLWyRAPEILlgCK-YYSTAVDIWSLGCIFAEMVTRRAL-FPGDSEIDQLFRI 213
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
197-431 2.02e-15

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: 76.33  E-value: 2.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGlVRVAVKVI-SRDnllHQHTF-QAEIQAMKKLRHKHILSLYAvATAGD-----PVYIITELMPK 269
Cdd:cd14143    3 IGKGRFGEVWRGRWRG-EDVAVKIFsSRE---ERSWFrEAEIYQTVMLRHENILGFIA-ADNKDngtwtQLWLVSDYHEH 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 270 GSLLQLLrdsDEKDLPILELVDFASQVAEGMCYLESQ--------NYIHRDLAARNVLVTENNLCKVGDFGLArlVKED- 340
Cdd:cd14143   78 GSLFDYL---NRYTVTVEGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDLKSKNILVKKNGTCCIADLGLA--VRHDs 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 341 ----IYLSRDHNVPYK-WTAPEALSRG----HY-SIK-SDVWSFGVLLHEIFSRG---------QMPY----PGMSNHET 396
Cdd:cd14143  153 atdtIDIAPNHRVGTKrYMAPEVLDDTinmkHFeSFKrADIYALGLVFWEIARRCsiggihedyQLPYydlvPSDPSIEE 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 157822719 397 FLRV--DAGYRMPCP-----LECPPNIHKLMLSCWSRDPKQR 431
Cdd:cd14143  233 MRKVvcEQKLRPNIPnrwqsCEALRVMAKIMRECWYANGAAR 274
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
189-430 2.03e-15

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: 76.61  E-value: 2.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFE-------GLWKGLVRVAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAG---- 257
Cdd:cd07862    1 QQYECVAEIGEGAYGKVFKardlkngGRFVALKRVRVQTGEEGMPLSTIREVAVLRHLETFEHPNVVRLFDVCTVSrtdr 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 258 -DPVYIITELMPKgSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARL 336
Cdd:cd07862   81 eTKLTLVFEHVDQ-DLTTYLDKVPEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLARI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 337 VKEDIYLSrDHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQMpYPGMSNHETFLRVDAGYRMPCPLECPPNI 416
Cdd:cd07862  160 YSFQMALT-SVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPL-FRGSSDVDQLGKILDVIGLPGEEDWPRDV 237
                        250
                 ....*....|....
gi 157822719 417 hKLMLSCWSRDPKQ 430
Cdd:cd07862  238 -ALPRQAFHSKSAQ 250
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
191-439 2.49e-15

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: 75.50  E-value: 2.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEGLWKGLVR-VAVKVISRDNLLHQ--------HTFQAEIQAMKKLR---HKHILSLYAVATAGD 258
Cdd:cd14004    2 YTILKEMGEGAYGQVNLAIYKSKGKeVVIKFIFKERILVDtwvrdrklGTVPLEIHILDTLNkrsHPNIVKLLDFFEDDE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 259 PVYIITElmPKGSLLQLLRDSDEKDLpileLVDFAS-----QVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGL 333
Cdd:cd14004   82 FYYLVME--KHGSGMDLFDFIERKPN----MDEKEAkyifrQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 334 ARLVKE---DIYLSRDHnvpykWTAPEALSRGHYSIKS-DVWSFGVLLHEIFSRgQMPYpgmSNHETFLRVDagyrmpcp 409
Cdd:cd14004  156 AAYIKSgpfDTFVGTID-----YAAPEVLRGNPYGGKEqDIWALGVLLYTLVFK-ENPF---YNIEEILEAD-------- 218
                        250       260       270
                 ....*....|....*....|....*....|....
gi 157822719 410 LECPPNIHK----LMLSCWSRDPKQRPCFKDLCE 439
Cdd:cd14004  219 LRIPYAVSEdlidLISRMLNRDVGDRPTIEELLT 252
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
215-390 2.50e-15

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: 76.68  E-value: 2.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 215 RVAVKVISR--DNLLHQHTFQAEIQAMKKLRHKHILSLYAVATagdP---------VYIITELMpKGSLLQLL-RDSDEK 282
Cdd:cd07850   27 NVAIKKLSRpfQNVTHAKRAYRELVLMKLVNHKNIIGLLNVFT---PqksleefqdVYLVMELM-DANLCQVIqMDLDHE 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 283 DLPILelvdfASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSrdhnvPYKWT----APEA 358
Cdd:cd07850  103 RMSYL-----LYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMT-----PYVVTryyrAPEV 172
                        170       180       190
                 ....*....|....*....|....*....|..
gi 157822719 359 LSRGHYSIKSDVWSFGVLLHEIFsRGQMPYPG 390
Cdd:cd07850  173 ILGMGYKENVDIWSVGCIMGEMI-RGTVLFPG 203
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
196-392 2.53e-15

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: 75.85  E-value: 2.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 196 KLGSGYFGEVF--EGLWKGlVRVAVKVISRDNL-------LHQHTFQAEIQAMKKL-RHKHILSLYAVATAGDPVYIITE 265
Cdd:cd13993    7 PIGEGAYGVVYlaVDLRTG-RKYAIKCLYKSGPnskdgndFQKLPQLREIDLHRRVsRHPNIITLHDVFETEVAIYIVLE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMPKGSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTEN-NLCKVGDFGLArlVKEDIylS 344
Cdd:cd13993   86 YCPNGDLFEAITENRIYVGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDeGTVKLCDFGLA--TTEKI--S 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 157822719 345 RDHNV-PYKWTAPEALS------RGHYSIKSDVWSFGV-LLHEIFSRGQMPYPGMS 392
Cdd:cd13993  162 MDFGVgSEFYMAPECFDevgrslKGYPCAAGDIWSLGIiLLNLTFGRNPWKIASES 217
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
182-389 2.78e-15

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: 76.63  E-value: 2.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 182 DDWERPREeftlckkLGSGYFGEVFEGLWK--------GLVRVAVKVISRDNLLHqhtfqaEIQAMKKLRHKHILSLYAV 253
Cdd:cd06650    5 DDFEKISE-------LGAGNGGVVFKVSHKpsglvmarKLIHLEIKPAIRNQIIR------ELQVLHECNSPYIVGFYGA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 254 ATAGDPVYIITELMPKGSLLQLLRDSDEKDLPILELVDFAsqVAEGMCYL-ESQNYIHRDLAARNVLVTENNLCKVGDFG 332
Cdd:cd06650   72 FYSDGEISICMEHMDGGSLDQVLKKAGRIPEQILGKVSIA--VIKGLTYLrEKHKIMHRDVKPSNILVNSRGEIKLCDFG 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 157822719 333 LARLVKEDIYLSRDHNVPYkwTAPEALSRGHYSIKSDVWSFGVLLHEIfSRGQMPYP 389
Cdd:cd06650  150 VSGQLIDSMANSFVGTRSY--MSPERLQGTHYSVQSDIWSMGLSLVEM-AVGRYPIP 203
SH2_Src_Src cd10365
Src homology 2 (SH2) domain found in tyrosine kinase sarcoma (Src); Src is a member of the Src ...
74-158 2.86e-15

Src homology 2 (SH2) domain found in tyrosine kinase sarcoma (Src); Src is a member of the Src non-receptor type tyrosine kinase family of proteins. Src is thought to play a role in the regulation of embryonic development and cell growth. Members here include v-Src and c-Src. v-Src lacks the C-terminal inhibitory phosphorylation site and is therefore constitutively active as opposed to normal cellular src (c-Src) which is only activated under certain circumstances where it is required (e.g. growth factor signaling). v-Src is an oncogene whereas c-Src is a proto-oncogene. c-Src consists of three domains, an N-terminal SH3 domain, a central SH2 domain and a tyrosine kinase domain. The SH2 and SH3 domains work together in the auto-inhibition of the kinase domain. The phosphorylation of an inhibitory tyrosine near the c-terminus of the protein produces a binding site for the SH2 domain which then facilitates binding of the SH3 domain to a polyproline site within the linker between the SH2 domain and the kinase domain. Binding of the SH3 domain inactivates the enzyme. This allows for multiple mechanisms for c-Src activation: dephosphorylation of the C-terminal tyrosine by a protein tyrosine phosphatase, binding of the SH2 domain by a competitive phospho-tyrosine residue, or competitive binding of a polyproline binding site to the SH3 domain. Unlike most other Src members Src lacks cysteine residues in the SH4 domain that undergo palmitylation. Serine and threonine phosphorylation sites have also been identified in the unique domains of Src and are believed to modulate protein-protein interactions or regulate catalytic activity. Alternatively spliced forms of Src, which contain 6- or 11-amino acid insertions in the SH3 domain, are expressed in CNS neurons. c-Src has a unique N-terminal domain, an SH3 domain, an SH2 domain, a kinase domain and a regulatory tail, as do the other members of the family. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198228  Cd Length: 101  Bit Score: 71.23  E-value: 2.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719  74 ESEPWFFGCISRSEAMHRLQSEDYPKGTFLIRVSQKPGADYVLSVWDAEA-----VRHYRIWRNSAGRLHLNEVVSFSSL 148
Cdd:cd10365    1 QAEEWYFGKITRRESERLLLNAENPRGTFLVRESETTKGAYCLSVSDFDNakglnVKHYKIRKLDSGGFYITSRTQFNSL 80
                         90
                 ....*....|
gi 157822719 149 SELVNYHKTH 158
Cdd:cd10365   81 QQLVAYYSKH 90
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
181-393 3.37e-15

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 78.24  E-value: 3.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719  181 WDDWERPREEFTLCKKLGSGYFGEVFeglwkgLVR-------VAVKVISRDNLLHQHTFQ--AEIQAMKKLRHKHILSLY 251
Cdd:PTZ00266    5 YDDGESRLNEYEVIKKIGNGRFGEVF------LVKhkrtqefFCWKAISYRGLKEREKSQlvIEVNVMRELKHKNIVRYI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719  252 A--VATAGDPVYIITELMPKGSLLQLLRDSDEKDLPILE--LVDFASQVAEGMCYLES-------QNYIHRDLAARNVLV 320
Cdd:PTZ00266   79 DrfLNKANQKLYILMEFCDAGDLSRNIQKCYKMFGKIEEhaIVDITRQLLHALAYCHNlkdgpngERVLHRDLKPQNIFL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719  321 T------------ENNL-----CKVGDFGLARLVKEDIYLSRDHNVPYKWTaPEAL--SRGHYSIKSDVWSFGVLLHEIF 381
Cdd:PTZ00266  159 StgirhigkitaqANNLngrpiAKIGDFGLSKNIGIESMAHSCVGTPYYWS-PELLlhETKSYDDKSDMWALGCIIYELC 237
                         250
                  ....*....|..
gi 157822719  382 SrGQMPYPGMSN 393
Cdd:PTZ00266  238 S-GKTPFHKANN 248
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
216-437 4.31e-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: 75.44  E-value: 4.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 216 VAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSLLQLLRDSDEKDLPILELvdfASQ 295
Cdd:cd06657   48 VAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAV---CLA 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 296 VAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSRDH-NVPYkWTAPEALSRGHYSIKSDVWSFG 374
Cdd:cd06657  125 VLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLvGTPY-WMAPELISRLPYGPEVDIWSLG 203
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157822719 375 VLLHEIFSrGQMPY---PGMSNHEtFLRVDAGYRMPCPLECPPNIHKLMLSCWSRDPKQRPCFKDL 437
Cdd:cd06657  204 IMVIEMVD-GEPPYfnePPLKAMK-MIRDNLPPKLKNLHKVSPSLKGFLDRLLVRDPAQRATAAEL 267
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
189-431 4.40e-15

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: 75.55  E-value: 4.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFEGLWKGlVRVAVKVI-SRDnllHQHTF-QAEIQAMKKLRHKHILSLYA----VATAGDPVYI 262
Cdd:cd14142    5 RQITLVECIGKGRYGEVWRGQWQG-ESVAVKIFsSRD---EKSWFrETEIYNTVLLRHENILGFIAsdmtSRNSCTQLWL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 263 ITELMPKGSLLQLLRdsdEKDLPILELVDFASQVAEGMCYLESQNY--------IHRDLAARNVLVTENNLCKVGDFGLA 334
Cdd:cd14142   81 ITHYHENGSLYDYLQ---RTTLDHQEMLRLALSAASGLVHLHTEIFgtqgkpaiAHRDLKSKNILVKSNGQCCIADLGLA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 335 RL---VKEDIYLSRDHNVPYK-WTAPEALS-----RGHYSIK-SDVWSFGVLLHEIFSRG---------QMPY----PGM 391
Cdd:cd14142  158 VThsqETNQLDVGNNPRVGTKrYMAPEVLDetintDCFESYKrVDIYAFGLVLWEVARRCvsggiveeyKPPFydvvPSD 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 157822719 392 SNHETFLRV--DAGYR--MPCPLECPPN---IHKLMLSCWSRDPKQR 431
Cdd:cd14142  238 PSFEDMRKVvcVDQQRpnIPNRWSSDPTltaMAKLMKECWYQNPSAR 284
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
181-439 4.40e-15

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: 75.43  E-value: 4.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 181 WDDWERPREEFTLCKKLGSGYFGEVFEGLWK-GLVRVAVKVISRDNLLHQHtFQAEIQAMKKLR-HKHILSLYAV----- 253
Cdd:cd06638   10 FDSFPDPSDTWEIIETIGKGTYGKVFKVLNKkNGSKAAVKILDPIHDIDEE-IEAEYNILKALSdHPNVVKFYGMyykkd 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 254 ATAGDPVYIITELMPKGSLLQL----LRDSDEKDLPILELVdfASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVG 329
Cdd:cd06638   89 VKNGDQLWLVLELCNGGSVTDLvkgfLKRGERMEEPIIAYI--LHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLV 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 330 DFGL-ARLVKEDIYLSRDHNVPYkWTAPEALS-----RGHYSIKSDVWSFGVLLHEIfSRGQMPYPGMSNHETFLRVdag 403
Cdd:cd06638  167 DFGVsAQLTSTRLRRNTSVGTPF-WMAPEVIAceqqlDSTYDARCDVWSLGITAIEL-GDGDPPLADLHPMRALFKI--- 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 157822719 404 yrmpcPLECPPNIHKLML----------SCWSRDPKQRPCFKDLCE 439
Cdd:cd06638  242 -----PRNPPPTLHQPELwsnefndfirKCLTKDYEKRPTVSDLLQ 282
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
217-403 4.88e-15

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: 75.83  E-value: 4.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 217 AVKVISRDNllHQHTFQAEIqAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSLL-QLLRD---SDEKDLPILELVdf 292
Cdd:cd14176   48 AVKIIDKSK--RDPTEEIEI-LLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLdKILRQkffSEREASAVLFTI-- 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 293 aSQVAEgmcYLESQNYIHRDLAARNVLVTENN----LCKVGDFGLARLVKEDIYLSRDHNVPYKWTAPEALSRGHYSIKS 368
Cdd:cd14176  123 -TKTVE---YLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLERQGYDAAC 198
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 157822719 369 DVWSFGVLLHEIFSrGQMPY---PGMSNHETFLRVDAG 403
Cdd:cd14176  199 DIWSLGVLLYTMLT-GYTPFangPDDTPEEILARIGSG 235
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
214-403 5.98e-15

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: 75.05  E-value: 5.98e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 214 VRVAVKVISRDnllhQHTFQAEIQAMKKL-RHKHILSLYAVATAGDPVYIITELMPKGSLL-QLLRdsdEKDLPILELVD 291
Cdd:cd14178   29 TEYAVKIIDKS----KRDPSEEIEILLRYgQHPNIITLKDVYDDGKFVYLVMELMRGGELLdRILR---QKCFSEREASA 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 292 FASQVAEGMCYLESQNYIHRDLAARNVLVTENN----LCKVGDFGLARLVKEDIYLSRDHNVPYKWTAPEALSRGHYSIK 367
Cdd:cd14178  102 VLCTITKTVEYLHSQGVVHRDLKPSNILYMDESgnpeSIRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKRQGYDAA 181
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 157822719 368 SDVWSFGVLLHEIFSrGQMPY---PGMSNHETFLRVDAG 403
Cdd:cd14178  182 CDIWSLGILLYTMLA-GFTPFangPDDTPEEILARIGSG 219
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
191-388 7.86e-15

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: 75.08  E-value: 7.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFeglwkglvrvAVKVISRDnlLHQHTfQAEIQAMKKLR-HKHILSLYAVATAGDPVYIITELMPK 269
Cdd:cd14179   20 FSICRKCLHKKTNQEY----------AVKIVSKR--MEANT-QREIAALKLCEgHPNIVKLHEVYHDQLHTFLVMELLKG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 270 GSLLQLLRDsdEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVT---ENNLCKVGDFGLARLVKEDIYLSRD 346
Cdd:cd14179   87 GELLERIKK--KQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTdesDNSEIKIIDFGFARLKPPDNQPLKT 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 157822719 347 HNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPY 388
Cdd:cd14179  165 PCFTLHYAAPELLNYNGYDESCDLWSLGVILYTMLS-GQVPF 205
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
190-437 8.85e-15

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are three PIM2 isoforms resulting from alternative translation initiation sites. PIM2 is highly expressed in leukemia and lymphomas and has been shown to promote the survival and proliferation of tumor cells. The PIM2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 74.12  E-value: 8.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLCKKLGSGYFGEVFEG--LWKGLvRVAVKVISRDNLLH------QHTFQAEIQAMKKLrhkhilslyaVATAGDPvY 261
Cdd:cd14101    1 QYTMGNLLGKGGFGTVYAGhrISDGL-QVAIKQISRNRVQQwsklpgVNPVPNEVALLQSV----------GGGPGHR-G 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 262 IITEL----MPKGSLLQLlrdsdEKDLPILELVDFAS---------------QVAEGMCYLESQNYIHRDLAARNVLVTE 322
Cdd:cd14101   69 VIRLLdwfeIPEGFLLVL-----ERPQHCQDLFDYITergaldeslarrffkQVVEAVQHCHSKGVVHRDIKDENILVDL 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 323 NNLC-KVGDFGLARLVKEDIYLSRDHNVPYkwTAPEALSRGHY-SIKSDVWSFGVLLHEIFSrGQMPYpgmSNHETFLRV 400
Cdd:cd14101  144 RTGDiKLIDFGSGATLKDSMYTDFDGTRVY--SPPEWILYHQYhALPATVWSLGILLYDMVC-GDIPF---ERDTDILKA 217
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 157822719 401 DAGYRMPCPLECppniHKLMLSCWSRDPKQRPCFKDL 437
Cdd:cd14101  218 KPSFNKRVSNDC----RSLIRSCLAYNPSDRPSLEQI 250
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
197-332 1.09e-14

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


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 70.55  E-value: 1.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVF--EGLWKGlVRVAVKVISRDNLLHQHTFQAEIQAMKKLR--HKHILSLYAVATAGDPVYIITELMPKGSL 272
Cdd:cd13968    1 MGEGASAKVFwaEGECTT-IGVAVKIGDDVNNEEGEDLESEMDILRRLKglELNIPKVLVTEDVDGPNILLMELVKGGTL 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157822719 273 LQLL--RDSDEKDLPIlelvdFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFG 332
Cdd:cd13968   80 IAYTqeEELDEKDVES-----IMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
187-375 1.10e-14

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: 74.27  E-value: 1.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 187 PREEFTLCKKLGSGYFGEVFEG--LWKG-LVRVAVKVISRDnllHQHTFQAEIQAMKKL-RHKHILSLYAVATAGDP--- 259
Cdd:cd06636   14 PAGIFELVEVVGNGTYGQVYKGrhVKTGqLAAIKVMDVTED---EEEEIKLEINMLKKYsHHRNIATYYGAFIKKSPpgh 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 260 ---VYIITELMPKGSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLArl 336
Cdd:cd06636   91 ddqLWLVMEFCGAGSVTDLVKNTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVS-- 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 157822719 337 VKEDIYLSRDHN---VPYkWTAPEALS-----RGHYSIKSDVWSFGV 375
Cdd:cd06636  169 AQLDRTVGRRNTfigTPY-WMAPEVIAcdenpDATYDYRSDIWSLGI 214
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
191-441 1.14e-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: 73.87  E-value: 1.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFeglwkgLVR-------VAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYA-----VATAGD 258
Cdd:cd13986    2 YRIQRLLGEGGFSFVY------LVEdlstgrlYALKKILCHSKEDVKEAMREIENYRLFNHPNILRLLDsqivkEAGGKK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 259 PVYIITELMPKGSLLQLLRDSDEKDLPILE--LVDFASQVAEGMCYLESQN---YIHRDLAARNVLVTENNLCKVGDFGL 333
Cdd:cd13986   76 EVYLLLPYYKRGSLQDEIERRLVKGTFFPEdrILHIFLGICRGLKAMHEPElvpYAHRDIKPGNVLLSEDDEPILMDLGS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 334 ARLVKEDIYLSRD---------HNVPYKWTAPEALSRGHYSI---KSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLR-- 399
Cdd:cd13986  156 MNPARIEIEGRREalalqdwaaEHCTMPYRAPELFDVKSHCTideKTDIWSLGCTLYALMY-GESPFERIFQKGDSLAla 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 157822719 400 -VDAGYRMPCPLECPPNIHKLMLSCWSRDPKQRPCFKDLCEKL 441
Cdd:cd13986  235 vLSGNYSFPDNSRYSEELHQLVKSMLVVNPAERPSIDDLLSRV 277
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
217-441 1.19e-14

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: 74.36  E-value: 1.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 217 AVKVISRDN-----LLHQHTFQAEIQAMKKLRHKHILSLYAVATAGD-PVYIITELMPK--GSLLQLLRDSDEKDLPILE 288
Cdd:cd14001   32 AVKKINSKCdkgqrSLYQERLKEEAKILKSLNHPNIVGFRAFTKSEDgSLCLAMEYGGKslNDLIEERYEAGLGPFPAAT 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 289 LVDFASQVAEGMCYLESQNYI-HRDLAARNVLVTEN-NLCKVGDFGLARLVKEDIYLSRDHNVPY----KWTAPEALSRG 362
Cdd:cd14001  112 ILKVALSIARALEYLHNEKKIlHGDIKSGNVLIKGDfESVKLCDFGVSLPLTENLEVDSDPKAQYvgtePWKAKEALEEG 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 363 H-YSIKSDVWSFGVLLHEIFS-------RGQMP--YPGMSNHETFLRVDAGY-----RMPCPLECPPNIHKLMLS----C 423
Cdd:cd14001  192 GvITDKADIFAYGLVLWEMMTlsvphlnLLDIEddDEDESFDEDEEDEEAYYgtlgtRPALNLGELDDSYQKVIElfyaC 271
                        250
                 ....*....|....*...
gi 157822719 424 WSRDPKQRPCFKDLCEKL 441
Cdd:cd14001  272 TQEDPKDRPSAAHIVEAL 289
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
219-444 1.21e-14

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: 73.77  E-value: 1.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 219 KVISRDNLLHQHTFQAEIQAMK-----KLRHKHILSLYAVATAGDPVYIITELMPKGSLLQLLRDS----DEKDLPILEL 289
Cdd:cd14044   32 KVVILKDLKNNEGNFTEKQKIElnkllQIDYYNLTKFYGTVKLDTMIFGVIEYCERGSLRDVLNDKisypDGTFMDWEFK 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 290 VDFASQVAEGMCYLESQNY-IHRDLAARNVLVTENNLCKVGDFGLARLVKEdiylSRDhnvpyKWTAPEALSRGHYSIKS 368
Cdd:cd14044  112 ISVMYDIAKGMSYLHSSKTeVHGRLKSTNCVVDSRMVVKITDFGCNSILPP----SKD-----LWTAPEHLRQAGTSQKG 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 369 DVWSFGVLLHEIFSRGQMPYPGMSNHetflRVDAGYRMPCPLECPP---------------NIHKLMLSCWSRDPKQRPC 433
Cdd:cd14044  183 DVYSYGIIAQEIILRKETFYTAACSD----RKEKIYRVQNPKGMKPfrpdlnlesagererEVYGLVKNCWEEDPEKRPD 258
                        250
                 ....*....|.
gi 157822719 434 FKDLCEKLSGI 444
Cdd:cd14044  259 FKKIENTLAKI 269
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
197-441 1.22e-14

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: 73.46  E-value: 1.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGlWKGLVR--VAVKVISRDNLLHQHTfQAEIQAMKKLR------HKHILSLYAVATAGDPVYIITELMP 268
Cdd:cd14133    7 LGKGTFGQVVKC-YDLLTGeeVALKIIKNNKDYLDQS-LDEIRLLELLNkkdkadKYHIVRLKDVFYFKNHLCIVFELLS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 269 KgSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLC--KVGDFGLARLVKEDIYL--- 343
Cdd:cd14133   85 Q-NLYEFLKQNKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSRCqiKIIDFGSSCFLTQRLYSyiq 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 344 SRDhnvpYKwtAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRVDAgyrmpcpLECPPNIHklMLSC 423
Cdd:cd14133  164 SRY----YR--APEVILGLPYDEKIDMWSLGCILAELYT-GEPLFPGASEVDQLARIIG-------TIGIPPAH--MLDQ 227
                        250
                 ....*....|....*...
gi 157822719 424 WSRDpkqRPCFKDLCEKL 441
Cdd:cd14133  228 GKAD---DELFVDFLKKL 242
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
235-390 1.31e-14

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 74.80  E-value: 1.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 235 EIQAMKKLRHKHILSLYAVATAGDPVYIITELMpKGSLLQLL----RDSDEKDLPILelvdfaSQVAEGMCYLESQNYIH 310
Cdd:PTZ00024  70 ELKIMNEIKHENIMGLVDVYVEGDFINLVMDIM-ASDLKKVVdrkiRLTESQVKCIL------LQILNGLNVLHKWYFMH 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 311 RDLAARNVLVTENNLCKVGDFGLAR---------LVKEDIYLSRDHNVPYK-----WTAPEAL-SRGHYSIKSDVWSFGV 375
Cdd:PTZ00024 143 RDLSPANIFINSKGICKIADFGLARrygyppysdTLSKDETMQRREEMTSKvvtlwYRAPELLmGAEKYHFAVDMWSVGC 222
                        170
                 ....*....|....*
gi 157822719 376 LLHEIFSrGQMPYPG 390
Cdd:PTZ00024 223 IFAELLT-GKPLFPG 236
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
235-388 1.33e-14

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: 73.85  E-value: 1.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 235 EIQAMKKLRHKHILSLYAVAT--AGDPVYIITELMPKGSLLQLLRDsdeKDLPILELVDFASQVAEGMCYLESQNYIHRD 312
Cdd:cd14199   75 EIAILKKLDHPNVVKLVEVLDdpSEDHLYMVFELVKQGPVMEVPTL---KPLSEDQARFYFQDLIKGIEYLHYQKIIHRD 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 313 LAARNVLVTENNLCKVGDFGLARLVK-EDIYLSRDHNVPyKWTAPEALS--RGHYSIKS-DVWSFGVLLHeIFSRGQMPY 388
Cdd:cd14199  152 VKPSNLLVGEDGHIKIADFGVSNEFEgSDALLTNTVGTP-AFMAPETLSetRKIFSGKAlDVWAMGVTLY-CFVFGQCPF 229
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
190-432 1.38e-14

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: 73.69  E-value: 1.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLCKKLGSGYFGEVFEGLWK--GLVRVAVKVISRDNLLHQHTFQ----------AEIQAMK-KLRHKHILSLYAVATA 256
Cdd:cd08528    1 EYAVLELLGSGAFGCVYKVRKKsnGQTLLALKEINMTNPAFGRTEQerdksvgdiiSEVNIIKeQLRHPNIVRYYKTFLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 257 GDPVYIITELMPKGSLLQLLRDSDEKDLPILE--LVDFASQVAEGMCYLESQNYI-HRDLAARNVLVTENNLCKVGDFGL 333
Cdd:cd08528   81 NDRLYIVMELIEGAPLGEHFSSLKEKNEHFTEdrIWNIFVQMVLALRYLHKEKQIvHRDLKPNNIMLGEDDKVTITDFGL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 334 ARLVKEDIYLSRDHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIfsrGQMPYPGMSNHETFLR---VDAGYRmPCP- 409
Cdd:cd08528  161 AKQKGPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQM---CTLQPPFYSTNMLTLAtkiVEAEYE-PLPe 236
                        250       260
                 ....*....|....*....|...
gi 157822719 410 LECPPNIHKLMLSCWSRDPKQRP 432
Cdd:cd08528  237 GMYSDDITFVIRSCLTPDPEARP 259
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
195-431 1.40e-14

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: 74.36  E-value: 1.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFeglwkgLVRvavKVISRDnllhqhtfQAEIQAMKKL-----------------------RHKHILSL- 250
Cdd:cd05582    1 KVLGQGSFGKVF------LVR---KITGPD--------AGTLYAMKVLkkatlkvrdrvrtkmerdiladvNHPFIVKLh 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 251 YAVATAGDpVYIITELMPKGSLLQLLRDS---DEKDLPIlelvdFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCK 327
Cdd:cd05582   64 YAFQTEGK-LYLILDFLRGGDLFTRLSKEvmfTEEDVKF-----YLAELALALDHLHSLGIIYRDLKPENILLDEDGHIK 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 328 VGDFGLArlvKEDIYlsrDHNVPY------KWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRV- 400
Cdd:cd05582  138 LTDFGLS---KESID---HEKKAYsfcgtvEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GSLPFQGKDRKETMTMIl 210
                        250       260       270
                 ....*....|....*....|....*....|.
gi 157822719 401 DAGYRMPCPLEcpPNIHKLMLSCWSRDPKQR 431
Cdd:cd05582  211 KAKLGMPQFLS--PEAQSLLRALFKRNPANR 239
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
197-403 1.51e-14

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: 74.06  E-value: 1.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWK--GLVrVAVKVIsrDNLLHQHTFQA---EIQAMKKLRHKHILSLYAVAT--AGDPVYIITELMPK 269
Cdd:cd13988    1 LGQGATANVFRGRHKktGDL-YAVKVF--NNLSFMRPLDVqmrEFEVLKKLNHKNIVKLFAIEEelTTRHKVLVMELCPC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 270 GSLLQLLRD-SDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVL--VTENNLC--KVGDFGLARLVKED---- 340
Cdd:cd13988   78 GSLYTVLEEpSNAYGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMrvIGEDGQSvyKLTDFGAARELEDDeqfv 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157822719 341 -IYLSRDHNVP--YKwtapEALSRGH----YSIKSDVWSFGVLLHEIfSRGQMPY----PGMSNHETFLRVDAG 403
Cdd:cd13988  158 sLYGTEEYLHPdmYE----RAVLRKDhqkkYGATVDLWSIGVTFYHA-ATGSLPFrpfeGPRRNKEVMYKIITG 226
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
184-439 1.56e-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: 73.94  E-value: 1.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 184 WERPREEFTLCKKLGSGYFGEVFEGLWKGLVRV-AVKVI-SRDNLLHQHTFQAEIQAMKKLRH-KHILSLY-AVATAGDp 259
Cdd:cd06616    1 YEFTAEDLKDLGEIGRGAFGTVNKMLHKPSGTImAVKRIrSTVDEKEQKRLLMDLDVVMRSSDcPYIVKFYgALFREGD- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 260 VYIITELMPKgSLLQLLR---DSDEKDLP--ILELVDFAsqVAEGMCYL-ESQNYIHRDLAARNVLVTENNLCKVGDFGL 333
Cdd:cd06616   80 CWICMELMDI-SLDKFYKyvyEVLDSVIPeeILGKIAVA--TVKALNYLkEELKIIHRDVKPSNILLDRNGNIKLCDFGI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 334 ARLVKEDIYLSRDHNV-PYkwTAPEAL----SRGHYSIKSDVWSFGVLLHEIfSRGQMPYPG-MSNHETFLRVDAGYrmp 407
Cdd:cd06616  157 SGQLVDSIAKTRDAGCrPY--MAPERIdpsaSRDGYDVRSDVWSLGITLYEV-ATGKFPYPKwNSVFDQLTQVVKGD--- 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 157822719 408 cplecPP---NIHKLMLS---------CWSRDPKQRPCFKDLCE 439
Cdd:cd06616  231 -----PPilsNSEEREFSpsfvnfvnlCLIKDESKRPKYKELLK 269
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
190-404 1.59e-14

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: 73.82  E-value: 1.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLCKKLGSGYFGEVFEGLWKGL-VRVAVKVIS---RDNllhqhtfQAEIQAMkkLR---HKHILSLYAVATAGDPVYI 262
Cdd:cd14091    1 EYEIKEEIGKGSYSVCKRCIHKATgKEYAVKIIDkskRDP-------SEEIEIL--LRygqHPNIITLRDVYDDGNSVYL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 263 ITELMPKGSLL-QLLRdsdEKDLPILElvdfASQV----AEGMCYLESQNYIHRDLAARNVLVTENN-------LCkvgD 330
Cdd:cd14091   72 VTELLRGGELLdRILR---QKFFSERE----ASAVmktlTKTVEYLHSQGVVHRDLKPSNILYADESgdpeslrIC---D 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 331 FGLARLVkediylsRDHN----VP-Y--KWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPY---PGMSNHETFLRV 400
Cdd:cd14091  142 FGFAKQL-------RAENgllmTPcYtaNFVAPEVLKKQGYDAACDIWSLGVLLYTMLA-GYTPFasgPNDTPEVILARI 213

                 ....
gi 157822719 401 DAGY 404
Cdd:cd14091  214 GSGK 217
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
185-383 1.91e-14

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


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 73.93  E-value: 1.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 185 ERPREEFTLCKKLGSGYFGEVFeglWKGLVR----VAVKVISRDNLLHQHTFQ---AEIQAMKKLRHKHILSLYAVATAG 257
Cdd:cd06635   21 EDPEKLFSDLREIGHGSFGAVY---FARDVRtsevVAIKKMSYSGKQSNEKWQdiiKEVKFLQRIKHPNSIEYKGCYLRE 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 258 DPVYIITELMpKGSLLQLLrDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLV 337
Cdd:cd06635   98 HTAWLVMEYC-LGSASDLL-EVHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIA 175
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 157822719 338 KEDIYLSrdhNVPYkWTAPE---ALSRGHYSIKSDVWSFGVLLHEIFSR 383
Cdd:cd06635  176 SPANSFV---GTPY-WMAPEvilAMDEGQYDGKVDVWSLGITCIELAER 220
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
195-431 2.22e-14

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: 73.89  E-value: 2.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVF------EGLWKGL--VRVAVkVISRDNLLHQHTfqaEIQAMKKLRHKHILSL-YAVATAgDPVYIITE 265
Cdd:cd05595    1 KLLGKGTFGKVIlvrekaTGRYYAMkiLRKEV-IIAKDEVAHTVT---ESRVLQNTRHPFLTALkYAFQTH-DRLCFVME 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMPKGSLLQLLrdSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSR 345
Cdd:cd05595   76 YANGGELFFHL--SRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGITDGATMK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 346 DHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGmSNHETFLRVDAGYRMPCPLECPPNIHKLMLSCWS 425
Cdd:cd05595  154 TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYN-QDHERLFELILMEEIRFPRTLSPEAKSLLAGLLK 231

                 ....*.
gi 157822719 426 RDPKQR 431
Cdd:cd05595  232 KDPKQR 237
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
200-383 2.24e-14

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: 73.13  E-value: 2.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 200 GYFGEVfeglWKGLVR---VAVKVIsrdNLLHQHTFQAE--IQAMKKLRHKHILSLYAVATAGDPVY----IITELMPKG 270
Cdd:cd14053    6 GRFGAV----WKAQYLnrlVAVKIF---PLQEKQSWLTEreIYSLPGMKHENILQFIGAEKHGESLEaeywLITEFHERG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 271 SLLQLLRdsdEKDLPILELVDFASQVAEGMCYLESQ----------NYIHRDLAARNVLVTENNLCKVGDFGLARLVKED 340
Cdd:cd14053   79 SLCDYLK---GNVISWNELCKIAESMARGLAYLHEDipatngghkpSIAHRDFKSKNVLLKSDLTACIADFGLALKFEPG 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157822719 341 IYLSRDH-NVPYK-WTAPEAL------SRGHYsIKSDVWSFGVLLHEIFSR 383
Cdd:cd14053  156 KSCGDTHgQVGTRrYMAPEVLegainfTRDAF-LRIDMYAMGLVLWELLSR 205
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
191-409 2.58e-14

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: 73.00  E-value: 2.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEGLWKGLVR-VAVKVISRDNLLHQHT-FQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMP 268
Cdd:cd14169    5 YELKEKLGEGAFSEVVLAQERGSQRlVALKCIPKKALRGKEAmVENEIAVLRRINHENIVSLEDIYESPTHLYLAMELVT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 269 KGSLLQ--LLRDS-DEKDLPILelvdfASQVAEGMCYLESQNYIHRDLAARNVLVT---ENNLCKVGDFGLARlVKEDIY 342
Cdd:cd14169   85 GGELFDriIERGSyTEKDASQL-----IGQVLQAVKYLHQLGIVHRDLKPENLLYAtpfEDSKIMISDFGLSK-IEAQGM 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157822719 343 LSRDHNVPyKWTAPEALSRGHYSIKSDVWSFGVLLHeIFSRGQMPYPGMSNHETF-LRVDAGYRMPCP 409
Cdd:cd14169  159 LSTACGTP-GYVAPELLEQKPYGKAVDVWAIGVISY-ILLCGYPPFYDENDSELFnQILKAEYEFDSP 224
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
195-388 2.76e-14

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: 72.87  E-value: 2.76e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVfeGLWKGLV---RVAVKVISR--DNLLHQHTFQAEIQAMKK-------------LRHKHILSLYAVATA 256
Cdd:cd14077    7 KTIGAGSMGKV--KLAKHIRtgeKCAIKIIPRasNAGLKKEREKRLEKEISRdirtireaalsslLNHPHICRLRDFLRT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 257 GDPVYIITELMPKGSLLQLLRDS---DEKdlpilELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGL 333
Cdd:cd14077   85 PNHYYMLFEYVDGGQLLDYIISHgklKEK-----QARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGL 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 157822719 334 ARLVKEDIYLSRDHNVPYkWTAPEALSRGHYS-IKSDVWSFGVLLHEIFSrGQMPY 388
Cdd:cd14077  160 SNLYDPRRLLRTFCGSLY-FAAPELLQAQPYTgPEVDVWSFGVVLYVLVC-GKVPF 213
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
216-432 2.81e-14

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: 73.37  E-value: 2.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 216 VAVKVISRDNLLHQH--TFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSLLQLLRDSDEKDLPILELVDFA 293
Cdd:cd08226   28 VTVKITNLDNCSEEHlkALQNEVVLSHFFRHPNIMTHWTVFTEGSWLWVISPFMAYGSARGLLKTYFPEGMNEALIGNIL 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 294 SQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKV-GDFGLARLVKEDIYLSRDHNVP------YKWTAPEALSRG--HY 364
Cdd:cd08226  108 YGAIKALNYLHQNGCIHRSVKASHILISGDGLVSLsGLSHLYSMVTNGQRSKVVYDFPqfstsvLPWLSPELLRQDlhGY 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 365 SIKSDVWSFGVLLHEIfSRGQMPYPGMSNHETFLR----------------------------VDAG------------- 403
Cdd:cd08226  188 NVKSDIYSVGITACEL-ARGQVPFQDMRRTQMLLQklkgppyspldifpfpelesrmknsqsgMDSGigesvatssmtrt 266
                        250       260       270
                 ....*....|....*....|....*....|....
gi 157822719 404 -----YRMPCPLECPPNIHKLMLSCWSRDPKQRP 432
Cdd:cd08226  267 mtserLQTPSSKTFSPAFHNLVELCLQQDPEKRP 300
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
195-400 2.97e-14

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: 72.65  E-value: 2.97e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWKGLVRV-AVKVIS--------RDNLLHQhtfQAEIQAMKKlrHKHILSLYAVATAGDPVYIITE 265
Cdd:cd14198   14 KELGRGKFAVVRQCISKSTGQEyAAKFLKkrrrgqdcRAEILHE---IAVLELAKS--NPRVVNLHEVYETTSEIILILE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMPKGSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNL---CKVGDFGLARLVKEDIY 342
Cdd:cd14198   89 YAAGGEIFNLCVPDLAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYPlgdIKIVDFGMSRKIGHACE 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 157822719 343 LSRDHNVPyKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRV 400
Cdd:cd14198  169 LREIMGTP-EYLAPEILNYDPITTATDMWNIGVIAYMLLT-HESPFVGEDNQETFLNI 224
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
189-395 3.43e-14

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: 72.73  E-value: 3.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFEG---LWKGLVrvAVKVIsrdNLLHQH----TFQAEIQAMKKLRHKHILSLYAVATAGDPVY 261
Cdd:cd07873    2 ETYIKLDKLGEGTYATVYKGrskLTDNLV--ALKEI---RLEHEEgapcTAIREVSLLKDLKHANIVTLHDIIHTEKSLT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 262 IITELMPKgSLLQLLRD-SDEKDLPILELvdFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARlVKED 340
Cdd:cd07873   77 LVFEYLDK-DLKQYLDDcGNSINMHNVKL--FLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLAR-AKSI 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 157822719 341 IYLSRDHNVPYKWTAPEALSRG--HYSIKSDVWSFGVLLHEIfSRGQMPYPGMSNHE 395
Cdd:cd07873  153 PTKTYSNEVVTLWYRPPDILLGstDYSTQIDMWGVGCIFYEM-STGRPLFPGSTVEE 208
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
197-397 3.44e-14

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


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 73.40  E-value: 3.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGLVRV-AVKVISRDNLLHQHTFQAEIQAMKKL----RHKHILSLYAVATAGDPVYIITELMPKGS 271
Cdd:cd05590    3 LGKGSFGKVMLARLKESGRLyAVKVLKKDVILQDDDVECTMTEKRILslarNHPFLTQLYCCFQTPDRLFFVMEFVNGGD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 272 LLQLLRDSDEKDLPILELvdFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARL-VKEDIYLSRDHNVP 350
Cdd:cd05590   83 LMFHIQKSRRFDEARARF--YAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEgIFNGKTTSTFCGTP 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 157822719 351 yKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETF 397
Cdd:cd05590  161 -DYIAPEILQEMLYGPSVDWWAMGVLLYEMLC-GHAPFEAENEDDLF 205
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
217-388 3.67e-14

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: 72.67  E-value: 3.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 217 AVKVISRDNLLHQHTFQ--------------------------AEIQAMKKLRHKHILSLYAVAT--AGDPVYIITELMP 268
Cdd:cd14200   29 AMKVLSKKKLLKQYGFPrrppprgskaaqgeqakplaplervyQEIAILKKLDHVNIVKLIEVLDdpAEDNLYMVFDLLR 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 269 KGSLLQLLRDSD-EKDLPILELVDfasqVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLA-RLVKEDIYLSRD 346
Cdd:cd14200  109 KGPVMEVPSDKPfSEDQARLYFRD----IVLGIEYLHYQKIVHRDIKPSNLLLGDDGHVKIADFGVSnQFEGNDALLSST 184
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 157822719 347 HNVPyKWTAPEALS--RGHYSIKS-DVWSFGVLLHeIFSRGQMPY 388
Cdd:cd14200  185 AGTP-AFMAPETLSdsGQSFSGKAlDVWAMGVTLY-CFVYGKCPF 227
SH2_Tec_family cd09934
Src homology 2 (SH2) domain found in Tec-like proteins; The Tec protein tyrosine kinase is the ...
71-164 3.71e-14

Src homology 2 (SH2) domain found in Tec-like proteins; The Tec protein tyrosine kinase is the founding member of a family that includes Btk, Itk, Bmx, and Txk. The members have a PH domain, a zinc-binding motif, a SH3 domain, a SH2 domain, and a protein kinase catalytic domain. Btk is involved in B-cell receptor signaling with mutations in Btk responsible for X-linked agammaglobulinemia (XLA) in humans and X-linked immunodeficiency (xid) in mice. Itk is involved in T-cell receptor signaling. Tec is expressed in both T and B cells, and is thought to function in activated and effector T lymphocytes to induce the expression of genes regulated by NFAT transcription factors. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198188  Cd Length: 104  Bit Score: 68.20  E-value: 3.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719  71 ETVESEPWFFGCISRSEAMHRLQSEDyPKGTFLIRVSQKPGAdYVLSVW----DAEAVRHYRIWRNSAGRLHLNEVVSFS 146
Cdd:cd09934    1 LNLEKYEWYVGDMSRQRAESLLKQED-KEGCFVVRNSSTKGL-YTVSLFtkvpGSPHVKHYHIKQNARSEFYLAEKHCFE 78
                         90
                 ....*....|....*...
gi 157822719 147 SLSELVNYHKtHNlSPGL 164
Cdd:cd09934   79 TIPELINYHQ-HN-SGGL 94
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
195-409 4.05e-14

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: 73.20  E-value: 4.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWKGLVR-VAVKVISR--DNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDP------VYIITE 265
Cdd:cd07874   23 KPIGSGAQGIVCAAYDAVLDRnVAIKKLSRpfQNQTHAKRAYRELVLMKCVNHKNIISLLNVFTPQKSleefqdVYLVME 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMpKGSLLQLLR-DSDEKDLPILelvdfASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDiYLS 344
Cdd:cd07874  103 LM-DANLCQVIQmELDHERMSYL-----LYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTS-FMM 175
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157822719 345 RDHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFsRGQMPYPGMSNHETFLRVDAGYRMPCP 409
Cdd:cd07874  176 TPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMV-RHKILFPGRDYIDQWNKVIEQLGTPCP 239
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
195-381 4.17e-14

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


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 72.96  E-value: 4.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGL-WKGLVRVAVKVIsRDNL-LHQhtfQA--EIQAMKKLRHKHILSLYAVATAGDPVY------IIT 264
Cdd:cd14210   19 SVLGKGSFGQVVKCLdHKTGQLVAIKII-RNKKrFHQ---QAlvEVKILKHLNDNDPDDKHNIVRYKDSFIfrghlcIVF 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 265 ELMPKgSLLQLLRDSDEKDLPiLELVD-FASQVAEGMCYLESQNYIHRDLAARNVLVTENNL--CKVGDFGLARLVKEDI 341
Cdd:cd14210   95 ELLSI-NLYELLKSNNFQGLS-LSLIRkFAKQILQALQFLHKLNIIHCDLKPENILLKQPSKssIKVIDFGSSCFEGEKV 172
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 157822719 342 YL---SRDhnvpYKwtAPEALSRGHYSIKSDVWSFGVLLHEIF 381
Cdd:cd14210  173 YTyiqSRF----YR--APEVILGLPYDTAIDMWSLGCILAELY 209
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
188-431 4.30e-14

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: 72.77  E-value: 4.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 188 REEFTLCKKLGSGYFGEVFEGLWKGLVRV-AVKVISRDNLL-HQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITE 265
Cdd:cd14168    9 KKIFEFKEVLGTGAFSEVVLAEERATGKLfAVKCIPKKALKgKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQ 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMPKGSLLQLLRDS---DEKDLPILelvdfASQVAEGMCYLESQNYIHRDLAARNVLV---TENNLCKVGDFGLARLVKE 339
Cdd:cd14168   89 LVSGGELFDRIVEKgfyTEKDASTL-----IRQVLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMISDFGLSKMEGK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 340 DIYLSRDHNVPyKWTAPEALSRGHYSIKSDVWSFGVLLHeIFSRGQMPYPGMSNHETF---LRVDAGYRMPCPLECPPNI 416
Cdd:cd14168  164 GDVMSTACGTP-GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFeqiLKADYEFDSPYWDDISDSA 241
                        250
                 ....*....|....*
gi 157822719 417 HKLMLSCWSRDPKQR 431
Cdd:cd14168  242 KDFIRNLMEKDPNKR 256
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
195-437 4.55e-14

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: 72.04  E-value: 4.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVF------EGLWKGLVRVAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVAT--AGDPVYIITEL 266
Cdd:cd06651   13 KLLGQGAFGRVYlcydvdTGRELAAKQVQFDPESPETSKEVSALECEIQLLKNLQHERIVQYYGCLRdrAEKTLTIFMEY 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 267 MPKGSLlqllRDSDEKDLPILELV--DFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVkEDIYLS 344
Cdd:cd06651   93 MPGGSV----KDQLKAYGALTESVtrKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRL-QTICMS 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 345 RD-----HNVPYkWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGqmpyPGMSNHETFLRVDAGYRMPCPLECPPNIH-- 417
Cdd:cd06651  168 GTgirsvTGTPY-WMSPEVISGEGYGRKADVWSLGCTVVEMLTEK----PPWAEYEAMAAIFKIATQPTNPQLPSHISeh 242
                        250       260
                 ....*....|....*....|.
gi 157822719 418 -KLMLSCWSRDPKQRPCFKDL 437
Cdd:cd06651  243 aRDFLGCIFVEARHRPSAEEL 263
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
190-383 4.75e-14

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: 72.45  E-value: 4.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLCKKLGSGYFGEVFEGLWKGLVR-VAVKVISRDNLLH--QHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITEL 266
Cdd:cd07861    1 DYTKIEKIGEGTYGVVYKGRNKKTGQiVAMKKIRLESEEEgvPSTAIREISLLKELQHPNIVCLEDVLMQENRLYLVFEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 267 MP---KGSLLQLLRDsdeKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARL--VKEDI 341
Cdd:cd07861   81 LSmdlKKYLDSLPKG---KYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARAfgIPVRV 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 157822719 342 YlsrDHNVPYKW-TAPEALSRG-HYSIKSDVWSFGVLLHEIFSR 383
Cdd:cd07861  158 Y---THEVVTLWyRAPEVLLGSpRYSTPVDIWSIGTIFAEMATK 198
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
189-389 5.11e-14

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: 72.47  E-value: 5.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFEglwkgLVRVAVKVISRDNLLHQHTFQA-------EIQAMKKLRHKHILSLYAVATAGDPVY 261
Cdd:cd06615    1 DDFEKLGELGAGNGGVVTK-----VLHRPSGLIMARKLIHLEIKPAirnqiirELKVLHECNSPYIVGFYGAFYSDGEIS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 262 IITELMPKGSLLQLLRDSDEKDLPILELVDFAsqVAEGMCYL-ESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKED 340
Cdd:cd06615   76 ICMEHMDGGSLDQVLKKAGRIPENILGKISIA--VLRGLTYLrEKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDS 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 157822719 341 IYLSRDHNVPYkwTAPEALSRGHYSIKSDVWSFGVLLHEIfSRGQMPYP 389
Cdd:cd06615  154 MANSFVGTRSY--MSPERLQGTHYTVQSDIWSLGLSLVEM-AIGRYPIP 199
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
186-442 5.99e-14

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of NF-kB proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 71.77  E-value: 5.99e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 186 RPREEFTLCK-KLGSGYFGEVFE------GLWKGLVRVAVKVISRDnllhqhtfqaEIQAMKKLRHKHILSLYAVATAGD 258
Cdd:cd13991    2 REEVHWATHQlRIGRGSFGEVHRmedkqtGFQCAVKKVRLEVFRAE----------ELMACAGLTSPRVVPLYGAVREGP 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 259 PVYIITELMPKGSLLQLLRDSDEkdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENN----LCkvgDFGLA 334
Cdd:cd13991   72 WVNIFMDLKEGGSLGQLIKEQGC--LPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGsdafLC---DFGHA 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 335 RLVKED---IYLSRDHNVPYKWT--APEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRVdagYRMPCP 409
Cdd:cd13991  147 ECLDPDglgKSLFTGDYIPGTEThmAPEVVLGKPCDAKVDVWSSCCMMLHMLN-GCHPWTQYYSGPLCLKI---ANEPPP 222
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 157822719 410 L-ECPPNIHKLMLSCWS----RDPKQRPCFKDLCEKLS 442
Cdd:cd13991  223 LrEIPPSCAPLTAQAIQaglrKEPVHRASAAELRRKTN 260
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
257-439 6.72e-14

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: 6.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 257 GDpVYIITELMpKGSLLQLLRDSDEKDLPILE--LVDFASQVAEGMCYLESQ-NYIHRDLAARNVLVTENNLCKVGDFGL 333
Cdd:cd06617   73 GD-VWICMEVM-DTSLDKFYKKVYDKGLTIPEdiLGKIAVSIVKALEYLHSKlSVIHRDVKPSNVLINRNGQVKLCDFGI 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 334 ARLVKEDIYLSRDHNV-PYkwTAPE----ALSRGHYSIKSDVWSFGVLLHEIfSRGQMPYPgmSNHETFLRVDAGYRMPC 408
Cdd:cd06617  151 SGYLVDSVAKTIDAGCkPY--MAPErinpELNQKGYDVKSDVWSLGITMIEL-ATGRFPYD--SWKTPFQQLKQVVEEPS 225
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 157822719 409 PlECP-----PNIHKLMLSCWSRDPKQRPCFKDLCE 439
Cdd:cd06617  226 P-QLPaekfsPEFQDFVNKCLKKNYKERPNYPELLQ 260
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
189-388 7.39e-14

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: 71.67  E-value: 7.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFeglwkgLVR-------VAVKVISRDNLLH----QHTFQaEIQAMKKLRHKHILSLYAVATAG 257
Cdd:cd14209    1 DDFDRIKTLGTGSFGRVM------LVRhketgnyYAMKILDKQKVVKlkqvEHTLN-EKRILQAINFPFLVKLEYSFKDN 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 258 DPVYIITELMPKGSLLQLLRDSDEKDLPILELvdFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLV 337
Cdd:cd14209   74 SNLYMVMEYVPGGEMFSHLRRIGRFSEPHARF--YAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRV 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 338 KEdiylsrdhnvpYKWT--------APE-ALSRGhYSIKSDVWSFGVLLHEiFSRGQMPY 388
Cdd:cd14209  152 KG-----------RTWTlcgtpeylAPEiILSKG-YNKAVDWWALGVLIYE-MAAGYPPF 198
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
235-376 7.64e-14

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


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 71.10  E-value: 7.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 235 EIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSLLQLLrdSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLA 314
Cdd:cd14110   49 EYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELCSGPELLYNL--AERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLR 126
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157822719 315 ARNVLVTENNLCKVGDFGLARLVKEDIYLSRDHNVPYKWT-APEALSRGHYSIKSDVWSFGVL 376
Cdd:cd14110  127 SENMIITEKNLLKIVDLGNAQPFNQGKVLMTDKKGDYVETmAPELLEGQGAGPQTDIWAIGVT 189
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
217-390 7.71e-14

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: 71.83  E-value: 7.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 217 AVKVISRDnlLHQHTfQAEIQAMKKLR-HKHILSLYAVATAGDPVYIITELMPKGSLLQLLRDsdEKDLPILELVDFASQ 295
Cdd:cd14180   35 AVKIISRR--MEANT-QREVAALRLCQsHPNIVALHEVLHDQYHTYLVMELLRGGELLDRIKK--KARFSESEASQLMRS 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 296 VAEGMCYLESQNYIHRDLAARNVLV---TENNLCKVGDFGLARLVKEDiylSRDHNVP---YKWTAPEALSRGHYSIKSD 369
Cdd:cd14180  110 LVSAVSFMHEAGVVHRDLKPENILYadeSDGAVLKVIDFGFARLRPQG---SRPLQTPcftLQYAAPELFSNQGYDESCD 186
                        170       180
                 ....*....|....*....|.
gi 157822719 370 VWSFGVLLHEIFSrGQMPYPG 390
Cdd:cd14180  187 LWSLGVILYTMLS-GQVPFQS 206
SH2_Src_Src42 cd10370
Src homology 2 (SH2) domain found in the Src oncogene at 42A (Src42); Src42 is a member of the ...
74-155 8.18e-14

Src homology 2 (SH2) domain found in the Src oncogene at 42A (Src42); Src42 is a member of the Src non-receptor type tyrosine kinase family of proteins. The integration of receptor tyrosine kinase-induced RAS and Src42 signals by Connector eNhancer of KSR (CNK) as a two-component input is essential for RAF activation in Drosophila. Src42 is present in a wide variety of organisms including: California sea hare, pea aphid, yellow fever mosquito, honey bee, Panamanian leafcutter ant, and sea urchin. Src42 has a unique N-terminal domain, an SH3 domain, an SH2 domain, a kinase domain and a regulatory tail, as do the other members of the family. Like the other members of the Src family the SH2 domain in addition to binding the target, also plays an autoinhibitory role by binding to its C-terminal tail. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198233  Cd Length: 96  Bit Score: 67.14  E-value: 8.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719  74 ESEPWFFGCISRSEAMHRLQSEDYPKGTFLIRVSQKPGADYVLSVWDAEAVRHYRIWRNSAGRLHLNEVVSFSSLSELVN 153
Cdd:cd10370    1 EAEPWYFGKIKRIEAEKKLLLPENEHGAFLIRDSESRHNDYSLSVRDGDTVKHYRIRQLDEGGFFIARRTTFRTLQELVE 80

                 ..
gi 157822719 154 YH 155
Cdd:cd10370   81 HY 82
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
247-400 8.74e-14

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: 71.12  E-value: 8.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 247 ILSLYAVATAGDPVYIITELMPKGSLL-QLLRDSDE--KDLPILELVdfaSQVAEGMCYLESQNYIHRDLAARNVLVTEN 323
Cdd:cd14197   71 VINLHEVYETASEMILVLEYAAGGEIFnQCVADREEafKEKDVKRLM---KQILEGVSFLHNNNVVHLDLKPQNILLTSE 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 324 NL---CKVGDFGLARLVKEDIYLSRDHNVPyKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRV 400
Cdd:cd14197  148 SPlgdIKIVDFGLSRILKNSEELREIMGTP-EYVAPEILSYEPISTATDMWSIGVLAYVMLT-GISPFLGDDKQETFLNI 225
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
217-378 9.22e-14

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: 71.23  E-value: 9.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 217 AVKVISRDNLLH--------QHTFQAEIQAMKKL-RHKHILSLYAVATAGDPVYIITELMPKGSLLQLLRD----SDEKD 283
Cdd:cd14093   32 AVKIIDITGEKSseneaeelREATRREIEILRQVsGHPNIIELHDVFESPTFIFLVFELCRKGELFDYLTEvvtlSEKKT 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 284 LPILElvdfasQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSRDHNVPyKWTAPEALSR-- 361
Cdd:cd14093  112 RRIMR------QLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATRLDEGEKLRELCGTP-GYLAPEVLKCsm 184
                        170       180
                 ....*....|....*....|.
gi 157822719 362 --GH--YSIKSDVWSFGVLLH 378
Cdd:cd14093  185 ydNApgYGKEVDMWACGVIMY 205
SH2_ABL cd09935
Src homology 2 (SH2) domain found in Abelson murine lymphosarcoma virus (ABL) proteins; ...
74-158 9.65e-14

Src homology 2 (SH2) domain found in Abelson murine lymphosarcoma virus (ABL) proteins; ABL-family proteins are highly conserved tyrosine kinases. Each ABL protein contains an SH3-SH2-TK (Src homology 3-Src homology 2-tyrosine kinase) domain cassette, which confers autoregulated kinase activity and is common among nonreceptor tyrosine kinases. Several types of posttranslational modifications control ABL catalytic activity, subcellular localization, and stability, with consequences for both cytoplasmic and nuclear ABL functions. Binding partners provide additional regulation of ABL catalytic activity, substrate specificity, and downstream signaling. By combining this cassette with actin-binding and -bundling domain, ABL proteins are capable of connecting phosphoregulation with actin-filament reorganization. Vertebrate paralogs, ABL1 and ABL2, have evolved to perform specialized functions. ABL1 includes nuclear localization signals and a DNA binding domain which is used to mediate DNA damage-repair functions, while ABL2 has additional binding capacity for actin and for microtubules to enhance its cytoskeletal remodeling functions. SH2 is involved in several autoinhibitory mechanism that constrain the enzymatic activity of the ABL-family kinases. In one mechanism SH2 and SH3 cradle the kinase domain while a cap sequence stabilizes the inactive conformation resulting in a locked inactive state. Another involves phosphatidylinositol 4,5-bisphosphate (PIP2) which binds the SH2 domain through residues normally required for phosphotyrosine binding in the linker segment between the SH2 and kinase domains. The SH2 domain contributes to ABL catalytic activity and target site specificity. It is thought that the ABL catalytic site and SH2 pocket have coevolved to recognize the same sequences. Recent work now supports a hierarchical processivity model in which the substrate target site most compatible with ABL kinase domain preferences is phosphorylated with greatest efficiency. If this site is compatible with the ABL SH2 domain specificity, it will then reposition and dock in the SH2 pocket. This mechanism also explains how ABL kinases phosphorylates poor targets on the same substrate if they are properly positioned and how relatively poor substrate proteins might be recruited to ABL through a complex with strong substrates that can also dock with the SH2 pocket. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198189  Cd Length: 94  Bit Score: 66.64  E-value: 9.65e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719  74 ESEPWFFGCISRSEAMHRLQSEdyPKGTFLIRVSQKPGADYVLSVWDAEAVRHYRIWRNSAGRLHLNEVVSFSSLSELVN 153
Cdd:cd09935    1 EKHSWYHGPISRNAAEYLLSSG--INGSFLVRESESSPGQYSISLRYDGRVYHYRISEDSDGKVYVTQEHRFNTLAELVH 78

                 ....*
gi 157822719 154 YHKTH 158
Cdd:cd09935   79 HHSKN 83
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
195-450 1.05e-13

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: 71.15  E-value: 1.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFeglwKGLVR-----VAVKVISRdNLLHQHTFQA--EIQAMKKLRHKHILSLYAVATAGDPVYIITELM 267
Cdd:cd07870    6 EKLGEGSYATVY----KGISRingqlVALKVISM-KTEEGVPFTAirEASLLKGLKHANIVLLHDIIHTKETLTFVFEYM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 268 pKGSLLQLLrDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARL--VKEDIYLSR 345
Cdd:cd07870   81 -HTDLAQYM-IQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLARAksIPSQTYSSE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 346 DHNVPYKwtAPEAL-SRGHYSIKSDVWSFGVLLHEIFsRGQMPYPGMSN-HETFLRVDAGYRMPCPlECPPNIHKL--ML 421
Cdd:cd07870  159 VVTLWYR--PPDVLlGATDYSSALDIWGAGCIFIEML-QGQPAFPGVSDvFEQLEKIWTVLGVPTE-DTWPGVSKLpnYK 234
                        250       260
                 ....*....|....*....|....*....
gi 157822719 422 SCWSRDPKQrPCFKDLCEKLSGITRYENL 450
Cdd:cd07870  235 PEWFLPCKP-QQLRVVWKRLSRPPKAEDL 262
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
196-437 1.27e-13

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: 70.91  E-value: 1.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 196 KLGSGYFGEVFEGL-WKGLVRVAVKVISRDNLL--HQHTFQAEIQAMKKLRHKHILSLY----AVATAGDPVYIITELMP 268
Cdd:cd14031   17 ELGRGAFKTVYKGLdTETWVEVAWCELQDRKLTkaEQQRFKEEAEMLKGLQHPNIVRFYdsweSVLKGKKCIVLVTELMT 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 269 KGSLLQLLRDSDEKDLPILElvDFASQVAEGMCYLESQN--YIHRDLAARNVLVT-ENNLCKVGDFGLARLVKEDiYLSR 345
Cdd:cd14031   97 SGTLKTYLKRFKVMKPKVLR--SWCRQILKGLQFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLATLMRTS-FAKS 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 346 DHNVPyKWTAPEaLSRGHYSIKSDVWSFGVLLHEIfSRGQMPYPGMSN-HETFLRVDAGYRmPCPLE--CPPNIHKLMLS 422
Cdd:cd14031  174 VIGTP-EFMAPE-MYEEHYDESVDVYAFGMCMLEM-ATSEYPYSECQNaAQIYRKVTSGIK-PASFNkvTDPEVKEIIEG 249
                        250
                 ....*....|....*
gi 157822719 423 CWSRDPKQRPCFKDL 437
Cdd:cd14031  250 CIRQNKSERLSIKDL 264
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
197-387 1.57e-13

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: 71.01  E-value: 1.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGLVrVAVKVISRDNLLH----QHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSL 272
Cdd:cd14159    1 IGEGGFGCVYQAVMRNTE-YAVKRLKEDSELDwsvvKNSFLTEVEKLSRFRHPNIVDLAGYSAQQGNYCLIYVYLPNGSL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 273 L-QLLRDSDEKDLPILELVDFASQVAEGMCYL--ESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSRDHNV 349
Cdd:cd14159   80 EdRLHCQVSCPCLSWSQRLHVLLGTARAIQYLhsDSPSLIHGDVKSSNILLDAALNPKLGDFGLARFSRRPKQPGMSSTL 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 157822719 350 PYKWTA--------PEALSRGHYSIKSDVWSFGVLLHEIFSrGQMP 387
Cdd:cd14159  160 ARTQTVrgtlaylpEEYVKTGTLSVEIDVYSFGVVLLELLT-GRRA 204
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
190-397 1.76e-13

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: 71.18  E-value: 1.76e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLCKKLGSGYFGEVFEGLWKGLVRV-AVKVISRDNLLHQHTFQAEIQAMKKL----RHKHILSLYAVATAGDPVYIIT 264
Cdd:cd05615   11 DFNFLMVLGKGSFGKVMLAERKGSDELyAIKILKKDVVIQDDDVECTMVEKRVLalqdKPPFLTQLHSCFQTVDRLYFVM 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 265 ELMPKGSLLQLLRDSDEKDLPilELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLS 344
Cdd:cd05615   91 EYVNGGDLMYHIQQVGKFKEP--QAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMVEGVTT 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 157822719 345 RDHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETF 397
Cdd:cd05615  169 RTFCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLA-GQPPFDGEDEDELF 220
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
189-349 1.76e-13

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


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 71.45  E-value: 1.76e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFEGLWKGLVRV-AVKVISRDNLLHQ---HTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIIT 264
Cdd:cd05610    4 EEFVIVKPISRGAFGKVYLGRKKNNSKLyAVKVVKKADMINKnmvHQVQAERDALALSKSPFIVHLYYSLQSANNVYLVM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 265 ELMPKGSLLQLLRDSDEKDLPILelVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARlvkedIYLS 344
Cdd:cd05610   84 EYLIGGDVKSLLHIYGYFDEEMA--VKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSK-----VTLN 156

                 ....*
gi 157822719 345 RDHNV 349
Cdd:cd05610  157 RELNM 161
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
185-389 1.78e-13

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: 71.23  E-value: 1.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 185 ERPREEFTLCKKLGSGYFGEVFEG--------LWKGLVRVAVKVISRDNLLHqhtfqaEIQAMKKLRHKHILSLYAVATA 256
Cdd:cd06649    1 ELKDDDFERISELGAGNGGVVTKVqhkpsgliMARKLIHLEIKPAIRNQIIR------ELQVLHECNSPYIVGFYGAFYS 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 257 GDPVYIITELMPKGSLLQLLRDSDEKDLPILELVDFAsqVAEGMCYL-ESQNYIHRDLAARNVLVTENNLCKVGDFGLAR 335
Cdd:cd06649   75 DGEISICMEHMDGGSLDQVLKEAKRIPEEILGKVSIA--VLRGLAYLrEKHQIMHRDVKPSNILVNSRGEIKLCDFGVSG 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 157822719 336 LVKEDIYLSRDHNVPYkwTAPEALSRGHYSIKSDVWSFGVLLHEIfSRGQMPYP 389
Cdd:cd06649  153 QLIDSMANSFVGTRSY--MSPERLQGTHYSVQSDIWSMGLSLVEL-AIGRYPIP 203
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
196-437 2.22e-13

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: 70.11  E-value: 2.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 196 KLGSGYFGEVFEGL-WKGLVRVAVKVISRDNL--LHQHTFQAEIQAMKKLRHKHILSLY----AVATAGDPVYIITELMP 268
Cdd:cd14032    8 ELGRGSFKTVYKGLdTETWVEVAWCELQDRKLtkVERQRFKEEAEMLKGLQHPNIVRFYdfweSCAKGKRCIVLVTELMT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 269 KGSLLQLLRDSDEKDLPILElvDFASQVAEGMCYLESQN--YIHRDLAARNVLVT-ENNLCKVGDFGLARLvKEDIYLSR 345
Cdd:cd14032   88 SGTLKTYLKRFKVMKPKVLR--SWCRQILKGLLFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLATL-KRASFAKS 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 346 DHNVPyKWTAPEaLSRGHYSIKSDVWSFGVLLHEIfSRGQMPYPGMSN-HETFLRVDAGYRmPCPLE--CPPNIHKLMLS 422
Cdd:cd14032  165 VIGTP-EFMAPE-MYEEHYDESVDVYAFGMCMLEM-ATSEYPYSECQNaAQIYRKVTCGIK-PASFEkvTDPEIKEIIGE 240
                        250
                 ....*....|....*
gi 157822719 423 CWSRDPKQRPCFKDL 437
Cdd:cd14032  241 CICKNKEERYEIKDL 255
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
215-383 2.23e-13

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: 71.31  E-value: 2.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 215 RVAVKVISR--DNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDP-----VYIITELMPkgSLL-------QLLRDSD 280
Cdd:cd07853   27 RVALKKMPNvfQNLVSCKRVFRELKMLCFFKHDNVLSALDILQPPHIdpfeeIYVVTELMQ--SDLhkiivspQPLSSDH 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 281 EKDlpilelvdFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSRDHNVPYK-WTAPEAL 359
Cdd:cd07853  105 VKV--------FLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVEEPDESKHMTQEVVTQyYRAPEIL 176
                        170       180
                 ....*....|....*....|....*.
gi 157822719 360 --SRgHYSIKSDVWSFGVLLHEIFSR 383
Cdd:cd07853  177 mgSR-HYTSAVDIWSVGCIFAELLGR 201
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
10-68 2.26e-13

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 64.48  E-value: 2.26e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719    10 GPKYVGLWDFKARTDEELSFQAGDLLHVTRKEEQ-WWWATLLDaeGKalaEGYVPHNYLA 68
Cdd:smart00326   2 GPQVRALYDYTAQDPDELSFKKGDIITVLEKSDDgWWKGRLGR--GK---EGLFPSNYVE 56
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
187-432 2.54e-13

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 71.01  E-value: 2.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 187 PREEFTLCKKLGSGYFGEVFEGLWKGLVRV-AVKVI---SRDNLLHQHTfqAEIQAMKKLRHKHILSLYAVATAGDPVYI 262
Cdd:PLN00034  72 SLSELERVNRIGSGAGGTVYKVIHRPTGRLyALKVIygnHEDTVRRQIC--REIEILRDVNHPNVVKCHDMFDHNGEIQV 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 263 ITELMPKGSLlQLLRDSDEkdlpiLELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKE--D 340
Cdd:PLN00034 150 LLEFMDGGSL-EGTHIADE-----QFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRILAQtmD 223
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 341 IYLSRDHNVPYkwTAPEA----LSRGHYS-IKSDVWSFGVLLHEiFSRGQMPYpGMSNHETFLRVDAGYRMPCPLECPPN 415
Cdd:PLN00034 224 PCNSSVGTIAY--MSPERintdLNHGAYDgYAGDIWSLGVSILE-FYLGRFPF-GVGRQGDWASLMCAICMSQPPEAPAT 299
                        250       260
                 ....*....|....*....|.
gi 157822719 416 IHK----LMLSCWSRDPKQRP 432
Cdd:PLN00034 300 ASRefrhFISCCLQREPAKRW 320
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
195-409 2.57e-13

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: 70.84  E-value: 2.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWKGLVR-VAVKVISR--DNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDP------VYIITE 265
Cdd:cd07875   30 KPIGSGAQGIVCAAYDAILERnVAIKKLSRpfQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQKSleefqdVYIVME 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMpKGSLLQLLR-DSDEKDLPILelvdfASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDiYLS 344
Cdd:cd07875  110 LM-DANLCQVIQmELDHERMSYL-----LYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTS-FMM 182
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157822719 345 RDHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFsRGQMPYPGMSNHETFLRVDAGYRMPCP 409
Cdd:cd07875  183 TPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMI-KGGVLFPGTDHIDQWNKVIEQLGTPCP 246
SH2_Srm cd10360
Src homology 2 (SH2) domain found in Src-related kinase lacking C-terminal regulatory tyrosine ...
77-155 2.71e-13

Src homology 2 (SH2) domain found in Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristoylation sites (srm); Srm is a nonreceptor protein kinase that has two SH2 domains, a SH3 domain, and a kinase domain with a tyrosine residue for autophosphorylation. However it lacks an N-terminal glycine for myristoylation and a C-terminal tyrosine which suppresses kinase activity when phosphorylated. Srm is most similar to members of the Tec family who other members include: Tec, Btk/Emb, and Itk/Tsk/Emt. However Srm differs in its N-terminal unique domain it being much smaller than in the Tec family and is closer to Src. Srm is thought to be a new family of nonreceptor tyrosine kinases that may be redundant in function. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198223  Cd Length: 79  Bit Score: 64.98  E-value: 2.71e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157822719  77 PWFFGCISRSEAMHRLQSEDYPKGTFLIRVSQKPGADYVLSVWDAEAVRHYRIWRNSAGRLHLNEVVSFSSLSELVNYH 155
Cdd:cd10360    1 PWYFSGISRTQAQQLLLSPPNEPGAFLIRPSESSLGGYSLSVRAQAKVCHYRICMAPSGSLYLQKGRLFPGLEELLAYY 79
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
195-383 2.81e-13

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: 70.10  E-value: 2.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVfeglWKGLVR---------VAVKVISRDNllhQHTFQAE--IQAMKKLRHKHILSLYAV---ATAGDPV 260
Cdd:cd14055    1 KLVGKGRFAEV----WKAKLKqnasgqyetVAVKIFPYEE---YASWKNEkdIFTDASLKHENILQFLTAeerGVGLDRQ 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 261 Y-IITELMPKGSLLQLLRDSDekdLPILELVDFASQVAEGMCYLESQNY---------IHRDLAARNVLVTENNLCKVGD 330
Cdd:cd14055   74 YwLITAYHENGSLQDYLTRHI---LSWEDLCKMAGSLARGLAHLHSDRTpcgrpkipiAHRDLKSSNILVKNDGTCVLAD 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157822719 331 FGLArlVKEDIYLSRDH--NV----PYKWTAPEAL-SRGHY----SIKS-DVWSFGVLLHEIFSR 383
Cdd:cd14055  151 FGLA--LRLDPSLSVDElaNSgqvgTARYMAPEALeSRVNLedleSFKQiDVYSMALVLWEMASR 213
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
189-400 2.98e-13

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: 70.42  E-value: 2.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVfeglwkGLVR-------VAVKVISRDNLLHQHT---FQAEIQAMKKLRHKHILSL-YAVATAg 257
Cdd:cd05601    1 KDFEVKNVIGRGHFGEV------QVVKekatgdiYAMKVLKKSETLAQEEvsfFEEERDIMAKANSPWITKLqYAFQDS- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 258 DPVYIITELMPKGSLLQLLRDSDEkdlpILE--LVDF-ASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLA 334
Cdd:cd05601   74 ENLYLVMEYHPGGDLLSLLSRYDD----IFEesMARFyLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSA 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157822719 335 rlvkedIYLSRDHNVPYK-------WTAPEAL------SRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRV 400
Cdd:cd05601  150 ------AKLSSDKTVTSKmpvgtpdYIAPEVLtsmnggSKGTYGVECDWWSLGIVAYEMLY-GKTPFTEDTVIKTYSNI 221
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
184-432 3.90e-13

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Heme-Regulated Inhibitor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HRI (or EIF2AK1) contains an N-terminal regulatory heme-binding domain and a C-terminal catalytic kinase domain. It is suppressed under normal conditions by binding of the heme iron, and is activated during heme deficiency. It functions as a critical regulator that ensures balanced synthesis of globins and heme, in order to form stable hemoglobin during erythroid differentiation and maturation. HRI also protects cells and enhances survival under iron-deficient conditions. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The HRI subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 69.46  E-value: 3.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 184 WERPREEFTLCKKLGSGYFGEVF------EGLWKGLVRVAVKVISRDNLLhqhTFQAEIQAMKKLRHKHILSLYAVATag 257
Cdd:cd14049    1 TSRYLNEFEEIARLGKGGYGKVYkvrnklDGQYYAIKKILIKKVTKRDCM---KVLREVKVLAGLQHPNIVGYHTAWM-- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 258 DPV----YIITELMPKgSLLQLLRDSDEK-----------DLPILELV-DFASQVAEGMCYLESQNYIHRDLAARNVLVT 321
Cdd:cd14049   76 EHVqlmlYIQMQLCEL-SLWDWIVERNKRpceeefksapyTPVDVDVTtKILQQLLEGVTYIHSMGIVHRDLKPRNIFLH 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 322 ENNL-CKVGDFGLA-RLVKEDIYLSRDHNVPYKWT-----------APEALSRGHYSIKSDVWSFGVLLHEIFsrgqMPY 388
Cdd:cd14049  155 GSDIhVRIGDFGLAcPDILQDGNDSTTMSRLNGLThtsgvgtclyaAPEQLEGSHYDFKSDMYSIGVILLELF----QPF 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 157822719 389 -PGMSNHETFLRVDAGyRMPCPLECP-PNIHKLMLSCWSRDPKQRP 432
Cdd:cd14049  231 gTEMERAEVLTQLRNG-QIPKSLCKRwPVQAKYIKLLTSTEPSERP 275
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
197-377 4.41e-13

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: 68.89  E-value: 4.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGL-VRVAVKVISRDNLlHQHTFQAEIQAMKKLR-HKHILSLYAVATAGDPVYIIT-ELMPKGSLL 273
Cdd:cd13987    1 LGEGTYGKVLLAVHKGSgTKMALKFVPKPST-KLKDFLREYNISLELSvHPHIIKTYDVAFETEDYYVFAqEYAPYGDLF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 274 QLLRDSDEKDLPILELVdfASQVAEGMCYLESQNYIHRDLAARNVLVTENNL--CKVGDFGLAR----LVKediylSRDH 347
Cdd:cd13987   80 SIIPPQVGLPEERVKRC--AAQLASALDFMHSKNLVHRDIKPENVLLFDKDCrrVKLCDFGLTRrvgsTVK-----RVSG 152
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 157822719 348 NVPYkwTAPEALSRG-HYSIK----SDVWSFGVLL 377
Cdd:cd13987  153 TIPY--TAPEVCEAKkNEGFVvdpsIDVWAFGVLL 185
SH2_Src_Fgr cd10367
Src homology 2 (SH2) domain found in Gardner-Rasheed feline sarcoma viral (v-fgr) oncogene ...
74-159 4.46e-13

Src homology 2 (SH2) domain found in Gardner-Rasheed feline sarcoma viral (v-fgr) oncogene homolog, Fgr; Fgr is a member of the Src non-receptor type tyrosine kinase family of proteins. The protein contains N-terminal sites for myristoylation and palmitoylation, a PTK domain, and SH2 and SH3 domains which are involved in mediating protein-protein interactions with phosphotyrosine-containing and proline-rich motifs, respectively. Fgr is expressed in B-cells and myeloid cells, localizes to plasma membrane ruffles, and functions as a negative regulator of cell migration and adhesion triggered by the beta-2 integrin signal transduction pathway. Multiple alternatively spliced variants, encoding the same protein, have been identified Fgr has been shown to interact with Wiskott-Aldrich syndrome protein. Fgr has a unique N-terminal domain, an SH3 domain, an SH2 domain, a kinase domain and a regulatory tail, as do the other members of the family. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198230  Cd Length: 101  Bit Score: 64.93  E-value: 4.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719  74 ESEPWFFGCISRSEAMHRLQSEDYPKGTFLIRVSQKPGADYVLSV--WDA---EAVRHYRIWRNSAGRLHLNEVVSFSSL 148
Cdd:cd10367    1 QAEEWYFGKIGRKDAERQLLSPGNPRGAFLIRESETTKGAYSLSIrdWDQnrgDHVKHYKIRKLDTGGYYITTRAQFDTV 80
                         90
                 ....*....|.
gi 157822719 149 SELVNYHKTHN 159
Cdd:cd10367   81 QELVQHYMEVN 91
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
235-392 4.77e-13

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L1, also called PITSLRE, exists in different isoforms which are named using the alias CDK11(p). The CDC2L1 gene produces two protein products, CDK11(p110) and CDK11(p58). CDC2L1 is also represented by the caspase-processed CDK11(p46). CDK11(p110), the major isoform, associates with cyclin L and is expressed throughout the cell cycle. It is involved in RNA processing and the regulation of transcription. CDK11(p58) associates with cyclin D3 and is expressed during the G2/M phase of the cell cycle. It plays roles in spindle morphogenesis, centrosome maturation, sister chromatid cohesion, and the completion of mitosis. CDK11(p46) is formed from the larger isoforms by caspases during TNFalpha- and Fas-induced apoptosis. It functions as a downstream effector kinase in apoptotic signaling pathways and interacts with eukaryotic initiation factor 3f (eIF3f), p21-activated kinase (PAK1), and Ran-binding protein (RanBPM). CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 69.56  E-value: 4.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 235 EIQAMKKLRHKHILSL--YAVATAGDPVYIITELMPKGslLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRD 312
Cdd:cd07843   54 EINILLKLQHPNIVTVkeVVVGSNLDKIYMVMEYVEHD--LKSLMETMKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRD 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 313 LAARNVLVTENNLCKVGDFGLARLVKEDIYlSRDHNVPYKW-TAPEAL-SRGHYSIKSDVWSFGVLLHEIFSRGQMpYPG 390
Cdd:cd07843  132 LKTSNLLLNNRGILKICDFGLAREYGSPLK-PYTQLVVTLWyRAPELLlGAKEYSTAIDMWSVGCIFAELLTKKPL-FPG 209

                 ..
gi 157822719 391 MS 392
Cdd:cd07843  210 KS 211
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
197-436 4.95e-13

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


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 69.14  E-value: 4.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGLVRV-AVKVISRDNLLHQHTFQA---EIQAMKKLRHKHILSL-YAVATAGDPVYIITeLMPKGS 271
Cdd:cd05608    9 LGKGGFGEVSACQMRATGKLyACKKLNKKRLKKRKGYEGamvEKRILAKVHSRFIVSLaYAFQTKTDLCLVMT-IMNGGD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 272 LLQLLRDSDEKD--LPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSRDHNV 349
Cdd:cd05608   88 LRYHIYNVDEENpgFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVELKDGQTKTKGYAG 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 350 PYKWTAPEALSRGHYSIKSDVWSFGVLLHE-IFSRGQMPYPG--MSNHETFLRV--DAgyrMPCPLECPPNIHKLMLSCW 424
Cdd:cd05608  168 TPGFMAPELLLGEEYDYSVDYFTLGVTLYEmIAARGPFRARGekVENKELKQRIlnDS---VTYSEKFSPASKSICEALL 244
                        250
                 ....*....|..
gi 157822719 425 SRDPKQRPCFKD 436
Cdd:cd05608  245 AKDPEKRLGFRD 256
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
196-392 5.35e-13

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: 69.24  E-value: 5.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 196 KLGSGYFGEVFEGLWKGLVR-VAVKVISrdnlLHQH------TFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMP 268
Cdd:cd07835    6 KIGEGTYGVVYKARDKLTGEiVALKKIR----LETEdegvpsTAIREISLLKELNHPNIVRLLDVVHSENKLYLVFEFLD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 269 KGslLQLLRDSDEKDLPILELVD-FASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARL--VKEDIYlsr 345
Cdd:cd07835   82 LD--LKKYMDSSPLTGLDPPLIKsYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLARAfgVPVRTY--- 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 157822719 346 DHNVPYKW-TAPEAL--SRgHYSIKSDVWSFGVLLHEIFSRGQMpYPGMS 392
Cdd:cd07835  157 THEVVTLWyRAPEILlgSK-HYSTPVDIWSVGCIFAEMVTRRPL-FPGDS 204
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
191-396 5.82e-13

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: 69.12  E-value: 5.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEGLW----KGLVRVAVKVISRDNLLhqhtFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITEL 266
Cdd:cd14104    2 YMIAEELGRGQFGIVHRCVEtsskKTYMAKFVKVKGADQVL----VKKEISILNIARHRNILRLHESFESHEELVMIFEF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 267 MPKGSLLQLLRDSdEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVT--ENNLCKVGDFGLARLVKEDIYLS 344
Cdd:cd14104   78 ISGVDIFERITTA-RFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCtrRGSYIKIIEFGQSRQLKPGDKFR 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 157822719 345 RDHNVPyKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHET 396
Cdd:cd14104  157 LQYTSA-EFYAPEVHQHESVSTATDMWSLGCLVYVLLS-GINPFEAETNQQT 206
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
197-441 6.04e-13

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: 68.76  E-value: 6.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGLVrVAVKVISRDNLL----HQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSL 272
Cdd:cd14160    1 IGEGEIFEVYRVRIGNRS-YAVKLFKQEKKMqwkkHWKRFLSELEVLLLFQHPNILELAAYFTETEKFCLVYPYMQNGTL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 273 L-QLLRDSDEKDLPILELVDFASQVAEGMCYLESQN---YIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSRDHN 348
Cdd:cd14160   80 FdRLQCHGVTKPLSWHERINILIGIAKAIHYLHNSQpctVICGNISSANILLDDQMQPKLTDFALAHFRPHLEDQSCTIN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 349 V-----PYKWTAPEALSR-GHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHeTFLR-----------VDAGYRM----- 406
Cdd:cd14160  160 MttalhKHLWYMPEEYIRqGKLSVKTDVYSFGIVIMEVLT-GCKVVLDDPKH-LQLRdllhelmekrgLDSCLSFldlkf 237
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 157822719 407 -PCPLECPPNIHKLMLSCWSRDPKQRPCFKDLCEKL 441
Cdd:cd14160  238 pPCPRNFSAKLFRLAGRCTATKAKLRPDMDEVLQRL 273
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
189-381 6.11e-13

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 69.62  E-value: 6.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFEGLWKG--LVRVAVKVISRDNLLHQ----HTFqAEIQAMKKLRHKHILSLYAVATAGDPVYI 262
Cdd:PTZ00426  30 EDFNFIRTLGTGSFGRVILATYKNedFPPVAIKRFEKSKIIKQkqvdHVF-SERKILNYINHPFCVNLYGSFKDESYLYL 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 263 ITELMPKGSLLQLLRDSdeKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIY 342
Cdd:PTZ00426 109 VLEFVIGGEFFTFLRRN--KRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAKVVDTRTY 186
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 157822719 343 LSrdHNVPyKWTAPEALSRGHYSIKSDVWSFGVLLHEIF 381
Cdd:PTZ00426 187 TL--CGTP-EYIAPEILLNVGHGKAADWWTLGIFIYEIL 222
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
184-382 6.37e-13

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: 69.60  E-value: 6.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 184 WERPrEEFTLCKKLGSGYFGEVFEGL-WKGLVRVAVKVISR---DNLLHQHTFQaEIQAMKKLRHKHILSLYAVATAGDP 259
Cdd:cd07880   11 WEVP-DRYRDLKQVGSGAYGTVCSALdRRTGAKVAIKKLYRpfqSELFAKRAYR-ELRLLKHMKHENVIGLLDVFTPDLS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 260 V------YIITELMPK--GSLLQLLRDSDEKdlpILELVdfaSQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDF 331
Cdd:cd07880   89 LdrfhdfYLVMPFMGTdlGKLMKHEKLSEDR---IQFLV---YQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDF 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 157822719 332 GLARLVKEDIylsrDHNVPYKW-TAPEA-LSRGHYSIKSDVWSFGVLLHEIFS 382
Cdd:cd07880  163 GLARQTDSEM----TGYVVTRWyRAPEViLNWMHYTQTVDIWSVGCIMAEMLT 211
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
196-439 6.49e-13

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: 68.49  E-value: 6.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 196 KLGSGYFGEVFEGL-WKGLVRVA-----VKVISRdnlLHQHTFQAEIQAMKKLRHKHILSLY----AVATAGDPVYIITE 265
Cdd:cd14033    8 EIGRGSFKTVYRGLdTETTVEVAwcelqTRKLSK---GERQRFSEEVEMLKGLQHPNIVRFYdswkSTVRGHKCIILVTE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMPKGSLLQLLRDSDEKDLPILElvDFASQVAEGMCYLESQN--YIHRDLAARNVLVT-ENNLCKVGDFGLARLvKEDIY 342
Cdd:cd14033   85 LMTSGTLKTYLKRFREMKLKLLQ--RWSRQILKGLHFLHSRCppILHRDLKCDNIFITgPTGSVKIGDLGLATL-KRASF 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 343 LSRDHNVPyKWTAPEaLSRGHYSIKSDVWSFGVLLHEIfSRGQMPYPGMSN-HETFLRVDAGYRMPCPLECP-PNIHKLM 420
Cdd:cd14033  162 AKSVIGTP-EFMAPE-MYEEKYDEAVDVYAFGMCILEM-ATSEYPYSECQNaAQIYRKVTSGIKPDSFYKVKvPELKEII 238
                        250
                 ....*....|....*....
gi 157822719 421 LSCWSRDPKQRPCFKDLCE 439
Cdd:cd14033  239 EGCIRTDKDERFTIQDLLE 257
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
284-383 6.98e-13

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: 68.84  E-value: 6.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 284 LPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLsrDHNVPYKW-TAPEALSRG 362
Cdd:cd07863  105 LPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLARIYSCQMAL--TPVVVTLWyRAPEVLLQS 182
                         90       100
                 ....*....|....*....|.
gi 157822719 363 HYSIKSDVWSFGVLLHEIFSR 383
Cdd:cd07863  183 TYATPVDMWSVGCIFAEMFRR 203
SH2_Src_HCK cd10363
Src homology 2 (SH2) domain found in HCK; HCK is a member of the Src non-receptor type ...
74-170 7.17e-13

Src homology 2 (SH2) domain found in HCK; HCK is a member of the Src non-receptor type tyrosine kinase family of proteins and is expressed in hemopoietic cells. HCK is proposed to couple the Fc receptor to the activation of the respiratory burst. It may also play a role in neutrophil migration and in the degranulation of neutrophils. It has two different translational starts that have different subcellular localization. HCK has been shown to interact with BCR gene, ELMO1 Cbl gene, RAS p21 protein activator 1, RASA3, Granulocyte colony-stimulating factor receptor, ADAM15 and RAPGEF1. Like the other members of the Src family the SH2 domain in addition to binding the target, also plays an autoinhibitory role by binding to its C-terminal tail. In general SH2 domains are involved in signal transduction. HCK has a unique N-terminal domain, an SH3 domain, an SH2 domain, a kinase domain and a regulatory tail, as do the other members of the family. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198226  Cd Length: 104  Bit Score: 64.60  E-value: 7.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719  74 ESEPWFFGCISRSEAMHRLQSEDYPKGTFLIRVSQKPGADYVLSVWDAE-----AVRHYRIWRNSAGRLHLNEVVSFSSL 148
Cdd:cd10363    1 ETEEWFFKGISRKDAERQLLAPGNMLGSFMIRDSETTKGSYSLSVRDYDpqhgdTVKHYKIRTLDNGGFYISPRSTFSTL 80
                         90       100
                 ....*....|....*....|....
gi 157822719 149 SELVNYHKthNLSPGL--QLSMAC 170
Cdd:cd10363   81 QELVDHYK--KGNDGLcqKLSVPC 102
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
217-388 8.24e-13

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


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 68.87  E-value: 8.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 217 AVKVISRdnllhQHTFQAEIQAMKKLR-HKHILSLYAVATAGDPVYIITELMPKGSLLQLLRDS---DEKdlpilELVDF 292
Cdd:cd14092   35 AVKIVSR-----RLDTSREVQLLRLCQgHPNIVKLHEVFQDELHTYLVMELLRGGELLERIRKKkrfTES-----EASRI 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 293 ASQVAEGMCYLESQNYIHRDLAARNVLVT---ENNLCKVGDFGLARLVKEDIYLSRD-HNVPYkwTAPEALSRGH----Y 364
Cdd:cd14092  105 MRQLVSAVSFMHSKGVVHRDLKPENLLFTdedDDAEIKIVDFGFARLKPENQPLKTPcFTLPY--AAPEVLKQALstqgY 182
                        170       180
                 ....*....|....*....|....
gi 157822719 365 SIKSDVWSFGVLLHEIFSrGQMPY 388
Cdd:cd14092  183 DESCDLWSLGVILYTMLS-GQVPF 205
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
189-395 9.96e-13

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: 68.50  E-value: 9.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFEG---LWKGLVrvAVKVIsrdNLLHQH----TFQAEIQAMKKLRHKHILSLYAVATAGDPVY 261
Cdd:cd07871    5 ETYVKLDKLGEGTYATVFKGrskLTENLV--ALKEI---RLEHEEgapcTAIREVSLLKNLKHANIVTLHDIIHTERCLT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 262 IITELMpKGSLLQLLrDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARlVKEDI 341
Cdd:cd07871   80 LVFEYL-DSDLKQYL-DNCGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLAR-AKSVP 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 157822719 342 YLSRDHNVPYKWTAPEALSRG--HYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHE 395
Cdd:cd07871  157 TKTYSNEVVTLWYRPPDVLLGstEYSTPIDMWGVGCILYEMAT-GRPMFPGSTVKE 211
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
196-391 9.98e-13

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: 68.55  E-value: 9.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 196 KLGSGYFGEVFEGLWKGLVR-VAVKVISRDNLLHQHTFQA--EIQAMKKLRHKHILSLYAV----ATAGD----PVYIIT 264
Cdd:cd07865   19 KIGQGTFGEVFKARHRKTGQiVALKKVLMENEKEGFPITAlrEIKILQLLKHENVVNLIEIcrtkATPYNrykgSIYLVF 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 265 ELMPKgSLLQLLRDSDEK-DLPilELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLV------ 337
Cdd:cd07865   99 EFCEH-DLAGLLSNKNVKfTLS--EIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGLARAFslakns 175
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 157822719 338 KEDIYLSRDHNVPYKwtAPEAL--SRgHYSIKSDVWSFGVLLHEIFSRgqmpYPGM 391
Cdd:cd07865  176 QPNRYTNRVVTLWYR--PPELLlgER-DYGPPIDMWGAGCIMAEMWTR----SPIM 224
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
196-390 1.00e-12

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: 68.23  E-value: 1.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 196 KLGSGYFGEVFEGLWK--GLVrVAVKVISRDNLLHQHTFQA--EIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGs 271
Cdd:cd07839    7 KIGEGTYGTVFKAKNRetHEI-VALKRVRLDDDDEGVPSSAlrEICLLKELKHKNIVRLYDVLHSDKKLTLVFEYCDQD- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 272 lLQLLRDS--DEKDLPILELvdFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARL----VKediylSR 345
Cdd:cd07839   85 -LKKYFDScnGDIDPEIVKS--FMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARAfgipVR-----CY 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 157822719 346 DHNVPYKWTAPEALSRGH--YSIKSDVWSFGVLLHEIFSRGQMPYPG 390
Cdd:cd07839  157 SAEVVTLWYRPPDVLFGAklYSTSIDMWSAGCIFAELANAGRPLFPG 203
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
195-397 1.04e-12

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: 68.57  E-value: 1.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWKGLVRV-AVKVISRDNLLHQHTFQAEIQAMKKL----RHKHILSLYAVATAGDPVYIITELMPK 269
Cdd:cd05592    1 KVLGKGSFGKVMLAELKGTNQYfAIKALKKDVVLEDDDVECTMIERRVLalasQHPFLTHLFCTFQTESHLFFVMEYLNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 270 GSLLQLLRDSDEKDLPILELvdFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLArlvKEDIYLSRDHN- 348
Cdd:cd05592   81 GDLMFHIQQSGRFDEDRARF--YGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMC---KENIYGENKASt 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 157822719 349 ---VPyKWTAPEALSRGHYSIKSDVWSFGVLLHEIFsRGQMPYPGMSNHETF 397
Cdd:cd05592  156 fcgTP-DYIAPEILKGQKYNQSVDWWSFGVLLYEML-IGQSPFHGEDEDELF 205
SH2_C-SH2_Zap70 cd10402
C-terminal Src homology 2 (SH2) domain found in Zeta-chain-associated protein kinase 70 ...
74-156 1.17e-12

C-terminal Src homology 2 (SH2) domain found in Zeta-chain-associated protein kinase 70 (ZAP-70); ZAP-70 and Syk comprise a family of hematopoietic cell specific protein tyrosine kinases (PTKs) that are required for antigen and antibody receptor function. ZAP-70 is expressed in T and natural killer (NK) cells and Syk is expressed in B cells, mast cells, polymorphonuclear leukocytes, platelets, macrophages, and immature T cells. They are required for the proper development of T and B cells, immune receptors, and activating NK cells. They consist of two N-terminal Src homology 2 (SH2) domains and a C-terminal kinase domain separated from the SH2 domains by a linker or hinge region. Phosphorylation of both tyrosine residues within the Immunoreceptor Tyrosine-based Activation Motifs (ITAM; consensus sequence Yxx[LI]x(7,8)Yxx[LI]) by the Src-family PTKs is required for efficient interaction of ZAP-70 and Syk with the receptor subunits and for receptor function. ZAP-70 forms two phosphotyrosine binding pockets, one of which is shared by both SH2 domains. In Syk the two SH2 domains do not form such a phosphotyrosine-binding site. The SH2 domains here are believed to function independently. In addition, the two SH2 domains of Syk display flexibility in their relative orientation, allowing Syk to accommodate a greater variety of spacing sequences between the ITAM phosphotyrosines and singly phosphorylated non-classical ITAM ligands. This model contains the C-terminus SH2 domains of Zap70. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198265  Cd Length: 105  Bit Score: 64.17  E-value: 1.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719  74 ESEPWFFGCISRSEAMHRLQSEDYPKGTFLIRVSQKPGAdYVLSVWDAEAVRHYRIWRNSAGRLHLNEVVSFSSLSELVN 153
Cdd:cd10402    8 ERMPWYHGSIARDEAERRLYSGAQPDGKFLLRERKESGT-YALSLVYGKTVYHYRIDQDKSGKYSIPEGTKFDTLWQLVE 86

                 ...
gi 157822719 154 YHK 156
Cdd:cd10402   87 YLK 89
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
189-390 1.25e-12

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 68.48  E-value: 1.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFEGLWKGLVR-VAVKVIsrdNLLHQH----TFQAEIQAMKKLRHKHILSLYAVATAGDPVYII 263
Cdd:cd07872    6 ETYIKLEKLGEGTYATVFKGRSKLTENlVALKEI---RLEHEEgapcTAIREVSLLKDLKHANIVTLHDIVHTDKSLTLV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 264 TELMPKgSLLQLLRDSDEKdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARlVKEDIYL 343
Cdd:cd07872   83 FEYLDK-DLKQYMDDCGNI-MSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLAR-AKSVPTK 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 157822719 344 SRDHNVPYKWTAPE--ALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPG 390
Cdd:cd07872  160 TYSNEVVTLWYRPPdvLLGSSEYSTQIDMWGVGCIFFEMAS-GRPLFPG 207
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
190-388 1.35e-12

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: 67.89  E-value: 1.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLCKKLGSGYFGEVFEGlWK-------GLVRVAVKVISRDNLL---HQHTFQAEIQAMKKLRHKHILSLYAVATAGDP 259
Cdd:cd14076    2 PYILGRTLGEGEFGKVKLG-WPlpkanhrSGVQVAIKLIRRDTQQencQTSKIMREINILKGLTHPNIVRLLDVLKTKKY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 260 VYIITELMPKGSLLQ-LLRDSDEKDLPILELvdFAsQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVK 338
Cdd:cd14076   81 IGIVLEFVSGGELFDyILARRRLKDSVACRL--FA-QLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTFD 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 157822719 339 EDI--YLSRDHNVPYkWTAPE--ALSRGHYSIKSDVWSFGVLLHEIFSrGQMPY 388
Cdd:cd14076  158 HFNgdLMSTSCGSPC-YAAPElvVSDSMYAGRKADIWSCGVILYAMLA-GYLPF 209
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
196-393 1.44e-12

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: 67.78  E-value: 1.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 196 KLGSGYFGEVFEGLWK--GLVrVAVK--VISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGS 271
Cdd:cd07847    8 KIGEGSYGVVFKCRNRetGQI-VAIKkfVESEDDPVIKKIALREIRMLKQLKHPNLVNLIEVFRRKRKLHLVFEYCDHTV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 272 LLQLlrDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVK--EDIYlsrDHNV 349
Cdd:cd07847   87 LNEL--EKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARILTgpGDDY---TDYV 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 157822719 350 PYKW-TAPEAL-SRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSN 393
Cdd:cd07847  162 ATRWyRAPELLvGDTQYGPPVDVWAIGCVFAELLT-GQPLWPGKSD 206
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
262-431 1.46e-12

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: 68.14  E-value: 1.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 262 IITELMPKGSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTE---NNLCKVGDFGLARLVK 338
Cdd:cd14170   76 IVMECLDGGELFSRIQDRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSkrpNAILKLTDFGFAKETT 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 339 EDIYLSRDHNVPYkWTAPEALSRGHYSIKSDVWSFGVLLHeIFSRGQMPY---------PGMSNhetflRVDAG-YRMPC 408
Cdd:cd14170  156 SHNSLTTPCYTPY-YVAPEVLGPEKYDKSCDMWSLGVIMY-ILLCGYPPFysnhglaisPGMKT-----RIRMGqYEFPN 228
                        170       180
                 ....*....|....*....|....*
gi 157822719 409 P--LECPPNIHKLMLSCWSRDPKQR 431
Cdd:cd14170  229 PewSEVSEEVKMLIRNLLKTEPTQR 253
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
189-439 1.58e-12

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: 67.83  E-value: 1.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFEGLWKGLVR-VAVKVI--SRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITE 265
Cdd:cd07846    1 EKYENLGLVGEGSYGMVMKCRHKETGQiVAIKKFleSEDDKMVKKIAMREIKMLKQLRHENLVNLIEVFRRKKRWYLVFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMPKGSLLQLLRDSDEKDLPILELVDFasQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKE--DIYl 343
Cdd:cd07846   81 FVDHTVLDDLEKYPNGLDESRVRKYLF--QILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAApgEVY- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 344 srDHNVPYKW-TAPEAL-SRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSN------------------HETFLR--VD 401
Cdd:cd07846  158 --TDYVATRWyRAPELLvGDTKYGKAVDVWAVGCLVTEMLT-GEPLFPGDSDidqlyhiikclgnliprhQELFQKnpLF 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 157822719 402 AGYRMPC-----PLE-----CPPNIHKLMLSCWSRDPKQRPCFKDLCE 439
Cdd:cd07846  235 AGVRLPEvkevePLErrypkLSGVVIDLAKKCLHIDPDKRPSCSELLH 282
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
302-448 1.59e-12

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: 67.78  E-value: 1.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 302 YL-ESQNYIHRDLAARNVLVTENNLCKVGDFGLA-RLVkEDIYLSRDHNVPyKWTAPEALS---RGHYSIKSDVWSFGVL 376
Cdd:cd06618  129 YLkEKHGVIHRDVKPSNILLDESGNVKLCDFGISgRLV-DSKAKTRSAGCA-AYMAPERIDppdNPKYDIRADVWSLGIS 206
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157822719 377 LHEIfSRGQMPYPGM-SNHETFLRV--DAGYRMPCPLECPPNIHKLMLSCWSRDPKQRPCFKDLCEKlSGITRYE 448
Cdd:cd06618  207 LVEL-ATGQFPYRNCkTEFEVLTKIlnEEPPSLPPNEGFSPDFCSFVDLCLTKDHRYRPKYRELLQH-PFIRRYE 279
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
190-422 1.67e-12

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: 67.71  E-value: 1.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLCKKLGSGYFGEVFEGLWKGLVR-VAVKVI--SRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITEL 266
Cdd:cd07848    2 KFEVLGVVGEGAYGVVLKCRHKETKEiVAIKKFkdSEENEEVKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 267 MPKgSLLQLLRDSDEKDLPIlELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSRD 346
Cdd:cd07848   82 VEK-NMLELLEEMPNGVPPE-KVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSEGSNANYT 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157822719 347 HNVPYKW-TAPEALSRGHYSIKSDVWSFGVLLHEIfSRGQMPYPGMSNHETFLRVDagyRMPCPLecPPNIHKLMLS 422
Cdd:cd07848  160 EYVATRWyRSPELLLGAPYGKAVDMWSVGCILGEL-SDGQPLFPGESEIDQLFTIQ---KVLGPL--PAEQMKLFYS 230
SH3_ASPP cd11807
Src homology 3 domain of Apoptosis Stimulating of p53 proteins (ASPP); The ASPP family of ...
10-68 2.03e-12

Src homology 3 domain of Apoptosis Stimulating of p53 proteins (ASPP); The ASPP family of proteins bind to important regulators of apoptosis (p53, Bcl-2, and RelA) and cell growth (APCL, PP1). They share similarity at their C-termini, where they harbor a proline-rich region, four ankyrin (ANK) repeats, and an SH3 domain. Vertebrates contain three members of the family: ASPP1, ASPP2, and iASPP. ASPP1 and ASPP2 activate the apoptotic function of the p53 family of tumor suppressors (p53, p63, and p73), while iASPP is an oncoprotein that specifically inhibits p53-induced apoptosis. The expression of ASPP proteins is altered in tumors; ASPP1 and ASPP2 are downregulated whereas iASPP is upregulated is some cancer types. ASPP proteins also bind and regulate protein phosphatase 1 (PP1), and this binding is competitive with p53 binding. The SH3 domain and the ANK repeats of ASPP contribute to the p53 binding site; they bind to the DNA binding domain of p53. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212741 [Multi-domain]  Cd Length: 57  Bit Score: 61.63  E-value: 2.03e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157822719  10 GPKYvGLWDFKARTDEELSFQAGDLLHVTRK----EEQWWWATLLDaegkalAEGYVPHNYLA 68
Cdd:cd11807    1 GVVY-ALFDYEAENGDELSFREGDELTVLRKgdddETEWWWARLND------KEGYVPRNLLG 56
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
197-383 2.07e-12

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: 67.30  E-value: 2.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGLVR-VAVK---VISRDNLLHQHTFQaEIQAMKKLR---HKHILSLYAVATAGD-----PVYIIT 264
Cdd:cd07838    7 IGEGAYGTVYKARDLQDGRfVALKkvrVPLSEEGIPLSTIR-EIALLKQLEsfeHPNVVRLLDVCHGPRtdrelKLTLVF 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 265 ELMPKgSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVkeDIYLS 344
Cdd:cd07838   86 EHVDQ-DLATYLDKCPKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFGLARIY--SFEMA 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 157822719 345 RDHNVPYKW-TAPEALSRGHYSIKSDVWSFGVLLHEIFSR 383
Cdd:cd07838  163 LTSVVVTLWyRAPEVLLQSSYATPVDMWSVGCIFAELFNR 202
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
184-382 2.26e-12

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: 68.01  E-value: 2.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 184 WERPREEFTLCKkLGSGYFGEVFEGL-WKGLVRVAVKVISRdnllhqhTFQAEIQA---------MKKLRHKHILSLYAV 253
Cdd:cd07879   11 WELPERYTSLKQ-VGSGAYGSVCSAIdKRTGEKVAIKKLSR-------PFQSEIFAkrayreltlLKHMQHENVIGLLDV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 254 ---ATAGDPVYIITELMPKGSL-LQLLRDSDEKDLPILELVdfaSQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVG 329
Cdd:cd07879   83 ftsAVSGDEFQDFYLVMPYMQTdLQKIMGHPLSEDKVQYLV---YQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKIL 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 157822719 330 DFGLARLVKEDIylsRDHNVPYKWTAPEA-LSRGHYSIKSDVWSFGVLLHEIFS 382
Cdd:cd07879  160 DFGLARHADAEM---TGYVVTRWYRAPEViLNWMHYNQTVDIWSVGCIMAEMLT 210
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
197-388 2.30e-12

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: 66.79  E-value: 2.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVfeglwkglVRV---------AVKVISRDNLLHQhTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELM 267
Cdd:cd14087    9 IGRGSFSRV--------VRVehrvtrqpyAIKMIETKCRGRE-VCESELNVLRRVRHTNIIQLIEVFETKERVYMVMELA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 268 PKGSLLQLL----RDSDEKDLPILELvdfasqVAEGMCYLESQNYIHRDLAARNVLV----TENNLCkVGDFGLARLVK- 338
Cdd:cd14087   80 TGGELFDRIiakgSFTERDATRVLQM------VLDGVKYLHGLGITHRDLKPENLLYyhpgPDSKIM-ITDFGLASTRKk 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157822719 339 -EDIYLSRDHNVPyKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPY 388
Cdd:cd14087  153 gPNCLMKTTCGTP-EYIAPEILLRKPYTQSVDMWAVGVIAYILLS-GTMPF 201
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
189-392 2.46e-12

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 67.15  E-value: 2.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFeglwKGLVRVAVKVISRDNL-LHQH------TFQAEIQAMKKLRHKHILSLYAVATAGDPVY 261
Cdd:PLN00009   2 DQYEKVEKIGEGTYGVVY----KARDRVTNETIALKKIrLEQEdegvpsTAIREISLLKEMQHGNIVRLQDVVHSEKRLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 262 IITELMPkgslLQLLRDSDE-----KDLPILELvdFASQVAEGMCYLESQNYIHRDLAARNVLVTE-NNLCKVGDFGLAR 335
Cdd:PLN00009  78 LVFEYLD----LDLKKHMDSspdfaKNPRLIKT--YLYQILRGIAYCHSHRVLHRDLKPQNLLIDRrTNALKLADFGLAR 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157822719 336 LVKEDIYlSRDHNVPYKW-TAPEAL--SRgHYSIKSDVWSFGVLLHEIFSrgQMP-YPGMS 392
Cdd:PLN00009 152 AFGIPVR-TFTHEVVTLWyRAPEILlgSR-HYSTPVDIWSVGCIFAEMVN--QKPlFPGDS 208
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
196-382 3.46e-12

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: 66.53  E-value: 3.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 196 KLGSGYFGEVFeglwKGLVR-----VAVK-VISRDNLLHQHTFQAEIQAMKKLR-HKHILSLYAV---ATAGDpVYIITE 265
Cdd:cd07831    6 KIGEGTFSEVL----KAQSRktgkyYAIKcMKKHFKSLEQVNNLREIQALRRLSpHPNILRLIEVlfdRKTGR-LALVFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMpKGSLLQLLRDSdEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLcKVGDFGLARLVKED----I 341
Cdd:cd07831   81 LM-DMNLYELIKGR-KRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDDIL-KLADFGSCRGIYSKppytE 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 157822719 342 YLSRdhnvpyKW-TAPEA-LSRGHYSIKSDVWSFGVLLHEIFS 382
Cdd:cd07831  158 YIST------RWyRAPEClLTDGYYGPKMDIWAVGCVFFEILS 194
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
197-436 4.37e-12

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


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 66.40  E-value: 4.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGLVRV-AVKVISRDNLLHQHTFQA---EIQAMKKLRHKHILSL-YAVATAGDPVYIITeLMPKGS 271
Cdd:cd05577    1 LGRGGFGEVCACQVKATGKMyACKKLDKKRIKKKKGETMalnEKIILEKVSSPFIVSLaYAFETKDKLCLVLT-LMNGGD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 272 LLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSRDHNVPy 351
Cdd:cd05577   80 LKYHIYNVGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVEFKGGKKIKGRVGTH- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 352 KWTAPEALSRG-HYSIKSDVWSFGVLLHEIFsRGQMPY----PGMSNHETFLRVdagyrMPCPLECP----PNIHKLMLS 422
Cdd:cd05577  159 GYMAPEVLQKEvAYDFSVDWFALGCMLYEMI-AGRSPFrqrkEKVDKEELKRRT-----LEMAVEYPdsfsPEARSLCEG 232
                        250
                 ....*....|....
gi 157822719 423 CWSRDPKQRPCFKD 436
Cdd:cd05577  233 LLQKDPERRLGCRG 246
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
190-436 5.21e-12

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: 66.96  E-value: 5.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLCKKLGSGYFGEVFEGLWKG-LVRVAVKVISRDNLL----HQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIIT 264
Cdd:cd05602    8 DFHFLKVIGKGSFGKVLLARHKSdEKFYAVKVLQKKAILkkkeEKHIMSERNVLLKNVKHPFLVGLHFSFQTTDKLYFVL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 265 ELMPKGSLLQLLrdsdEKDLPILELVD--FASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLArlvKEDIy 342
Cdd:cd05602   88 DYINGGELFYHL----QRERCFLEPRArfYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLC---KENI- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 343 lsrDHN--------VPyKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRVdagyrMPCPLECPP 414
Cdd:cd05602  160 ---EPNgttstfcgTP-EYLAPEVLHKQPYDRTVDWWCLGAVLYEMLY-GLPPFYSRNTAEMYDNI-----LNKPLQLKP 229
                        250       260
                 ....*....|....*....|....*.
gi 157822719 415 NI----HKLMLSCWSRDPKQRPCFKD 436
Cdd:cd05602  230 NItnsaRHLLEGLLQKDRTKRLGAKD 255
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
195-388 6.05e-12

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


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 66.36  E-value: 6.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWKGLVRV-AVKVISRDNLLHQHTFQAEIQAMKKL----RHKHILSLYAVATAGDPVYIITELMPK 269
Cdd:cd05591    1 KVLGKGSFGKVMLAERKGTDEVyAIKVLKKDVILQDDDVDCTMTEKRILalaaKHPFLTALHSCFQTKDRLFFVMEYVNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 270 GSLLQLLRDSDEKDLPILELvdFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLArlvKEDIYLSRDHN- 348
Cdd:cd05591   81 GDLMFQIQRARKFDEPRARF--YAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMC---KEGILNGKTTTt 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 157822719 349 ---VPyKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPY 388
Cdd:cd05591  156 fcgTP-DYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPF 196
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
186-381 6.10e-12

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: 66.24  E-value: 6.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 186 RPREEFTLCKKLGSGYFGEVFEG--LWKGLVrVAVKVI----SRDNLlhQHTFQAEIQAMKKLRHKHILSLYAVATAG-- 257
Cdd:cd07845    4 RSVTEFEKLNRIGEGTYGIVYRArdTTSGEI-VALKKVrmdnERDGI--PISSLREITLLLNLRHPNIVELKEVVVGKhl 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 258 DPVYIITELMPK--GSLLqllrDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLAR 335
Cdd:cd07845   81 DSIFLVMEYCEQdlASLL----DNMPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLAR 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 157822719 336 LVkEDIYLSRDHNVPYKW-TAPEAL-SRGHYSIKSDVWSFGVLLHEIF 381
Cdd:cd07845  157 TY-GLPAKPMTPKVVTLWyRAPELLlGCTTYTTAIDMWAVGCILAELL 203
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
195-400 7.00e-12

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: 66.59  E-value: 7.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWKGL-VRVAVKVISR--DNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDP------VYIITE 265
Cdd:cd07876   27 KPIGSGAQGIVCAAFDTVLgINVAVKKLSRpfQNQTHAKRAYRELVLLKCVNHKNIISLLNVFTPQKSleefqdVYLVME 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMpKGSLLQLLR-DSDEKDLPILelvdfASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDiYLS 344
Cdd:cd07876  107 LM-DANLCQVIHmELDHERMSYL-----LYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTACTN-FMM 179
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 157822719 345 RDHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFsRGQMPYPGMSNHETFLRV 400
Cdd:cd07876  180 TPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELV-KGSVIFQGTDHIDQWNKV 234
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
191-397 7.17e-12

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: 66.17  E-value: 7.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEGLWKGLVRV-AVK------VISRDNLlhqHTFQAE---IQAMKKLRHKHILSLYAVATAGDPV 260
Cdd:cd05589    1 FRCIAVLGRGHFGKVLLAEYKPTGELfAIKalkkgdIIARDEV---ESLMCEkriFETVNSARHPFLVNLFACFQTPEHV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 261 YIITELMPKGSLLQLLRdSDEKDLPilELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLArlvKED 340
Cdd:cd05589   78 CFVMEYAAGGDLMMHIH-EDVFSEP--RAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLC---KEG 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157822719 341 I-YLSRDHN---VPyKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETF 397
Cdd:cd05589  152 MgFGDRTSTfcgTP-EFLAPEVLTDTSYTRAVDWWGLGVLIYEMLV-GESPFPGDDEEEVF 210
SH2_Fps_family cd10361
Src homology 2 (SH2) domain found in feline sarcoma, Fujinami poultry sarcoma, and fes-related ...
71-161 7.33e-12

Src homology 2 (SH2) domain found in feline sarcoma, Fujinami poultry sarcoma, and fes-related (Fes/Fps/Fer) proteins; The Fps family consists of members Fps/Fes and Fer/Flk/Tyk3. They are cytoplasmic protein-tyrosine kinases implicated in signaling downstream from cytokines, growth factors and immune receptors. Fes/Fps/Fer contains three coiled-coil regions, an SH2 (Src-homology-2) and a TK (tyrosine kinase catalytic) domain signature. Members here include: Fps/Fes, Fer, Kin-31, and In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198224  Cd Length: 90  Bit Score: 61.39  E-value: 7.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719  71 ETVESEPWFFGCISRSEAMHRLQSEdypkGTFLIRVSQKPGAD---YVLSV-WDAEaVRHYRIWRNSAGRLHLNEVvSFS 146
Cdd:cd10361    1 KDLENEPYYHGLLPREDAEELLKND----GDFLVRKTEPKGGGkrkLVLSVrWDGK-IRHFVINRDDGGKYYIEGK-SFK 74
                         90
                 ....*....|....*
gi 157822719 147 SLSELVNYHKTHNLS 161
Cdd:cd10361   75 SISELINYYQKTKEP 89
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
190-403 7.60e-12

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 66.38  E-value: 7.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLCKKLGSGYFGEVFEGLWKGLVR-VAVKVISRDNLLH----QHTFQaEIQAMKKLRHKHILSLYAVATAGDPVYIIT 264
Cdd:PTZ00263  19 DFEMGETLGTGSFGRVRIAKHKGTGEyYAIKCLKKREILKmkqvQHVAQ-EKSILMELSHPFIVNMMCSFQDENRVYFLL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 265 ELMPKGSLLQLLRDSDEkdlpilelvdFASQVAEGMC--------YLESQNYIHRDLAARNVLVTENNLCKVGDFGLARL 336
Cdd:PTZ00263  98 EFVVGGELFTHLRKAGR----------FPNDVAKFYHaelvlafeYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKK 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157822719 337 VKEDIYLSrdHNVPyKWTAPEAL-SRGHySIKSDVWSFGVLLHEiFSRGQMPYPGMSNHETFLRVDAG 403
Cdd:PTZ00263 168 VPDRTFTL--CGTP-EYLAPEVIqSKGH-GKAVDWWTMGVLLYE-FIAGYPPFFDDTPFRIYEKILAG 230
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
191-400 8.11e-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: 66.11  E-value: 8.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFeglwkgLVRV-------AVKVISR-----DNLLHQHTFQAEIQAmkKLRHKHILSLYAVATAGD 258
Cdd:cd05574    3 FKKIKLLGKGDVGRVY------LVRLkgtgklfAMKVLDKeemikRNKVKRVLTEREILA--TLDHPFLPTLYASFQTST 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 259 PVYIITELMPKGSLLQLLRDSDEKDLPIlELVDF-ASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGL---- 333
Cdd:cd05574   75 HLCFVMDYCPGGELFRLLQKQPGKRLPE-EVARFyAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLskqs 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 334 ----ARLVKEDIYLSRDHNVPY---------------------KWTAPEALS-RGHYSiKSDVWSFGVLLHEIFSrGQMP 387
Cdd:cd05574  154 svtpPPVRKSLRKGSRRSSVKSieketfvaepsarsnsfvgteEYIAPEVIKgDGHGS-AVDWWTLGILLYEMLY-GTTP 231
                        250
                 ....*....|...
gi 157822719 388 YPGMSNHETFLRV 400
Cdd:cd05574  232 FKGSNRDETFSNI 244
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
191-395 8.25e-12

Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PRP4 phosphorylates a number of factors involved in the formation of active spliceosomes, which catalyze pre-mRNA splicing. It phosphorylates PRP6 and PRP31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), during spliceosomal complex formation. In fission yeast, PRP4 phosphorylates the splicing factor PRP1 (U5-102 kD in mammals). Thus, PRP4 plays a key role in regulating spliceosome assembly and pre-mRNA splicing. It also plays an important role in mitosis by acting as a spindle assembly checkpoint kinase that is required for chromosome alignment and the recruitment of the checkpoint proteins MPS1, MAD1, and MAD2 at kinetochores. The PRP4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 66.09  E-value: 8.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVF--EGLWKGLVRVAVKVIsRDNLLHQHTFQAEIQAMKKLR------HKHILSLYAVATAGDPVYI 262
Cdd:cd14135    2 YRVYGYLGKGVFSNVVraRDLARGNQEVAIKII-RNNELMHKAGLKELEILKKLNdadpddKKHCIRLLRHFEHKNHLCL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 263 ITELMpKGSLLQLLRD-SDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTEN-NLCKVGDFGLARLVKE- 339
Cdd:cd14135   81 VFESL-SMNLREVLKKyGKNVGLNIKAVRSYAQQLFLALKHLKKCNILHADIKPDNILVNEKkNTLKLCDFGSASDIGEn 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 157822719 340 DI--YL-SRDhnvpYKwtAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHE 395
Cdd:cd14135  160 EItpYLvSRF----YR--APEIILGLPYDYPIDMWSVGCTLYELYT-GKILFPGKTNNH 211
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
191-376 9.76e-12

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: 65.62  E-value: 9.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEGLWKGLVR-VAVKVISRDnlLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPK 269
Cdd:cd14085    5 FEIESELGRGATSVVYRCRQKGTQKpYAVKKLKKT--VDKKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLELVTG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 270 GSLLQLLRDS---DEKDLpilelVDFASQVAEGMCYLESQNYIHRDLAARNVLVT---ENNLCKVGDFGLARLVKEDIYL 343
Cdd:cd14085   83 GELFDRIVEKgyySERDA-----ADAVKQILEAVAYLHENGIVHRDLKPENLLYAtpaPDAPLKIADFGLSKIVDQQVTM 157
                        170       180       190
                 ....*....|....*....|....*....|...
gi 157822719 344 SRDHNVPyKWTAPEALSRGHYSIKSDVWSFGVL 376
Cdd:cd14085  158 KTVCGTP-GYCAPEILRGCAYGPEVDMWSVGVI 189
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
183-400 1.15e-11

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: 66.19  E-value: 1.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 183 DWERP-----------REEFTLCKKLGSGYFGEVFEGLWKGLVRV-AVKVISRDNLLHQhtfqAEIQAMKKLRH------ 244
Cdd:cd05624   55 EWAKPftqlvkemqlhRDDFEIIKVIGRGAFGEVAVVKMKNTERIyAMKILNKWEMLKR----AETACFREERNvlvngd 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 245 -KHILSLYAVATAGDPVYIITELMPKGSLLQLLRDSDEKdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTEN 323
Cdd:cd05624  131 cQWITTLHYAFQDENYLYLVMDYYVGGDLLTLLSKFEDK-LPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMN 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 324 NLCKVGDFGLARLVKED--IYLSRDHNVPyKWTAPEALS-----RGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHET 396
Cdd:cd05624  210 GHIRLADFGSCLKMNDDgtVQSSVAVGTP-DYISPEILQamedgMGKYGPECDWWSLGVCMYEMLY-GETPFYAESLVET 287

                 ....
gi 157822719 397 FLRV 400
Cdd:cd05624  288 YGKI 291
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
189-431 1.18e-11

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: 65.01  E-value: 1.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKK-LGSGYFGEVFEGLWKGL-VRVAVKVISrDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDP-VYIITE 265
Cdd:cd14172    3 DDYKLSKQvLGLGVNGKVLECFHRRTgQKCALKLLY-DSPKARREVEHHWRASGGPHIVHILDVYENMHHGKRcLLIIME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMPKGSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVT---ENNLCKVGDFGLARLVKEDIY 342
Cdd:cd14172   82 CMEGGELFSRIQERGDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTskeKDAVLKLTDFGFAKETTVQNA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 343 LSRDHNVPYkWTAPEALSRGHYSIKSDVWSFGVLLHEIF--------SRGQMPYPGMSNhetflRVDAG-YRMPCP--LE 411
Cdd:cd14172  162 LQTPCYTPY-YVAPEVLGPEKYDKSCDMWSLGVIMYILLcgfppfysNTGQAISPGMKR-----RIRMGqYGFPNPewAE 235
                        250       260
                 ....*....|....*....|
gi 157822719 412 CPPNIHKLMLSCWSRDPKQR 431
Cdd:cd14172  236 VSEEAKQLIRHLLKTDPTER 255
SH2_C-SH2_PLC_gamma_like cd09932
C-terminal Src homology 2 (C-SH2) domain in Phospholipase C gamma; Phospholipase C gamma is a ...
74-167 1.19e-11

C-terminal Src homology 2 (C-SH2) domain in Phospholipase C gamma; Phospholipase C gamma is a signaling molecule that is recruited to the C-terminal tail of the receptor upon autophosphorylation of a highly conserved tyrosine. PLCgamma is composed of a Pleckstrin homology (PH) domain followed by an elongation factor (EF) domain, 2 catalytic regions of PLC domains that flank 2 tandem SH2 domains (N-SH2, C-SH2), and ending with a SH3 domain and C2 domain. N-SH2 SH2 domain-mediated interactions represent a crucial step in transmembrane signaling by receptor tyrosine kinases. SH2 domains recognize phosphotyrosine (pY) in the context of particular sequence motifs in receptor phosphorylation sites. Both N-SH2 and C-SH2 have a very similar binding affinity to pY. But in growth factor stimulated cells these domains bind to different target proteins. N-SH2 binds to pY containing sites in the C-terminal tails of tyrosine kinases and other receptors. Recently it has been shown that this interaction is mediated by phosphorylation-independent interactions between a secondary binding site found exclusively on the N-SH2 domain and a region of the FGFR1 tyrosine kinase domain. This secondary site on the SH2 cooperates with the canonical pY site to regulate selectivity in mediating a specific cellular process. C-SH2 binds to an intramolecular site on PLCgamma itself which allows it to hydrolyze phosphatidylinositol-4,5-bisphosphate into diacylglycerol and inositol triphosphate. These then activate protein kinase C and release calcium. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198186  Cd Length: 104  Bit Score: 61.13  E-value: 1.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719  74 ESEPWFFGCISRSEAMHRLQSedYPK-GTFLIRVSQKPGADYVLSVWDAEAVRHYRIWRNsaGRLHLNEVVSFSSLSELV 152
Cdd:cd09932    2 ESKEWFHANLTREQAEEMLMR--VPRdGAFLVRPSETDPNSFAISFRAEGKIKHCRIKQE--GRLFVIGTSQFESLVELV 77
                         90
                 ....*....|....*
gi 157822719 153 NYHKTHNLSPGLQLS 167
Cdd:cd09932   78 SYYEKHPLYRKIKLR 92
SH2_Src_Fyn_isoform_a_like cd10418
Src homology 2 (SH2) domain found in Fyn isoform a like proteins; Fyn is a member of the Src ...
74-155 1.23e-11

Src homology 2 (SH2) domain found in Fyn isoform a like proteins; Fyn is a member of the Src non-receptor type tyrosine kinase family of proteins. This cd contains the SH2 domain found in Fyn isoform a type proteins. Fyn is involved in the control of cell growth and is required in the following pathways: T and B cell receptor signaling, integrin-mediated signaling, growth factor and cytokine receptor signaling, platelet activation, ion channel function, cell adhesion, axon guidance, fertilization, entry into mitosis, and differentiation of natural killer cells, oligodendrocytes and keratinocytes. The protein associates with the p85 subunit of phosphatidylinositol 3-kinase and interacts with the Fyn-binding protein. Alternatively spliced transcript variants encoding distinct isoforms exist. Fyn is primarily localized to the cytoplasmic leaflet of the plasma membrane. Tyrosine phosphorylation of target proteins by Fyn serves to either regulate target protein activity, and/or to generate a binding site on the target protein that recruits other signaling molecules. FYN has been shown to interact with a number of proteins including: BCAR1, Cbl, Janus kinase, nephrin, Sky, tyrosine kinase, Wiskott-Aldrich syndrome protein, and Zap-70. Fyn has a unique N-terminal domain, an SH3 domain, an SH2 domain, a kinase domain and a regulatory tail, as do the other members of the family. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198281  Cd Length: 101  Bit Score: 61.17  E-value: 1.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719  74 ESEPWFFGCISRSEAMHRLQSEDYPKGTFLIRVSQKPGADYVLSV--WDAEA---VRHYRIWRNSAGRLHLNEVVSFSSL 148
Cdd:cd10418    1 QAEEWYFGKLGRKDAERQLLSFGNPRGTFLIRESETTKGAYSLSIrdWDDMKgdhVKHYKIRKLDNGGYYITTRAQFETL 80

                 ....*..
gi 157822719 149 SELVNYH 155
Cdd:cd10418   81 QQLVQHY 87
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
197-380 1.59e-11

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: 64.78  E-value: 1.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFegLWKGL---VRVAVKVISRDNLLHQHTFQA---EIQAMKKLRHKHILS-------LYAVATAGDPVyII 263
Cdd:cd13989    1 LGSGGFGYVT--LWKHQdtgEYVAIKKCRQELSPSDKNRERwclEVQIMKKLNHPNVVSardvppeLEKLSPNDLPL-LA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 264 TELMPKGSLLQLLRDSDE----KDLPILELVdfaSQVAEGMCYLESQNYIHRDLAARNVLVTENN---LCKVGDFGLAR- 335
Cdd:cd13989   78 MEYCSGGDLRKVLNQPENccglKESEVRTLL---SDISSAISYLHENRIIHRDLKPENIVLQQGGgrvIYKLIDLGYAKe 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 157822719 336 LVKEDIYLSRDHNVPYkwTAPEALSRGHYSIKSDVWSFGVLLHEI 380
Cdd:cd13989  155 LDQGSLCTSFVGTLQY--LAPELFESKKYTCTVDYWSFGTLAFEC 197
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
215-390 1.60e-11

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: 65.19  E-value: 1.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 215 RVAVKVISR--DNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDP-----VYIITELMpKGSLLQLLRDSDekDLPIL 287
Cdd:cd07859   27 KVAIKKINDvfEHVSDATRILREIKLLRLLRHPDIVEIKHIMLPPSRrefkdIYVVFELM-ESDLHQVIKAND--DLTPE 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 288 ELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKED----IYLSrDHnVPYKW-TAPEALSR- 361
Cdd:cd07859  104 HHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLARVAFNDtptaIFWT-DY-VATRWyRAPELCGSf 181
                        170       180       190
                 ....*....|....*....|....*....|
gi 157822719 362 -GHYSIKSDVWSFGVLLHEIFsRGQMPYPG 390
Cdd:cd07859  182 fSKYTPAIDIWSIGCIFAEVL-TGKPLFPG 210
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
191-400 1.60e-11

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: 64.61  E-value: 1.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEGLWKGLVR-VAVKVISRdNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMPK 269
Cdd:cd14113    9 YSEVAELGRGRFSVVKKCDQRGTKRaVATKFVNK-KLMKRDQVTHELGVLQSLQHPQLVGLLDTFETPTSYILVLEMADQ 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 270 GSLLQLLRD----SDEKdlpileLVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENN---LCKVGDFGLARLVKEDIY 342
Cdd:cd14113   88 GRLLDYVVRwgnlTEEK------IRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLskpTIKLADFGDAVQLNTTYY 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 157822719 343 LSRDHNVPyKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETFLRV 400
Cdd:cd14113  162 IHQLLGSP-EFAAPEIILGNPVSLTSDLWSIGVLTYVLLS-GVSPFLDESVEETCLNI 217
pknD PRK13184
serine/threonine-protein kinase PknD;
189-431 1.71e-11

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 66.33  E-value: 1.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFEGLWKGLVR-VAVKVISRD---NLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIIT 264
Cdd:PRK13184   2 QRYDIIRLIGKGGMGEVYLAYDPVCSRrVALKKIREDlseNPLLKKRFLREAKIAADLIHPGIVPVYSICSDGDPVYYTM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 265 ELMPKGSLLQLLR-----DSDEKDLPILELVD-FAS---QVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLAR 335
Cdd:PRK13184  82 PYIEGYTLKSLLKsvwqkESLSKELAEKTSVGaFLSifhKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAAI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 336 LVK--EDIYLSRDHNVPYK----------------WTAPEALsRGH-YSIKSDVWSFGVLLHEIFSRgQMPY-----PGM 391
Cdd:PRK13184 162 FKKleEEDLLDIDVDERNIcyssmtipgkivgtpdYMAPERL-LGVpASESTDIYALGVILYQMLTL-SFPYrrkkgRKI 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 157822719 392 SNHETFLRVD--AGYRmpcplECPPNIHKLMLSCWSRDPKQR 431
Cdd:PRK13184 240 SYRDVILSPIevAPYR-----EIPPFLSQIAMKALAVDPAER 276
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
195-436 1.75e-11

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: 64.98  E-value: 1.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWKGLVRV-AVKVISRDNLLHQHTfQAEIQA-----MKKLRHKHILSLYAVATAGDPVYIITELMP 268
Cdd:cd05604    2 KVIGKGSFGKVLLAKRKRDGKYyAVKVLQKKVILNRKE-QKHIMAernvlLKNVKHPFLVGLHYSFQTTDKLYFVLDFVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 269 KGSLLQLLRDsdEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLArlvKEDIYLSrDHN 348
Cdd:cd05604   81 GGELFFHLQR--ERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLC---KEGISNS-DTT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 349 VPY----KWTAPEALSRGHYSIKSDVWSFGVLLHEIFsRGQMPYPGMSNHETFLRVdagyrMPCPLECPPNIHklmLSCW 424
Cdd:cd05604  155 TTFcgtpEYLAPEVIRKQPYDNTVDWWCLGSVLYEML-YGLPPFYCRDTAEMYENI-----LHKPLVLRPGIS---LTAW 225
                        250
                 ....*....|....*....
gi 157822719 425 S-------RDPKQRPCFKD 436
Cdd:cd05604  226 SileelleKDRQLRLGAKE 244
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
12-66 1.82e-11

Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction domains that bind proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. Thus, they are referred to as proline-recognition domains (PRDs). SH3 domains are less selective and show more diverse specificity compared to other PRDs. They have been shown to bind peptide sequences that lack the PxxP motif; examples include the PxxDY motif of Eps8 and the RKxxYxxY sequence in SKAP55. SH3 domain containing proteins play versatile and diverse roles in the cell, including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies, among others. Many members of this superfamily are adaptor proteins that associate with a number of protein partners, facilitating complex formation and signal transduction.


Pssm-ID: 212690 [Multi-domain]  Cd Length: 51  Bit Score: 59.01  E-value: 1.82e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 157822719  12 KYVGLWDFKARTDEELSFQAGDLLHVTRKEEQ-WWWATLLDAEgkalaEGYVPHNY 66
Cdd:cd00174    1 YARALYDYEAQDDDELSFKKGDIITVLEKDDDgWWEGELNGGR-----EGLFPANY 51
SH2_csk_like cd09937
Src homology 2 (SH2) domain found in Carboxyl-Terminal Src Kinase (Csk); Both the C-terminal ...
77-156 2.05e-11

Src homology 2 (SH2) domain found in Carboxyl-Terminal Src Kinase (Csk); Both the C-terminal Src kinase (CSK) and CSK-homologous kinase (CHK) are members of the CSK-family of protein tyrosine kinases. These proteins suppress activity of Src-family kinases (SFK) by selectively phosphorylating the conserved C-terminal tail regulatory tyrosine by a similar mechanism. CHK is also capable of inhibiting SFKs by a non-catalytic mechanism that involves binding of CHK to SFKs to form stable protein complexes. The unphosphorylated form of SFKs is inhibited by CSK and CHK by a two-step mechanism. The first step involves the formation of a complex of SFKs with CSK/CHK with the SFKs in the complex are inactive. The second step, involves the phosphorylation of the C-terminal tail tyrosine of SFKs, which then dissociates and adopt an inactive conformation. The structural basis of how the phosphorylated SFKs dissociate from CSK/CHK to adopt the inactive conformation is not known. The inactive conformation of SFKs is stabilized by two intramolecular inhibitory interactions: (a) the pYT:SH2 interaction in which the phosphorylated C-terminal tail tyrosine (YT) binds to the SH2 domain, and (b) the linker:SH3 interaction of which the SH2-kinase domain linker binds to the SH3 domain. SFKs are activated by multiple mechanisms including binding of the ligands to the SH2 and SH3 domains to displace the two inhibitory intramolecular interactions, autophosphorylation, and dephosphorylation of YT. By selective phosphorylation and the non-catalytic inhibitory mechanism CSK and CHK are able to inhibit the active forms of SFKs. CSK and CHK are regulated by phosphorylation and inter-domain interactions. They both contain SH3, SH2, and kinase domains separated by the SH3-SH2 connector and SH2 kinase linker, intervening segments separating the three domains. They lack a conserved tyrosine phosphorylation site in the kinase domain and the C-terminal tail regulatory tyrosine phosphorylation site. The CSK SH2 domain is crucial for stabilizing the kinase domain in the active conformation. A disulfide bond here regulates CSK kinase activity. The subcellular localization and activity of CSK are regulated by its SH2 domain. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198190  Cd Length: 98  Bit Score: 60.38  E-value: 2.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719  77 PWFFGCISRSEAMHRLQ-SEDypkGTFLIRVSQK-PGaDYVLSVWDAEAVRHYRIWRNSaGRLHLNEVVSFSSLSELVNY 154
Cdd:cd09937    4 PWFHGKISREEAERLLQpPED---GLFLVRESTNyPG-DYTLCVSFEGKVEHYRVIYRN-GKLTIDEEEYFENLIQLVEH 78

                 ..
gi 157822719 155 HK 156
Cdd:cd09937   79 YT 80
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
195-409 2.14e-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: 63.85  E-value: 2.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWKGL-VRVAVKVIsRDNL-------LHqhtfqaeiqaMKKLRHKH---ILSLYAVATAGDPVY-I 262
Cdd:cd14089    7 QVLGLGINGKVLECFHKKTgEKFALKVL-RDNPkarreveLH----------WRASGCPHivrIIDVYENTYQGRKCLlV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 263 ITELMPKGSLLQllRDSDEKDLPILE--LVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENN---LCKVGDFGLARLV 337
Cdd:cd14089   76 VMECMEGGELFS--RIQERADSAFTEreAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGpnaILKLTDFGFAKET 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 338 KEDIYLSRDHNVPYkWTAPEALSRGHYSIKSDVWSFGVLLHEI-------FSRGQMPY-PGMSNhetflRVDAG-YRMPC 408
Cdd:cd14089  154 TTKKSLQTPCYTPY-YVAPEVLGPEKYDKSCDMWSLGVIMYILlcgyppfYSNHGLAIsPGMKK-----RIRNGqYEFPN 227

                 .
gi 157822719 409 P 409
Cdd:cd14089  228 P 228
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
197-437 2.23e-11

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 isoforms resulting from alternative translation initiation sites. PIM1 is the founding member of the PIM subfamily. It is involved in regulating cell growth, differentiation, and apoptosis. It promotes cancer development when overexpressed by inhibiting apoptosis, promoting cell proliferation, and promoting genomic instability. The PIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 63.84  E-value: 2.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGL-WKGLVRVAVKVISRD------NLLHQHTFQAEIQAMKKLRH--KHILSLYAVATAGDPVYIITElm 267
Cdd:cd14100    8 LGSGGFGSVYSGIrVADGAPVAIKHVEKDrvsewgELPNGTRVPMEIVLLKKVGSgfRGVIRLLDWFERPDSFVLVLE-- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 268 pKGSLLQLLRD--SDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENN-LCKVGDFGLARLVKEDIYLS 344
Cdd:cd14100   86 -RPEPVQDLFDfiTERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDLNTgELKLIDFGSGALLKDTVYTD 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 345 RDHNVPYkwTAPEALSRGHYSIKS-DVWSFGVLLHEIFSrGQMPYpgmSNHETFLRVDAGYRMPCPLECppniHKLMLSC 423
Cdd:cd14100  165 FDGTRVY--SPPEWIRFHRYHGRSaAVWSLGILLYDMVC-GDIPF---EHDEEIIRGQVFFRQRVSSEC----QHLIKWC 234
                        250
                 ....*....|....
gi 157822719 424 WSRDPKQRPCFKDL 437
Cdd:cd14100  235 LALRPSDRPSFEDI 248
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
190-431 2.67e-11

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: 64.72  E-value: 2.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLCKKLGSGYFGEVFeglwkgLVR-------VAVKVISRDNLLHQ----HTFqAEIQAMKKLRHKHILSLYAVATAGD 258
Cdd:cd05593   16 DFDYLKLLGKGTFGKVI------LVRekasgkyYAMKILKKEVIIAKdevaHTL-TESRVLKNTRHPFLTSLKYSFQTKD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 259 PVYIITELMPKGSLLQLLrdSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVK 338
Cdd:cd05593   89 RLCFVMEYVNGGELFFHL--SRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGI 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 339 EDIYLSRDHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGmSNHETFLRVDAGYRMPCPLECPPNIHK 418
Cdd:cd05593  167 TDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYN-QDHEKLFELILMEDIKFPRTLSADAKS 244
                        250
                 ....*....|...
gi 157822719 419 LMLSCWSRDPKQR 431
Cdd:cd05593  245 LLSGLLIKDPNKR 257
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
235-388 2.89e-11

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: 63.89  E-value: 2.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 235 EIQAMKKLRHKHILSL-YAVATAgDPVYIITELMPKGSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDL 313
Cdd:cd05630   50 EKQILEKVNSRFVVSLaYAYETK-DALCLVLTLMNGGDLKFHIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDL 128
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157822719 314 AARNVLVTENNLCKVGDFGLARLVKEDIYLS-RDHNVPYkwTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPY 388
Cdd:cd05630  129 KPENILLDDHGHIRISDLGLAVHVPEGQTIKgRVGTVGY--MAPEVVKNERYTFSPDWWALGCLLYEMIA-GQSPF 201
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
189-388 3.05e-11

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


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 63.51  E-value: 3.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFEGLWK--GLVRVAVKVISRDNLLHQHTFQAEIQAMKKLRHKHILSLYAVATAGDPVYIITEL 266
Cdd:cd14088    1 DRYDLGQVIKTEEFCEIFRAKDKttGKLYTCKKFLKRDGRKVRKAAKNEINILKMVKHPNILQLVDVFETRKEYFIFLEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 267 MPKGSLLQLLRDS---DEKDLPilelvDFASQVAEGMCYLESQNYIHRDLAARNVLV---TENNLCKVGDFGLARLvkED 340
Cdd:cd14088   81 ATGREVFDWILDQgyySERDTS-----NVIRQVLEAVAYLHSLKIVHRNLKLENLVYynrLKNSKIVISDFHLAKL--EN 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 157822719 341 IYLSRDHNVPyKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPY 388
Cdd:cd14088  154 GLIKEPCGTP-EYLAPEVVGRQRYGRPVDCWAIGVIMYILLS-GNPPF 199
SH2_Nterm_shark_like cd10347
N-terminal Src homology 2 (SH2) domain found in SH2 domains, ANK, and kinase domain (shark) ...
78-155 3.24e-11

N-terminal Src homology 2 (SH2) domain found in SH2 domains, ANK, and kinase domain (shark) proteins; These non-receptor protein-tyrosine kinases contain two SH2 domains, five ankyrin (ANK)-like repeats, and a potential tyrosine phosphorylation site in the carboxyl-terminal tail which resembles the phosphorylation site in members of the src family. Like, mammalian non-receptor protein-tyrosine kinases, ZAP-70 and syk proteins, they do not have SH3 domains. However, the presence of ANK makes these unique among protein-tyrosine kinases. Both tyrosine kinases and ANK repeats have been shown to transduce developmental signals, and SH2 domains are known to participate intimately in tyrosine kinase signaling. These tyrosine kinases are believed to be involved in epithelial cell polarity. The members of this family include the shark (SH2 domains, ANK, and kinase domain) gene in Drosophila and yellow fever mosquitos, as well as the hydra protein HTK16. Drosophila Shark is proposed to transduce intracellularly the Crumbs, a protein necessary for proper organization of ectodermal epithelia, intercellular signal. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198210  Cd Length: 81  Bit Score: 58.93  E-value: 3.24e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157822719  78 WFFGCISRSEAMHRLQSEDYPKGTFLIRVSQKPGADYVLSVWDAEAVRHYRIWRNSAGRLHL-NEVVSFSSLSELVNYH 155
Cdd:cd10347    3 WYHGKISREVAEALLLREGGRDGLFLVRESTSAPGDYVLSLLAQGEVLHYQIRRHGEDAFFSdDGPLIFHGLDTLIEHY 81
SH2_Src_Fyn cd10368
Src homology 2 (SH2) domain found in Fyn; Fyn is a member of the Src non-receptor type ...
74-155 3.28e-11

Src homology 2 (SH2) domain found in Fyn; Fyn is a member of the Src non-receptor type tyrosine kinase family of proteins. Fyn is involved in the control of cell growth and is required in the following pathways: T and B cell receptor signaling, integrin-mediated signaling, growth factor and cytokine receptor signaling, platelet activation, ion channel function, cell adhesion, axon guidance, fertilization, entry into mitosis, and differentiation of natural killer cells, oligodendrocytes and keratinocytes. The protein associates with the p85 subunit of phosphatidylinositol 3-kinase and interacts with the Fyn-binding protein. Alternatively spliced transcript variants encoding distinct isoforms exist. Fyn is primarily localized to the cytoplasmic leaflet of the plasma membrane. Tyrosine phosphorylation of target proteins by Fyn serves to either regulate target protein activity, and/or to generate a binding site on the target protein that recruits other signaling molecules. FYN has been shown to interact with a number of proteins including: BCAR1, Cbl, Janus kinase, nephrin, Sky, tyrosine kinase, Wiskott-Aldrich syndrome protein, and Zap-70. Fyn has a unique N-terminal domain, an SH3 domain, an SH2 domain, a kinase domain and a regulatory tail, as do the other members of the family. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198231 [Multi-domain]  Cd Length: 101  Bit Score: 59.66  E-value: 3.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719  74 ESEPWFFGCISRSEAMHRLQSEDYPKGTFLIRVSQKPGADYVLSV--WD---AEAVRHYRIWRNSAGRLHLNEVVSFSSL 148
Cdd:cd10368    1 QAEEWYFGKLGRKDAERQLLSFGNPRGTFLIRESETTKGAYSLSIrdWDdmkGDHVKHYKIRKLDNGGYYITTRAQFETL 80

                 ....*..
gi 157822719 149 SELVNYH 155
Cdd:cd10368   81 QQLVQHY 87
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
235-434 3.30e-11

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


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 63.30  E-value: 3.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 235 EIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSLLQLLRDS---DEKDLpilelVDFASQVAEGMCYLESQNYIHR 311
Cdd:cd14111   49 EYEILKSLHHERIMALHEAYITPRYLVLIAEFCSGKELLHSLIDRfrySEDDV-----VGYLVQILQGLEYLHGRRVLHL 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 312 DLAARNVLVTENNLCKVGDFGLARLVKEDIYLSRDHNV-PYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPG 390
Cdd:cd14111  124 DIKPDNIMVTNLNAIKIVDFGSAQSFNPLSLRQLGRRTgTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLS-GRSPFED 202
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 157822719 391 MSNHETFLRVDAGYRMPCPLEcpPNIH-------KLMLSC--WSRdPKQRPCF 434
Cdd:cd14111  203 QDPQETEAKILVAKFDAFKLY--PNVSqsaslflKKVLSSypWSR-PTTKDCF 252
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
187-439 3.45e-11

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: 63.86  E-value: 3.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 187 PREEFTLCKKLGSGYFGEVFEGLWK-GLVRVAVKVISRDNLLHQHtFQAEIQAMKKL-RHKHILSLYAV-----ATAGDP 259
Cdd:cd06639   20 PSDTWDIIETIGKGTYGKVYKVTNKkDGSLAAVKILDPISDVDEE-IEAEYNILRSLpNHPNVVKFYGMfykadQYVGGQ 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 260 VYIITELMPKGSLLQL----LRDSDEKDLPILELVDFASQVaeGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGL-A 334
Cdd:cd06639   99 LWLVLELCNGGSVTELvkglLKCGQRLDEAMISYILYGALL--GLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVsA 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 335 RLVKEDIYLSRDHNVPYkWTAPEALS-----RGHYSIKSDVWSFGVLLHEIfSRGQMPYPGMSNHETFLRVDagyRMPCP 409
Cdd:cd06639  177 QLTSARLRRNTSVGTPF-WMAPEVIAceqqyDYSYDARCDVWSLGITAIEL-ADGDPPLFDMHPVKALFKIP---RNPPP 251
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 157822719 410 LECPP-----NIHKLMLSCWSRDPKQRPCFKDLCE 439
Cdd:cd06639  252 TLLNPekwcrGFSHFISQCLIKDFEKRPSVTHLLE 286
SH3_ASPP1 cd11954
Src Homology 3 domain of Apoptosis Stimulating of p53 protein 1; ASPP1, like ASPP2, activates ...
16-67 4.31e-11

Src Homology 3 domain of Apoptosis Stimulating of p53 protein 1; ASPP1, like ASPP2, activates the apoptotic function of the p53 family of tumor suppressors (p53, p63, and p73). In addition, it functions in the cytoplasm to regulate the nuclear localization of the transcriptional cofactors YAP and TAZ by inihibiting their phosphorylation; YAP and TAZ are important regulators of cell expansion, differentiation, migration, and invasion. ASPP1 is downregulated in breast tumors expressing wild-type p53. It contains a proline-rich region, four ankyrin (ANK) repeats, and an SH3 domain at its C-terminal half. The SH3 domain and the ANK repeats of ASPP1 contribute to the p53 binding site; they bind to the DNA binding domain of p53. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212887 [Multi-domain]  Cd Length: 57  Bit Score: 58.11  E-value: 4.31e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 157822719  16 LWDFKARTDEELSFQAGDLLHVTRK----EEQWWWATLLDaegkalAEGYVPHNYL 67
Cdd:cd11954    6 LWDYEAQNADELSFQEGDAITILRRkddsETEWWWARLND------KEGYVPKNLL 55
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
197-439 4.97e-11

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: 62.83  E-value: 4.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEV-----FEG----LWK--GLVRVAVKVisRDNLLHqhtfqaEIQAMKKLRHKHILSLYAVATAGDPVYIITE 265
Cdd:cd08221    8 LGRGAFGEAvlyrkTEDnslvVWKevNLSRLSEKE--RRDALN------EIDILSLLNHDNIITYYNHFLDGESLFIEME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMPKGSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSR 345
Cdd:cd08221   80 YCNGGNLHDKIAQQKNQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLDSESSMAE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 346 DH-NVPYkWTAPEALSRGHYSIKSDVWSFGVLLHEIFSRGQmpypgmsnheTF-----LR-----VDAGYRMPCPlECPP 414
Cdd:cd08221  160 SIvGTPY-YMSPELVQGVKYNFKSDIWAVGCVLYELLTLKR----------TFdatnpLRlavkiVQGEYEDIDE-QYSE 227
                        250       260
                 ....*....|....*....|....*
gi 157822719 415 NIHKLMLSCWSRDPKQRPCFKDLCE 439
Cdd:cd08221  228 EIIQLVHDCLHQDPEDRPTAEELLE 252
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
189-400 5.76e-11

Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CdkB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 63.32  E-value: 5.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFEGLWKGLVR-VAVKV--ISRDNLLHQHTFQAEIQAMKKLRHK-HILSLYAVATA---GDP-V 260
Cdd:cd07837    1 DAYEKLEKIGEGTYGKVYKARDKNTGKlVALKKtrLEMEEEGVPSTALREVSLLQMLSQSiYIVRLLDVEHVeenGKPlL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 261 YIITELMPKG--SLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLV-TENNLCKVGDFGLARLV 337
Cdd:cd07837   81 YLVFEYLDTDlkKFIDSYGRGPHNPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVdKQKGLLKIADLGLGRAF 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157822719 338 KEDIYlSRDHNVPYKW-TAPEALSRG-HYSIKSDVWSFGVLLHEIfSRGQMPYPGMSNHETFLRV 400
Cdd:cd07837  161 TIPIK-SYTHEIVTLWyRAPEVLLGStHYSTPVDMWSVGCIFAEM-SRKQPLFPGDSELQQLLHI 223
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
195-397 6.00e-11

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: 63.39  E-value: 6.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWKGLVRV-AVKVISRDNLLHQHtfQAEIQAMKK------LRHKHILSLYAVATAGDPVYIITELM 267
Cdd:cd05570    1 KVLGKGSFGKVMLAERKKTDELyAIKVLKKEVIIEDD--DVECTMTEKrvlalaNRHPFLTGLHACFQTEDRLYFVMEYV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 268 PKGSLL---QLLRDSDEKdlpilELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLArlvKEDIYLS 344
Cdd:cd05570   79 NGGDLMfhiQRARRFTEE-----RARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMC---KEGIWGG 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 157822719 345 RDHN----VPyKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETF 397
Cdd:cd05570  151 NTTStfcgTP-DYIAPEILREQDYGFSVDWWALGVLLYEMLA-GQSPFEGDDEDELF 205
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
191-437 6.64e-11

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


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 62.25  E-value: 6.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEG--LWKGLvRVAVKVISRDNLLH------QHTFQAEIQAMKK---LRHKHILSLYAVATAGDP 259
Cdd:cd14005    2 YEVGDLLGKGGFGTVYSGvrIRDGL-PVAVKFVPKSRVTEwamingPVPVPLEIALLLKaskPGVPGVIRLLDWYERPDG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 260 VYIITElMPKGS--LLQLLRDSDekDLPILELVDFASQVAEG--MCYleSQNYIHRDLAARNVLVTENNLC-KVGDFGLA 334
Cdd:cd14005   81 FLLIME-RPEPCqdLFDFITERG--ALSENLARIIFRQVVEAvrHCH--QRGVLHRDIKDENLLINLRTGEvKLIDFGCG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 335 RLVKEDIYLSRDHNVPYkwTAPEALSRGHYSIKS-DVWSFGVLLHEIFSrGQMPYpgmsnHETFLRVDAGYRMPCPL--E 411
Cdd:cd14005  156 ALLKDSVYTDFDGTRVY--SPPEWIRHGRYHGRPaTVWSLGILLYDMLC-GDIPF-----ENDEQILRGNVLFRPRLskE 227
                        250       260
                 ....*....|....*....|....*.
gi 157822719 412 CppniHKLMLSCWSRDPKQRPCFKDL 437
Cdd:cd14005  228 C----CDLISRCLQFDPSKRPSLEQI 249
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
284-389 7.13e-11

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 63.36  E-value: 7.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 284 LPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARL-VKEDIYLSRDHNVpyKWTAPEALSRG 362
Cdd:PHA03209 154 LPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLGAAQFpVVAPAFLGLAGTV--ETNAPEVLARD 231
                         90       100
                 ....*....|....*....|....*..
gi 157822719 363 HYSIKSDVWSFGVLLHEIFSrgqmpYP 389
Cdd:PHA03209 232 KYNSKADIWSAGIVLFEMLA-----YP 253
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
191-388 9.30e-11

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: 62.61  E-value: 9.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEGLWKGLVRV-AVKVISRDNLLHQHTFQA---EIQAMKKLRHKHILSL-YAVATAGDPVYIITe 265
Cdd:cd05607    4 FYEFRVLGKGGFGEVCAVQVKNTGQMyACKKLDKKRLKKKSGEKMallEKEILEKVNSPFIVSLaYAFETKTHLCLVMS- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 266 LMPKGSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLSR 345
Cdd:cd05607   83 LMNGGDLKYHIYNVGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEVKEGKPITQ 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 157822719 346 DHNVPyKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPY 388
Cdd:cd05607  163 RAGTN-GYMAPEILKEESYSYPVDWFAMGCSIYEMVA-GRTPF 203
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
197-437 1.03e-10

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3). PIM3 can inhibit apoptosis and promote cell survival and protein translation, therefore, it can enhance the proliferation of normal and cancer cells. Mice deficient with PIM3 show minimal effects, suggesting that PIM3 msy not be essential. Since its expression is enhanced in several cancers, it may make a good molecular target for cancer drugs. The PIM3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 61.89  E-value: 1.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEG--LWKGLVrVAVKVISRDNLLHQHTFQAEIQAMKklrhkhILSLYAVATAGDPVYIITELM--PKGSL 272
Cdd:cd14102    8 LGSGGFGTVYAGsrIADGLP-VAVKHVVKERVTEWGTLNGVMVPLE------IVLLKKVGSGFRGVIKLLDWYerPDGFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 273 LQLLRDSDEKDL--------PILELV--DFASQVAEGMCYLESQNYIHRDLAARNVLV-TENNLCKVGDFGLARLVKEDI 341
Cdd:cd14102   81 IVMERPEPVKDLfdfitekgALDEDTarGFFRQVLEAVRHCYSCGVVHRDIKDENLLVdLRTGELKLIDFGSGALLKDTV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 342 YLSRDHNVPYkwTAPEALSRGHYSIKS-DVWSFGVLLHEIFSrGQMPYpgmSNHETFLRVDAGYRMPCPLECppniHKLM 420
Cdd:cd14102  161 YTDFDGTRVY--SPPEWIRYHRYHGRSaTVWSLGVLLYDMVC-GDIPF---EQDEEILRGRLYFRRRVSPEC----QQLI 230
                        250
                 ....*....|....*..
gi 157822719 421 LSCWSRDPKQRPCFKDL 437
Cdd:cd14102  231 KWCLSLRPSDRPTLEQI 247
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
191-431 1.08e-10

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: 61.93  E-value: 1.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGeVFEGLWKGLVR--VAVKVISRDNLLHQHTfQAEIQAMKKLRHKHILSLYAVATAGDPVYIITELMP 268
Cdd:cd14665    2 YELVKDIGSGNFG-VARLMRDKQTKelVAVKYIERGEKIDENV-QREIINHRSLRHPNIVRFKEVILTPTHLAIVMEYAA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 269 KGSLLQLL----RDSDEkdlpilELVDFASQVAEGMCYLESQNYIHRDLAARNVLV--TENNLCKVGDFGLARlvkediy 342
Cdd:cd14665   80 GGELFERIcnagRFSED------EARFFFQQLISGVSYCHSMQICHRDLKLENTLLdgSPAPRLKICDFGYSK------- 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 343 LSRDHNVPYK------WTAPEALSRGHYSIK-SDVWSFGVLLHeIFSRGQMPYPGMSNHETFLR-----VDAGYRMPCPL 410
Cdd:cd14665  147 SSVLHSQPKStvgtpaYIAPEVLLKKEYDGKiADVWSCGVTLY-VMLVGAYPFEDPEEPRNFRKtiqriLSVQYSIPDYV 225
                        250       260
                 ....*....|....*....|.
gi 157822719 411 ECPPNIHKLMLSCWSRDPKQR 431
Cdd:cd14665  226 HISPECRHLISRIFVADPATR 246
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
195-396 1.11e-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: 62.42  E-value: 1.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFE-----GLWKGLVrVAVKV-----ISRDNLLHQHTfQAEIQAMKKLRHKHILSL-YAVATAGDpVYII 263
Cdd:cd05584    2 KVLGKGGYGKVFQvrkttGSDKGKI-FAMKVlkkasIVRNQKDTAHT-KAERNILEAVKHPFIVDLhYAFQTGGK-LYLI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 264 TELMPKGSLLQLLrdsdEKDLPILElvDFAS----QVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLArlvKE 339
Cdd:cd05584   79 LEYLSGGELFMHL----EREGIFME--DTACfylaEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLC---KE 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157822719 340 DIylSRDHNV-----PYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHET 396
Cdd:cd05584  150 SI--HDGTVThtfcgTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLT-GAPPFTAENRKKT 208
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
189-432 1.15e-10

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: 62.05  E-value: 1.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFEGLWK--GLVrVAVKVI------SRDnllHQhTFQAEIQAMKKLRHKHILSLYAVATAGDPV 260
Cdd:cd14086    1 DEYDLKEELGKGAFSVVRRCVQKstGQE-FAAKIIntkklsARD---HQ-KLEREARICRLLKHPNIVRLHDSISEEGFH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 261 YIITELMPKGSLLQ--LLRD-SDEKDlpilelvdfAS----QVAEGMCYLESQNYIHRDLAARNVLV---TENNLCKVGD 330
Cdd:cd14086   76 YLVFDLVTGGELFEdiVAREfYSEAD---------AShciqQILESVNHCHQNGIVHRDLKPENLLLaskSKGAAVKLAD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 331 FGLARLVKEDIYLSRDHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHeIFSRGQMPYPGMSNHETFLRVDAG-YRMPCP 409
Cdd:cd14086  147 FGLAIEVQGDQQAWFGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILY-ILLVGYPPFWDEDQHRLYAQIKAGaYDYPSP 225
                        250       260
                 ....*....|....*....|....*
gi 157822719 410 L--ECPPNIHKLMLSCWSRDPKQRP 432
Cdd:cd14086  226 EwdTVTPEAKDLINQMLTVNPAKRI 250
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
191-399 1.21e-10

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: 61.95  E-value: 1.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEGL-WKGLVRVAVKV--ISRDnlLHQHTFQA-------EIQAMKKLRHKHILSLYAVATAG-DP 259
Cdd:cd13990    2 YLLLNLLGKGGFSEVYKAFdLVEQRYVACKIhqLNKD--WSEEKKQNyikhalrEYEIHKSLDHPRIVKLYDVFEIDtDS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 260 VYIITELMPKGSLLQLLRDSdeKDLPILELVDFASQVAEGMCYLE--SQNYIHRDLAARNVLVTENNLC---KVGDFGLA 334
Cdd:cd13990   80 FCTVLEYCDGNDLDFYLKQH--KSIPEREARSIIMQVVSALKYLNeiKPPIIHYDLKPGNILLHSGNVSgeiKITDFGLS 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157822719 335 RLVKEDIY------LSRDHNVPYKWTAPEALSRG----HYSIKSDVWSFGVLLHEIFsRGQMPYPGMSNHETFLR 399
Cdd:cd13990  158 KIMDDESYnsdgmeLTSQGAGTYWYLPPECFVVGktppKISSKVDVWSVGVIFYQML-YGRKPFGHNQSQEAILE 231
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
183-400 1.28e-10

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: 63.11  E-value: 1.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 183 DWERP-----------REEFTLCKKLGSGYFGEVFEGLWKGLVRV-AVKVISRDNLLHQHT---FQAEIQAMKKLRHKHI 247
Cdd:cd05623   55 EWAKPftskvkqmrlhKEDFEILKVIGRGAFGEVAVVKLKNADKVfAMKILNKWEMLKRAEtacFREERDVLVNGDSQWI 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 248 LSLYAVATAGDPVYIITELMPKGSLLQLLRDSDEKdLPiLELVDFasQVAEGMCYLES---QNYIHRDLAARNVLVTENN 324
Cdd:cd05623  135 TTLHYAFQDDNNLYLVMDYYVGGDLLTLLSKFEDR-LP-EDMARF--YLAEMVLAIDSvhqLHYVHRDIKPDNILMDMNG 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 325 LCKVGDFGLARLVKED--IYLSRDHNVPyKWTAPEALS-----RGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETF 397
Cdd:cd05623  211 HIRLADFGSCLKLMEDgtVQSSVAVGTP-DYISPEILQamedgKGKYGPECDWWSLGVCMYEMLY-GETPFYAESLVETY 288

                 ...
gi 157822719 398 LRV 400
Cdd:cd05623  289 GKI 291
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
189-388 1.39e-10

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: 62.72  E-value: 1.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFEGLWKGLVRV-AVKVISRDNLLHQHT---FQAEIQAMKKLRHKHILSLYAVATAGDPVYIIT 264
Cdd:cd05622   73 EDYEVVKVIGRGAFGEVQLVRHKSTRKVyAMKLLSKFEMIKRSDsafFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 265 ELMPKGSLLQLLRDSDekdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLS 344
Cdd:cd05622  153 EYMPGGDLVNLMSNYD---VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVR 229
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 157822719 345 RDHNVPY-KWTAPEALSR----GHYSIKSDVWSFGVLLHEIFSrGQMPY 388
Cdd:cd05622  230 CDTAVGTpDYISPEVLKSqggdGYYGRECDWWSVGVFLYEMLV-GDTPF 277
SH3_ASPP2 cd11953
Src Homology 3 (SH3) domain of Apoptosis Stimulating of p53 protein 2; ASPP2 is the full ...
16-67 1.46e-10

Src Homology 3 (SH3) domain of Apoptosis Stimulating of p53 protein 2; ASPP2 is the full length form of the previously-identified tumor supressor, p53-binding protein 2 (p53BP2). ASPP2 activates the apoptotic function of the p53 family of tumor suppressors (p53, p63, and p73). It plays a central role in regulating apoptosis and cell growth; ASPP2-deficient mice show postnatal death. Downregulated expression of ASPP2 is frequently found in breast tumors, lung cancer, and diffuse large B-cell lymphoma where it is correlated with a poor clinical outcome. ASPP2 contains a proline-rich region, four ankyrin (ANK) repeats, and an SH3 domain at its C-terminal half. The SH3 domain and the ANK repeats of ASPP2 contribute to the p53 binding site; they bind to the DNA binding domain of p53. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212886 [Multi-domain]  Cd Length: 57  Bit Score: 56.50  E-value: 1.46e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 157822719  16 LWDFKARTDEELSFQAGDLLHVTRKEE----QWWWATLLDaegkalAEGYVPHNYL 67
Cdd:cd11953    6 LWDYEGESDDELSFKEGDCMTILRREDedetEWWWARLND------KEGYVPRNLL 55
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
196-395 1.50e-10

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 61.63  E-value: 1.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 196 KLGSGYFGEVFEGLWKGLVR-VAVKVISrdnLLHQH--TFQA--EIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKg 270
Cdd:cd07844    7 KLGEGSYATVYKGRSKLTGQlVALKEIR---LEHEEgaPFTAirEASLLKDLKHANIVTLHDIIHTKKTLTLVFEYLDT- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 271 SLLQLLrDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARL--VKEDIYlsrDHN 348
Cdd:cd07844   83 DLKQYM-DDCGGGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLARAksVPSKTY---SNE 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 157822719 349 VPYKWTAPE--ALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHE 395
Cdd:cd07844  159 VVTLWYRPPdvLLGSTEYSTSLDMWGVGCIFYEMAT-GRPLFPGSTDVE 206
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
195-381 1.89e-10

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: 61.91  E-value: 1.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 195 KKLGSGYFGEVFEGLWKGLVRV-AVKVISRDNLLHQHTfQAEIQA-----MKKLRHKHILSLYAVATAGDPVYIITELMP 268
Cdd:cd05603    1 KVIGKGSFGKVLLAKRKCDGKFyAVKVLQKKTILKKKE-QNHIMAernvlLKNLKHPFLVGLHYSFQTSEKLYFVLDYVN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 269 KGSLLQLLRDSDEKDLPILELvdFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARL-VKEDIYLSRDH 347
Cdd:cd05603   80 GGELFFHLQRERCFLEPRARF--YAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEgMEPEETTSTFC 157
                        170       180       190
                 ....*....|....*....|....*....|....
gi 157822719 348 NVPyKWTAPEALSRGHYSIKSDVWSFGVLLHEIF 381
Cdd:cd05603  158 GTP-EYLAPEVLRKEPYDRTVDWWCLGAVLYEML 190
SH2_N-SH2_Zap70_Syk_like cd09938
N-terminal Src homology 2 (SH2) domain found in Zeta-chain-associated protein kinase 70 ...
77-157 2.03e-10

N-terminal Src homology 2 (SH2) domain found in Zeta-chain-associated protein kinase 70 (ZAP-70) and Spleen tyrosine kinase (Syk) proteins; ZAP-70 and Syk comprise a family of hematopoietic cell specific protein tyrosine kinases (PTKs) that are required for antigen and antibody receptor function. ZAP-70 is expressed in T and natural killer (NK) cells and Syk is expressed in B cells, mast cells, polymorphonuclear leukocytes, platelets, macrophages, and immature T cells. They are required for the proper development of T and B cells, immune receptors, and activating NK cells. They consist of two N-terminal Src homology 2 (SH2) domains and a C-terminal kinase domain separated from the SH2 domains by a linker or hinge region. Phosphorylation of both tyrosine residues within the Immunoreceptor Tyrosine-based Activation Motifs (ITAM; consensus sequence Yxx[LI]x(7,8)Yxx[LI]) by the Src-family PTKs is required for efficient interaction of ZAP-70 and Syk with the receptor subunits and for receptor function. ZAP-70 forms two phosphotyrosine binding pockets, one of which is shared by both SH2 domains. In Syk the two SH2 domains do not form such a phosphotyrosine-binding site. The SH2 domains here are believed to function independently. In addition, the two SH2 domains of Syk display flexibility in their relative orientation, allowing Syk to accommodate a greater variety of spacing sequences between the ITAM phosphotyrosines and singly phosphorylated non-classical ITAM ligands. This model contains the N-terminus SH2 domains of both Syk and Zap70. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198191  Cd Length: 104  Bit Score: 57.40  E-value: 2.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719  77 PWFFGCISRSEAMHRLQSEDYPKGTFLIRVSQKPGADYVLSVWDAEAVRHYRIWRNSAGRLHLNEVVSFSSLSELVNYHK 156
Cdd:cd09938    2 PFFYGSITREEAEEYLKLAGMSDGLFLLRQSLRSLGGYVLSVCHGRKFHHYTIERQLNGTYAIAGGKAHCGPAELCEYHS 81

                 .
gi 157822719 157 T 157
Cdd:cd09938   82 T 82
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
197-447 2.04e-10

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: 61.47  E-value: 2.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVF--------EGLWKGLVRVAVKVISRDNLLHqhtfqaEIQAMKKLRHKHILSLYAVA-----TAGDPVYII 263
Cdd:cd14039    1 LGTGGFGNVClyqnqetgEKIAIKSCRLELSVKNKDRWCH------EIQIMKKLNHPNVVKACDVPeemnfLVNDVPLLA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 264 TELMPKGSLLQLLRDSDE----KDLPILELVdfaSQVAEGMCYLESQNYIHRDLAARNVLVTENN---LCKVGDFGLARL 336
Cdd:cd14039   75 MEYCSGGDLRKLLNKPENccglKESQVLSLL---SDIGSGIQYLHENKIIHRDLKPENIVLQEINgkiVHKIIDLGYAKD 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 337 VKEDiYLSRDHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFsrgqmpypgmsnhetflrvdAGYRmpcplecpPNI 416
Cdd:cd14039  152 LDQG-SLCTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECI--------------------AGFR--------PFL 202
                        250       260       270
                 ....*....|....*....|....*....|..
gi 157822719 417 HKLMLSCWSRDPKQR-PCFKDLCEKLSGITRY 447
Cdd:cd14039  203 HNLQPFTWHEKIKKKdPKHIFAVEEMNGEVRF 234
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
197-397 2.09e-10

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: 61.64  E-value: 2.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 197 LGSGYFGEVFEGLWKGLVRV-AVKVISRDNLLHQHTFQAEIQAMKKL----RHKHILSLYAVATAGDPVYIITELMPKGS 271
Cdd:cd05587    4 LGKGSFGKVMLAERKGTDELyAIKILKKDVIIQDDDVECTMVEKRVLalsgKPPFLTQLHSCFQTMDRLYFVMEYVNGGD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 272 LLQLLRDSDEKDLPILelVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLArlvKEDIY---LSRDHN 348
Cdd:cd05587   84 LMYHIQQVGKFKEPVA--VFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMC---KEGIFggkTTRTFC 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 157822719 349 VPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGMSNHETF 397
Cdd:cd05587  159 GTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLA-GQPPFDGEDEDELF 206
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
235-400 2.49e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 62.40  E-value: 2.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 235 EIQAMKKLRHKHILSLYAVATAGDPVYIITELMpKGSLLQLLRDS--DEKDLPIL-ELVDFASQVAEGMCYLESQNYIHR 311
Cdd:PHA03210 213 EILALGRLNHENILKIEEILRSEANTYMITQKY-DFDLYSFMYDEafDWKDRPLLkQTRAIMKQLLCAVEYIHDKKLIHR 291
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 312 DLAARNVLVTENNLCKVGDFGLArLVKEDIYLSRDhnvpYKWT------APEALSRGHYSIKSDVWSFGVLLHEIFSRGQ 385
Cdd:PHA03210 292 DIKLENIFLNCDGKIVLGDFGTA-MPFEKEREAFD----YGWVgtvatnSPEILAGDGYCEITDIWSCGLILLDMLSHDF 366
                        170
                 ....*....|....*..
gi 157822719 386 MPYPGMSN--HETFLRV 400
Cdd:PHA03210 367 CPIGDGGGkpGKQLLKI 383
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
196-437 2.89e-10

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: 60.83  E-value: 2.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 196 KLGSGYFGEVFEGL-WKGLVRVAVKVISRDNLL--HQHTFQAEIQAMKKLRHKHILSLY----AVATAGDPVYIITELMP 268
Cdd:cd14030   32 EIGRGSFKTVYKGLdTETTVEVAWCELQDRKLSksERQRFKEEAGMLKGLQHPNIVRFYdsweSTVKGKKCIVLVTELMT 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 269 KGSLLQLLRDSDEKDLPILElvDFASQVAEGMCYLESQN--YIHRDLAARNVLVT-ENNLCKVGDFGLARLvKEDIYLSR 345
Cdd:cd14030  112 SGTLKTYLKRFKVMKIKVLR--SWCRQILKGLQFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLATL-KRASFAKS 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 346 DHNVPyKWTAPEALSRgHYSIKSDVWSFGVLLHEIfSRGQMPYPGMSN-HETFLRVDAGYRmPCPLE--CPPNIHKLMLS 422
Cdd:cd14030  189 VIGTP-EFMAPEMYEE-KYDESVDVYAFGMCMLEM-ATSEYPYSECQNaAQIYRRVTSGVK-PASFDkvAIPEVKEIIEG 264
                        250
                 ....*....|....*
gi 157822719 423 CWSRDPKQRPCFKDL 437
Cdd:cd14030  265 CIRQNKDERYAIKDL 279
SH2_Src_Lyn cd10364
Src homology 2 (SH2) domain found in Lyn; Lyn is a member of the Src non-receptor type ...
74-156 3.00e-10

Src homology 2 (SH2) domain found in Lyn; Lyn is a member of the Src non-receptor type tyrosine kinase family of proteins and is expressed in the hematopoietic cells, in neural tissues, liver, and adipose tissue. There are two alternatively spliced forms of Lyn. Lyn plays an inhibitory role in myeloid lineage proliferation. Following engagement of the B cell receptors, Lyn undergoes rapid phosphorylation and activation, triggering a cascade of signaling events mediated by Lyn phosphorylation of tyrosine residues within the immunoreceptor tyrosine-based activation motifs (ITAM) of the receptor proteins, and subsequent recruitment and activation of other kinases including Syk, phospholipase C2 (PLC2) and phosphatidyl inositol-3 kinase. These kinases play critical roles in proliferation, Ca2+ mobilization and cell differentiation. Lyn plays an essential role in the transmission of inhibitory signals through phosphorylation of tyrosine residues within the immunoreceptor tyrosine-based inhibitory motifs (ITIM) in regulatory proteins such as CD22, PIR-B and FC RIIb1. Their ITIM phosphorylation subsequently leads to recruitment and activation of phosphatases such as SHIP-1 and SHP-1 which further down modulate signaling pathways, attenuate cell activation and can mediate tolerance. Lyn also plays a role in the insulin signaling pathway. Activated Lyn phosphorylates insulin receptor substrate 1 (IRS1) leading to an increase in translocation of Glut-4 to the cell membrane and increased glucose utilization. It is the primary Src family member involved in signaling downstream of the B cell receptor. Lyn plays an unusual, 2-fold role in B cell receptor signaling; it is essential for initiation of signaling but is also later involved in negative regulation of the signal. Lyn has a unique N-terminal domain, an SH3 domain, an SH2 domain, a kinase domain and a regulatory tail, as do the other members of the family. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198227  Cd Length: 101  Bit Score: 56.92  E-value: 3.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719  74 ESEPWFFGCISRSEAMHRLQSEDYPKGTFLIRVSQKPGADYVLSVWDAEA-----VRHYRIWRNSAGRLHLNEVVSFSSL 148
Cdd:cd10364    1 ETEEWFFKDITRKDAERQLLAPGNSAGAFLIRESETLKGSYSLSVRDYDPqhgdvIKHYKIRSLDNGGYYISPRITFPCI 80

                 ....*....
gi 157822719 149 SELV-NYHK 156
Cdd:cd10364   81 SDMIkHYQK 89
SH2_C-SH2_Syk_like cd10401
C-terminal Src homology 2 (SH2) domain found in Spleen tyrosine kinase (Syk) proteins; ZAP-70 ...
74-155 3.07e-10

C-terminal Src homology 2 (SH2) domain found in Spleen tyrosine kinase (Syk) proteins; ZAP-70 and Syk comprise a family of hematopoietic cell specific protein tyrosine kinases (PTKs) that are required for antigen and antibody receptor function. ZAP-70 is expressed in T and natural killer (NK) cells and Syk is expressed in B cells, mast cells, polymorphonuclear leukocytes, platelets, macrophages, and immature T cells. They are required for the proper development of T and B cells, immune receptors, and activating NK cells. They consist of two N-terminal Src homology 2 (SH2) domains and a C-terminal kinase domain separated from the SH2 domains by a linker or hinge region. Phosphorylation of both tyrosine residues within the Immunoreceptor Tyrosine-based Activation Motifs (ITAM; consensus sequence Yxx[LI]x(7,8)Yxx[LI]) by the Src-family PTKs is required for efficient interaction of ZAP-70 and Syk with the receptor subunits and for receptor function. ZAP-70 forms two phosphotyrosine binding pockets, one of which is shared by both SH2 domains. In Syk the two SH2 domains do not form such a phosphotyrosine-binding site. The SH2 domains here are believed to function independently. In addition, the two SH2 domains of Syk display flexibility in their relative orientation, allowing Syk to accommodate a greater variety of spacing sequences between the ITAM phosphotyrosines and singly phosphorylated non-classical ITAM ligands. This model contains the C-terminus SH2 domains of Syk. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198264  Cd Length: 99  Bit Score: 56.82  E-value: 3.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719  74 ESEPWFFGCISRSEAMHRLQSEDYPKGTFLIRVSQKPGAdYVLSVWDAEAVRHYRIWRNSAGRLHLNEVVSFSSLSELVN 153
Cdd:cd10401    1 EKMPWFHGKISREESEQILLIGSKTNGKFLIRERDNNGS-YALCLLHDGKVLHYRIDKDKTGKLSIPDGKKFDTLWQLVE 79

                 ..
gi 157822719 154 YH 155
Cdd:cd10401   80 HY 81
SH2_C-SH2_SHP_like cd09931
C-terminal Src homology 2 (C-SH2) domain found in SH2 domain Phosphatases (SHP) proteins; The ...
78-158 3.31e-10

C-terminal Src homology 2 (C-SH2) domain found in SH2 domain Phosphatases (SHP) proteins; The SH2 domain phosphatases (SHP-1, SHP-2/Syp, Drosophila corkscrew (csw), and Caenorhabditis elegans Protein Tyrosine Phosphatase (Ptp-2)) are cytoplasmic signaling enzymes. They are both targeted and regulated by interactions of their SH2 domains with phosphotyrosine docking sites. These proteins contain two SH2 domains (N-SH2, C-SH2) followed by a tyrosine phosphatase (PTP) domain, and a C-terminal extension. Shp1 and Shp2 have two tyrosyl phosphorylation sites in their C-tails, which are phosphorylated differentially by receptor and nonreceptor PTKs. Csw retains the proximal tyrosine and Ptp-2 lacks both sites. Shp-binding proteins include receptors, scaffolding adapters, and inhibitory receptors. Some of these bind both Shp1 and Shp2 while others bind only one. Most proteins that bind a Shp SH2 domain contain one or more immuno-receptor tyrosine-based inhibitory motifs (ITIMs): [SIVL]xpYxx[IVL]. Shp1 N-SH2 domain blocks the catalytic domain and keeps the enzyme in the inactive conformation, and is thus believed to regulate the phosphatase activity of SHP-1. Its C-SH2 domain is thought to be involved in searching for phosphotyrosine activators. The SHP2 N-SH2 domain is a conformational switch; it either binds and inhibits the phosphatase, or it binds phosphoproteins and activates the enzyme. The C-SH2 domain contributes binding energy and specificity, but it does not have a direct role in activation. Csw SH2 domain function is essential, but either SH2 domain can fulfill this requirement. The role of the csw SH2 domains during Sevenless receptor tyrosine kinase (SEV) signaling is to bind Daughter of Sevenless rather than activated SEV. Ptp-2 acts in oocytes downstream of sheath/oocyte gap junctions to promote major sperm protein (MSP)-induced MAP Kinase (MPK-1) phosphorylation. Ptp-2 functions in the oocyte cytoplasm, not at the cell surface to inhibit multiple RasGAPs, resulting in sustained Ras activation. It is thought that MSP triggers PTP-2/Ras activation and ROS production to stimulate MPK-1 activity essential for oocyte maturation and that secreted MSP domains and Cu/Zn superoxide dismutases function antagonistically to control ROS and MAPK signaling. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198185  Cd Length: 99  Bit Score: 56.90  E-value: 3.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719  78 WFFGCISRSEAMHRLQSEDYPkGTFLIRVSQ-KPGaDYVLSVW-DAEAVRHYRIwRNSAGRLHLNEVVSFSSLSELVNYH 155
Cdd:cd09931    2 WFHGHLSGKEAEKLLLEKGKP-GSFLVRESQsKPG-DFVLSVRtDDDKVTHIMI-RCQGGKYDVGGGEEFDSLTDLVEHY 78

                 ...
gi 157822719 156 KTH 158
Cdd:cd09931   79 KKN 81
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
189-388 3.50e-10

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: 61.55  E-value: 3.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 189 EEFTLCKKLGSGYFGEVFEGLWKGLVRV-AVKVISRDNLLHQHT---FQAEIQAMKKLRHKHILSLYAVATAGDPVYIIT 264
Cdd:cd05621   52 EDYDVVKVIGRGAFGEVQLVRHKASQKVyAMKLLSKFEMIKRSDsafFWEERDIMAFANSPWVVQLFCAFQDDKYLYMVM 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 265 ELMPKGSLLQLLRDSDekdLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLVTENNLCKVGDFGLARLVKEDIYLS 344
Cdd:cd05621  132 EYMPGGDLVNLMSNYD---VPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGTCMKMDETGMVH 208
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 157822719 345 RDHNVPY-KWTAPEALSR----GHYSIKSDVWSFGVLLHEIFSrGQMPY 388
Cdd:cd05621  209 CDTAVGTpDYISPEVLKSqggdGYYGRECDWWSVGVFLFEMLV-GDTPF 256
SH2_N-SH2_PLC_gamma_like cd10341
N-terminal Src homology 2 (N-SH2) domain in Phospholipase C gamma; Phospholipase C gamma is a ...
75-160 4.65e-10

N-terminal Src homology 2 (N-SH2) domain in Phospholipase C gamma; Phospholipase C gamma is a signaling molecule that is recruited to the C-terminal tail of the receptor upon autophosphorylation of a highly conserved tyrosine. PLCgamma is composed of a Pleckstrin homology (PH) domain followed by an elongation factor (EF) domain, 2 catalytic regions of PLC domains that flank 2 tandem SH2 domains (N-SH2, C-SH2), and ending with a SH3 domain and C2 domain. N-SH2 SH2 domain-mediated interactions represent a crucial step in transmembrane signaling by receptor tyrosine kinases. SH2 domains recognize phosphotyrosine (pY) in the context of particular sequence motifs in receptor phosphorylation sites. Both N-SH2 and C-SH2 have a very similar binding affinity to pY. But in growth factor stimulated cells these domains bind to different target proteins. N-SH2 binds to pY containing sites in the C-terminal tails of tyrosine kinases and other receptors. Recently it has been shown that this interaction is mediated by phosphorylation-independent interactions between a secondary binding site found exclusively on the N-SH2 domain and a region of the FGFR1 tyrosine kinase domain. This secondary site on the SH2 cooperates with the canonical pY site to regulate selectivity in mediating a specific cellular process. C-SH2 binds to an intramolecular site on PLCgamma itself which allows it to hydrolyze phosphatidylinositol-4,5-bisphosphate into diacylglycerol and inositol triphosphate. These then activate protein kinase C and release calcium. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 199829  Cd Length: 99  Bit Score: 56.21  E-value: 4.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719  75 SEPWFFGCIS--RSEAMHRLQS-EDYPKGTFLIRVSQKPGADYVLSVWDAEAVRHYRIW-RNSAG--RLHLNEVVSFSSL 148
Cdd:cd10341    3 TEPWFHGKLGdgRDEAEKLLLEyCEGGDGTFLVRESETFVGDYTLSFWRNGKVQHCRIRsRQENGekKYYLTDNLVFDSL 82
                         90
                 ....*....|..
gi 157822719 149 SELVNYHKTHNL 160
Cdd:cd10341   83 YELIDYYRQNPL 94
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
190-431 5.00e-10

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: 60.81  E-value: 5.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 190 EFTLCKKLGSGYFGEVFEGLWKGLVRV-AVKVISRDNLLHQ----HTFqAEIQAMKKLRHKHILSLYAVATAGDPVYIIT 264
Cdd:cd05594   26 DFEYLKLLGKGTFGKVILVKEKATGRYyAMKILKKEVIVAKdevaHTL-TENRVLQNSRHPFLTALKYSFQTHDRLCFVM 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 265 ELMPKGSLLQLLrdSDEKDLPILELVDFASQVAEGMCYLESQ-NYIHRDLAARNVLVTENNLCKVGDFGLARL-VKEDIY 342
Cdd:cd05594  105 EYANGGELFFHL--SRERVFSEDRARFYGAEIVSALDYLHSEkNVVYRDLKLENLMLDKDGHIKITDFGLCKEgIKDGAT 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 343 LSRDHNVPyKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPYPGmSNHETFLRVDAGYRMPCPLECPPNIHKLMLS 422
Cdd:cd05594  183 MKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYN-QDHEKLFELILMEEIRFPRTLSPEAKSLLSG 259

                 ....*....
gi 157822719 423 CWSRDPKQR 431
Cdd:cd05594  260 LLKKDPKQR 268
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
235-403 5.33e-10

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: 59.83  E-value: 5.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 235 EIQAMKKLRHKHILSLY-AVATAGDPVYIITELMPKGSLLQ--LLRDSD---EKDLPIlelvdFASQVAEGMCYLESQNY 308
Cdd:cd14109   46 EVDIHNSLDHPNIVQMHdAYDDEKLAVTVIDNLASTIELVRdnLLPGKDyytERQVAV-----FVRQLLLALKHMHDLGI 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 309 IHRDLAARNVLVTENNLCkVGDFGLARLVKEDIYLSRDHNVPyKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPY 388
Cdd:cd14109  121 AHLDLRPEDILLQDDKLK-LADFGQSRRLLRGKLTTLIYGSP-EFVSPEIVNSYPVTLATDMWSVGVLTYVLLG-GISPF 197
                        170
                 ....*....|....*
gi 157822719 389 PGMSNHETFLRVDAG 403
Cdd:cd14109  198 LGDNDRETLTNVRSG 212
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
235-390 5.47e-10

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


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 60.37  E-value: 5.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 235 EIQAMKKLRHKHILSLYAVATAGDPVYIITELMPKGSLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLA 314
Cdd:cd05632   52 EKQILEKVNSQFVVNLAYAYETKDALCLVLTIMNGGDLKFHIYNMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLK 131
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157822719 315 ARNVLVTENNLCKVGDFGLARLVKE-DIYLSRDHNVPYkwTAPEALSRGHYSIKSDVWSFGVLLHEIFsRGQMPYPG 390
Cdd:cd05632  132 PENILLDDYGHIRISDLGLAVKIPEgESIRGRVGTVGY--MAPEVLNNQRYTLSPDYWGLGCLIYEMI-EGQSPFRG 205
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
191-378 6.85e-10

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: 59.40  E-value: 6.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVfeglwkGLVR-------VAVKVISRDNLLHQHTfQAEIQAMKKLRHKHILSLYAVATAGDPVYII 263
Cdd:cd14662    2 YELVKDIGSGNFGVA------RLMRnketkelVAVKYIERGLKIDENV-QREIINHRSLRHPNIIRFKEVVLTPTHLAIV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 264 TELMPKGSLLQllRDSDEKDLPILELVDFASQVAEGMCYLESQNYIHRDLAARNVLV--TENNLCKVGDFGLArlvKEDI 341
Cdd:cd14662   75 MEYAAGGELFE--RICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLdgSPAPRLKICDFGYS---KSSV 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 157822719 342 YLSRDHN---VPyKWTAPEALSRGHYSIK-SDVWSFGVLLH 378
Cdd:cd14662  150 LHSQPKStvgTP-AYIAPEVLSRKEYDGKvADVWSCGVTLY 189
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
191-379 8.01e-10

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 59.90  E-value: 8.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVfeglW-----KGLVRVAVKVISRDnllhQH---TFQAEIQAMKKLRH--------KHILSLY--- 251
Cdd:cd14136   12 YHVVRKLGWGHFSTV----WlcwdlQNKRFVALKVVKSA----QHyteAALDEIKLLKCVREadpkdpgrEHVVQLLddf 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 252 -AVATAGDPVYIITELMpkG-SLLQLLRDSDEKDLPILELVDFASQVAEGMCYLESQ-NYIHRDLAARNVLVTENNL-CK 327
Cdd:cd14136   84 kHTGPNGTHVCMVFEVL--GpNLLKLIKRYNYRGIPLPLVKKIARQVLQGLDYLHTKcGIIHTDIKPENVLLCISKIeVK 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 157822719 328 VGDFGLARLVK----EDIYlSRdhnvPYKwtAPEALSRGHYSIKSDVWSFGVLLHE 379
Cdd:cd14136  162 IADLGNACWTDkhftEDIQ-TR----QYR--SPEVILGAGYGTPADIWSTACMAFE 210
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
191-382 8.69e-10

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: 59.61  E-value: 8.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEGLWKGLVR---VAVKVISRDNLLHQHTFQA---EIQAMKKLRHKHILSLyavatagdpVYIIT 264
Cdd:cd07842    2 YEIEGCIGRGTYGRVYKAKRKNGKDgkeYAIKKFKGDKEQYTGISQSacrEIALLRELKHENVVSL---------VEVFL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 265 ELMPKgsLLQLLRDSDEKDLpiLELVDFAS-----------------QVAEGMCYLESQNYIHRDLAARNVLVT----EN 323
Cdd:cd07842   73 EHADK--SVYLLFDYAEHDL--WQIIKFHRqakrvsippsmvksllwQILNGIHYLHSNWVLHRDLKPANILVMgegpER 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157822719 324 NLCKVGDFGLARLVKEDIYLSRDHN---VPYKWTAPEAL--SRgHYSIKSDVWSFGVLLHEIFS 382
Cdd:cd07842  149 GVVKIGDLGLARLFNAPLKPLADLDpvvVTIWYRAPELLlgAR-HYTKAIDIWAIGCIFAELLT 211
SH3_OSTF1 cd11772
Src Homology 3 domain of metazoan osteoclast stimulating factor 1; OSTF1, also named OSF or ...
13-69 9.97e-10

Src Homology 3 domain of metazoan osteoclast stimulating factor 1; OSTF1, also named OSF or SH3P2, is a signaling protein containing SH3 and ankyrin-repeat domains. It acts through a Src-related pathway to enhance the formation of osteoclasts and bone resorption. It also acts as a negative regulator of cell motility. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212706 [Multi-domain]  Cd Length: 53  Bit Score: 53.84  E-value: 9.97e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 157822719  13 YVGLWDFKARTDEELSFQAGDLLHVTRKEE-QWWWATLldaEGKalaEGYVPHNYLAE 69
Cdd:cd11772    2 FRALYDYEAQHPDELSFEEGDLLYISDKSDpNWWKATC---GGK---TGLIPSNYVEE 53
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
196-442 1.07e-09

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: 59.21  E-value: 1.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 196 KLGSGYFGEVFegLWKGL---VRVAVKVISRD-NLLHQHTFQAEIQAMKKLRHKHILS-------LYAVATAGDPVyIIT 264
Cdd:cd14038    1 RLGTGGFGNVL--RWINQetgEQVAIKQCRQElSPKNRERWCLEIQIMKRLNHPNVVAardvpegLQKLAPNDLPL-LAM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 265 ELMPKGSLLQLLRDSDE----KDLPILELVdfaSQVAEGMCYLESQNYIHRDLAARNVLVTENN---LCKVGDFGLARLV 337
Cdd:cd14038   78 EYCQGGDLRKYLNQFENccglREGAILTLL---SDISSALRYLHENRIIHRDLKPENIVLQQGEqrlIHKIIDLGYAKEL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 338 KEDiYLSRDHNVPYKWTAPEALSRGHYSIKSDVWSFGVLLHEIFSrGQMPY-PG------------MSNHETFLRVDAG- 403
Cdd:cd14038  155 DQG-SLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECIT-GFRPFlPNwqpvqwhgkvrqKSNEDIVVYEDLTg 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 157822719 404 -YRMPCPLECPPNIHKLM-------LSC---WS-----RDPKQRP--CFKDLCEKLS 442
Cdd:cd14038  233 aVKFSSVLPTPNNLNGILagklerwLQCmlmWHprqrgTDPPQNPngCFQALDSILN 289
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
191-335 1.18e-09

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 59.01  E-value: 1.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822719 191 FTLCKKLGSGYFGEVFEG---LWKglVRVAVKVISRDNllHQHTFQAEIQAMKKLR-HKHILSLYAVATAGDPVYIITEL 266
Cdd:cd14016    2 YKLVKKIGSGSFGEVYLGidlKTG--EEVAIKIEKKDS--KHPQLEYEAKVYKLLQgGPGIPRLYWFGQEGDYNVMVMDL 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157822719 267 MPKgSLLQLLRDSDEK-DLP-ILELVDfasQVAEGMCYLESQNYIHRDLAARNVLVTENNLCK---VGDFGLAR 335
Cdd:cd14016   78 LGP-SLEDLFNKCGRKfSLKtVLMLAD---QMISRLEYLHSKGYIHRDIKPENFLMGLGKNSNkvyLIDFGLAK 147
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH