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Conserved domains on  [gi|1207186103|ref|XP_021334709|]
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tensin-1 isoform X6 [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 145-303 4.30e-115

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.


The actual alignment was detected with superfamily member cd14560:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 159  Bit Score: 360.45  E-value: 4.30e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103  145 DLVYITERIISVTFPSNAEEPSYSANIKEVANMLRSKHGDNYLLFNLSEKRLDISKLNPKVLDFGWPDHHAPALDKICSI 224
Cdd:cd14560      1 DLVYITERIISVSFPSTAEEPSFRSNLKEVAQMLKSKHGDNYLLFNLSERRHDISKLHPKVLDFGWPDLHAPALEKICSI 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207186103  225 CKAMDTWMNAGSHNVVVIHNKGNRGRTGVVVAAYMHYSNISASADQALDRFAMKRFYEDKVLPVGQPSQRRYVQYFSGL 303
Cdd:cd14560     81 CKAMDTWLNADPHNVVVIHNKGNRGRTGVVIAAYMHYSNISASADQALDRFAMKRFYEDKVVPVGQPSQKRYVHYFSGL 159
PTB_tensin cd01213
Tensin Phosphotyrosine-binding (PTB) domain; Tensin is a a focal adhesion protein, which ...
 1664-1796 1.38e-79

Tensin Phosphotyrosine-binding (PTB) domain; Tensin is a a focal adhesion protein, which contains a C-terminal SH2 domain followed by a PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


:

Pssm-ID: 269924  Cd Length: 136  Bit Score: 258.33  E-value: 1.38e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1664 GHACNVLYINSVDMESLTGPQAIAKAISETMNASPAPSATIVHFKVSAQGITLTDNQRKLFFRRHYPIGTVTFCDIDPQE 1743
Cdd:cd01213      1 GAACNVLYLGSVDTESLTGPQAVRKAVSETLERDPLPTPTVVHFKVSEQGITLTDNQRKLFFRRHYPLNTVSFCGMDPEN 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207186103 1744 RKWNKPE---GGTAKFFGFVARKQGSTTDNVSHLFAEMDPDQPATAIVNFVSKVMI 1796
Cdd:cd01213     81 RKWQKYDlrgSKPSRIFGFVARKQGSSTENVCHLFAELDPEQPASAIVNFVNKVLL 136
SH2_Tensin_like cd09927
Src homology 2 domain found in Tensin-like proteins; SH2 domain found in Tensin-like proteins. ...
 1518-1633 1.42e-71

Src homology 2 domain found in Tensin-like proteins; SH2 domain found in Tensin-like proteins. The Tensins are a family of intracellular proteins that interact with receptor tyrosine kinases (RTKs), integrins, and actin. They are thought act as signaling bridges between the extracellular space and the cytoskeleton. There are four homologues: Tensin1, Tensin2 (TENC1, C1-TEN), Tensin3 and Tensin4 (cten), all of which contain a C-terminal tandem SH2-PTB domain pairing, as well as actin-binding regions that may localize them to focal adhesions. The isoforms of Tensin2 and Tensin3 contain N-terminal C1 domains, which are atypical and not expected to bind to phorbol esters. Tensins 1-3 contain a phosphatase (PTPase) and C2 domain pairing which resembles PTEN (phosphatase and tensin homologue deleted on chromosome 10) protein. PTEN is a lipid phosphatase that dephosphorylates phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) to yield phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). As PtdIns(3,4,5)P3 is the product of phosphatidylinositol 3-kinase (PI3K) activity, PTEN is therefore a key negative regulator of the PI3K pathway. Because of their PTEN-like domains, the Tensins may also possess phosphoinositide-binding or phosphatase capabilities. However, only Tensin2 and Tensin3 have the potential to be phosphatases since only their PTPase domains contain a cysteine residue that is essential for catalytic activity. 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: 198181 [Multi-domain]  Cd Length: 116  Bit Score: 234.63  E-value: 1.42e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1518 TSKFWYKPDISRDQAINMLKDQDPGAFVIRDSHSFRGAYGLAMKVASPPPTTQPTKKAGDVTNELVRHFLIETSPKGVRL 1597
Cdd:cd09927      1 TSKYWYKPNISRDQAIALLKDKPPGTFLVRDSTTYKGAYGLAVKVATPPPGVNPFEAKGDPESELVRHFLIEPSPKGVKL 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1207186103 1598 KGCPNEPYFGCLSALVYQHSITPLALPCKLVIPTRD 1633
Cdd:cd09927     81 KGCPNEPVFGSLSALVYQHSITPLALPCKLRIPDRD 116
PTEN_C2 pfam10409
C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key ...
 310-436 1.09e-48

C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key form, of the PTEN protein, phosphatidyl-inositol triphosphate phosphatase, and it is the C-terminus. This domain may well include a CBR3 loop which means it plays a central role in membrane binding. This domain associates across an extensive interface with the N-terminal phosphatase domain DSPc (pfam00782) suggesting that the C2 domain productively positions the catalytic part of the protein onto the membrane.


:

Pssm-ID: 463081  Cd Length: 133  Bit Score: 169.77  E-value: 1.09e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103  310 INNKPLFLHHVIMHGIPNFESKGGCRPFLKIYQAMQPV-YTSGIYNVQGDSQTSICITIEP-GLLLKGDILLKCYHKRFR 387
Cdd:pfam10409    1 PPPKPLTLHSIILHGIPNFKSGGGCRPYIRIYQNKKKVfSTSGKYKKLKEYQQDDCVILFPkGIPVQGDVLVEFYHKGSD 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207186103  388 SPCRDVIFRVQFHTCAVHDLGIVFGKDELDETFKD---DRFPEYGKVEFVFS 436
Cdd:pfam10409   81 LLSEEKMFRFWFNTSFIEDNTLTLPKNELDKADKDkkdKRFPKDFKVELLFS 132
C1_TNS1_v cd20888
protein kinase C conserved region 1 (C1 domain) found in tensin-1 (TNS1) variant and similar ...
 40-96 1.49e-28

protein kinase C conserved region 1 (C1 domain) found in tensin-1 (TNS1) variant and similar proteins; Tensin-1 (TNS1) plays a role in fibrillar adhesion formation. It may be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton. This model corresponds to the C1 domain found in TNS1 variant. Typical TNS1 does not contain C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


:

Pssm-ID: 410438  Cd Length: 57  Bit Score: 109.58  E-value: 1.49e-28
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207186103   40 EAVHSHTFRLKTFKKGKHCGVCKQTVNNEGLICRVCRLACHRKCEVKVSSSCVPVAN 96
Cdd:cd20888      1 EAPHTHTFKVKTFKKVKSCGICKQAITREGSTCRVCKLSCHKKCEAKVATPCVPAVN 57
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 806-1171 1.93e-06

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.40  E-value: 1.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103  806 PALTQVPkshSAPSGESGVVTTQPSFSQTQARPSYQADT---------AIHDRGAASSMGFPLTFQQVTGEPSQPTMKQQ 876
Cdd:PHA03247  2483 PAEARFP---FAAGAAPDPGGGGPPDPDAPPAPSRLAPAilpdepvgePVHPRMLTWIRGLEELASDDAGDPPPPLPPAA 2559

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103  877 KPTTTSQHV---EFASEAGGQAPMSQSTVPSSTfgvlqlkplniyPSSTTSQSPEPQETQRSYSSSSSPLPKESEPED-- 951
Cdd:PHA03247  2560 PPAAPDRSVpppRPAPRPSEPAVTSRARRPDAP------------PQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDpp 2627

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103  952 ----SSYKLEGLVAHRVAGLPSGEmsPDEAAVPGRCRTLSEGLSQDESPTRGSSVRSPIRCISPE----LANTIALNPGG 1023
Cdd:PHA03247  2628 ppspSPAANEPDPHPPPTVPPPER--PRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPtvgsLTSLADPPPPP 2705

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1024 RPKERHMH-------------SYREAFEEMDGGPVsPPPIVGGEVLPQTPAFPVSPQTPYFNMCRSPP-GLAKTPLSFLG 1089
Cdd:PHA03247  2706 PTPEPAPHalvsatplppgpaAARQASPALPAAPA-PPAVPAGPATPGGPARPARPPTTAGPPAPAPPaAPAAGPPRRLT 2784

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1090 LKPHNPAEILLNQTGSESEDEEEPrsyvesVAKAAAVPASPTYDSDSLARPAGPSHAYNAPLSSSSPIQNPDPVESTLAD 1169
Cdd:PHA03247  2785 RPAVASLSESRESLPSPWDPADPP------AAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAP 2858


                   ..
gi 1207186103 1170 SG 1171
Cdd:PHA03247  2859 GG 2860
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 1112-1506 9.62e-04

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.39  E-value: 9.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1112 EPRSYVESVAKAAAVPASPTYDSDSLARPAGPSHAYNAPLSSSSPIQNPDPVESTLADSGVGMNSLSQAAVDIFHFQPSE 1191
Cdd:PHA03307    62 CDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPV 141

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1192 ipyQPPPPPYPTSMLGSYISPSPAEAMQNNTTTIQPLSGSPGTRHHTILSDMASVPNFQHRLANQDGPILGRQ--QAPAN 1269
Cdd:PHA03307   142 ---GSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSpiSASAS 218

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1270 GHVPGIAGSPVQGRHTMVSQGTQSSPILSRQYPVTQGIQSSPILSRQPMGQAVQSSPVLNRQASLNQANQSSPVLSRqqs 1349
Cdd:PHA03307   219 SPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERS--- 295

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1350 itlpnqGSPVLSRQSSLSHPSQGSPVLGRHPSLTQGSPSLDR-----HPMYSGYTTPEERHGALSRQSSSSGYQPPSTPS 1424
Cdd:PHA03307   296 ------PSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSssessRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRP 369

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1425 FPVSPAGYIEGAGFRQGSPAFQPQLPEKRRMssSDRTngglsyGTLNGKMSSPVSSGGSTPSVHFFHTLPdfskLNMCDG 1504
Cdd:PHA03307   370 RPSRAPSSPAASAGRPTRRRARAAVAGRARR--RDAT------GRFPAGRPRPSPLDAGAASGAFYARYP----LLTPSG 437


                   ..
gi 1207186103 1505 SP 1506
Cdd:PHA03307   438 EP 439
 
Name Accession Description Interval E-value
PTP_tensin-1 cd14560
protein tyrosine phosphatase-like domain of tensin-1; Tensin-1 (TNS1) is part of the tensin ...
 145-303 4.30e-115

protein tyrosine phosphatase-like domain of tensin-1; Tensin-1 (TNS1) is part of the tensin family of intracellular proteins (tensin-1, -2, -3 and -4), which act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. It plays an essential role in TGF-beta-induced myofibroblast differentiation and myofibroblast-mediated formation of extracellular fibronectin and collagen matrix. It also positively regulates RhoA activity through its interaction with DLC1, a RhoGAP-containing tumor suppressor; the tensin-1-DLC1-RhoA signaling axis is critical in regulating cellular functions that lead to angiogenesis. Tensin-1 contains an N-terminal region with a protein tyrosine phosphatase (PTP)-like domain followed by a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains.


Pssm-ID: 350408 [Multi-domain]  Cd Length: 159  Bit Score: 360.45  E-value: 4.30e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103  145 DLVYITERIISVTFPSNAEEPSYSANIKEVANMLRSKHGDNYLLFNLSEKRLDISKLNPKVLDFGWPDHHAPALDKICSI 224
Cdd:cd14560      1 DLVYITERIISVSFPSTAEEPSFRSNLKEVAQMLKSKHGDNYLLFNLSERRHDISKLHPKVLDFGWPDLHAPALEKICSI 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207186103  225 CKAMDTWMNAGSHNVVVIHNKGNRGRTGVVVAAYMHYSNISASADQALDRFAMKRFYEDKVLPVGQPSQRRYVQYFSGL 303
Cdd:cd14560     81 CKAMDTWLNADPHNVVVIHNKGNRGRTGVVIAAYMHYSNISASADQALDRFAMKRFYEDKVVPVGQPSQKRYVHYFSGL 159
PTB_tensin cd01213
Tensin Phosphotyrosine-binding (PTB) domain; Tensin is a a focal adhesion protein, which ...
 1664-1796 1.38e-79

Tensin Phosphotyrosine-binding (PTB) domain; Tensin is a a focal adhesion protein, which contains a C-terminal SH2 domain followed by a PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269924  Cd Length: 136  Bit Score: 258.33  E-value: 1.38e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1664 GHACNVLYINSVDMESLTGPQAIAKAISETMNASPAPSATIVHFKVSAQGITLTDNQRKLFFRRHYPIGTVTFCDIDPQE 1743
Cdd:cd01213      1 GAACNVLYLGSVDTESLTGPQAVRKAVSETLERDPLPTPTVVHFKVSEQGITLTDNQRKLFFRRHYPLNTVSFCGMDPEN 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207186103 1744 RKWNKPE---GGTAKFFGFVARKQGSTTDNVSHLFAEMDPDQPATAIVNFVSKVMI 1796
Cdd:cd01213     81 RKWQKYDlrgSKPSRIFGFVARKQGSSTENVCHLFAELDPEQPASAIVNFVNKVLL 136
SH2_Tensin_like cd09927
Src homology 2 domain found in Tensin-like proteins; SH2 domain found in Tensin-like proteins. ...
 1518-1633 1.42e-71

Src homology 2 domain found in Tensin-like proteins; SH2 domain found in Tensin-like proteins. The Tensins are a family of intracellular proteins that interact with receptor tyrosine kinases (RTKs), integrins, and actin. They are thought act as signaling bridges between the extracellular space and the cytoskeleton. There are four homologues: Tensin1, Tensin2 (TENC1, C1-TEN), Tensin3 and Tensin4 (cten), all of which contain a C-terminal tandem SH2-PTB domain pairing, as well as actin-binding regions that may localize them to focal adhesions. The isoforms of Tensin2 and Tensin3 contain N-terminal C1 domains, which are atypical and not expected to bind to phorbol esters. Tensins 1-3 contain a phosphatase (PTPase) and C2 domain pairing which resembles PTEN (phosphatase and tensin homologue deleted on chromosome 10) protein. PTEN is a lipid phosphatase that dephosphorylates phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) to yield phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). As PtdIns(3,4,5)P3 is the product of phosphatidylinositol 3-kinase (PI3K) activity, PTEN is therefore a key negative regulator of the PI3K pathway. Because of their PTEN-like domains, the Tensins may also possess phosphoinositide-binding or phosphatase capabilities. However, only Tensin2 and Tensin3 have the potential to be phosphatases since only their PTPase domains contain a cysteine residue that is essential for catalytic activity. 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: 198181 [Multi-domain]  Cd Length: 116  Bit Score: 234.63  E-value: 1.42e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1518 TSKFWYKPDISRDQAINMLKDQDPGAFVIRDSHSFRGAYGLAMKVASPPPTTQPTKKAGDVTNELVRHFLIETSPKGVRL 1597
Cdd:cd09927      1 TSKYWYKPNISRDQAIALLKDKPPGTFLVRDSTTYKGAYGLAVKVATPPPGVNPFEAKGDPESELVRHFLIEPSPKGVKL 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1207186103 1598 KGCPNEPYFGCLSALVYQHSITPLALPCKLVIPTRD 1633
Cdd:cd09927     81 KGCPNEPVFGSLSALVYQHSITPLALPCKLRIPDRD 116
PTEN_C2 pfam10409
C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key ...
 310-436 1.09e-48

C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key form, of the PTEN protein, phosphatidyl-inositol triphosphate phosphatase, and it is the C-terminus. This domain may well include a CBR3 loop which means it plays a central role in membrane binding. This domain associates across an extensive interface with the N-terminal phosphatase domain DSPc (pfam00782) suggesting that the C2 domain productively positions the catalytic part of the protein onto the membrane.


Pssm-ID: 463081  Cd Length: 133  Bit Score: 169.77  E-value: 1.09e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103  310 INNKPLFLHHVIMHGIPNFESKGGCRPFLKIYQAMQPV-YTSGIYNVQGDSQTSICITIEP-GLLLKGDILLKCYHKRFR 387
Cdd:pfam10409    1 PPPKPLTLHSIILHGIPNFKSGGGCRPYIRIYQNKKKVfSTSGKYKKLKEYQQDDCVILFPkGIPVQGDVLVEFYHKGSD 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207186103  388 SPCRDVIFRVQFHTCAVHDLGIVFGKDELDETFKD---DRFPEYGKVEFVFS 436
Cdd:pfam10409   81 LLSEEKMFRFWFNTSFIEDNTLTLPKNELDKADKDkkdKRFPKDFKVELLFS 132
PTB pfam08416
Phosphotyrosine-binding domain; The phosphotyrosine-binding domain (PTB, also ...
 1666-1801 4.89e-40

Phosphotyrosine-binding domain; The phosphotyrosine-binding domain (PTB, also phosphotyrosine-interaction or PI domain) in the protein tensin tends to be found at the C-terminus. Tensin is a multi-domain protein that binds to actin filaments and functions as a focal-adhesion molecule (focal adhesions are regions of plasma membrane through which cells attach to the extracellular matrix). Human tensin has actin-binding sites, an SH2 (pfam00017) domain and a region similar to the tumour suppressor PTEN. The PTB domain interacts with the cytoplasmic tails of beta integrin by binding to an NPXY motif.


Pssm-ID: 429984  Cd Length: 131  Bit Score: 144.80  E-value: 4.89e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1666 ACNVLYINSVDMESLTGPQAIAKAI--SETMNASPAPSATIVHFKVSAQGITLTDNQRKLFFrRHYPIGTVTFCDIDPQE 1743
Cdd:pfam08416    1 QYRVEHLTTFELDSLTGLQAVEDAIrkLQLLDAQGRVWTQEMLLQVSDQGITLTDNETKEEL-ESYPLDSISHCQAVLND 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1744 RKWNkpeggtaKFFGFVARKQGSTTDNVsHLFA--EMDPDQPATAIVNFVSKVMISSQKR 1801
Cdd:pfam08416   80 GRYN-------SILALVCQEPGQSKPDV-HLFQcdELGAELIAEDIESALSDVRLGKPKK 131
C1_TNS1_v cd20888
protein kinase C conserved region 1 (C1 domain) found in tensin-1 (TNS1) variant and similar ...
 40-96 1.49e-28

protein kinase C conserved region 1 (C1 domain) found in tensin-1 (TNS1) variant and similar proteins; Tensin-1 (TNS1) plays a role in fibrillar adhesion formation. It may be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton. This model corresponds to the C1 domain found in TNS1 variant. Typical TNS1 does not contain C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410438  Cd Length: 57  Bit Score: 109.58  E-value: 1.49e-28
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207186103   40 EAVHSHTFRLKTFKKGKHCGVCKQTVNNEGLICRVCRLACHRKCEVKVSSSCVPVAN 96
Cdd:cd20888      1 EAPHTHTFKVKTFKKVKSCGICKQAITREGSTCRVCKLSCHKKCEAKVATPCVPAVN 57
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 1663-1801 2.20e-18

Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains.


Pssm-ID: 214675  Cd Length: 134  Bit Score: 83.13  E-value: 2.20e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103  1663 DGHACNVLYINSVDMESLTGPQAIAKAISE--TMNASPAPSATIVHFKVSAQGITLTDNQRKlFFRRHYPIGTVTFCDID 1740
Cdd:smart00462    2 SGVSFRVKYLGSVEVPEARGLQVVQEAIRKlrAAQGSEKKEPQKVILSISSRGVKLIDEDTK-AVLHEHPLRRISFCAVG 80

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207186103  1741 PQerkwnkpeggTAKFFGFVARKQGStTDNVSHLFAEMDP--DQPATAIVNFVSKVMISSQKR 1801
Cdd:smart00462   81 PD----------DLDVFGYIARDPGS-SRFACHVFRCEKAaeDIALAIGQAFQLAYELKLKAR 132
SH2 smart00252
Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides ...
 1522-1621 3.63e-13

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: 66.48  E-value: 3.63e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103  1522 WYKPDISRDQAINMLKDQDPGAFVIRDSHSFRGAYGLAMKVaspppttqptkkagdvtNELVRHFLIETSPKGVRlkGCP 1601
Cdd:smart00252    3 WYHGFISREEAEKLLKNEGDGDFLVRDSESSPGDYVLSVRV-----------------KGKVKHYRIRRNEDGKF--YLE 63

                            90       100
                    ....*....|....*....|
gi 1207186103  1602 NEPYFGCLSALVYQHSITPL 1621
Cdd:smart00252   64 GGRKFPSLVELVEHYQKNSL 83
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
208-323 3.51e-11

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 61.61  E-value: 3.51e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103   208 FGWPDHHAPAL-DKICSICKAMDTWMNA-GSHNVVVIHNKGNRGRTGVVVAAYMHYSNIsasadqaldrfaMKRFYEDKV 285
Cdd:smart00404    8 TGWPDHGVPESpDSILELLRAVKKNLNQsESSGPVVVHCSAGVGRTGTFVAIDILLQQL------------EAEAGEVDI 75

                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 1207186103   286 LpvgqpsqrRYVQYFSGLLSGHIKINNKPLFLHHVIMH 323
Cdd:smart00404   76 F--------DTVKELRSQRPGMVQTEEQYLFLYRALLE 105
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
210-300 3.15e-09

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 57.29  E-value: 3.15e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103  210 WPDHHAPALDKICSICKAMDTWMNAGSHnvVVIHNKGNRGRTGVVVAAYMHYSNIsaSADQALDRFAMKRfyeDKVLPvg 289
Cdd:COG2453     55 IPDFGAPDDEQLQEAVDFIDEALREGKK--VLVHCRGGIGRTGTVAAAYLVLLGL--SAEEALARVRAAR---PGAVE-- 125

                           90
                   ....*....|.
gi 1207186103  290 QPSQRRYVQYF 300
Cdd:COG2453    126 TPAQRAFLERF 136
SH2 pfam00017
SH2 domain;
1522-1616 6.49e-09

SH2 domain;


Pssm-ID: 425423 [Multi-domain]  Cd Length: 77  Bit Score: 54.14  E-value: 6.49e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1522 WYKPDISRDQAINMLKDQDP-GAFVIRDSHSFRGAYGLAMKvaspppttqptkkagdvTNELVRHFLIETSPKGVRLkgC 1600
Cdd:pfam00017    1 WYHGKISRQEAERLLLNGKPdGTFLVRESESTPGGYTLSVR-----------------DDGKVKHYKIQSTDNGGYY--I 61

                           90
                   ....*....|....*.
gi 1207186103 1601 PNEPYFGCLSALVYQH 1616
Cdd:pfam00017   62 SGGVKFSSLAELVEHY 77
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 45-91 1.16e-08

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 52.47  E-value: 1.16e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1207186103    45 HTFRLKTFKKGKHCGVCKQT---VNNEGLICRVCRLACHRKCEVKVSSSC 91
Cdd:smart00109    1 HKHVFRTFTKPTFCCVCRKSiwgSFKQGLRCSECKVKCHKKCADKVPKAC 50
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 45-93 2.21e-07

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 395079  Cd Length: 53  Bit Score: 48.98  E-value: 2.21e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207186103   45 HTFRLKTFKKGKHCGVCKQTVNNE---GLICRVCRLACHRKCEVKVSSSCVP 93
Cdd:pfam00130    1 HHFVHRNFKQPTFCDHCGEFLWGLgkqGLKCSWCKLNVHKRCHEKVPPECGC 52
PHA03247 PHA03247
large tegument protein UL36; Provisional
 806-1171 1.93e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.40  E-value: 1.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103  806 PALTQVPkshSAPSGESGVVTTQPSFSQTQARPSYQADT---------AIHDRGAASSMGFPLTFQQVTGEPSQPTMKQQ 876
Cdd:PHA03247  2483 PAEARFP---FAAGAAPDPGGGGPPDPDAPPAPSRLAPAilpdepvgePVHPRMLTWIRGLEELASDDAGDPPPPLPPAA 2559

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103  877 KPTTTSQHV---EFASEAGGQAPMSQSTVPSSTfgvlqlkplniyPSSTTSQSPEPQETQRSYSSSSSPLPKESEPED-- 951
Cdd:PHA03247  2560 PPAAPDRSVpppRPAPRPSEPAVTSRARRPDAP------------PQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDpp 2627

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103  952 ----SSYKLEGLVAHRVAGLPSGEmsPDEAAVPGRCRTLSEGLSQDESPTRGSSVRSPIRCISPE----LANTIALNPGG 1023
Cdd:PHA03247  2628 ppspSPAANEPDPHPPPTVPPPER--PRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPtvgsLTSLADPPPPP 2705

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1024 RPKERHMH-------------SYREAFEEMDGGPVsPPPIVGGEVLPQTPAFPVSPQTPYFNMCRSPP-GLAKTPLSFLG 1089
Cdd:PHA03247  2706 PTPEPAPHalvsatplppgpaAARQASPALPAAPA-PPAVPAGPATPGGPARPARPPTTAGPPAPAPPaAPAAGPPRRLT 2784

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1090 LKPHNPAEILLNQTGSESEDEEEPrsyvesVAKAAAVPASPTYDSDSLARPAGPSHAYNAPLSSSSPIQNPDPVESTLAD 1169
Cdd:PHA03247  2785 RPAVASLSESRESLPSPWDPADPP------AAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAP 2858


                   ..
gi 1207186103 1170 SG 1171
Cdd:PHA03247  2859 GG 2860
PRK12361 PRK12361
hypothetical protein; Provisional
 197-273 9.03e-04

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 43.84  E-value: 9.03e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207186103  197 DISKLNPKVLDfgwpdHHAPALDKICSICKAMDTWMNAGSHnvVVIHNKGNRGRTGVVVAAYMHYSNISASADQALD 273
Cdd:PRK12361   142 DIDYLNIPILD-----HSVPTLAQLNQAINWIHRQVRANKS--VVVHCALGRGRSVLVLAAYLLCKDPDLTVEEVLQ 211
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 1112-1506 9.62e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.39  E-value: 9.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1112 EPRSYVESVAKAAAVPASPTYDSDSLARPAGPSHAYNAPLSSSSPIQNPDPVESTLADSGVGMNSLSQAAVDIFHFQPSE 1191
Cdd:PHA03307    62 CDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPV 141

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1192 ipyQPPPPPYPTSMLGSYISPSPAEAMQNNTTTIQPLSGSPGTRHHTILSDMASVPNFQHRLANQDGPILGRQ--QAPAN 1269
Cdd:PHA03307   142 ---GSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSpiSASAS 218

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1270 GHVPGIAGSPVQGRHTMVSQGTQSSPILSRQYPVTQGIQSSPILSRQPMGQAVQSSPVLNRQASLNQANQSSPVLSRqqs 1349
Cdd:PHA03307   219 SPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERS--- 295

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1350 itlpnqGSPVLSRQSSLSHPSQGSPVLGRHPSLTQGSPSLDR-----HPMYSGYTTPEERHGALSRQSSSSGYQPPSTPS 1424
Cdd:PHA03307   296 ------PSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSssessRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRP 369

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1425 FPVSPAGYIEGAGFRQGSPAFQPQLPEKRRMssSDRTngglsyGTLNGKMSSPVSSGGSTPSVHFFHTLPdfskLNMCDG 1504
Cdd:PHA03307   370 RPSRAPSSPAASAGRPTRRRARAAVAGRARR--RDAT------GRFPAGRPRPSPLDAGAASGAFYARYP----LLTPSG 437


                   ..
gi 1207186103 1505 SP 1506
Cdd:PHA03307   438 EP 439
 
Name Accession Description Interval E-value
PTP_tensin-1 cd14560
protein tyrosine phosphatase-like domain of tensin-1; Tensin-1 (TNS1) is part of the tensin ...
 145-303 4.30e-115

protein tyrosine phosphatase-like domain of tensin-1; Tensin-1 (TNS1) is part of the tensin family of intracellular proteins (tensin-1, -2, -3 and -4), which act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. It plays an essential role in TGF-beta-induced myofibroblast differentiation and myofibroblast-mediated formation of extracellular fibronectin and collagen matrix. It also positively regulates RhoA activity through its interaction with DLC1, a RhoGAP-containing tumor suppressor; the tensin-1-DLC1-RhoA signaling axis is critical in regulating cellular functions that lead to angiogenesis. Tensin-1 contains an N-terminal region with a protein tyrosine phosphatase (PTP)-like domain followed by a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains.


Pssm-ID: 350408 [Multi-domain]  Cd Length: 159  Bit Score: 360.45  E-value: 4.30e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103  145 DLVYITERIISVTFPSNAEEPSYSANIKEVANMLRSKHGDNYLLFNLSEKRLDISKLNPKVLDFGWPDHHAPALDKICSI 224
Cdd:cd14560      1 DLVYITERIISVSFPSTAEEPSFRSNLKEVAQMLKSKHGDNYLLFNLSERRHDISKLHPKVLDFGWPDLHAPALEKICSI 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207186103  225 CKAMDTWMNAGSHNVVVIHNKGNRGRTGVVVAAYMHYSNISASADQALDRFAMKRFYEDKVLPVGQPSQRRYVQYFSGL 303
Cdd:cd14560     81 CKAMDTWLNADPHNVVVIHNKGNRGRTGVVIAAYMHYSNISASADQALDRFAMKRFYEDKVVPVGQPSQKRYVHYFSGL 159
PTP_tensin cd14508
protein tyrosine phosphatase-like domain of tensins; The tensin family of intracellular ...
 145-303 3.35e-93

protein tyrosine phosphatase-like domain of tensins; The tensin family of intracellular proteins (tensin-1, -2, -3 and -4) act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. Dysregulation of tensin expression has been implicated in human cancer. Tensin-1, -2, and -3 contain an N-terminal region with a protein tyrosine phosphatase (PTP)-like domain followed by a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains. In addition, tensin-2 contains a zinc finger N-terminal to its PTP domain. Tensin-4 is not included in this model as it does not contain a PTP-like domain.


Pssm-ID: 350358 [Multi-domain]  Cd Length: 159  Bit Score: 298.15  E-value: 3.35e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103  145 DLVYITERIISVTFPSNAEEPSYSANIKEVANMLRSKHGDNYLLFNLSEKRLDISKLNPKVLDFGWPDHHAPALDKICSI 224
Cdd:cd14508      1 DLTYITERIIALSFPSTCSEQTYRHNLREAAHLLQSKHGDNYMVFNLSERRHDLRSLNPKVLDFGWPELHAPPLEKLCSI 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207186103  225 CKAMDTWMNAGSHNVVVIHNKGNRGRTGVVVAAYMHYSNISASADQALDRFAMKRFYEDKVLPVGQPSQRRYVQYFSGL 303
Cdd:cd14508     81 CKNMDSWLNADPQNVVVLHCKGGKGRLGVVVSAYMHYSKISATADQALDRFAMKRFYDDKVGPLGQPSQKRYVGYFSGL 159
PTP_tensin-2 cd14562
protein tyrosine phosphatase-like domain of tensin-2; Tensin-2 (TNS2) is also called ...
 145-303 7.69e-84

protein tyrosine phosphatase-like domain of tensin-2; Tensin-2 (TNS2) is also called tensin-like C1 domain-containing phosphatase (TENC1) or C1 domain-containing phosphatase and tensin homolog (C1-TEN). It is part of the tensin family of intracellular proteins (tensin-1, -2, -3 and -4), which act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. Tensin-2 is an essential component for the maintenance of glomerular basement membrane (GBM) structures. It also modulates cell contractility and remodeling of collagen fibers through the DLC1, a RhoGAP that binds to tensins in focal adhesions. Tensin-2 may have phosphatase activity; it reduces AKT1 phosphorylation. It contains an N-terminal region with a zinc finger, a protein tyrosine phosphatase (PTP)-like domain and a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains.


Pssm-ID: 350410 [Multi-domain]  Cd Length: 159  Bit Score: 271.44  E-value: 7.69e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103  145 DLVYITERIISVTFPSNAEEPSYSANIKEVANMLRSKHGDNYLLFNLSEKRLDISKLNPKVLDFGWPDHHAPALDKICSI 224
Cdd:cd14562      1 DLTYITERIISVFFPPALEEQRYRGNLREVAQMLKSKHEDKYLLFNLSEKRHDITRLNPKVQDFGWPDLHAPPLDKICSI 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207186103  225 CKAMDTWMNAGSHNVVVIHNKGNRGRTGVVVAAYMHYSNISASADQALDRFAMKRFYEDKVLPVGQPSQRRYVQYFSGL 303
Cdd:cd14562     81 CKAMETWLNADPQHVVVLHCKGNKGKTGVIVAAYMHYSKISAGADQALSTLAMRKFCEDKVATSLQPSQRRYISYFGGL 159
PTP_tensin-3 cd14561
protein tyrosine phosphatase-like domain of tensin-3; Tensin-3 (TNS3) is also called ...
 145-303 3.82e-81

protein tyrosine phosphatase-like domain of tensin-3; Tensin-3 (TNS3) is also called tensin-like SH2 domain-containing protein 1 (TENS1) or tumor endothelial marker (TEM6). It is part of the tensin family of intracellular proteins (tensin-1, -2, -3 and -4), which act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. Tensin-3 contributes to cell migration, anchorage-independent growth, tumorigenesis, and metastasis of cancer cells. It cooperates with Dock5, an exchange factor for the small GTPase Rac, for osteoclast activity to ensure the correct organization of podosomes. Tensin-3 contains an N-terminal region with a protein tyrosine phosphatase (PTP)-like domain followed by a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains.


Pssm-ID: 350409 [Multi-domain]  Cd Length: 159  Bit Score: 263.73  E-value: 3.82e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103  145 DLVYITERIISVTFPSNAEEPSYSANIKEVANMLRSKHGDNYLLFNLSEKRLDISKLNPKVLDFGWPDHHAPALDKICSI 224
Cdd:cd14561      1 DLTYITERIIAVSFPADCSEETYLHNLQDVTRMLKSKHGDNYLVLNLSEKRYELTKLNPKIMDVGWPDLHAPPLDKMCTI 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207186103  225 CKAMDTWMNAGSHNVVVIHNKGNRGRTGVVVAAYMHYSNISASADQALDRFAMKRFYEDKVLPVGQPSQRRYVQYFSGL 303
Cdd:cd14561     81 CKAMESWLNSDPLHVVVIHCRGGKGRIGVVISSYMHFTNVSASADQALDRFAMKKFYDDKVSALMQPSQKRYVQFLSGL 159
PTB_tensin cd01213
Tensin Phosphotyrosine-binding (PTB) domain; Tensin is a a focal adhesion protein, which ...
 1664-1796 1.38e-79

Tensin Phosphotyrosine-binding (PTB) domain; Tensin is a a focal adhesion protein, which contains a C-terminal SH2 domain followed by a PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269924  Cd Length: 136  Bit Score: 258.33  E-value: 1.38e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1664 GHACNVLYINSVDMESLTGPQAIAKAISETMNASPAPSATIVHFKVSAQGITLTDNQRKLFFRRHYPIGTVTFCDIDPQE 1743
Cdd:cd01213      1 GAACNVLYLGSVDTESLTGPQAVRKAVSETLERDPLPTPTVVHFKVSEQGITLTDNQRKLFFRRHYPLNTVSFCGMDPEN 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207186103 1744 RKWNKPE---GGTAKFFGFVARKQGSTTDNVSHLFAEMDPDQPATAIVNFVSKVMI 1796
Cdd:cd01213     81 RKWQKYDlrgSKPSRIFGFVARKQGSSTENVCHLFAELDPEQPASAIVNFVNKVLL 136
SH2_Tensin_like cd09927
Src homology 2 domain found in Tensin-like proteins; SH2 domain found in Tensin-like proteins. ...
 1518-1633 1.42e-71

Src homology 2 domain found in Tensin-like proteins; SH2 domain found in Tensin-like proteins. The Tensins are a family of intracellular proteins that interact with receptor tyrosine kinases (RTKs), integrins, and actin. They are thought act as signaling bridges between the extracellular space and the cytoskeleton. There are four homologues: Tensin1, Tensin2 (TENC1, C1-TEN), Tensin3 and Tensin4 (cten), all of which contain a C-terminal tandem SH2-PTB domain pairing, as well as actin-binding regions that may localize them to focal adhesions. The isoforms of Tensin2 and Tensin3 contain N-terminal C1 domains, which are atypical and not expected to bind to phorbol esters. Tensins 1-3 contain a phosphatase (PTPase) and C2 domain pairing which resembles PTEN (phosphatase and tensin homologue deleted on chromosome 10) protein. PTEN is a lipid phosphatase that dephosphorylates phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) to yield phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). As PtdIns(3,4,5)P3 is the product of phosphatidylinositol 3-kinase (PI3K) activity, PTEN is therefore a key negative regulator of the PI3K pathway. Because of their PTEN-like domains, the Tensins may also possess phosphoinositide-binding or phosphatase capabilities. However, only Tensin2 and Tensin3 have the potential to be phosphatases since only their PTPase domains contain a cysteine residue that is essential for catalytic activity. 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: 198181 [Multi-domain]  Cd Length: 116  Bit Score: 234.63  E-value: 1.42e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1518 TSKFWYKPDISRDQAINMLKDQDPGAFVIRDSHSFRGAYGLAMKVASPPPTTQPTKKAGDVTNELVRHFLIETSPKGVRL 1597
Cdd:cd09927      1 TSKYWYKPNISRDQAIALLKDKPPGTFLVRDSTTYKGAYGLAVKVATPPPGVNPFEAKGDPESELVRHFLIEPSPKGVKL 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1207186103 1598 KGCPNEPYFGCLSALVYQHSITPLALPCKLVIPTRD 1633
Cdd:cd09927     81 KGCPNEPVFGSLSALVYQHSITPLALPCKLRIPDRD 116
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 145-303 1.50e-63

protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar proteins; Phosphatase and tensin homolog (PTEN) is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It dephosphorylates phosphoinositide trisphosphate. In addition to PTEN, this family includes tensins, voltage-sensitive phosphatases (VSPs), and auxilins. They all contain a protein tyrosine phosphatase-like domain although not all are active phosphatases. Tensins are intracellular proteins that act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility, and they may or may not have phosphatase activity. VSPs are phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. Auxilins are J domain-containing proteins that facilitate Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles, and they do not exhibit phosphatase activity.


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 213.21  E-value: 1.50e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103  145 DLVYITERIISVTFPSNAE-EPSYSANIKEVANMLRSKHGDNYLLFNLSEKRLDI-SKLNPKVLDFGWPDHHAPALDKIC 222
Cdd:cd14497      1 DLSYITPRIIAMSFPATGYpESLYRNSIDDVANFLNTHHPDHYMIFNLSEEEYDDdSKFEGRVLHYGFPDHHPPPLGLLL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103  223 SICKAMDTWMNAGSHNVVVIHNKGNRGRTGVVVAAYMHYSNISASADQALDRFAMKRFYEdKVLPVGQPSQRRYVQYFSG 302
Cdd:cd14497     81 EIVDDIDSWLSEDPNNVAVVHCKAGKGRTGTVICAYLLYYGQYSTADEALEYFAKKRFKE-GLPGVTIPSQLRYLQYFER 159


                   .
gi 1207186103  303 L 303
Cdd:cd14497    160 L 160
PTEN_C2 pfam10409
C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key ...
 310-436 1.09e-48

C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key form, of the PTEN protein, phosphatidyl-inositol triphosphate phosphatase, and it is the C-terminus. This domain may well include a CBR3 loop which means it plays a central role in membrane binding. This domain associates across an extensive interface with the N-terminal phosphatase domain DSPc (pfam00782) suggesting that the C2 domain productively positions the catalytic part of the protein onto the membrane.


Pssm-ID: 463081  Cd Length: 133  Bit Score: 169.77  E-value: 1.09e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103  310 INNKPLFLHHVIMHGIPNFESKGGCRPFLKIYQAMQPV-YTSGIYNVQGDSQTSICITIEP-GLLLKGDILLKCYHKRFR 387
Cdd:pfam10409    1 PPPKPLTLHSIILHGIPNFKSGGGCRPYIRIYQNKKKVfSTSGKYKKLKEYQQDDCVILFPkGIPVQGDVLVEFYHKGSD 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207186103  388 SPCRDVIFRVQFHTCAVHDLGIVFGKDELDETFKD---DRFPEYGKVEFVFS 436
Cdd:pfam10409   81 LLSEEKMFRFWFNTSFIEDNTLTLPKNELDKADKDkkdKRFPKDFKVELLFS 132
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 145-303 3.40e-44

protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; Phosphatase and tensin homolog (PTEN), also phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN or mutated in multiple advanced cancers 1 (MMAC1), is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It is a critical endogenous inhibitor of phosphoinositide signaling. It dephosphorylates phosphoinositide trisphosphate, and therefore, has the function of negatively regulating Akt. The PTEN/PI3K/AKT pathway regulates the signaling of multiple biological processes such as apoptosis, metabolism, cell proliferation, and cell growth. PTEN contains an N-terminal PIP-binding domain, a protein tyrosine phosphatase (PTP)-like catalytic domain, a regulatory C2 domain responsible for its cellular location, a C-tail containing phosphorylation sites, and a C-terminal PDZ domain.


Pssm-ID: 350359 [Multi-domain]  Cd Length: 158  Bit Score: 157.75  E-value: 3.40e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103  145 DLVYITERIISVTFPSNAEEPSYSANIKEVANMLRSKHGDNYLLFNL-SEKRLDISKLNPKVLDFGWPDHHAPALDKICS 223
Cdd:cd14509      1 DLTYITPNIIAMGFPAEGVEGVYRNPIDDVQRFLETKHKGHYKVYNLcSERSYDPSKFNGRVAEYPFDDHNPPPLELIKP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103  224 ICKAMDTWMNAGSHNVVVIHNKGNRGRTGVVVAAYMHYSNISASADQALDRFAMKRFYEDKVLPVgqPSQRRYVQYFSGL 303
Cdd:cd14509     81 FCEDVDEWLKEDEKNVAAVHCKAGKGRTGVMICCYLLYLGKFPSAKEALDFYGAKRTKNKKGVTI--PSQRRYVYYYSRL 158
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 138-303 4.44e-41

protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase/transmembrane phosphatase with tensin homology; Voltage-sensitive phosphatase (VSP) proteins comprise a family of phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. This family is conserved in deuterostomes; VSP was first identified as a sperm flagellar plasma membrane protein in Ciona intestinalis. Gene duplication events in primates resulted in the presence of paralogs, transmembrane phosphatase with tensin homology (TPTE) and TPTE2, that retain protein domain architecture but, in the case of TPTE, have lost catalytic activity. TPTE, also called cancer/testis antigen 44 (CT44), may play a role in the signal transduction pathways of the endocrine or spermatogenic function of the testis. TPTE2, also called TPTE and PTEN homologous inositol lipid phosphatase (TPIP), occurs in several differentially spliced forms; TPIP alpha displays phosphoinositide 3-phosphatase activity and is localized on the endoplasmic reticulum, while TPIP beta is cytosolic and lacks detectable phosphatase activity. VSP/TPTE proteins contain an N-terminal voltage sensor consisting of four transmembrane segments, a protein tyrosine phosphatase (PTP)-like phosphoinositide phosphatase catalytic domain, followed by a regulatory C2 domain.


Pssm-ID: 350360 [Multi-domain]  Cd Length: 177  Bit Score: 149.82  E-value: 4.44e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103  138 MEENYEVDLVYITERIISVTFPSNAEEPSYSANIKEVANMLRSKHGDNYLLFNL-SEKRLDISKLNPKVLDFGWPDHHAP 216
Cdd:cd14510      8 QKDGFDLDLTYVTDRVIAMSFPSSGKQAFYRNPIEEVVRFLDTKHPDHYKVYNLcSERGYDPKYFHNRVERVPIDDHNVP 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103  217 ALDKICSICKAMDTWMNAGSHNVVVIHNKGNRGRTGVVVAAYMHYSNISASADQALDRFAMKRF---YEDKVLPVGQPSQ 293
Cdd:cd14510     88 TLDEMLSFTAEVREWMAADPKNVVAIHCKGGKGRTGTMVCAWLIYSGQFESAKEALEYFGERRTdksVSSKFQGVETPSQ 167

                          170
                   ....*....|
gi 1207186103  294 RRYVQYFSGL 303
Cdd:cd14510    168 SRYVGYFEKL 177
PTB pfam08416
Phosphotyrosine-binding domain; The phosphotyrosine-binding domain (PTB, also ...
 1666-1801 4.89e-40

Phosphotyrosine-binding domain; The phosphotyrosine-binding domain (PTB, also phosphotyrosine-interaction or PI domain) in the protein tensin tends to be found at the C-terminus. Tensin is a multi-domain protein that binds to actin filaments and functions as a focal-adhesion molecule (focal adhesions are regions of plasma membrane through which cells attach to the extracellular matrix). Human tensin has actin-binding sites, an SH2 (pfam00017) domain and a region similar to the tumour suppressor PTEN. The PTB domain interacts with the cytoplasmic tails of beta integrin by binding to an NPXY motif.


Pssm-ID: 429984  Cd Length: 131  Bit Score: 144.80  E-value: 4.89e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1666 ACNVLYINSVDMESLTGPQAIAKAI--SETMNASPAPSATIVHFKVSAQGITLTDNQRKLFFrRHYPIGTVTFCDIDPQE 1743
Cdd:pfam08416    1 QYRVEHLTTFELDSLTGLQAVEDAIrkLQLLDAQGRVWTQEMLLQVSDQGITLTDNETKEEL-ESYPLDSISHCQAVLND 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1744 RKWNkpeggtaKFFGFVARKQGSTTDNVsHLFA--EMDPDQPATAIVNFVSKVMISSQKR 1801
Cdd:pfam08416   80 GRYN-------SILALVCQEPGQSKPDV-HLFQcdELGAELIAEDIESALSDVRLGKPKK 131
PTP_auxilin-like cd14511
protein tyrosine phosphatase-like domain of auxilin and similar proteins; This subfamily ...
 143-303 1.23e-36

protein tyrosine phosphatase-like domain of auxilin and similar proteins; This subfamily contains proteins similar to auxilin, characterized by also containing a J domain. It includes auxilin, also called auxilin-1, and cyclin-G-associated kinase (GAK), also called auxilin-2. Auxilin-1 and -2 facilitate Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, while auxilin-1 which is nerve-specific. Both proteins contain a protein tyrosine phosphatase (PTP)-like domain similar to the PTP-like domain of PTEN (a phosphoinositide 3-phosphatase), and a C-terminal region with clathrin-binding and J domains. In addition, GAK contains an N-terminal protein kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2.


Pssm-ID: 350361 [Multi-domain]  Cd Length: 164  Bit Score: 136.33  E-value: 1.23e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103  143 EVDLVYITERIISVTFPSNAEEPSYSAN-IKEVANMLRSKHGDNYLLFNLSEKRLDISKLNPKVLDFGWPDHHAPALDKI 221
Cdd:cd14511      8 DLDISYITSRIIVMPFPAEGIESTYRKNnIEDVRAFLDSRHPQKYSVYNLSPRSYPTLRLPSRVVECSWPYRRAPSLHAL 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103  222 CSICKAMDTWMNAGSHNVVVIHNKGNRGRTGVVVAAYMHYSNISASADQALDRFAMKRfyedkvLPVG-QPSQRRYVQYF 300
Cdd:cd14511     88 YALCRDIYQWLNKDPKNVIVIHCTDGKAASATVVCALLVYCGLFKTPEDALQMFAVKR------CPPGlSPSELRYLYYF 161


                   ...
gi 1207186103  301 SGL 303
Cdd:cd14511    162 SDI 164
C1_TNS1_v cd20888
protein kinase C conserved region 1 (C1 domain) found in tensin-1 (TNS1) variant and similar ...
 40-96 1.49e-28

protein kinase C conserved region 1 (C1 domain) found in tensin-1 (TNS1) variant and similar proteins; Tensin-1 (TNS1) plays a role in fibrillar adhesion formation. It may be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton. This model corresponds to the C1 domain found in TNS1 variant. Typical TNS1 does not contain C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410438  Cd Length: 57  Bit Score: 109.58  E-value: 1.49e-28
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207186103   40 EAVHSHTFRLKTFKKGKHCGVCKQTVNNEGLICRVCRLACHRKCEVKVSSSCVPVAN 96
Cdd:cd20888      1 EAPHTHTFKVKTFKKVKSCGICKQAITREGSTCRVCKLSCHKKCEAKVATPCVPAVN 57
PTP_GAK cd14564
protein tyrosine phosphatase-like domain of cyclin-G-associated kinase; cyclin-G-associated ...
 143-299 8.21e-27

protein tyrosine phosphatase-like domain of cyclin-G-associated kinase; cyclin-G-associated kinase (GAK), also called auxilin-2, contains an N-terminal protein kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of a protein tyrosine phosphatase (PTP)-like domain similar to the PTP-like domain of PTEN (a phosphoinositide 3-phosphatase), and a C-terminal region with clathrin-binding and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor.


Pssm-ID: 350412 [Multi-domain]  Cd Length: 163  Bit Score: 108.45  E-value: 8.21e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103  143 EVDLVYITERIISVTFPSNAEEPSYSANIKEVANMLRSKHGDNYLLFNLSEKRLDISKLNPKVLDFGWPDHHAPALDKIC 222
Cdd:cd14564      8 DLDISYITSRIAVMSFPAEGVESAIKNNIEDVRLFLDSRHPGHYAVYNLSQRTYRPSRFHNRVSECGWPARRAPNLQNLY 87

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207186103  223 SICKAMDTWMNAGSHNVVVIHNKGNRGRTGVVVAAYMHYSNISASADQALDRFAMKRfyedkvLPVG-QPSQRRYVQY 299
Cdd:cd14564     88 SICKNMHLWLKQDQKNICIVHCLDGRAASAVVVCSFLCFCRLFTTAEAAVYMFSMKR------CPPGiWPSHKRYIEY 159
PTP_auxilin_N cd14563
N-terminal protein tyrosine phosphatase-like domain of auxilin; Auxilin, also called auxilin-1 ...
 143-303 9.60e-25

N-terminal protein tyrosine phosphatase-like domain of auxilin; Auxilin, also called auxilin-1 or DnaJ homolog subfamily C member 6 (DNAJC6), is a J-domain containing protein that recruits the ATP-dependent chaperone Hsc70 to newly budded clathrin-coated vesicles and promotes uncoating of clathrin-coated vesicles, driving the clathrin assembly#disassembly cycle. Mutations in the DNAJC6 gene, encoding auxilin, are associated with early-onset Parkinson's disease. Auxilin contains an N-terminal protein tyrosine phosphatase (PTP)-like domain similar to the PTP-like domain of PTEN, a phosphoinositide 3-phosphatase, and a C-terminal region with clathrin-binding and J domains.


Pssm-ID: 350411 [Multi-domain]  Cd Length: 163  Bit Score: 102.27  E-value: 9.60e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103  143 EVDLVYITERIISVTFPSNAEEPSYSANIKEVANMLRSKHGDNYLLFNLSEKRLDISKLNPKVLDFGWPDHHAPALDKIC 222
Cdd:cd14563      8 ELDISYITSRIIVMSYPAEGVELGFRNHIEDVRSFLDSRHLDHYTVFNLSQKSYRSAKFHNRVSECSWPVRQAPSLHNLF 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103  223 SICKAMDTWMNAGSHNVVVIHNKGNRGRTGVVVAAYMHYSNISASADQALDRFAMKRfyedkVLPVGQPSQRRYVQYFSG 302
Cdd:cd14563     88 AVCKNMHNWLQQNPKNVCVIHCMDGRAASAVLVSAMFCFCHLFSNPVPAMQLLNAKR-----PGIGLWPSHRRYIGYICD 162


                   .
gi 1207186103  303 L 303
Cdd:cd14563    163 L 163
C1_TNS2-like cd20826
protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; ...
 44-94 8.82e-23

protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; The TNS2-like group includes TNS2, and variants of TNS1 and TNS3. Tensin-2 (TNS2), also called C1 domain-containing phosphatase and tensin (C1-TEN), or tensin-like C1 domain-containing phosphatase (TENC1), is an essential component for the maintenance of glomerular basement membrane (GBM) structures. It regulates cell motility and proliferation. It may have phosphatase activity. TNS2 reduces AKT1 phosphorylation, lowers AKT1 kinase activity and interferes with AKT1 signaling. Tensin-1 (TNS1) plays a role in fibrillar adhesion formation. It may be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton. Tensin-3 (TNS3), also called tensin-like SH2 domain-containing protein 1 (TENS1), or tumor endothelial marker 6 (TEM6), may play a role in actin remodeling. It is involved in the dissociation of the integrin-tensin-actin complex. Typical TNS1 and TNS3 do not contain C1 domains, but some isoforms/variants do. Members of this family contain an N-terminal region with a zinc finger (C1 domain), a protein tyrosine phosphatase (PTP)-like domain and a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410376  Cd Length: 52  Bit Score: 92.84  E-value: 8.82e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207186103   44 SHTFRLKTFKKGKHCGVCKQTVNNEGLICRVCRLACHRKCEVKVSSSCVPV 94
Cdd:cd20826      2 SHSFKEKSFRKPRTCDVCKQIIWNEGSSCRVCKYACHRKCEPKVTAACSPS 52
C1_TNS3_v cd20889
protein kinase C conserved region 1 (C1 domain) found in tensin-3 (TNS3) variant and similar ...
 44-98 3.69e-22

protein kinase C conserved region 1 (C1 domain) found in tensin-3 (TNS3) variant and similar proteins; Tensin-3 (TNS3), also called tensin-like SH2 domain-containing protein 1 (TENS1), or tumor endothelial marker 6 (TEM6), may play a role in actin remodeling. It is involved in the dissociation of the integrin-tensin-actin complex. This model corresponds to the C1 domain found in TNS3 variant. Typical TNS3 does not contain C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410439  Cd Length: 56  Bit Score: 91.10  E-value: 3.69e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1207186103   44 SHTFRLKTFKKGKHCGVCKQTVNNEGLICRVCRLACHRKCEVKVSSSCVPVANYE 98
Cdd:cd20889      2 SHTFKNKTFKKPKVCSICKQVIDSQGISCRVCKYACHKKCEAKVVTPCFPPVNYE 56
C1_TNS2 cd20887
protein kinase C conserved region 1 (C1 domain) found in tensin-2 and similar proteins; ...
 45-93 2.51e-19

protein kinase C conserved region 1 (C1 domain) found in tensin-2 and similar proteins; Tensin-2 (TNS2), also called C1 domain-containing phosphatase and tensin (C1-TEN), or tensin-like C1 domain-containing phosphatase (TENC1), is an essential component for the maintenance of glomerular basement membrane (GBM) structures. It regulates cell motility and proliferation. It may have phosphatase activity. TNS2 reduces AKT1 phosphorylation, lowers AKT1 kinase activity, and interferes with AKT1 signaling. It contains an N-terminal region with a zinc finger (C1 domain), a protein tyrosine phosphatase (PTP)-like domain and a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410437  Cd Length: 53  Bit Score: 82.91  E-value: 2.51e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1207186103   45 HTFRLKTFKKGKHCGVCKQTVNNEGLICRVCRLACHRKCEVKVSSSCVP 93
Cdd:cd20887      3 HSFKEKTFKKKRACAVCREPVGGQGLVCRVCKVASHKKCEAKVTSACQP 51
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 1663-1801 2.20e-18

Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains.


Pssm-ID: 214675  Cd Length: 134  Bit Score: 83.13  E-value: 2.20e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103  1663 DGHACNVLYINSVDMESLTGPQAIAKAISE--TMNASPAPSATIVHFKVSAQGITLTDNQRKlFFRRHYPIGTVTFCDID 1740
Cdd:smart00462    2 SGVSFRVKYLGSVEVPEARGLQVVQEAIRKlrAAQGSEKKEPQKVILSISSRGVKLIDEDTK-AVLHEHPLRRISFCAVG 80

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207186103  1741 PQerkwnkpeggTAKFFGFVARKQGStTDNVSHLFAEMDP--DQPATAIVNFVSKVMISSQKR 1801
Cdd:smart00462   81 PD----------DLDVFGYIARDPGS-SRFACHVFRCEKAaeDIALAIGQAFQLAYELKLKAR 132
SH2 cd00173
Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they ...
 1522-1616 1.08e-14

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: 70.56  E-value: 1.08e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1522 WYKPDISRDQAINMLKDQDPGAFVIRDSHSFRGAYGLAMKVAspppttqptkkagdvtNELVRHFLIETSPKGVRLKGCP 1601
Cdd:cd00173      2 WFHGSISREEAERLLRGKPDGTFLVRESSSEPGDYVLSVRSG----------------DGKVKHYLIERNEGGYYLLGGS 65

                           90
                   ....*....|....*
gi 1207186103 1602 NePYFGCLSALVYQH 1616
Cdd:cd00173     66 G-RTFPSLPELVEHY 79
SH2 smart00252
Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides ...
 1522-1621 3.63e-13

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: 66.48  E-value: 3.63e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103  1522 WYKPDISRDQAINMLKDQDPGAFVIRDSHSFRGAYGLAMKVaspppttqptkkagdvtNELVRHFLIETSPKGVRlkGCP 1601
Cdd:smart00252    3 WYHGFISREEAEKLLKNEGDGDFLVRDSESSPGDYVLSVRV-----------------KGKVKHYRIRRNEDGKF--YLE 63

                            90       100
                    ....*....|....*....|
gi 1207186103  1602 NEPYFGCLSALVYQHSITPL 1621
Cdd:smart00252   64 GGRKFPSLVELVEHYQKNSL 83
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
 45-91 2.65e-12

protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.


Pssm-ID: 410341  Cd Length: 50  Bit Score: 62.92  E-value: 2.65e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207186103   45 HTFRLKTFKKGKHCGVCKQTV---NNEGLICRVCRLACHRKCEVKVSSSC 91
Cdd:cd00029      1 HRFVPTTFSSPTFCDVCGKLIwglFKQGLKCSDCGLVCHKKCLDKAPSPC 50
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
208-323 3.51e-11

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 61.61  E-value: 3.51e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103   208 FGWPDHHAPAL-DKICSICKAMDTWMNA-GSHNVVVIHNKGNRGRTGVVVAAYMHYSNIsasadqaldrfaMKRFYEDKV 285
Cdd:smart00404    8 TGWPDHGVPESpDSILELLRAVKKNLNQsESSGPVVVHCSAGVGRTGTFVAIDILLQQL------------EAEAGEVDI 75

                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 1207186103   286 LpvgqpsqrRYVQYFSGLLSGHIKINNKPLFLHHVIMH 323
Cdd:smart00404   76 F--------DTVKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 208-323 3.51e-11

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine phosphatases. Homologues detected by this profile and not by those of "PTPc" or "DSPc" are predicted to be protein phosphatases with a similar fold to DSPs and PTPs, yet with unpredicted specificities.


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 61.61  E-value: 3.51e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103   208 FGWPDHHAPAL-DKICSICKAMDTWMNA-GSHNVVVIHNKGNRGRTGVVVAAYMHYSNIsasadqaldrfaMKRFYEDKV 285
Cdd:smart00012    8 TGWPDHGVPESpDSILELLRAVKKNLNQsESSGPVVVHCSAGVGRTGTFVAIDILLQQL------------EAEAGEVDI 75

                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 1207186103   286 LpvgqpsqrRYVQYFSGLLSGHIKINNKPLFLHHVIMH 323
Cdd:smart00012   76 F--------DTVKELRSQRPGMVQTEEQYLFLYRALLE 105
C1_MgcRacGAP cd20821
protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and ...
 45-95 4.38e-11

protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and similar proteins; MgcRacGAP, also called Rac GTPase-activating protein 1 (RACGAP1) or protein CYK4, plays an important dual role in cytokinesis: i) it is part of centralspindlin-complex, together with the mitotic kinesin MKLP1, which is critical for the structure of the central spindle by promoting microtuble bundling; and ii) after phosphorylation by aurora B, MgcRacGAP becomes an effective regulator of RhoA and plays an important role in the assembly of the contractile ring and the initiation of cytokinesis. MgcRacGAP-like proteins contain an N-terminal C1 domain, and a C-terminal RhoGAP domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410371  Cd Length: 55  Bit Score: 59.73  E-value: 4.38e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207186103   45 HTFRLKTFKKGKHCGVCKQTV--NNEGLICRVCRLACHRKCEVKVSSSCVPVA 95
Cdd:cd20821      3 HRFVSKTVIKPETCVVCGKRIkfGKKALKCKDCRVVCHPDCKDKLPLPCVPTS 55
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 1665-1795 1.36e-09

Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to bind peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains.


Pssm-ID: 269911  Cd Length: 120  Bit Score: 57.52  E-value: 1.36e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1665 HACNVLYINSVDMESLTGPQAIAKAISETMNA--SPAPSATIVHFKVSAQGITLTDNQRKLFFRRHyPIGTVTFCDIDPQ 1742
Cdd:cd00934      1 ASFQVKYLGSVEVGSSRGVDVVEEALKALAAAlkSSKRKPGPVLLEVSSKGVKLLDLDTKELLLRH-PLHRISYCGRDPD 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207186103 1743 ERKWnkpeggtakfFGFVARKQGStTDNVSHLFAEMDPDQpATAIVNFVSKVM 1795
Cdd:cd00934     80 NPNV----------FAFIAGEEGG-SGFRCHVFQCEDEEE-AEEILQAIGQAF 120
C1_SpBZZ1-like cd20824
protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein ...
 44-91 2.19e-09

protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein BZZ1 and similar proteins; BZZ1 is a syndapin-like F-BAR protein that plays a role in endocytosis and trafficking to the vacuole. It functions with type I myosins to restore polarity of the actin cytoskeleton after NaCl stress. BZZ1 contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), a central coiled-coil, and two C-terminal SH3 domains. Schizosaccharomyces pombe BZZ1 also harbors a C1 domain, but Saccharomyces cerevisiae BZZ1 doesn't have any. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410374  Cd Length: 53  Bit Score: 54.63  E-value: 2.19e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207186103   44 SHTFRLKTFKKGKHCGVCKQTV---NNEGLICRVCRLACHRKCEVKVSSSC 91
Cdd:cd20824      1 PHNFKPHSFSIPTKCDYCGEKIwglSKKGLSCKDCGFNCHIKCELKVPPEC 51
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
210-300 3.15e-09

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 57.29  E-value: 3.15e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103  210 WPDHHAPALDKICSICKAMDTWMNAGSHnvVVIHNKGNRGRTGVVVAAYMHYSNIsaSADQALDRFAMKRfyeDKVLPvg 289
Cdd:COG2453     55 IPDFGAPDDEQLQEAVDFIDEALREGKK--VLVHCRGGIGRTGTVAAAYLVLLGL--SAEEALARVRAAR---PGAVE-- 125

                           90
                   ....*....|.
gi 1207186103  290 QPSQRRYVQYF 300
Cdd:COG2453    126 TPAQRAFLERF 136
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 208-279 5.09e-09

protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine phosphatase domain-containing protein 1 (PTPDC1) is an uncharacterized non-receptor class protein-tyrosine phosphatase (PTP). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Small interfering RNA (siRNA) knockdown of the ptpdc1 gene is associated with elongated cilia.


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 58.13  E-value: 5.09e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207186103  208 FGWPDHHAPALDKICSICKAMDTWMNAGSHnvVVIHNKGNRGRTGVVVAAYMHYSNiSASADQALDRFAMKR 279
Cdd:cd14506     82 FGWKDYGVPSLTTILDIVKVMAFALQEGGK--VAVHCHAGLGRTGVLIACYLVYAL-RMSADQAIRLVRSKR 150
C1_KSR cd20812
protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) ...
 44-91 5.43e-09

protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) family; 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. KSR proteins contain a SAM-like domain, a zinc finger cysteine-rich domain (C1), and a pseudokinase domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410362  Cd Length: 48  Bit Score: 53.48  E-value: 5.43e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1207186103   44 SHTFRlKTFKKGKHCGVCKQTVNNeGLICRVCRLACHRKCEVKVSSSC 91
Cdd:cd20812      2 KHRFS-KKLFMRQTCDYCHKQMFF-GLKCKDCKYKCHKKCAKKAPPSC 47
SH2 pfam00017
SH2 domain;
1522-1616 6.49e-09

SH2 domain;


Pssm-ID: 425423 [Multi-domain]  Cd Length: 77  Bit Score: 54.14  E-value: 6.49e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1522 WYKPDISRDQAINMLKDQDP-GAFVIRDSHSFRGAYGLAMKvaspppttqptkkagdvTNELVRHFLIETSPKGVRLkgC 1600
Cdd:pfam00017    1 WYHGKISRQEAERLLLNGKPdGTFLVRESESTPGGYTLSVR-----------------DDGKVKHYKIQSTDNGGYY--I 61

                           90
                   ....*....|....*.
gi 1207186103 1601 PNEPYFGCLSALVYQH 1616
Cdd:pfam00017   62 SGGVKFSSLAELVEHY 77
C1_dGM13116p-like cd20831
protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and ...
 42-91 7.72e-09

protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and similar proteins; This group contains uncharacterized proteins including Drosophila melanogaster GM13116p and Caenorhabditis elegans hypothetical protein R11G1.4, both of which contain C2 (a calcium-binding domain) and C1 domains. This model describes the C1 domain, a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410381  Cd Length: 58  Bit Score: 53.50  E-value: 7.72e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207186103   42 VHSHTFRLKTFKKGKHCGVCKQTV----NNEGLICRVCRLACHRKCEVKVSSSC 91
Cdd:cd20831      3 YNDHTFVATHFKGGPSCAVCNKLIpgrfGKQGYQCRDCGLICHKRCHVKVETHC 56
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 45-91 1.16e-08

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 52.47  E-value: 1.16e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1207186103    45 HTFRLKTFKKGKHCGVCKQT---VNNEGLICRVCRLACHRKCEVKVSSSC 91
Cdd:smart00109    1 HKHVFRTFTKPTFCCVCRKSiwgSFKQGLRCSECKVKCHKKCADKVPKAC 50
C1_DGK_typeI_rpt1 cd20799
first protein kinase C conserved region 1 (C1 domain) found in type I diacylglycerol kinases; ...
 44-92 4.53e-08

first protein kinase C conserved region 1 (C1 domain) found in type I diacylglycerol kinases; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. Type I DAG kinases (DGKs) contain EF-hand structures that bind Ca(2+) and recoverin homology domains, in addition to C1 and catalytic domains that are present in all DGKs. Type I DGKs, regulated by calcium binding, include three DGK isozymes (alpha, beta and gamma). DAG kinase alpha, also called 80 kDa DAG kinase, or diglyceride kinase alpha (DGK-alpha), is active upon cell stimulation, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity. DAG kinase beta, also called 90 kDa DAG kinase, or diglyceride kinase beta (DGK-beta), exhibits high phosphorylation activity for long-chain diacylglycerols. DAG kinase gamma, also called diglyceride kinase gamma (DGK-gamma), reverses the normal flow of glycerolipid biosynthesis by phosphorylating diacylglycerol back to phosphatidic acid. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. DGK-alpha contains atypical C1 domains, while DGK-beta and DGK-gamma contain typical C1 domains that bind DAG and phorbol esters. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410349  Cd Length: 62  Bit Score: 51.22  E-value: 4.53e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207186103   44 SHTFRLKTFKKGKHCGVCKQT---VNNEGLICRVCRLACHRKCEVKVSSSCV 92
Cdd:cd20799      5 QHVWRLKHFNKPAYCNVCENMlvgLRKQGLCCTFCKYTVHERCVSRAPASCI 56
C1_DGK_typeII_rpt1 cd20800
first protein kinase C conserved region 1 (C1 domain) found in type II diacylglycerol kinases; ...
 44-91 6.70e-08

first protein kinase C conserved region 1 (C1 domain) found in type II diacylglycerol kinases; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. Type II DAG kinases (DGKs) contain pleckstrin homology (PH) and sterile alpha motifs (SAM) domains, in addition to C1 and catalytic domains that are present in all DGKs. The SAM domain mediates oligomerization of type II DGKs. Three DGK isozymes (delta, eta and kappa) are classified as type II. DAG kinase delta, also called 130 kDa DAG kinase, or diglyceride kinase delta (DGK-delta), is a residential lipid kinase in the endoplasmic reticulum. It promotes lipogenesis and is involved in triglyceride biosynthesis. DAG kinase eta, also called diglyceride kinase eta (DGK-eta), plays a key role in promoting cell growth. The DAG kinase eta gene, DGKH, is a replicated risk gene of bipolar disorder (BPD). DAG kinase kappa is also called diglyceride kinase kappa (DGK-kappa) or 142 kDa DAG kinase. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410350  Cd Length: 60  Bit Score: 50.78  E-value: 6.70e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207186103   44 SHTFRLKTFKKGKHCGVCKQT---VNNEGLICRVCRLACHRKCEVKVSSSC 91
Cdd:cd20800      4 SHNWYACSHARPTYCNVCREAlsgVTSHGLSCEVCKFKAHKRCAVKAPNNC 54
C1_PKD_rpt2 cd20796
second protein kinase C conserved region 1 (C1 domain) found in the family of protein kinase D ...
 45-91 9.86e-08

second protein kinase C conserved region 1 (C1 domain) found in the family of protein kinase D (PKD); 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 are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs contain N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410346  Cd Length: 54  Bit Score: 49.98  E-value: 9.86e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207186103   45 HTFRLKTFKKGKHCGVCKQTVN---NEGLICRVCRLACHRKCEVKVSSSC 91
Cdd:cd20796      2 HTFVVHTYTKPTVCQHCKKLLKglfRQGLQCKDCKFNCHKKCAEKVPKDC 51
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 45-93 2.21e-07

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 395079  Cd Length: 53  Bit Score: 48.98  E-value: 2.21e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207186103   45 HTFRLKTFKKGKHCGVCKQTVNNE---GLICRVCRLACHRKCEVKVSSSCVP 93
Cdd:pfam00130    1 HHFVHRNFKQPTFCDHCGEFLWGLgkqGLKCSWCKLNVHKRCHEKVPPECGC 52
C1_PIK3R-like_rpt2 cd20830
second protein kinase C conserved region 1 (C1 domain) found in uncharacterized ...
 45-83 2.46e-07

second protein kinase C conserved region 1 (C1 domain) found in uncharacterized phosphatidylinositol 3-kinase regulatory subunit-like proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate phosphatidylinositol 3-kinase regulatory subunits (PIK3Rs), which bind to activated (phosphorylated) protein-tyrosine kinases through its SH2 domain and regulate their kinase activity. Unlike typical PIK3Rs, members of this family have two C1 domains. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410380  Cd Length: 52  Bit Score: 48.79  E-value: 2.46e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1207186103   45 HTFRLKTFKKGKHCGVCKQT---VNNEGLICRVCRLACHRKC 83
Cdd:cd20830      1 HRFVEQSFSTLQWCDKCGKFlfgLVHQGLQCQDCGLVCHRTC 42
C1_Myosin-IX cd20818
protein kinase C conserved region 1 (C1 domain) found in the unconventional myosin-IX family; ...
 45-91 7.24e-07

protein kinase C conserved region 1 (C1 domain) found in the unconventional myosin-IX family; Myosins IX (Myo9) is a class of unique motor proteins with a common structure of an N-terminal extension preceding a myosin head homologous to the Ras-association (RA) domain, a head (motor) domain, a neck with IQ motifs that bind light chains, and a C-terminal tail containing cysteine-rich zinc binding (C1) and Rho-GTPase activating protein (RhoGAP) domains. There are two genes for myosins IX in humans, IXa and IXb, that are different in their expression and localization. IXa is expressed abundantly in brain and testis, and IXb is expressed abundantly in tissues of the immune system. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410368  Cd Length: 56  Bit Score: 47.68  E-value: 7.24e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1207186103   45 HTFRLKTFKKGKHCGVCKQTVNN--EGLICRVCRLACHRKCEVKVSSSC 91
Cdd:cd20818      4 HKFATVQFNIPTYCEVCNSFIWLmeKGLVCQVCKFTCHKKCYSKITAPC 52
C1_cPKC_nPKC_rpt1 cd20792
first protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ...
 45-91 7.32e-07

first protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) protein kinase C (cPKC), novel protein kinase C (nPKC), and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. 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. nPKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs (aPKCs) 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. This family includes classical PKCs (cPKCs) and novel PKCs (nPKCs). There are four cPKC isoforms (named alpha, betaI, betaII, and gamma) and four nPKC isoforms (delta, epsilon, eta, and theta). Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410342  Cd Length: 53  Bit Score: 47.62  E-value: 7.32e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207186103   45 HTFRLKTFKKGKHCGVCKQ---TVNNEGLICRVCRLACHRKCEVKVSSSC 91
Cdd:cd20792      2 HKFVATFFKQPTFCSHCKDfiwGLGKQGYQCQVCRFVVHKRCHEYVVFKC 51
C1_DGKtheta_typeV_rpt1 cd20803
first protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, ...
 45-95 1.61e-06

first protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, DAG kinase theta, and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase theta, also called diglyceride kinase theta (DGK-theta), is the only isoform classified as type V; it contains a pleckstrin homology (PH)-like domain and an additional C1 domain, compared to other DGKs. It may regulate the activity of protein kinase C by controlling the balance between the two signaling lipids, diacylglycerol and phosphatidic acid. DAG kinase theta contains three copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410353  Cd Length: 56  Bit Score: 46.92  E-value: 1.61e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207186103   45 HTFRLKTFKKGKHCGVCKQT---VNNEGLICRVCRLACHRKCEVKVSSSCVPVA 95
Cdd:cd20803      2 HSFRKKTFHKPTYCHHCTDLlwgLLNQGYQCEVCNFVSHERCLKTVVTPCSSIA 55
PHA03247 PHA03247
large tegument protein UL36; Provisional
 806-1171 1.93e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.40  E-value: 1.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103  806 PALTQVPkshSAPSGESGVVTTQPSFSQTQARPSYQADT---------AIHDRGAASSMGFPLTFQQVTGEPSQPTMKQQ 876
Cdd:PHA03247  2483 PAEARFP---FAAGAAPDPGGGGPPDPDAPPAPSRLAPAilpdepvgePVHPRMLTWIRGLEELASDDAGDPPPPLPPAA 2559

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103  877 KPTTTSQHV---EFASEAGGQAPMSQSTVPSSTfgvlqlkplniyPSSTTSQSPEPQETQRSYSSSSSPLPKESEPED-- 951
Cdd:PHA03247  2560 PPAAPDRSVpppRPAPRPSEPAVTSRARRPDAP------------PQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDpp 2627

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103  952 ----SSYKLEGLVAHRVAGLPSGEmsPDEAAVPGRCRTLSEGLSQDESPTRGSSVRSPIRCISPE----LANTIALNPGG 1023
Cdd:PHA03247  2628 ppspSPAANEPDPHPPPTVPPPER--PRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPtvgsLTSLADPPPPP 2705

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1024 RPKERHMH-------------SYREAFEEMDGGPVsPPPIVGGEVLPQTPAFPVSPQTPYFNMCRSPP-GLAKTPLSFLG 1089
Cdd:PHA03247  2706 PTPEPAPHalvsatplppgpaAARQASPALPAAPA-PPAVPAGPATPGGPARPARPPTTAGPPAPAPPaAPAAGPPRRLT 2784

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1090 LKPHNPAEILLNQTGSESEDEEEPrsyvesVAKAAAVPASPTYDSDSLARPAGPSHAYNAPLSSSSPIQNPDPVESTLAD 1169
Cdd:PHA03247  2785 RPAVASLSESRESLPSPWDPADPP------AAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAP 2858


                   ..
gi 1207186103 1170 SG 1171
Cdd:PHA03247  2859 GG 2860
C1_Stac cd20817
protein kinase C conserved region 1 (C1 domain) found in the SH3 and cysteine-rich ...
 45-89 3.00e-06

protein kinase C conserved region 1 (C1 domain) found in the SH3 and cysteine-rich domain-containing protein (Stac) family; Stac proteins are putative adaptor proteins that are important for neuronal function. There are three mammalian members (Stac1, Stac2 and Stac3) of this family. Stac1 and Stac3 contain two SH3 domains while Stac2 contains a single SH3 domain at the C-terminus. Stac1 and Stac2 have been found to be expressed differently in mature dorsal root ganglia (DRG) neurons. Stac1 is mainly expressed in peptidergic neurons while Stac2 is found in a subset of nonpeptidergic and all trkB+ neurons. Stac proteins contain a cysteine-rich C1 domain and one or two SH3 domains at the C-terminus. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410367  Cd Length: 51  Bit Score: 45.78  E-value: 3.00e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1207186103   45 HTFRLKTFKKGKHCGVCKQT---VNNEGLICRVCRLACHRKCEVKVSS 89
Cdd:cd20817      1 HSFQEHTFKKPTFCDVCKELlvgLSKQGLRCKNCKMNVHHKCQEGVPD 48
C1_CeDKF1-like_rpt2 cd20798
second protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine ...
 45-92 3.40e-06

second protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine/threonine-protein kinase DKF-1 and similar proteins; DKF-1 converts transient diacylglycerol (DAG) signals into prolonged physiological effects, independently of PKC. It plays a role in the regulation of growth and neuromuscular control of movement. It is involved in immune response to Staphylococcus aureus bacterium by activating transcription factor hlh-30 downstream of phospholipase plc-1. Members of this group contain two copies of the C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410348  Cd Length: 54  Bit Score: 45.95  E-value: 3.40e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207186103   45 HTFRLKTFKKGKHCGVCKQTVN---NEGLICRVCRLACHRKCEVKVSSSCV 92
Cdd:cd20798      2 HTLAEHNYKKPTVCKVCDKLLVglvRQGLKCRDCGVNVHKKCASLLPSNCR 52
C1_Raf cd20811
protein kinase C conserved region 1 (C1 domain) found in the Raf (Rapidly Accelerated ...
 44-92 7.87e-06

protein kinase C conserved region 1 (C1 domain) found in the Raf (Rapidly Accelerated Fibrosarcoma) kinase family; Raf kinases are serine/threonine kinases (STKs) that catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. They 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 (C1), 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. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410361  Cd Length: 49  Bit Score: 44.59  E-value: 7.87e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1207186103   44 SHTFRLKTFKKGKHCGVCKQTVNNeGLICRVCRLACHRKCEVKVSSSCV 92
Cdd:cd20811      2 SHNFVRKTFFTLAFCDVCRKLLFQ-GFRCQTCGFKFHQRCSDQVPALCE 49
C1_nPKC_theta-like_rpt1 cd20834
first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
 42-91 1.68e-05

first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) theta, delta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. 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. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410384  Cd Length: 61  Bit Score: 43.85  E-value: 1.68e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207186103   42 VHSHTFRLKTFKKGKHCGVCKQTV---NNEGLICRVCRLACHRKCEVKVSSSC 91
Cdd:cd20834      5 VKGHEFIAKFFRQPTFCSVCKEFLwgfNKQGYQCRQCNAAVHKKCHDKILGKC 57
C1_ScPKC1-like_rpt1 cd20822
first protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae ...
 43-91 2.72e-05

first protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae protein kinase C-like 1 (ScPKC1) and similar proteins; ScPKC1 is required for cell growth and for the G2 to M transition of the cell division cycle. It mediates a protein kinase cascade, activating BCK1 which itself activates MKK1/MKK2. The family also includes Schizosaccharomyces pombe PKC1 and PKC2, which are involved in the control of cell shape and act as targets of the inhibitor staurosporine. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410372  Cd Length: 52  Bit Score: 43.05  E-value: 2.72e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1207186103   43 HSHTFRLKTFKKGKHCGVCKQTVNNEGLICRVCRLACHRKCEVKVSSSC 91
Cdd:cd20822      1 RGHKFVQKQFYQIMRCAVCGEFLVNAGYQCEDCKYTCHKKCYEKVVTKC 49
C1_PKD2_rpt2 cd20843
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and ...
 45-104 3.12e-05

second protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and similar proteins; PKD2, also called PRKD2, HSPC187, or serine/threonine-protein kinase D2 (nPKC-D2), is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress-induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion. PKD2 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410393  Cd Length: 79  Bit Score: 43.81  E-value: 3.12e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207186103   45 HTFRLKTFKKGKHCGVCKQTVNN---EGLICRVCRLACHRKCEVKVSSSCV--PVANYELAPSNE 104
Cdd:cd20843     12 HTFVIHSYTRPTVCQFCKKLLKGlfrQGLQCKDCKFNCHKRCATRVPNDCLgeTLFNGDLVPMEA 76
SH2_Tec_family cd09934
Src homology 2 (SH2) domain found in Tec-like proteins; The Tec protein tyrosine kinase is the ...
 1522-1630 3.71e-05

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: 44.31  E-value: 3.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1522 WYKPDISRDQAINMLKDQDP-GAFVIRDShSFRGAYGLAMKvaspppttqpTKKAGDVTnelVRHFLIETSPKG---VRL 1597
Cdd:cd09934      8 WYVGDMSRQRAESLLKQEDKeGCFVVRNS-STKGLYTVSLF----------TKVPGSPH---VKHYHIKQNARSefyLAE 73

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1207186103 1598 KGCpnepyFGCLSALVYQHSITPLALPCKLVIP 1630
Cdd:cd09934     74 KHC-----FETIPELINYHQHNSGGLATRLKYP 101
C1_PKD3_rpt2 cd20844
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and ...
 45-103 4.10e-05

second protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and similar proteins; PKD3 is also called PRKD3, PRKCN, serine/threonine-protein kinase D3 (nPKC-D3), protein kinase C nu type (nPKC-nu), or protein kinase EPK2. It converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. It is involved in the regulation of the cell cycle by modulating microtubule nucleation and dynamics. PKD3 acts as a key mediator in several cancer development signaling pathways. PKD3 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410394  Cd Length: 69  Bit Score: 43.08  E-value: 4.10e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207186103   45 HTFRLKTFKKGKHCGVCKQTVNN---EGLICRVCRLACHRKCEVKVSSSCVPVANYELAPSN 103
Cdd:cd20844      6 HTFAVHSYTRPTICQYCKRLLKGlfrQGMQCKDCRFNCHKRCASKVPRDCLGEVTFNGEPAS 67
C1_GMIP-like cd20816
protein kinase C conserved region 1 (C1 domain) found in the GEM-interacting protein (GMIP) ...
 44-91 4.38e-05

protein kinase C conserved region 1 (C1 domain) found in the GEM-interacting protein (GMIP)-like family; The GMIP-like family includes GMIP, Rho GTPase-activating protein 29 (ARHGAP29) and Rho GTPase-activating protein 45 (ARHGAP45). GMIP is a RhoA-specific GTPase-activating protein that acts as a key factor in saltatory neuronal migration. It associates with the Rab27a effector JFC1 and modulates vesicular transport and exocytosis. ARHGAP29, also called PTPL1-associated RhoGAP protein 1 (PARG1) or Rho-type GTPase-activating protein 29, is a GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. It has strong activity toward RHOA, and weaker activity toward RAC1 and CDC42. ARHGAP29 may act as a specific effector of RAP2A to regulate Rho. In concert with RASIP1, ARHGAP29 suppresses RhoA signaling and dampens ROCK and MYH9 activities in endothelial cells and plays an essential role in blood vessel tubulogenesis. ARHGAP45, also called minor histocompatibility antigen HA-1 (mHag HA-1), is a Rac-GAP (GTPase-Activating Protein) in endothelial cells. It acts as a novel regulator of endothelial integrity. ARHGAP45 contains a GTPase activator for the Rho-type GTPases (RhoGAP) domain that would be able to negatively regulate the actin cytoskeleton as well as cell spreading. However, it also contains N-terminally a BAR-domin which can play an autoinhibitory effect on this RhoGAP activity. Members of this family contain a zinc-binding C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410366  Cd Length: 51  Bit Score: 42.63  E-value: 4.38e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1207186103   44 SHTF-RLKTFKKgkhCGVCKQTVNNEGLICRVCRLACHRKCEVKVSSSC 91
Cdd:cd20816      2 THRFrRLRTPSK---CRECDSYVYFNGAECEECGLACHKKCLETLAIQC 47
SH2_cSH2_p85_like cd09930
C-terminal Src homology 2 (cSH2) domain found in p85; Phosphoinositide 3-kinases (PI3Ks) are ...
 1522-1617 4.55e-05

C-terminal Src homology 2 (cSH2) domain found in p85; Phosphoinositide 3-kinases (PI3Ks) are essential for cell growth, migration, and survival. p110, the catalytic subunit, is composed of an adaptor-binding domain, a Ras-binding domain, a C2 domain, a helical domain, and a kinase domain. The regulatory unit is called p85 and is composed of an SH3 domain, a RhoGap domain, a N-terminal SH2 (nSH2) domain, a inter SH2 (iSH2) domain, and C-terminal (cSH2) domain. There are 2 inhibitory interactions between p110alpha and p85 of P13K: 1) p85 nSH2 domain with the C2, helical, and kinase domains of p110alpha and 2) p85 iSH2 domain with C2 domain of p110alpha. There are 3 inhibitory interactions between p110beta and p85 of P13K: 1) p85 nSH2 domain with the C2, helical, and kinase domains of p110beta, 2) p85 iSH2 domain with C2 domain of p110alpha, and 3) p85 cSH2 domain with the kinase domain of p110alpha. It is interesting to note that p110beta is oncogenic as a wild type protein while p110alpha lacks this ability. One explanation is the idea that the regulation of p110beta by p85 is unique because of the addition of inhibitory contacts from the cSH2 domain and the loss of contacts in the iSH2 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: 198184  Cd Length: 104  Bit Score: 44.33  E-value: 4.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1522 WYKPDISRDQAINMLKDQDPGAFVIRDShSFRGAYGLAMKVaspppttqptkkagdvtNELVRHFLIETSPKGVRLKgcp 1601
Cdd:cd09930      8 WLVGDINRTQAEELLRGKPDGTFLIRES-STQGCYACSVVC-----------------NGEVKHCVIYKTETGYGFA--- 66

                           90       100
                   ....*....|....*....|
gi 1207186103 1602 nEPY--FGCLSALV--YQHS 1617
Cdd:cd09930     67 -EPYnlYESLKELVlhYAHN 85
C1_RASSF5 cd20886
protein kinase C conserved region 1 (C1 domain) found in Ras association domain-containing ...
 58-91 6.53e-05

protein kinase C conserved region 1 (C1 domain) found in Ras association domain-containing protein 5 (RASSF5) and similar proteins; RASSF5, also called new ras effector 1 (NORE1), or regulator for cell adhesion and polarization enriched in lymphoid tissues (RAPL), is a member of a family of RAS effectors, of which there are currently 8 members (RASSF1-8), all containing a Ras-association (RA) domain of the Ral-GDS/AF6 type. It is expressed as three transcripts (A-C) via differential promoter usage and alternative splicing. RASSF5A is a pro-apoptotic Ras effector and functions as a Ras regulated tumor suppressor. RASSF5C is regulated by Ras related protein and modulates cellular adhesion. RASSF5 is a potential tumor suppressor that seems to be involved in lymphocyte adhesion by linking RAP1A activation upon T-cell receptor or chemokine stimulation to integrin activation. It contains a C1 domain, which is descibed in this model. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410436  Cd Length: 50  Bit Score: 41.98  E-value: 6.53e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1207186103   58 CGVCKQTVNNEGLICRVCRLACHRKCEVKVSSSC 91
Cdd:cd20886     16 CDLCGRYILSQALRCTNCKYTCHSECRDLVQLDC 49
C1_nPKC_theta-like_rpt2 cd20837
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
 45-91 7.73e-05

second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) theta, delta, and similar proteins; 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. 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. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410387  Cd Length: 50  Bit Score: 41.65  E-value: 7.73e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207186103   45 HTFRLKTFKKG---KHCGVCKQTVNNEGLICRVCRLACHRKCEVKVSSSC 91
Cdd:cd20837      1 HRFKVYNYMSPtfcDHCGSLLWGLFRQGLKCEECGMNVHHKCQKKVANLC 50
C1_PKD1_rpt2 cd20842
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and ...
 45-92 7.81e-05

second protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and similar proteins; PKD is also called PKD1, PRKD1, protein kinase C mu type (nPKC-mu), PRKCM, serine/threonine-protein kinase D1, or nPKC-D1. It is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of MAPK8/JNK1 and Ras signaling, Golgi membrane integrity and trafficking, cell survival through NF-kappa-B activation, cell migration, cell differentiation by mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response. PKD contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410392  Cd Length: 94  Bit Score: 43.08  E-value: 7.81e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207186103   45 HTFRLKTFKKGKHCGVCKQTVNN---EGLICRVCRLACHRKCEVKVSSSCV 92
Cdd:cd20842     35 HTFVIHSYTRPTVCQYCKKLLKGlfrQGLQCKDCKFNCHKRCAPKVPNNCL 85
C1_VAV cd20810
protein kinase C conserved region 1 (C1 domain) found in VAV proteins; VAV proteins function ...
 43-91 8.67e-05

protein kinase C conserved region 1 (C1 domain) found in VAV proteins; VAV proteins function both as cytoplasmic guanine nucleotide exchange factors (GEFs) for Rho GTPases and as scaffold proteins, and they play important roles in cell signaling by coupling cell surface receptors to various effector functions. They play key roles in processes that require cytoskeletal reorganization including immune synapse formation, phagocytosis, cell spreading, and platelet aggregation, among others. Vertebrates have three VAV proteins (VAV1, VAV2, and VAV3). VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410360  Cd Length: 52  Bit Score: 41.86  E-value: 8.67e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207186103   43 HSHTFRLKTFKKGKHCGVCK--------QtvnneGLICRVCRLACHRKCeVKVSSSC 91
Cdd:cd20810      1 TGHSFELTTFKEPTTCSVCKkllkglffQ-----GYKCSVCGAAVHKEC-IAKVKRC 51
C1_DGKgamma_rpt1 cd20846
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase gamma ...
 45-92 1.01e-04

first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase gamma (DAG kinase gamma) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase gamma, also called diglyceride kinase gamma (DGK-gamma), reverses the normal flow of glycerolipid biosynthesis by phosphorylating diacylglycerol back to phosphatidic acid. It is classified as a type I DAG kinase (DGK), containing EF-hand structures that bind Ca(2+) and a recoverin homology domain, in addition to C1 and catalytic domains that are present in all DGKs. As a type I DGK, it is regulated by calcium binding. DGK-gamma contains two copies of the C1 domain. This model corresponds to the first one. DGK-gamma contains typical C1 domains that bind DAG and phorbol esters. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410396  Cd Length: 73  Bit Score: 42.23  E-value: 1.01e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207186103   45 HTFRLKTFKKGKHCGVCKQT---VNNEGLICRVCRLACHRKCEVKVSSSCV 92
Cdd:cd20846     17 HAWRLKHFKKPAYCNFCHTMllgVRKQGLCCSFCKYTVHERCVSKDIASCI 67
C1_cPKC_nPKC_rpt2 cd20793
second protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ...
 45-91 1.65e-04

second protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) protein kinase C (cPKC), novel protein kinase C (nPKC), and similar proteins; 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. nPKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs (aPKCs) 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. This family includes classical PKCs (cPKCs) and novel PKCs (nPKCs). There are four cPKC isoforms (named alpha, betaI, betaII, and gamma) and four nPKC isoforms (delta, epsilon, eta, and theta). Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410343  Cd Length: 50  Bit Score: 40.72  E-value: 1.65e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207186103   45 HTFRLKTFKKGKHCGVCKQTV---NNEGLICRVCRLACHRKCEVKVSSSC 91
Cdd:cd20793      1 HKFKVHTYYSPTFCDHCGSLLyglVRQGLKCKDCGMNVHHRCKENVPHLC 50
SH2_nSH2_p85_like cd09942
N-terminal Src homology 2 (nSH2) domain found in p85; Phosphoinositide 3-kinases (PI3Ks) are ...
 1522-1561 2.15e-04

N-terminal Src homology 2 (nSH2) domain found in p85; Phosphoinositide 3-kinases (PI3Ks) are essential for cell growth, migration, and survival. p110, the catalytic subunit, is composed of an adaptor-binding domain, a Ras-binding domain, a C2 domain, a helical domain, and a kinase domain. The regulatory unit is called p85 and is composed of an SH3 domain, a RhoGap domain, a N-terminal SH2 (nSH2) domain, an internal SH2 (iSH2) domain, and C-terminal (cSH2) domain. There are 2 inhibitory interactions between p110alpha and p85 of P13K: (1) p85 nSH2 domain with the C2, helical, and kinase domains of p110alpha and (2) p85 iSH2 domain with C2 domain of p110alpha. There are 3 inhibitory interactions between p110beta and p85 of P13K: (1) p85 nSH2 domain with the C2, helical, and kinase domains of p110beta, (2) p85 iSH2 domain with C2 domain of p110alpha, and (3) p85 cSH2 domain with the kinase domain of p110alpha. It is interesting to note that p110beta is oncogenic as a wild type protein while p110alpha lacks this ability. One explanation is the idea that the regulation of p110beta by p85 is unique because of the addition of inhibitory contacts from the cSH2 domain and the loss of contacts in the iSH2 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: 198195  Cd Length: 110  Bit Score: 42.31  E-value: 2.15e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1207186103 1522 WYKPDISRDQAINMLKDQDPGAFVIRDSHSFRGAYGLAMK 1561
Cdd:cd09942      9 WYWGDISREEVNEKMRDTPDGTFLVRDASTMKGDYTLTLR 48
SH2_Cterm_RasGAP cd10354
C-terminal Src homology 2 (SH2) domain found in Ras GTPase-activating protein 1 (GAP); RasGAP ...
 1522-1613 2.37e-04

C-terminal Src homology 2 (SH2) domain found in Ras GTPase-activating protein 1 (GAP); RasGAP is part of the GAP1 family of GTPase-activating proteins. The protein is located in the cytoplasm and stimulates the GTPase activity of normal RAS p21, but not its oncogenic counterpart. Acting as a suppressor of RAS function, the protein enhances the weak intrinsic GTPase activity of RAS proteins resulting in RAS inactivation, thereby allowing control of cellular proliferation and differentiation. Mutations leading to changes in the binding sites of either protein are associated with basal cell carcinomas. Alternative splicing results in two isoforms. The shorter isoform which lacks the N-terminal hydrophobic region, has the same activity, and is expressed in placental tissues. In general longer isoform contains 2 SH2 domains, a SH3 domain, a pleckstrin homology (PH) domain, and a calcium-dependent phospholipid-binding C2 domain. The C-terminus contains the catalytic domain of RasGap which catalyzes the activation of Ras by hydrolyzing GTP-bound active Ras into an inactive GDP-bound form of Ras. This model contains the C-terminal 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: 198217  Cd Length: 77  Bit Score: 41.25  E-value: 2.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1522 WYKPDISRDQAINML-KDQDPGAFVIRDSHSFRGAYGLAMKVaspppttqptkkagdvtNELVRHFLIETSPKGVRLKGc 1600
Cdd:cd10354      2 WFHGKISREEAYNMLvKVGGPGSFLVRESDNTPGDYSLSFRV-----------------NEGIKHFKIIPTGNNQFMMG- 63

                           90
                   ....*....|...
gi 1207186103 1601 pnEPYFGCLSALV 1613
Cdd:cd10354     64 --GRYFSSLDDVI 74
C1_MRCK cd20809
protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related ...
 45-94 2.38e-04

protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related Cdc42-binding kinase (MRCK) family; MRCK is thought to be a coincidence detector of signaling by the small GTPase Cdc42 and phosphoinositides. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. MRCK has been shown to promote cytoskeletal reorganization, which affects many biological processes. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. MRCK consists of a serine/threonine kinase domain, a cysteine rich (C1) region, a PH domain and a p21 binding motif. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410359  Cd Length: 53  Bit Score: 40.33  E-value: 2.38e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207186103   45 HTFRLKTFKKGKHCGVC--------KQtvnneGLICRVCRLACHRKCEVKVSSSCvPV 94
Cdd:cd20809      1 HKFIVRTFSTPTKCNHCtslmvglvRQ-----GLVCEVCGYACHVSCADKAPQVC-PV 52
C1_nPKC_epsilon-like_rpt2 cd20838
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
 45-91 3.68e-04

second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) epsilon, eta, and similar proteins; 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. 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. 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. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410388  Cd Length: 55  Bit Score: 39.95  E-value: 3.68e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207186103   45 HTFRLKTFKKG---KHCGVCKQTVNNEGLICRVCRLACHRKCEVKVSSSC 91
Cdd:cd20838      3 HRFSVHNYKRPtfcDHCGSLLYGLYKQGLQCKVCKMNVHKRCQKNVANNC 52
C1_Myosin-IXa cd20883
protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXa and similar ...
 40-91 4.20e-04

protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXa and similar proteins; Myosin-IXa, also called unconventional myosin-9a (Myo9a), is a single-headed, actin-dependent motor protein of the unconventional myosin IX class. It is expressed in several tissues and is enriched in the brain and testes. Myosin-IXa contains a Ras-associating (RA) domain, a motor domain, a protein kinase C conserved region 1 (C1), and a Rho GTPase activating domain (RhoGAP). Myosin-IXa binds the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor (AMPAR) GluA2 subunit, and plays a key role in controlling the molecular structure and function of hippocampal synapses. Moreover, Myosin-IXa functions in epithelial cell morphology and differentiation, such that its knockout mice develop hydrocephalus and kidney dysfunction. Myosin-IXa regulates collective epithelial cell migration by targeting RhoGAP activity to cell-cell junctions. Myosin-IXa negatively regulates Rho GTPase signaling, and functions as a regulator of kidney tubule function. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410433  Cd Length: 58  Bit Score: 39.95  E-value: 4.20e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207186103   40 EAVHSHTFRLKTFKKGKHCGVCKQTV--NNEGLICRVCRLACHRKCEVKVSSSC 91
Cdd:cd20883      1 EEHNGHIFKSTQYSIPTYCEYCSSLIwmMDRAYVCKLCRYACHKKCCLKTTTKC 54
SH2_Srm cd10360
Src homology 2 (SH2) domain found in Src-related kinase lacking C-terminal regulatory tyrosine ...
 1522-1561 4.28e-04

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: 40.71  E-value: 4.28e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1207186103 1522 WYKPDISRDQAINML--KDQDPGAFVIRDSHSFRGAYGLAMK 1561
Cdd:cd10360      2 WYFSGISRTQAQQLLlsPPNEPGAFLIRPSESSLGGYSLSVR 43
C1_aPKC_iota cd21094
protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) ...
 45-91 6.71e-04

protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) iota type; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. Members of this family contain C1 domain found in aPKC isoform iota. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410447  Cd Length: 55  Bit Score: 39.22  E-value: 6.71e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207186103   45 HTFRLKTFKKGKHCGVCKQTV---NNEGLICRVCRLACHRKCEVKVSSSC 91
Cdd:cd21094      3 HTFQAKRFNRRAHCAICTDRIwglGRQGYKCINCKLLVHKKCHKLVTIEC 52
C1_RASGRP4 cd20863
protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 4 ...
 45-91 6.79e-04

protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 4 (RASGRP4) and similar proteins; RASGRP4 functions as a cation- and diacylglycerol (DAG)-regulated nucleotide exchange factor activating Ras through the exchange of bound GDP for GTP. It may function in mast cell differentiation. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410413  Cd Length: 57  Bit Score: 39.38  E-value: 6.79e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207186103   45 HTFRLKTFKKGKHCGVCKQ---TVNNEGLICRVCRLACHRKCEVKVSSSC 91
Cdd:cd20863      4 HNFHETTFKKPTFCDSCSGflwGVTKQGYRCQDCGINCHKHCKDQVDVEC 53
C1_DGKbeta_rpt1 cd20845
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase beta (DAG ...
 44-92 7.23e-04

first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase beta (DAG kinase beta) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase beta, also called 90 kDa diacylglycerol kinase, or diglyceride kinase beta (DGK-beta), exhibits high phosphorylation activity for long-chain diacylglycerols. It is classified as a type I DAG kinase (DGK), containing EF-hand structures that bind Ca(2+) and a recoverin homology domain, in addition to C1 and catalytic domains that are present in all DGKs. As a type I DGK, it is regulated by calcium binding. DAG kinase beta contains two copies of the C1 domain. This model corresponds to the first one. DGK-beta contains typical C1 domains that bind DAG and phorbol esters. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410395  Cd Length: 66  Bit Score: 39.45  E-value: 7.23e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207186103   44 SHTFRLKTFKKGKHCGVCKQT---VNNEGLICRVCRLACHRKCEVKVSSSCV 92
Cdd:cd20845      7 QHVWRLKHFNKPAYCNLCLNMlvgLGKQGLCCSFCKYTVHERCVQRAPASCI 58
SH2_Grb2_like cd09941
Src homology 2 domain found in Growth factor receptor-bound protein 2 (Grb2) and similar ...
 1522-1594 8.82e-04

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: 40.33  E-value: 8.82e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207186103 1522 WYKPDISRDQAINMLKDQDP-GAFVIRDSHSFRGAYGLAMKVaspppttqptkkagdvtNELVRHFLIETSPKG 1594
Cdd:cd09941      5 WFHGKISRAEAEEILMNQRPdGAFLIRESESSPGDFSLSVKF-----------------GNDVQHFKVLRDGAG 61
PRK12361 PRK12361
hypothetical protein; Provisional
 197-273 9.03e-04

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 43.84  E-value: 9.03e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207186103  197 DISKLNPKVLDfgwpdHHAPALDKICSICKAMDTWMNAGSHnvVVIHNKGNRGRTGVVVAAYMHYSNISASADQALD 273
Cdd:PRK12361   142 DIDYLNIPILD-----HSVPTLAQLNQAINWIHRQVRANKS--VVVHCALGRGRSVLVLAAYLLCKDPDLTVEEVLQ 211
SH2_Grb7_family cd09944
Src homology 2 (SH2) domain found in the growth factor receptor bound, subclass 7 (Grb7) ...
 1519-1627 9.60e-04

Src homology 2 (SH2) domain found in the growth factor receptor bound, subclass 7 (Grb7) proteins; The Grb family binds to the epidermal growth factor receptor (EGFR, erbB1) via their SH2 domains. There are 3 members of the Grb7 family of proteins: Grb7, Grb10, and Grb14. They are composed of an N-terminal Proline-rich domain, a Ras Associating-like (RA) domain, a Pleckstrin Homology (PH) domain, a phosphotyrosine interaction region (PIR, BPS) and a C-terminal SH2 domain. The SH2 domains of Grb7, Grb10 and Grb14 preferentially bind to a different RTK. Grb7 binds strongly to the erbB2 receptor, unlike Grb10 and Grb14 which bind weakly to it. Grb14 binds to Fibroblast Growth Factor Receptor (FGFR). Grb10 has been shown to interact with many different proteins, including the insulin and IGF1 receptors, platelet-derived growth factor (PDGF) receptor-beta, Ret, Kit, Raf1 and MEK1, and Nedd4. Grb7 family proteins are phosphorylated on serine/threonine as well as tyrosine residues. 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: 198197 [Multi-domain]  Cd Length: 108  Bit Score: 40.48  E-value: 9.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1519 SKFWYKPDISRDQAINMLKDQD--PGAFVIRDSHSFRGAYGLAMKvaspppttqptkkagdvTNELVRHFLIETSPKGVR 1596
Cdd:cd09944      4 SQPWFHGGISRDEAARLIRQQGlvDGVFLVRESQSNPGAFVLSLK-----------------HGQKIKHYQIIPIEDEGQ 66

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1207186103 1597 L-----KGCPNepyFGCLSALVYQHSITPLALPCKL 1627
Cdd:cd09944     67 WyftldDGVTK---FYDLLQLVEFYQLNAGSLPTRL 99
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 1112-1506 9.62e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.39  E-value: 9.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1112 EPRSYVESVAKAAAVPASPTYDSDSLARPAGPSHAYNAPLSSSSPIQNPDPVESTLADSGVGMNSLSQAAVDIFHFQPSE 1191
Cdd:PHA03307    62 CDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPV 141

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1192 ipyQPPPPPYPTSMLGSYISPSPAEAMQNNTTTIQPLSGSPGTRHHTILSDMASVPNFQHRLANQDGPILGRQ--QAPAN 1269
Cdd:PHA03307   142 ---GSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSpiSASAS 218

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1270 GHVPGIAGSPVQGRHTMVSQGTQSSPILSRQYPVTQGIQSSPILSRQPMGQAVQSSPVLNRQASLNQANQSSPVLSRqqs 1349
Cdd:PHA03307   219 SPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERS--- 295

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1350 itlpnqGSPVLSRQSSLSHPSQGSPVLGRHPSLTQGSPSLDR-----HPMYSGYTTPEERHGALSRQSSSSGYQPPSTPS 1424
Cdd:PHA03307   296 ------PSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSssessRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRP 369

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1425 FPVSPAGYIEGAGFRQGSPAFQPQLPEKRRMssSDRTngglsyGTLNGKMSSPVSSGGSTPSVHFFHTLPdfskLNMCDG 1504
Cdd:PHA03307   370 RPSRAPSSPAASAGRPTRRRARAAVAGRARR--RDAT------GRFPAGRPRPSPLDAGAASGAFYARYP----LLTPSG 437


                   ..
gi 1207186103 1505 SP 1506
Cdd:PHA03307   438 EP 439
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 216-299 1.15e-03

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 40.41  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103  216 PALDKICSICKAMDTWmNAGSHnVVVIHNKGNRGRTGVVVAAY-MHYSNIsaSADQALDRFAMKRfyedkvlPVGQP--- 291
Cdd:cd14494     37 LTLAMVDRFLEVLDQA-EKPGE-PVLVHCKAGVGRTGTLVACYlVLLGGM--SAEEAVRIVRLIR-------PGGIPqti 105


                   ....*...
gi 1207186103  292 SQRRYVQY 299
Cdd:cd14494    106 EQLDFLIK 113
C1_DGKtheta_typeV_rpt2 cd20804
second protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, ...
 44-91 1.19e-03

second protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, DAG kinase theta, and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase theta, also called diglyceride kinase theta (DGK-theta), is the only isoform classified as type V; it contains a pleckstrin homology (PH)-like domain and an additional C1 domain, compared to other DGKs. It may regulate the activity of protein kinase C by controlling the balance between the two signaling lipids, diacylglycerol and phosphatidic acid. DAG kinase theta contains three copies of the C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410354  Cd Length: 57  Bit Score: 38.82  E-value: 1.19e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1207186103   44 SHTFRLKTFKKGKHCGVC-KQTVNNEGLICRVCRLACHRKCEVKVSSSC 91
Cdd:cd20804      5 AHCWSEPGHSKRKFCNVCrKRLEDSPAFRCEVCEYYVHSDCQDFAVSDC 53
C1_DGKeta_rpt1 cd20848
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase eta (DAG ...
 34-91 1.33e-03

first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase eta (DAG kinase eta) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase eta, also called diglyceride kinase eta (DGK-eta), plays a key role in promoting cell growth. It is classified as a type II DAG kinase (DGK), containing pleckstrin homology (PH) and sterile alpha motifs (SAM) domains, in addition to C1 and catalytic domains that are present in all DGKs. The SAM domain mediates oligomerization of type II DGKs. The diacylglycerol kinase eta gene, DGKH, is a replicated risk gene of bipolar disorder (BPD). DAG kinase eta contains two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410398  Cd Length: 86  Bit Score: 39.38  E-value: 1.33e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207186103   34 FKPEEFEAVHShtFRLKTFKKGKHCGVCKQT---VNNEGLICRVCRLACHRKCEVKVSSSC 91
Cdd:cd20848     21 FNVEHFSGMHN--WYACSHARPTFCNVCRESlsgVTSHGLSCEVCKFKAHKRCAVRATNNC 79
C1_Stac1 cd20880
protein kinase C conserved region 1 (C1 domain) found in SH3 and cysteine-rich ...
 44-83 1.51e-03

protein kinase C conserved region 1 (C1 domain) found in SH3 and cysteine-rich domain-containing protein (Stac1) and similar proteins; Stac1, also called Src homology 3 and cysteine-rich domain-containing protein, promotes expression of the ion channel CACNA1H at the cell membrane, and thereby contributes to the regulation of channel activity. It plays a minor and redundant role in promoting the expression of calcium channel CACNA1S at the cell membrane, and thereby contributes to increased channel activity. It slows down the inactivation rate of the calcium channel CACNA1C. Stac1 contains a cysteine-rich C1 domain and two SH3 domains at the C-terminus. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410430  Cd Length: 57  Bit Score: 38.38  E-value: 1.51e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1207186103   44 SHTFRLKTFKKGKHCGVCKQ----TVNNEGLICRVCRLACHRKC 83
Cdd:cd20880      2 AHSFQEYIFKKPTFCDVCNHmivgTNAKHGLRCKACKMSIHHKC 45
C1_DGKdelta_rpt1 cd20847
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase delta ...
 26-91 1.93e-03

first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase delta (DAG kinase delta) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase delta, also called 130 kDa diacylglycerol kinase, or diglyceride kinase delta (DGK-delta), is a residential lipid kinase in the endoplasmic reticulum. It promotes lipogenesis and is involved in triglyceride biosynthesis. It is classified as a type II DAG kinase (DGK), containing pleckstrin homology (PH) and sterile alpha motifs (SAM) domains, in addition to C1 and catalytic domains that are present in all DGKs. The SAM domain mediates oligomerization of type II DGKs. DAG kinase delta contains two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410397  Cd Length: 85  Bit Score: 38.93  E-value: 1.93e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207186103   26 KKEEKRLLFKPEEFEAVH---SHTFRLKTFKKGKHCGVCKQT---VNNEGLICRVCRLACHRKCEVKVSSSC 91
Cdd:cd20847      3 KSVQNREHFESTQYSMDHfsgMHNWYACSHARPTYCNVCREAlsgVTSHGLSCEVCKFKAHKRCAVRATNNC 74
C1_nPKC_epsilon-like_rpt1 cd20835
first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
 42-91 2.38e-03

first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) epsilon, eta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. 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. 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. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410385  Cd Length: 64  Bit Score: 38.22  E-value: 2.38e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207186103   42 VHSHTFRLKTFKKGKHCGVCKQ----TVNNEGLICRVCRLACHRKCEVKVSSSC 91
Cdd:cd20835      7 VNGHKFMATYLRQPTYCSHCKDfiwgVIGKQGYQCQVCTCVVHKRCHQLVVTKC 60
C1_p190RhoGEF-like cd20815
protein kinase C conserved region 1 (C1 domain) found in the 190 kDa guanine nucleotide ...
 43-80 2.48e-03

protein kinase C conserved region 1 (C1 domain) found in the 190 kDa guanine nucleotide exchange factor (p190RhoGEF)-like family; The p190RhoGEF-like protein family includes p190RhoGEF, Rho guanine nucleotide exchange factor 2 (ARHGEF2), A-kinase anchor protein 13 (AKAP-13) and similar proteins. p190RhoGEF is a brain-enriched, RhoA-specific guanine nucleotide exchange factor that regulates signaling pathways downstream of integrins and growth factor receptors. It is involved in axonal branching, synapse formation and dendritic morphogenesis, as well as in focal adhesion formation, cell motility and B-lymphocytes activation. ARHGEF2 acts as a guanine nucleotide exchange factor (GEF) that activates Rho-GTPases by promoting the exchange of GDP for GTP. It is thought to play a role in actin cytoskeleton reorganization in different tissues since its activation induces formation of actin stress fibers. AKAP-13 is a scaffold protein that plays an important role in assembling signaling complexes downstream of several types of G protein-coupled receptors. It activates RhoA in response to signaling via G protein-coupled receptors via its function as Rho guanine nucleotide exchange factor. It may also activate other Rho family members. AKAP-13 plays a role in cell growth, cell development and actin fiber formation. Members of this family share a common domain architecture containing C1, RhoGEF or Dbl-homologous (DH), and Pleckstrin Homology (PH) domains. Some members may contain additional domains such as the DUF5401 domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410365  Cd Length: 54  Bit Score: 37.79  E-value: 2.48e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1207186103   43 HSHTFRLKTFKKGKHCGVCKQTVNN-EGLICRVCRLACH 80
Cdd:cd20815      2 NTHQFVPVSFSNSTKCDVCSKPLTNkPALQCENCSVNVH 40
SH2_Tec_Itk cd10396
Src homology 2 (SH2) domain found in Tec protein, IL2-inducible T-cell kinase (Itk); A member ...
 1522-1593 2.75e-03

Src homology 2 (SH2) domain found in Tec protein, IL2-inducible T-cell kinase (Itk); A member of the Tec protein tyrosine kinase Itk is expressed thymus, spleen, lymph node, T lymphocytes, NK and mast cells. It plays a role in T-cell proliferation and differentiation, analogous to Tec family kinases Txk. Itk has been shown to interact with Fyn, Wiskott-Aldrich syndrome protein, KHDRBS1, PLCG1, Lymphocyte cytosolic protein 2, Linker of activated T cells, Karyopherin alpha 2, Grb2, and Peptidylprolyl isomerase A. Most of the Tec family members have a PH domain (Txk and the short (type 1) splice variant of Drosophila Btk29A are exceptions), a Tec homology (TH) domain, a SH3 domain, a SH2 domain, and a protein kinase catalytic domain. The TH domain consists of a Zn2+-binding Btk motif and a proline-rich region. The Btk motif is found in Tec kinases, Ras GAP, and IGBP. It is crucial for the function of Tec PH domains and it's lack of presence in Txk is not surprising since it lacks a PH domain. The type 1 splice form of the Drosophila homolog also lacks both the PH domain and the Btk motif. The proline-rich regions are highly conserved for the most part with the exception of Bmx whose residues surrounding the PXXP motif are not conserved (TH-like) and Btk29A which is entirely unique with large numbers of glycine residues (TH-extended). Tec family members all lack a C-terminal tyrosine having an autoinhibitory function in its phosphorylated state. 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: 198259  Cd Length: 108  Bit Score: 39.39  E-value: 2.75e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207186103 1522 WYKPDISRDQAINMLKDQDP-GAFVIRDShSFRGAYglamkvaspppTTQPTKKAGDVTNELVRHFLIE---TSPK 1593
Cdd:cd10396      8 WYNKNINRSKAEKLLRDEGKeGGFMVRDS-SQPGLY-----------TVSLYTKAGGEGNPCIRHYHIKetnDSPK 71
C1_Myosin-IXb cd20884
protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXb and similar ...
 40-91 2.88e-03

protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXb and similar proteins; Myosin-IXb, also called unconventional myosin-9b (Myo9b), is an actin-dependent motor protein of the unconventional myosin IX class. It is expressed abundantly in tissues of the immune system, like lymph nodes, thymus, and spleen, and in several immune cells including dendritic cells, macrophages and CD4+ T cells. Myosin-IXb contains a Ras-associating (RA) domain, a motor domain, a protein kinase C conserved region 1 (C1), and a Rho GTPase activating (RhoGAP) domain. Myosin-IXb acts as a motorized signaling molecule that links Rho signaling to the dynamic actin cytoskeleton. It regulates leukocyte migration by controlling RhoA signaling. Myosin-IXb is also involved in the development of autoimmune diseases, including rheumatoid arthritis, systemic lupus erythematosus, and type 1 diabetes. Moreover, Myosin-IXb is a ROBO-interacting protein that suppresses RhoA activity in lung cancer cells. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410434  Cd Length: 58  Bit Score: 37.53  E-value: 2.88e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207186103   40 EAVHSHTFRLKTFKKGKHCGVCKQTV--NNEGLICRVCRLACHRKCEVKVSSSC 91
Cdd:cd20884      1 EEYNGHVFTSYQVNIMQSCEQCSSYIwaMEKALLCSVCKMTCHKKCLSKIQSHC 54
C1_RASGRP2 cd20861
protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 2 ...
 45-91 3.72e-03

protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 2 (RASGRP2) and similar proteins; RASGRP2, also called calcium and DAG-regulated guanine nucleotide exchange factor I (CalDAG-GEFI), Cdc25-like protein (CDC25L), or F25B3.3 kinase-like protein, functions as a calcium- and DAG-regulated nucleotide exchange factor specifically activating Rap through the exchange of bound GDP for GTP. It may also activate other GTPases such as RRAS, RRAS2, NRAS, KRAS but not HRAS. RASGRP2 is also involved in aggregation of platelets and adhesion of T-lymphocytes and neutrophils probably through inside-out integrin activation, as well as in the muscarinic acetylcholine receptor M1/CHRM1 signaling pathway. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410411  Cd Length: 56  Bit Score: 37.17  E-value: 3.72e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207186103   45 HTFRLKTFKKG---KHCGVCKQTVNNEGLICRVCRLACHRKCEVKVSSSC 91
Cdd:cd20861      4 HNFAERTFLRPvacRHCKNLILGIYKQGLKCRACGVNCHKQCKDHLSIEC 53
SH2_SOCS3 cd10384
Src homology 2 (SH2) domain found in suppressor of cytokine signaling (SOCS) proteins; SH2 ...
 1522-1624 4.06e-03

Src homology 2 (SH2) domain found in suppressor of cytokine signaling (SOCS) proteins; SH2 domain found in SOCS proteins. SOCS was first recognized as a group of cytokine-inducible SH2 (CIS) domain proteins comprising eight family members in human (CIS and SOCS1-SOCS7). In addition to the SH2 domain, SOCS proteins have a variable N-terminal domain and a conserved SOCS box in the C-terminal domain. SOCS proteins bind to a substrate via their SH2 domain. The prototypical members, CIS and SOCS1-SOCS3, have been shown to regulate growth hormone signaling in vitro and in a classic negative feedback response compete for binding at phosphotyrosine sites in JAK kinase and receptor pathways to displace effector proteins and target bound receptors for proteasomal degradation. Loss of SOCS activity results in excessive cytokine signaling associated with a variety of hematopoietic, autoimmune, and inflammatory diseases and certain cancers. Members (SOCS4-SOCS7) were identified by their conserved SOCS box, an adapter motif of 3 helices that associates substrate binding domains, such as the SOCS SH2 domain, ankryin, and WD40 with ubiquitin ligase components. These show limited cytokine induction. 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: 198247  Cd Length: 101  Bit Score: 38.57  E-value: 4.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1522 WYKPDISRDQAINMLKDQDPGAFVIRDSHSFRGAYGLAMKVASpppttqptkkagDVTNELV----RHFLIETSPKGVRl 1597
Cdd:cd10384     12 FYWSTVSGKEANLLLSAEPAGTFLIRDSSDQRHFFTLSVKTES------------GTKNLRIqcegGSFSLQTDPRSTQ- 78

                           90       100
                   ....*....|....*....|....*..
gi 1207186103 1598 kgcpNEPYFGCLSALVyQHSITPLALP 1624
Cdd:cd10384     79 ----PVPRFDCVLKLV-HHYMPPSAAP 100
SH2_SOCS_family cd09923
Src homology 2 (SH2) domain found in suppressor of cytokine signaling (SOCS) family; SH2 ...
 1522-1549 4.07e-03

Src homology 2 (SH2) domain found in suppressor of cytokine signaling (SOCS) family; SH2 domain found in SOCS proteins. SOCS was first recognized as a group of cytokine-inducible SH2 (CIS) domain proteins comprising eight family members in human (CIS and SOCS1-SOCS7). In addition to the SH2 domain, SOCS proteins have a variable N-terminal domain and a conserved SOCS box in the C-terminal domain. SOCS proteins bind to a substrate via their SH2 domain. The prototypical members, CIS and SOCS1-SOCS3, have been shown to regulate growth hormone signaling in vitro and in a classic negative feedback response compete for binding at phosphotyrosine sites in JAK kinase and receptor pathways to displace effector proteins and target bound receptors for proteasomal degradation. Loss of SOCS activity results in excessive cytokine signaling associated with a variety of hematopoietic, autoimmune, and inflammatory diseases and certain cancers. Members (SOCS4-SOCS7) were identified by their conserved SOCS box, an adapter motif of 3 helices that associates substrate binding domains, such as the SOCS SH2 domain, ankryin, and WD40 with ubiquitin ligase components. These show limited cytokine induction. 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: 198178  Cd Length: 81  Bit Score: 37.95  E-value: 4.07e-03
                           10        20
                   ....*....|....*....|....*...
gi 1207186103 1522 WYKPDISRDQAINMLKDQDPGAFVIRDS 1549
Cdd:cd09923      2 WYWGGITRYEAEELLAGKPEGTFLVRDS 29
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 170-301 4.11e-03

protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or PTP localized to the mitochondrion 1 (PTPMT1), also called phosphoinositide lipid phosphatase (PLIP), phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1, or PTEN-like phosphatase, is a lipid phosphatase or phosphatidylglycerophosphatase (EC 3.1.3.27) which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG). It is targeted to the mitochondrion by an N-terminal signal sequence and is found anchored to the matrix face of the inner membrane. It is essential for the biosynthesis of cardiolipin, a mitochondrial-specific phospholipid regulating the membrane integrity and activities of the organelle. PTPMT1 also plays a crucial role in hematopoietic stem cell (HSC) function, and has been shown to display activity toward phosphoprotein substrates.


Pssm-ID: 350374 [Multi-domain]  Cd Length: 149  Bit Score: 39.55  E-value: 4.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103  170 NIKEVANMLRSKHGdNYLLFNLSE-KRLDISKLNPKVLDFGwpdhHAPALDKICSICKAMDTWMNAGshNVVVIHNKGNR 248
Cdd:cd14524     28 NVRGVITMNEEYET-RFFCNSKEEwKALGVEQLRLPTVDFT----GVPSLEDLEKGVDFILKHREKG--KSVYVHCKAGR 100

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207186103  249 GRTGVVVAAYMHYSNiSASADQALDRFAMKRfyeDKVLPvgQPSQRRYVQYFS 301
Cdd:cd14524    101 GRSATIVACYLIQHK-GWSPEEAQEFLRSKR---PHILL--RLSQREVLEEFY 147
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 211-274 4.74e-03

cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of eukaryotic cyclin-dependent kinase inhibitor 3 (CDKN3) and related archaeal and bacterial proteins. CDKN3 is also known as kinase-associated phosphatase (KAP), CDK2-associated dual-specificity phosphatase, cyclin-dependent kinase interactor 1 (CDI1), or cyclin-dependent kinase-interacting protein 2 (CIP2). It has been characterized as dual-specificity phosphatase, which function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and protein-tyrosine-phosphatase (EC 3.1.3.48). It dephosphorylates CDK2 at a threonine residue in a cyclin-dependent manner, resulting in the inhibition of G1/S cell cycle progression. It also interacts with CDK1 and controls progression through mitosis by dephosphorylating CDC2. CDKN3 may also function as a tumor suppressor; its loss of function was found in a variety of cancers including glioblastoma and hepatocellular carcinoma. However, it has also been found over-expressed in many cancers such as breast, cervical, lung and prostate cancers, and may also have an oncogenic function.


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 39.55  E-value: 4.74e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207186103  211 PDHHAP-ALDKICSICKAMDTWMNAGSHnvVVIHNKGNRGRTGVVVAAYMHYSNISASADQALDR 274
Cdd:cd14505     81 PDGGVPsDIAQWQELLEELLSALENGKK--VLIHCKGGLGRTGLIAACLLLELGDTLDPEQAIAA 143
C1_aPKC_zeta cd21095
protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) ...
 43-91 5.59e-03

protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) zeta type; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. Members of this family contain C1 domain found in aPKC isoform zeta. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410448  Cd Length: 55  Bit Score: 36.89  E-value: 5.59e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207186103   43 HSHTFRLKTFKKGKHCGVCKQTV---NNEGLICRVCRLACHRKCEVKVSSSC 91
Cdd:cd21095      1 NGHLFQAKRFNRRAYCGQCSERIwglGRQGYKCINCKLLVHKRCHKLVPLTC 52
SH2_SLAP cd10344
Src homology 2 domain found in Src-like adaptor proteins; SLAP belongs to the subfamily of ...
 1522-1617 6.44e-03

Src homology 2 domain found in Src-like adaptor proteins; SLAP belongs to the subfamily of adapter proteins that negatively regulate cellular signaling initiated by tyrosine kinases. It has a myristylated N-terminus, SH3 and SH2 domains with high homology to Src family tyrosine kinases, and a unique C-terminal tail, which is important for c-Cbl binding. SLAP negatively regulates platelet-derived growth factor (PDGF)-induced mitogenesis in fibroblasts and regulates F-actin assembly for dorsal ruffles formation. c-Cbl mediated SLAP inhibition towards actin remodeling. Moreover, SLAP enhanced PDGF-induced c-Cbl phosphorylation by SFK. In contrast, SLAP mitogenic inhibition was not mediated by c-Cbl, but it rather involved a competitive mechanism with SFK for PDGF-receptor (PDGFR) association and mitogenic signaling. Accordingly, phosphorylation of the Src mitogenic substrates Stat3 and Shc were reduced by SLAP. Thus, we concluded that SLAP regulates PDGFR signaling by two independent mechanisms: a competitive mechanism for PDGF-induced Src mitogenic signaling and a non-competitive mechanism for dorsal ruffles formation mediated by c-Cbl. SLAP is a hematopoietic adaptor containing Src homology (SH)3 and SH2 motifs and a unique carboxy terminus. Unlike c-Src, SLAP lacks a tyrosine kinase domain. Unlike c-Src, SLAP does not impact resorptive function of mature osteoclasts but induces their early apoptosis. SLAP negatively regulates differentiation of osteoclasts and proliferation of their precursors. Conversely, SLAP decreases osteoclast death by inhibiting activation of caspase 3. 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: 198207  Cd Length: 104  Bit Score: 37.86  E-value: 6.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207186103 1522 WYKPDISRDQA--INMLKDQDPGAFVIRDSHSFRGAYGLAMkvaspppttqptKKAGDVTNELVRHFLIETSPKG----- 1594
Cdd:cd10344     12 WLFEGLSREKAeeLLMLPGNQVGSFLIRESETRRGCYSLSV------------RHRGSQSRDSVKHYRIFRLDNGwfyis 79

                           90       100
                   ....*....|....*....|...
gi 1207186103 1595 VRLKgcpnepyFGCLSALVYQHS 1617
Cdd:cd10344     80 PRLT-------FQCLEDMVNHYS 95
C1_Stac2 cd20881
protein kinase C conserved region 1 (C1 domain) found in SH3 and cysteine-rich ...
 42-88 6.74e-03

protein kinase C conserved region 1 (C1 domain) found in SH3 and cysteine-rich domain-containing protein 2 (Stac2) and similar proteins; Stac2, also called 24b2/Stac2, or Src homology 3 and cysteine-rich domain-containing protein 2, plays a redundant role in promoting the expression of calcium channel CACNA1S at the cell membrane, and thereby contributes to increased channel activity. It slows down the inactivation rate of the calcium channel CACNA1C. Stac2 contains a cysteine-rich C1 domain and one SH3 domain at the C-terminus. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410431  Cd Length: 59  Bit Score: 36.74  E-value: 6.74e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207186103   42 VHSHTFRLKTFKKGKHCGVCKQTV---NNEGLICRVCRLACHRKCEVKVS 88
Cdd:cd20881      3 MRTHSFQEHVFKKPSPCELCHQMIvgnSKQGLRCKMCKVSVHLWCSEEVS 52
C1_A_C-Raf cd20870
protein kinase C conserved region 1 (C1 domain) found in A- and C-Raf (Rapidly Accelerated ...
 44-92 7.77e-03

protein kinase C conserved region 1 (C1 domain) found in A- and C-Raf (Rapidly Accelerated Fibrosarcoma) kinases, and similar proteins; This group includes A-Raf and C-Raf, both of which are serine/threonine-protein kinases. A-Raf, also called proto-oncogene A-Raf or proto-oncogene A-Raf-1, 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. C-Raf, also known as proto-oncogene 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 mid-gestation 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. Both A- and C-Raf are mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), 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. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain (C1), and a catalytic kinase domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410420  Cd Length: 52  Bit Score: 36.47  E-value: 7.77e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1207186103   44 SHTFRLKTFKKGKHCGVCKQTVNNeGLICRVCRLACHRKCEVKVSSSCV 92
Cdd:cd20870      3 THNFVRKTFLKLAFCDICQKFLLN-GFRCQTCGYKFHEHCSTKVPTMCV 50
SH2_C-SH2_PLC_gamma_like cd09932
C-terminal Src homology 2 (C-SH2) domain in Phospholipase C gamma; Phospholipase C gamma is a ...
 1519-1562 8.30e-03

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: 37.63  E-value: 8.30e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1207186103 1519 SKFWYKPDISRDQAINMLK--DQDpGAFVIRDSHSFRGAYGLAMKV 1562
Cdd:cd09932      3 SKEWFHANLTREQAEEMLMrvPRD-GAFLVRPSETDPNSFAISFRA 47
SH2_HSH2_like cd09946
Src homology 2 domain found in hematopoietic SH2 (HSH2) protein; HSH2 is thought to function ...
 1522-1594 8.38e-03

Src homology 2 domain found in hematopoietic SH2 (HSH2) protein; HSH2 is thought to function as an adapter protein involved in tyrosine kinase signaling. It may also be involved in regulating cytokine signaling and cytoskeletal reorganization in hematopoietic cells. HSH2 contains several putative protein-binding motifs, SH3-binding proline-rich regions, and phosphotyrosine sites, but lacks enzymatic motifs. HSH2 was found to interact with cytokine-regulated tyrosine kinase c-FES and an activated Cdc42-associated tyrosine kinase ACK1. HSH2 binds c-FES through both its C-terminal region and its N-terminal region including the SH2 domain and binds ACK1 via its N-terminal proline-rich region. Both kinases bound and tyrosine-phosphorylated HSH2 in mammalian cells. 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: 198199  Cd Length: 102  Bit Score: 37.56  E-value: 8.38e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207186103 1522 WYKPDISRDQAINMLKDQDPGAFVIRDSHSFRGaYGLAMKVASPppttqptkkagdvtnelVRHFLIETSPKG 1594
Cdd:cd09946      9 WFHGAISREAAENMLESQPLGSFLIRVSHSHVG-YTLSYKAQSS-----------------CRHFMVKLLDDG 63
SH2_Tec_Btk cd10397
Src homology 2 (SH2) domain found in Tec protein, Bruton's tyrosine kinase (Btk); A member of ...
 1522-1594 8.44e-03

Src homology 2 (SH2) domain found in Tec protein, Bruton's tyrosine kinase (Btk); A member of the Tec protein tyrosine kinase Btk is expressed in bone marrow, spleen, all hematopoietic cells except T lymphocytes and plasma cells where it plays a crucial role in B cell maturation and mast cell activation. Btk has been shown to interact with GNAQ, PLCG2, protein kinase D1, B-cell linker, SH3BP5, caveolin 1, ARID3A, and GTF2I. Most of the Tec family members have a PH domain (Txk and the short (type 1) splice variant of Drosophila Btk29A are exceptions), a Tec homology (TH) domain, a SH3 domain, a SH2 domain, and a protein kinase catalytic domain. Btk is implicated in the primary immunodeficiency disease X-linked agammaglobulinemia (Bruton's agammaglobulinemia). The TH domain consists of a Zn2+-binding Btk motif and a proline-rich region. The Btk motif is found in Tec kinases, Ras GAP, and IGBP. It is crucial for the function of Tec PH domains and it's lack of presence in Txk is not surprising since it lacks a PH domain. The type 1 splice form of the Drosophila homolog also lacks both the PH domain and the Btk motif. The proline-rich regions are highly conserved for the most part with the exception of Bmx whose residues surrounding the PXXP motif are not conserved (TH-like) and Btk29A which is entirely unique with large numbers of glycine residues (TH-extended). Tec family members all lack a C-terminal tyrosine having an autoinhibitory function in its phosphorylated state. Two tyrosine phosphorylation (pY) sites have been identified in Btk: one located in the activation loop of the catalytic domain which regulates the transition between open (active) and closed (inactive) states and the other in its SH3 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: 198260 [Multi-domain]  Cd Length: 106  Bit Score: 37.89  E-value: 8.44e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207186103 1522 WYKPDISRDQAINMLKDQDP-GAFVIRDShSFRGAYglamkvaspppTTQPTKKAGDVTNELVRHFLIETSPKG 1594
Cdd:cd10397      8 WYSKNMTRSQAEQLLKQEGKeGGFIVRDS-SKAGKY-----------TVSVFAKSAGDPQGVIRHYVVCSTPQS 69
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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