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Conserved domains on  [gi|27372075|gb|AAN87886|]
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Yes-relayed kinase [Danio rerio]

Protein Classification

SH2_Src_Fgr and PTKc_Src_Fyn_like domain-containing protein (domain architecture ID 10346111)

protein containing domains SH3, SH2_Src_Fgr, and PTKc_Src_Fyn_like

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
263-510 0e+00

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: 572.25  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075 263 RKLGQGCFGDVWMGMWNGTTKVAVKTLKPGTMSPEAFLDEAQIMKRLRHDKLVQLYAVVSEEPIYIITEFMSQGSLLDFL 342
Cdd:cd14203   1 VKLGQGCFGEVWMGTWNGTTKVAIKTLKPGTMSPEAFLEEAQIMKKLRHDKLVQLYAVVSEEPIYIVTEFMSKGSLLDFL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075 343 KDGDGRNLKLPQLVDMAAQIAAGMAYIERMNYIHRDLRAANILVGDGLVCKIADFGLARLIEDNEYTARQGAKFPIKWTA 422
Cdd:cd14203  81 KDGEGKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQGAKFPIKWTA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075 423 PEAALYGKFTIKSDVWSFGILLTELITKGRVPYPGMNNREVLEQVERGYRMPCPQGSPASLHELMLQCWRKDPDERHTFE 502
Cdd:cd14203 161 PEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPPGCPESLHELMCQCWRKDPEERPTFE 240

                ....*...
gi 27372075 503 YLQSFLED 510
Cdd:cd14203 241 YLQSFLED 248
SH2_Src_Fgr cd10367
Src homology 2 (SH2) domain found in Gardner-Rasheed feline sarcoma viral (v-fgr) oncogene ...
136-236 1.63e-71

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: 222.86  E-value: 1.63e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075 136 QAEEWYFGKMGRKDAERQLLAQNNPRGTFLIRESETTKGAYSLSIRDWDDAKGDHVKHYKIRKLDNGGYYITTRTQFDTV 215
Cdd:cd10367   1 QAEEWYFGKIGRKDAERQLLSPGNPRGAFLIRESETTKGAYSLSIRDWDQNRGDHVKHYKIRKLDTGGYYITTRAQFDTV 80
                        90       100
                ....*....|....*....|.
gi 27372075 216 QQLVEHYTGSNDGLCCYLTKA 236
Cdd:cd10367  81 QELVQHYMEVNDGLCYLLTAP 101
SH3 super family cl17036
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
76-133 2.83e-32

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.


The actual alignment was detected with superfamily member cd12007:

Pssm-ID: 354299  Cd Length: 58  Bit Score: 117.44  E-value: 2.83e-32
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 27372075  76 TLFIALYEYDARTEDDLSFQKGEKFHIINNTEGDWWEARSLDTGKSGYIPSNYVAPVD 133
Cdd:cd12007   1 TIFVALYDYEARTTEDLSFKKGERFQIINNTEGDWWEARSIATGKNGYIPSNYVAPAD 58
 
Name Accession Description Interval E-value
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
263-510 0e+00

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: 572.25  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075 263 RKLGQGCFGDVWMGMWNGTTKVAVKTLKPGTMSPEAFLDEAQIMKRLRHDKLVQLYAVVSEEPIYIITEFMSQGSLLDFL 342
Cdd:cd14203   1 VKLGQGCFGEVWMGTWNGTTKVAIKTLKPGTMSPEAFLEEAQIMKKLRHDKLVQLYAVVSEEPIYIVTEFMSKGSLLDFL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075 343 KDGDGRNLKLPQLVDMAAQIAAGMAYIERMNYIHRDLRAANILVGDGLVCKIADFGLARLIEDNEYTARQGAKFPIKWTA 422
Cdd:cd14203  81 KDGEGKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQGAKFPIKWTA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075 423 PEAALYGKFTIKSDVWSFGILLTELITKGRVPYPGMNNREVLEQVERGYRMPCPQGSPASLHELMLQCWRKDPDERHTFE 502
Cdd:cd14203 161 PEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPPGCPESLHELMCQCWRKDPEERPTFE 240

                ....*...
gi 27372075 503 YLQSFLED 510
Cdd:cd14203 241 YLQSFLED 248
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
259-508 1.70e-139

Protein tyrosine kinase;


Pssm-ID: 336778 [Multi-domain]  Cd Length: 258  Bit Score: 402.65  E-value: 1.70e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075   259 LKLNRKLGQGCFGDVWMGMWNG-----TTKVAVKTLKPGTMSP--EAFLDEAQIMKRLRHDKLVQLYAVVS-EEPIYIIT 330
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGegentKIKVAVKTLKEGADEEerEEFLEEASIMKKLDHPNIVKLLGVCTqGEPLYIVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075   331 EFMSQGSLLDFLKDgDGRNLKLPQLVDMAAQIAAGMAYIERMNYIHRDLRAANILVGDGLVCKIADFGLARLIE-DNEYT 409
Cdd:pfam07714  81 EYMPGGDLLDFLRK-HKGKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNILVTENLVVKISDFGLSRDVYdDDYYR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075   410 ARQGAKFPIKWTAPEAALYGKFTIKSDVWSFGILLTELITKGRVPYPGMNNREVLEQVERGYRMPCPQGSPASLHELMLQ 489
Cdd:pfam07714 160 KRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEFLEDGYRLPQPENCPDELYDLMTQ 239
                         250
                  ....*....|....*....
gi 27372075   490 CWRKDPDERHTFEYLQSFL 508
Cdd:pfam07714 240 CWAYDPEDRPTFSELVEDL 258
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
259-508 9.71e-130

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: 377.66  E-value: 9.71e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075    259 LKLNRKLGQGCFGDVWMGMWNGT-----TKVAVKTLKPGTMS--PEAFLDEAQIMKRLRHDKLVQLYAVVSE-EPIYIIT 330
Cdd:smart00221   1 LTLGKKLGEGAFGEVYKGTLKGKgdgkeVEVAVKTLKEDASEqqIEEFLREARIMRKLDHPNIVKLLGVCTEeEPLMIVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075    331 EFMSQGSLLDFLKDGDGRNLKLPQLVDMAAQIAAGMAYIERMNYIHRDLRAANILVGDGLVCKIADFGLARLIEDNEYTA 410
Cdd:smart00221  81 EYMPGGDLLDYLRKNRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDYYK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075    411 RQGAKFPIKWTAPEAALYGKFTIKSDVWSFGILLTELITKGRVPYPGMNNREVLEQVERGYRMPCPQGSPASLHELMLQC 490
Cdd:smart00221 161 VKGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEEPYPGMSNAEVLEYLKKGYRLPKPPNCPPELYKLMLQC 240
                          250
                   ....*....|....*...
gi 27372075    491 WRKDPDERHTFEYLQSFL 508
Cdd:smart00221 241 WAEDPEDRPTFSELVEIL 258
SH2_Src_Fgr cd10367
Src homology 2 (SH2) domain found in Gardner-Rasheed feline sarcoma viral (v-fgr) oncogene ...
136-236 1.63e-71

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: 222.86  E-value: 1.63e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075 136 QAEEWYFGKMGRKDAERQLLAQNNPRGTFLIRESETTKGAYSLSIRDWDDAKGDHVKHYKIRKLDNGGYYITTRTQFDTV 215
Cdd:cd10367   1 QAEEWYFGKIGRKDAERQLLSPGNPRGAFLIRESETTKGAYSLSIRDWDQNRGDHVKHYKIRKLDTGGYYITTRAQFDTV 80
                        90       100
                ....*....|....*....|.
gi 27372075 216 QQLVEHYTGSNDGLCCYLTKA 236
Cdd:cd10367  81 QELVQHYMEVNDGLCYLLTAP 101
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
260-521 6.75e-35

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 134.87  E-value: 6.75e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075 260 KLNRKLGQGCFGDVWMGMwnGTTKVAVKTLKPGTMSP----EAFLDEAQIMKRLRHDK-LVQLYAV-VSEEPIYIITEFM 333
Cdd:COG0515   3 RILRKLGEGSFGEVYLAR--DRKLVALKVLAKKLESKskevERFLREIQILASLNHPPnIVKLYDFfQDEGSLYLVMEYV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075 334 SQGSLLDFLK-DGDGRNLKLPQLVDMAAQIAAGMAYIERMNYIHRDLRAANILVG-DGLVCKIADFGLARLIEDNEYTAR 411
Cdd:COG0515  81 DGGSLEDLLKkIGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDrDGRVVKLIDFGLAKLLPDPGSTSS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075 412 QGAKFPIK-----WTAPE---AALYGKFTIKSDVWSFGILLTELITkGRVPYPGMNNREVLEQVER------------GY 471
Cdd:COG0515 161 IPALPSTSvgtpgYMAPEvllGLSLAYASSSSDIWSLGITLYELLT-GLPPFEGEKNSSATSQTLKiilelptpslasPL 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 27372075 472 RMPCPQGSPASLHELMLQCWRKDPDERHT--FEYLQSFLEDYFTATEPQYQP 521
Cdd:COG0515 240 SPSNPELISKAASDLLKKLLAKDPKNRLSssSDLSHDLLAHLKLKESDLSDL 291
SH2 pfam00017
SH2 domain;
140-222 8.32e-34

SH2 domain;


Pssm-ID: 333769  Cd Length: 76  Bit Score: 122.32  E-value: 8.32e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075   140 WYFGKMGRKDAERQLLAQNnPRGTFLIRESETTKGAYSLSIRDWddakgDHVKHYKIRKLDNgGYYITTRTQFDTVQQLV 219
Cdd:pfam00017   1 WYHGKISRQEAERLLLNGK-PDGTFLVRESESTPGDYTLSVRDD-----GKVKHYKIQSTDN-GYYISGGVKFSSLAELV 73

                  ...
gi 27372075   220 EHY 222
Cdd:pfam00017  74 EHY 76
SH3_Yes cd12007
Src homology 3 domain of Yes Protein Tyrosine Kinase; Yes (or c-Yes) is a member of the Src ...
76-133 2.83e-32

Src homology 3 domain of Yes Protein Tyrosine Kinase; 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 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: 212940  Cd Length: 58  Bit Score: 117.44  E-value: 2.83e-32
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 27372075  76 TLFIALYEYDARTEDDLSFQKGEKFHIINNTEGDWWEARSLDTGKSGYIPSNYVAPVD 133
Cdd:cd12007   1 TIFVALYDYEARTTEDLSFKKGERFQIINNTEGDWWEARSIATGKNGYIPSNYVAPAD 58
SH2 smart00252
Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides ...
138-228 1.48e-30

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  Cd Length: 84  Bit Score: 113.86  E-value: 1.48e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075    138 EEWYFGKMGRKDAERQLlaQNNPRGTFLIRESETTKGAYSLSIRDwddakGDHVKHYKIRKLDNGGYYITTRTQFDTVQQ 217
Cdd:smart00252   1 QPWYHGFISREEAEKLL--KNEGDGDFLVRDSESSPGDYVLSVRV-----KGKVKHYRIRRNEDGKFYLEGGRKFPSLVE 73
                           90
                   ....*....|.
gi 27372075    218 LVEHYTGSNDG 228
Cdd:smart00252  74 LVEHYQKNSLG 84
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
74-130 1.93e-19

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  Cd Length: 56  Bit Score: 81.82  E-value: 1.93e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 27372075     74 GVTLFIALYEYDARTEDDLSFQKGEKFHIINNTEGDWWEARsLDTGKSGYIPSNYVA 130
Cdd:smart00326   1 EGPQVRALYDYTAQDPDELSFKKGDIITVLEKSDDGWWKGR-LGRGKEGLFPSNYVE 56
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
261-459 5.51e-18

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 84.81  E-value: 5.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075  261 LNRKLGQGCFGDVWMGMWNGT-TKVAVKTLKPGTMSPEAF---------------LDEAQIMKRLRHDKLVQLYAV-VSE 323
Cdd:PTZ00024  13 KGAHLGEGTYGKVEKAYDTLTgKIVAIKKVKIIEISNDVTkdrqlvgmcgihfttLRELKIMNEIKHENIMGLVDVyVEG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075  324 EPIYIITEFMSQgsllDFLKDGDGR-NLKLPQLVDMAAQIAAGMAYIERMNYIHRDLRAANILVGDGLVCKIADFGLAR- 401
Cdd:PTZ00024  93 DFINLVMDIMAS----DLKKVVDRKiRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLARr 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27372075  402 --------LIEDNEYTARQ---GAKFPIKWTAPEAALYG--KFTIKSDVWSFGILLTELITkGRVPYPGMN 459
Cdd:PTZ00024 169 ygyppysdTLSKDETMQRReemTSKVVTLWYRAPELLMGaeKYHFAVDMWSVGCIFAELLT-GKPLFPGEN 238
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
79-126 4.11e-17

SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organisation. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.


Pssm-ID: 333770  Cd Length: 47  Bit Score: 74.92  E-value: 4.11e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 27372075    79 IALYEYDARTEDDLSFQKGEKFHIINNTEGDWWEARSLDtGKSGYIPS 126
Cdd:pfam00018   1 VALYDYTAREPDELSFKKGDVIIVLEKSDDGWWKGRLKG-GKEGLIPS 47
 
Name Accession Description Interval E-value
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
263-510 0e+00

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: 572.25  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075 263 RKLGQGCFGDVWMGMWNGTTKVAVKTLKPGTMSPEAFLDEAQIMKRLRHDKLVQLYAVVSEEPIYIITEFMSQGSLLDFL 342
Cdd:cd14203   1 VKLGQGCFGEVWMGTWNGTTKVAIKTLKPGTMSPEAFLEEAQIMKKLRHDKLVQLYAVVSEEPIYIVTEFMSKGSLLDFL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075 343 KDGDGRNLKLPQLVDMAAQIAAGMAYIERMNYIHRDLRAANILVGDGLVCKIADFGLARLIEDNEYTARQGAKFPIKWTA 422
Cdd:cd14203  81 KDGEGKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQGAKFPIKWTA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075 423 PEAALYGKFTIKSDVWSFGILLTELITKGRVPYPGMNNREVLEQVERGYRMPCPQGSPASLHELMLQCWRKDPDERHTFE 502
Cdd:cd14203 161 PEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPPGCPESLHELMCQCWRKDPEERPTFE 240

                ....*...
gi 27372075 503 YLQSFLED 510
Cdd:cd14203 241 YLQSFLED 248
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
263-509 0e+00

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: 553.43  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075 263 RKLGQGCFGDVWMGMWNGTTKVAVKTLKPGTMSPEAFLDEAQIMKRLRHDKLVQLYAVVS-EEPIYIITEFMSQGSLLDF 341
Cdd:cd05034   1 KKLGAGQFGEVWMGVWNGTTKVAVKTLKPGTMSPEAFLQEAQIMKKLRHDKLVQLYAVCSdEEPIYIVTELMSKGSLLDY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075 342 LKDGDGRNLKLPQLVDMAAQIAAGMAYIERMNYIHRDLRAANILVGDGLVCKIADFGLARLIEDNEYTARQGAKFPIKWT 421
Cdd:cd05034  81 LRTGEGRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLARLIEDDEYTAREGAKFPIKWT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075 422 APEAALYGKFTIKSDVWSFGILLTELITKGRVPYPGMNNREVLEQVERGYRMPCPQGSPASLHELMLQCWRKDPDERHTF 501
Cdd:cd05034 161 APEAALYGRFTIKSDVWSFGILLYEIVTYGRVPYPGMTNREVLEQVERGYRMPKPPGCPDELYDIMLQCWKKEPEERPTF 240

                ....*...
gi 27372075 502 EYLQSFLE 509
Cdd:cd05034 241 EYLQSFLE 248
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
246-524 0e+00

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: 546.21  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075 246 GLGRDAWEIARDTLKLNRKLGQGCFGDVWMGMWNGTTKVAVKTLKPGTMSPEAFLDEAQIMKRLRHDKLVQLYAVVSEEP 325
Cdd:cd05069   1 GLAKDAWEIPRESLRLDVKLGQGCFGEVWMGTWNGTTKVAIKTLKPGTMMPEAFLQEAQIMKKLRHDKLVPLYAVVSEEP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075 326 IYIITEFMSQGSLLDFLKDGDGRNLKLPQLVDMAAQIAAGMAYIERMNYIHRDLRAANILVGDGLVCKIADFGLARLIED 405
Cdd:cd05069  81 IYIVTEFMGKGSLLDFLKEGDGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIED 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075 406 NEYTARQGAKFPIKWTAPEAALYGKFTIKSDVWSFGILLTELITKGRVPYPGMNNREVLEQVERGYRMPCPQGSPASLHE 485
Cdd:cd05069 161 NEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMVNREVLEQVERGYRMPCPQGCPESLHE 240
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 27372075 486 LMLQCWRKDPDERHTFEYLQSFLEDYFTATEPQYQPGEN 524
Cdd:cd05069 241 LMKLCWKKDPDERPTFEYIQSFLEDYFTATEPQYQPGDN 279
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
249-522 0e+00

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: 534.26  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075 249 RDAWEIARDTLKLNRKLGQGCFGDVWMGMWNGTTKVAVKTLKPGTMSPEAFLDEAQIMKRLRHDKLVQLYAVVSEEPIYI 328
Cdd:cd05070   1 KDVWEIPRESLQLIKRLGNGQFGEVWMGTWNGNTKVAIKTLKPGTMSPESFLEEAQIMKKLKHDKLVQLYAVVSEEPIYI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075 329 ITEFMSQGSLLDFLKDGDGRNLKLPQLVDMAAQIAAGMAYIERMNYIHRDLRAANILVGDGLVCKIADFGLARLIEDNEY 408
Cdd:cd05070  81 VTEYMSKGSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEY 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075 409 TARQGAKFPIKWTAPEAALYGKFTIKSDVWSFGILLTELITKGRVPYPGMNNREVLEQVERGYRMPCPQGSPASLHELML 488
Cdd:cd05070 161 TARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPQDCPISLHELMI 240
                       250       260       270
                ....*....|....*....|....*....|....
gi 27372075 489 QCWRKDPDERHTFEYLQSFLEDYFTATEPQYQPG 522
Cdd:cd05070 241 HCWKKDPEERPTFEYLQGFLEDYFTATEPQYQPG 274
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
249-525 0e+00

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: 519.63  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075 249 RDAWEIARDTLKLNRKLGQGCFGDVWMGMWNGTTKVAVKTLKPGTMSPEAFLDEAQIMKRLRHDKLVQLYAVVSEEPIYI 328
Cdd:cd05071   1 KDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEPIYI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075 329 ITEFMSQGSLLDFLKDGDGRNLKLPQLVDMAAQIAAGMAYIERMNYIHRDLRAANILVGDGLVCKIADFGLARLIEDNEY 408
Cdd:cd05071  81 VTEYMSKGSLLDFLKGEMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEY 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075 409 TARQGAKFPIKWTAPEAALYGKFTIKSDVWSFGILLTELITKGRVPYPGMNNREVLEQVERGYRMPCPQGSPASLHELML 488
Cdd:cd05071 161 TARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPCPPECPESLHDLMC 240
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 27372075 489 QCWRKDPDERHTFEYLQSFLEDYFTATEPQYQPGENL 525
Cdd:cd05071 241 QCWRKEPEERPTFEYLQAFLEDYFTSTEPQYQPGENL 277
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
250-513 2.11e-179

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: 504.63  E-value: 2.11e-179
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075 250 DAWEIARDTLKLNRKLGQGCFGDVWMGMWNGTTKVAVKTLKPGTMSPEAFLDEAQIMKRLRHDKLVQLYAVVS-EEPIYI 328
Cdd:cd05068   1 DQWEIDRKSLKLLRKLGSGQFGEVWEGLWNNTTPVAVKTLKPGTMDPEDFLREAQIMKKLRHPKLIQLYAVCTlEEPIYI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075 329 ITEFMSQGSLLDFLKdGDGRNLKLPQLVDMAAQIAAGMAYIERMNYIHRDLRAANILVGDGLVCKIADFGLARLIE-DNE 407
Cdd:cd05068  81 ITELMKHGSLLEYLQ-GKGRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGLARVIKvEDE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075 408 YTARQGAKFPIKWTAPEAALYGKFTIKSDVWSFGILLTELITKGRVPYPGMNNREVLEQVERGYRMPCPQGSPASLHELM 487
Cdd:cd05068 160 YEAREGAKFPIKWTAPEAANYNRFSIKSDVWSFGILLTEIVTYGRIPYPGMTNAEVLQQVERGYRMPCPPNCPPQLYDIM 239
                       250       260
                ....*....|....*....|....*.
gi 27372075 488 LQCWRKDPDERHTFEYLQSFLEDYFT 513
Cdd:cd05068 240 LECWKADPMERPTFETLQWKLEDFFV 265
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
252-514 2.20e-164

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: 466.29  E-value: 2.20e-164
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075 252 WEIARDTLKLNRKLGQGCFGDVWMGMWNGTTKVAVKTLKPGTMSPEAFLDEAQIMKRLRHDKLVQLYAVVSEEPIYIITE 331
Cdd:cd05067   2 WEVPRETLKLVERLGAGQFGEVWMGYYNGHTKVAIKSLKQGSMSPDAFLAEANLMKQLQHQRLVRLYAVVTQEPIYIITE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075 332 FMSQGSLLDFLKDGDGRNLKLPQLVDMAAQIAAGMAYIERMNYIHRDLRAANILVGDGLVCKIADFGLARLIEDNEYTAR 411
Cdd:cd05067  82 YMENGSLVDFLKTPSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLIEDNEYTAR 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075 412 QGAKFPIKWTAPEAALYGKFTIKSDVWSFGILLTELITKGRVPYPGMNNREVLEQVERGYRMPCPQGSPASLHELMLQCW 491
Cdd:cd05067 162 EGAKFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVTHGRIPYPGMTNPEVIQNLERGYRMPRPDNCPEELYQLMRLCW 241
                       250       260
                ....*....|....*....|...
gi 27372075 492 RKDPDERHTFEYLQSFLEDYFTA 514
Cdd:cd05067 242 KERPEDRPTFEYLRSVLEDFFTA 264
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
251-520 1.69e-159

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: 454.11  E-value: 1.69e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075 251 AWEIARDTLKLNRKLGQGCFGDVWMGMWNGTTKVAVKTLKPGTMSPEAFLDEAQIMKRLRHDKLVQLYAVVS-EEPIYII 329
Cdd:cd05072   1 AWEIPRESIKLVKKLGAGQFGEVWMGYYNNSTKVAVKTLKPGTMSVQAFLEEANLMKTLQHDKLVRLYAVVTkEEPIYII 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075 330 TEFMSQGSLLDFLKDGDGRNLKLPQLVDMAAQIAAGMAYIERMNYIHRDLRAANILVGDGLVCKIADFGLARLIEDNEYT 409
Cdd:cd05072  81 TEYMAKGSLLDFLKSDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIEDNEYT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075 410 ARQGAKFPIKWTAPEAALYGKFTIKSDVWSFGILLTELITKGRVPYPGMNNREVLEQVERGYRMPCPQGSPASLHELMLQ 489
Cdd:cd05072 161 AREGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLYEIVTYGKIPYPGMSNSDVMSALQRGYRMPRMENCPDELYDIMKT 240
                       250       260       270
                ....*....|....*....|....*....|.
gi 27372075 490 CWRKDPDERHTFEYLQSFLEDYFTATEPQYQ 520
Cdd:cd05072 241 CWKEKAEERPTFDYLQSVLDDFYTATEGQYQ 271
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
249-511 2.09e-147

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: 423.28  E-value: 2.09e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075 249 RDAWEIARDTLKLNRKLGQGCFGDVWMGMWNGTTKVAVKTLKPGTMSPEAFLDEAQIMKRLRHDKLVQLYAVVSEEPIYI 328
Cdd:cd05073   3 KDAWEIPRESLKLEKKLGAGQFGEVWMATYNKHTKVAVKTMKPGSMSVEAFLAEANVMKTLQHDKLVKLHAVVTKEPIYI 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075 329 ITEFMSQGSLLDFLKDGDGRNLKLPQLVDMAAQIAAGMAYIERMNYIHRDLRAANILVGDGLVCKIADFGLARLIEDNEY 408
Cdd:cd05073  83 ITEFMAKGSLLDFLKSDEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVIEDNEY 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075 409 TARQGAKFPIKWTAPEAALYGKFTIKSDVWSFGILLTELITKGRVPYPGMNNREVLEQVERGYRMPCPQGSPASLHELML 488
Cdd:cd05073 163 TAREGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTYGRIPYPGMSNPEVIRALERGYRMPRPENCPEELYNIMM 242
                       250       260
                ....*....|....*....|...
gi 27372075 489 QCWRKDPDERHTFEYLQSFLEDY 511
Cdd:cd05073 243 RCWKNRPEERPTFEYIQSVLDDF 265
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
259-508 1.70e-139

Protein tyrosine kinase;


Pssm-ID: 336778 [Multi-domain]  Cd Length: 258  Bit Score: 402.65  E-value: 1.70e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27372075   259 LKLNRKLGQGCFGDVWMGMWNG-----TTKVAVKTLKPGTMSP--EAFLDEAQIMKRLRHDKLVQLYAVVS-EEPI