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Conserved domains on  [gi|568906148|ref|XP_006495938|]
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tensin-1 isoform X20 [Mus musculus]

Protein Classification

phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN( domain architecture ID 13042393)

phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN acts as a dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins

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 ...
96-254 4.05e-114

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: 357.75  E-value: 4.05e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148   96 DLVYVTERIIAVSFPSTANEENFRSNLREVAQMLKSKHGGNYLLFNLSEQRPDITKLHAKVLEFGWPDLHTPALEKICSV 175
Cdd:cd14560     1 DLVYITERIISVSFPSTAEEPSFRSNLKEVAQMLKSKHGDNYLLFNLSERRHDISKLHPKVLDFGWPDLHAPALEKICSI 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568906148  176 CKAMDTWLNADPHNVVVLHNKGNRGRIGVVIAAYLHYSNISASADQALDRFAMKRFYEDKIVPIGQPSQRRYVHYFSGL 254
Cdd:cd14560    81 CKAMDTWLNADPHNVVVIHNKGNRGRTGVVIAAYMHYSNISASADQALDRFAMKRFYEDKVVPVGQPSQKRYVHYFSGL 159
PTB_tensin cd01213
Tensin Phosphotyrosine-binding (PTB) domain; Tensin is a a focal adhesion protein, which ...
1690-1823 1.97e-86

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: 277.97  E-value: 1.97e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1690 GAACNVLFVNSVDMESLTGPQAISKATSETLAADPTPAATIVHFKVSAQGITLTDNQRKLFFRRHYPLNTVTFCDLDPQE 1769
Cdd:cd01213     1 GAACNVLYLGSVDTESLTGPQAVRKAVSETLERDPLPTPTVVHFKVSEQGITLTDNQRKLFFRRHYPLNTVSFCGMDPEN 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568906148 1770 RKWMKTE--GGAPAKLFGFVARKQGSTTDNACHLFAELDPNQPASAIVNFVSKVML 1823
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. ...
1553-1668 2.66e-68

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: 225.38  E-value: 2.66e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1553 TSKYWYKPEISREQAIALLKDQEPGAFIIRDSHSFRGAYGLAMKVSSPPPTITQQGKKGDMTHELVRHFLIETGPRGVKL 1632
Cdd:cd09927     1 TSKYWYKPNISRDQAIALLKDKPPGTFLVRDSTTYKGAYGLAVKVATPPPGVNPFEAKGDPESELVRHFLIEPSPKGVKL 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568906148 1633 KGCPNEPNFGSLSALVYQHSVIPLALPCKLVIPSRD 1668
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 ...
261-387 7.40e-50

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: 173.23  E-value: 7.40e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148   261 MNNKPLFLHHVIMHGIPNFESKGGCRPFLRIYQAMQPV-YTSGIYNIPGDSQASICITIEP-GLLLKGDILLKCYHKKFR 338
Cdd:pfam10409    1 PPPKPLTLHSIILHGIPNFKSGGGCRPYIRIYQNKKKVfSTSGKYKKLKEYQQDDCVILFPkGIPVQGDVLVEFYHKGSD 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568906148   339 SPARDVIFRVQFHTCAIHDLGVVFGKEDLDEAFKD---DRFPDYGKVEFVFS 387
Cdd:pfam10409   81 LLSEEKMFRFWFNTSFIEDNTLTLPKNELDKADKDkkdKRFPKDFKVELLFS 132
PHA03247 super family cl33720
large tegument protein UL36; Provisional
980-1556 1.68e-11

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 69.97  E-value: 1.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  980 RQPAEPPGPLRRRAASD-GQYENQSPEAtsPRSPGVRSPVqcvspelALTIAlnPGGRPKEPHLHSYKEAFEEMEGTSPS 1058
Cdd:PHA03247 2481 RRPAEARFPFAAGAAPDpGGGGPPDPDA--PPAPSRLAPA-------ILPDE--PVGEPVHPRMLTWIRGLEELASDDAG 2549
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1059 SPPHSVARSPPGLA---KTPLSALGLKPHNPAdillhPTGVARRLIQPEEdegeevTKPPEEPRSYVESVARTAVAGPRA 1135
Cdd:PHA03247 2550 DPPPPLPPAAPPAApdrSVPPPRPAPRPSEPA-----VTSRARRPDAPPQ------SARPRAPVDDRGDPRGPAPPSPLP 2618
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1136 QDVEPKSFSAPAAHAYGHETPLRNGTPGGSFVSPSPLSTSSPI-LSADSTSVGSFPSVVSSDQGPRTPFQPMLDSSIRSG 1214
Cdd:PHA03247 2619 PDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVsRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSL 2698
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1215 SL-----GQPSPAALSYQSSSPVPVGgssynsPDYSLQPFSSSPESQGQPQYSAASVhmVPGSPQARHRTVGTNTPPSPG 1289
Cdd:PHA03247 2699 ADpppppPTPEPAPHALVSATPLPPG------PAAARQASPALPAAPAPPAVPAGPA--TPGGPARPARPPTTAGPPAPA 2770
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1290 FGRRAVNP-----TMAAPGSPSLSHRQVMGPSGPGFHGNVVSGhPASAATTPGSPSlgrhpvgshqvPGLHSSVVTTPGS 1364
Cdd:PHA03247 2771 PPAAPAAGpprrlTRPAVASLSESRESLPSPWDPADPPAAVLA-PAAALPPAASPA-----------GPLPPPTSAQPTA 2838
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1365 PSLGRHPgahqgnLASSLHSNAVISPGSPSLGRHLGGSGSVVPGSPS------LDRHAAYGGYST--------------- 1423
Cdd:PHA03247 2839 PPPPPGP------PPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPArppvrrLARPAVSRSTESfalppdqperppqpq 2912
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1424 -PEDRRPTLSRQSSASGYQAPSTPSFPVSPAYYPGLSSPATSPSPDSAAFRQGSPTPALPEKRRMSVGDRAGSLPNYATI 1502
Cdd:PHA03247 2913 aPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASS 2992
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1503 NGKVSSSPVAnGMASGSSTVSFsHTLPDFSKYSM------PDNSPETRAKVKFVQDTSKY 1556
Cdd:PHA03247 2993 TPPLTGHSLS-RVSSWASSLAL-HEETDPPPVSLkqtlwpPDDTEDSDADSLFDSDSERS 3050
C1 super family cl00040
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
2-23 7.79e-08

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.


The actual alignment was detected with superfamily member cd20888:

Pssm-ID: 412127  Cd Length: 57  Bit Score: 50.64  E-value: 7.79e-08
                          10        20
                  ....*....|....*....|..
gi 568906148    2 VCSFSCHRKCQAKVAAPCVPPS 23
Cdd:cd20888    35 VCKLSCHKKCEAKVATPCVPAV 56
PHA03247 super family cl33720
large tegument protein UL36; Provisional
644-1140 9.56e-08

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 57.64  E-value: 9.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  644 PYEAANRVIPVHSSHSAPIRPSYSAQEGlagyqregpHPAWSQQVTSAHCGCDPSGLFRSQSFPDVEPQLPQAPTRGGSS 723
Cdd:PHA03247 2560 PPAAPDRSVPPPRPAPRPSEPAVTSRAR---------RPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPS 2630
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  724 REAVQRGLNSWQQQQPHPPPRQQERSPLQSLARSKPSPQLSAETPVAALPEFPRAASQQEIEQSIETLnmlmldlepASA 803
Cdd:PHA03247 2631 PSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSL---------ADP 2701
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  804 AAPLHKSQSVPGAWPGASPLSSQPllGSSRQSHPLTQSRSGYIPSGHSLGTPelVSSGRPYSPYDyqlhPAGSNQSFHPK 883
Cdd:PHA03247 2702 PPPPPTPEPAPHALVSATPLPPGP--AAARQASPALPAAPAPPAVPAGPATP--GGPARPARPPT----TAGPPAPAPPA 2773
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  884 SPASStflPSPHSSAGPQEPPASLPGLIAQPQLPPKETTSDPSRTPEEEPlnleglvAHRVAVYNARLQSLRQSRGFQPS 963
Cdd:PHA03247 2774 APAAG---PPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPP-------AASPAGPLPPPTSAQPTAPPPPP 2843
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  964 PHWRRSASLSGVQArerqpaePPGPLRRRAASdgqyENQSPEATSPRSPGVRSPVQCVSPELALTIALNPGGRPKEPHLH 1043
Cdd:PHA03247 2844 GPPPPSLPLGGSVA-------PGGDVRRRPPS----RSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQ 2912
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1044 SYKEAFEEME---GTSPSSPPHSVARSPPGLAKTPLSALGLKPH----NPADILLHPTGVA--RRLIQPEEDEGEEVTKP 1114
Cdd:PHA03247 2913 APPPPQPQPQpppPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSgavpQPWLGALVPGRVAvpRFRVPQPAPSREAPASS 2992
                         490       500
                  ....*....|....*....|....*.
gi 568906148 1115 PEEPRSYVESvARTAVAGPRAQDVEP 1140
Cdd:PHA03247 2993 TPPLTGHSLS-RVSSWASSLALHEET 3017
 
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 ...
96-254 4.05e-114

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: 357.75  E-value: 4.05e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148   96 DLVYVTERIIAVSFPSTANEENFRSNLREVAQMLKSKHGGNYLLFNLSEQRPDITKLHAKVLEFGWPDLHTPALEKICSV 175
Cdd:cd14560     1 DLVYITERIISVSFPSTAEEPSFRSNLKEVAQMLKSKHGDNYLLFNLSERRHDISKLHPKVLDFGWPDLHAPALEKICSI 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568906148  176 CKAMDTWLNADPHNVVVLHNKGNRGRIGVVIAAYLHYSNISASADQALDRFAMKRFYEDKIVPIGQPSQRRYVHYFSGL 254
Cdd:cd14560    81 CKAMDTWLNADPHNVVVIHNKGNRGRTGVVIAAYMHYSNISASADQALDRFAMKRFYEDKVVPVGQPSQKRYVHYFSGL 159
PTB_tensin cd01213
Tensin Phosphotyrosine-binding (PTB) domain; Tensin is a a focal adhesion protein, which ...
1690-1823 1.97e-86

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: 277.97  E-value: 1.97e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1690 GAACNVLFVNSVDMESLTGPQAISKATSETLAADPTPAATIVHFKVSAQGITLTDNQRKLFFRRHYPLNTVTFCDLDPQE 1769
Cdd:cd01213     1 GAACNVLYLGSVDTESLTGPQAVRKAVSETLERDPLPTPTVVHFKVSEQGITLTDNQRKLFFRRHYPLNTVSFCGMDPEN 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568906148 1770 RKWMKTE--GGAPAKLFGFVARKQGSTTDNACHLFAELDPNQPASAIVNFVSKVML 1823
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. ...
1553-1668 2.66e-68

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: 225.38  E-value: 2.66e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1553 TSKYWYKPEISREQAIALLKDQEPGAFIIRDSHSFRGAYGLAMKVSSPPPTITQQGKKGDMTHELVRHFLIETGPRGVKL 1632
Cdd:cd09927     1 TSKYWYKPNISRDQAIALLKDKPPGTFLVRDSTTYKGAYGLAVKVATPPPGVNPFEAKGDPESELVRHFLIEPSPKGVKL 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568906148 1633 KGCPNEPNFGSLSALVYQHSVIPLALPCKLVIPSRD 1668
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 ...
261-387 7.40e-50

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: 173.23  E-value: 7.40e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148   261 MNNKPLFLHHVIMHGIPNFESKGGCRPFLRIYQAMQPV-YTSGIYNIPGDSQASICITIEP-GLLLKGDILLKCYHKKFR 338
Cdd:pfam10409    1 PPPKPLTLHSIILHGIPNFKSGGGCRPYIRIYQNKKKVfSTSGKYKKLKEYQQDDCVILFPkGIPVQGDVLVEFYHKGSD 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568906148   339 SPARDVIFRVQFHTCAIHDLGVVFGKEDLDEAFKD---DRFPDYGKVEFVFS 387
Cdd:pfam10409   81 LLSEEKMFRFWFNTSFIEDNTLTLPKNELDKADKDkkdKRFPKDFKVELLFS 132
PTB pfam08416
Phosphotyrosine-binding domain; The phosphotyrosine-binding domain (PTB, also ...
1692-1828 2.30e-37

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: 137.48  E-value: 2.30e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  1692 ACNVLFVNSVDMESLTGPQAISKAT--SETLAADPTPAATIVHFKVSAQGITLTDNQRKLFFrRHYPLNTVTFCDLDPQE 1769
Cdd:pfam08416    1 QYRVEHLTTFELDSLTGLQAVEDAIrkLQLLDAQGRVWTQEMLLQVSDQGITLTDNETKEEL-ESYPLDSISHCQAVLND 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568906148  1770 RKWmkteggapAKLFGFVARKQGSTTDNAcHLFA--ELDPNQPASAIVNFVSKVMLSAGQK 1828
Cdd:pfam08416   80 GRY--------NSILALVCQEPGQSKPDV-HLFQcdELGAELIAEDIESALSDVRLGKPKK 131
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
1689-1829 3.53e-22

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: 93.92  E-value: 3.53e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148   1689 QGAACNVLFVNSVDMESLTGPQAISKATSETLAADP--TPAATIVHFKVSAQGITLTDNQRKlFFRRHYPLNTVTFCDLD 1766
Cdd:smart00462    2 SGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAQGseKKEPQKVILSISSRGVKLIDEDTK-AVLHEHPLRRISFCAVG 80
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568906148   1767 PQErkwmkteggapAKLFGFVARKQGStTDNACHLFAELDP--NQPASAIVNFVSKVMLSAGQKR 1829
Cdd:smart00462   81 PDD-----------LDVFGYIARDPGS-SRFACHVFRCEKAaeDIALAIGQAFQLAYELKLKARS 133
SH2 smart00252
Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides ...
1557-1655 2.44e-12

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: 64.17  E-value: 2.44e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148   1557 WYKPEISREQAIALLKDQEPGAFIIRDSHSFRGAYGLAMKVssppptitqqgkkgdmtHELVRHFLIE-TGPRGVKLKGc 1635
Cdd:smart00252    3 WYHGFISREEAEKLLKNEGDGDFLVRDSESSPGDYVLSVRV-----------------KGKVKHYRIRrNEDGKFYLEG- 64
                            90       100
                    ....*....|....*....|..
gi 568906148   1636 pnEPNFGSLSALV--YQHSVIP 1655
Cdd:smart00252   65 --GRKFPSLVELVehYQKNSLG 84
PHA03247 PHA03247
large tegument protein UL36; Provisional
980-1556 1.68e-11

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 69.97  E-value: 1.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  980 RQPAEPPGPLRRRAASD-GQYENQSPEAtsPRSPGVRSPVqcvspelALTIAlnPGGRPKEPHLHSYKEAFEEMEGTSPS 1058
Cdd:PHA03247 2481 RRPAEARFPFAAGAAPDpGGGGPPDPDA--PPAPSRLAPA-------ILPDE--PVGEPVHPRMLTWIRGLEELASDDAG 2549
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1059 SPPHSVARSPPGLA---KTPLSALGLKPHNPAdillhPTGVARRLIQPEEdegeevTKPPEEPRSYVESVARTAVAGPRA 1135
Cdd:PHA03247 2550 DPPPPLPPAAPPAApdrSVPPPRPAPRPSEPA-----VTSRARRPDAPPQ------SARPRAPVDDRGDPRGPAPPSPLP 2618
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1136 QDVEPKSFSAPAAHAYGHETPLRNGTPGGSFVSPSPLSTSSPI-LSADSTSVGSFPSVVSSDQGPRTPFQPMLDSSIRSG 1214
Cdd:PHA03247 2619 PDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVsRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSL 2698
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1215 SL-----GQPSPAALSYQSSSPVPVGgssynsPDYSLQPFSSSPESQGQPQYSAASVhmVPGSPQARHRTVGTNTPPSPG 1289
Cdd:PHA03247 2699 ADpppppPTPEPAPHALVSATPLPPG------PAAARQASPALPAAPAPPAVPAGPA--TPGGPARPARPPTTAGPPAPA 2770
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1290 FGRRAVNP-----TMAAPGSPSLSHRQVMGPSGPGFHGNVVSGhPASAATTPGSPSlgrhpvgshqvPGLHSSVVTTPGS 1364
Cdd:PHA03247 2771 PPAAPAAGpprrlTRPAVASLSESRESLPSPWDPADPPAAVLA-PAAALPPAASPA-----------GPLPPPTSAQPTA 2838
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1365 PSLGRHPgahqgnLASSLHSNAVISPGSPSLGRHLGGSGSVVPGSPS------LDRHAAYGGYST--------------- 1423
Cdd:PHA03247 2839 PPPPPGP------PPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPArppvrrLARPAVSRSTESfalppdqperppqpq 2912
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1424 -PEDRRPTLSRQSSASGYQAPSTPSFPVSPAYYPGLSSPATSPSPDSAAFRQGSPTPALPEKRRMSVGDRAGSLPNYATI 1502
Cdd:PHA03247 2913 aPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASS 2992
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1503 NGKVSSSPVAnGMASGSSTVSFsHTLPDFSKYSM------PDNSPETRAKVKFVQDTSKY 1556
Cdd:PHA03247 2993 TPPLTGHSLS-RVSSWASSLAL-HEETDPPPVSLkqtlwpPDDTEDSDADSLFDSDSERS 3050
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
159-274 1.21e-09

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 57.37  E-value: 1.21e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148    159 FGWPDLHTPAL-EKICSVCKAMDTWLNA-DPHNVVVLHNKGNRGRIGVVIAAYLHYSNISASAdqaldrfamkrfyedki 236
Cdd:smart00404    8 TGWPDHGVPESpDSILELLRAVKKNLNQsESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEA----------------- 70
                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 568906148    237 vpiGQPSQRRYVHYFSGLLSGSIKMNNKPLFLHHVIMH 274
Cdd:smart00404   71 ---GEVDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
SH2 pfam00017
SH2 domain;
1557-1651 2.07e-08

SH2 domain;


Pssm-ID: 425423 [Multi-domain]  Cd Length: 77  Bit Score: 52.60  E-value: 2.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  1557 WYKPEISREQAIALLK-DQEPGAFIIRDSHSFRGAYGLAMKVssppptitqQGKkgdmthelVRHFLI-ETGPRGVKLKG 1634
Cdd:pfam00017    1 WYHGKISRQEAERLLLnGKPDGTFLVRESESTPGGYTLSVRD---------DGK--------VKHYKIqSTDNGGYYISG 63
                           90
                   ....*....|....*..
gi 568906148  1635 cpnEPNFGSLSALVYQH 1651
Cdd:pfam00017   64 ---GVKFSSLAELVEHY 77
C1_TNS1_v cd20888
protein kinase C conserved region 1 (C1 domain) found in tensin-1 (TNS1) variant and similar ...
2-23 7.79e-08

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: 50.64  E-value: 7.79e-08
                          10        20
                  ....*....|....*....|..
gi 568906148    2 VCSFSCHRKCQAKVAAPCVPPS 23
Cdd:cd20888    35 VCKLSCHKKCEAKVATPCVPAV 56
PHA03247 PHA03247
large tegument protein UL36; Provisional
644-1140 9.56e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 57.64  E-value: 9.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  644 PYEAANRVIPVHSSHSAPIRPSYSAQEGlagyqregpHPAWSQQVTSAHCGCDPSGLFRSQSFPDVEPQLPQAPTRGGSS 723
Cdd:PHA03247 2560 PPAAPDRSVPPPRPAPRPSEPAVTSRAR---------RPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPS 2630
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  724 REAVQRGLNSWQQQQPHPPPRQQERSPLQSLARSKPSPQLSAETPVAALPEFPRAASQQEIEQSIETLnmlmldlepASA 803
Cdd:PHA03247 2631 PSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSL---------ADP 2701
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  804 AAPLHKSQSVPGAWPGASPLSSQPllGSSRQSHPLTQSRSGYIPSGHSLGTPelVSSGRPYSPYDyqlhPAGSNQSFHPK 883
Cdd:PHA03247 2702 PPPPPTPEPAPHALVSATPLPPGP--AAARQASPALPAAPAPPAVPAGPATP--GGPARPARPPT----TAGPPAPAPPA 2773
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  884 SPASStflPSPHSSAGPQEPPASLPGLIAQPQLPPKETTSDPSRTPEEEPlnleglvAHRVAVYNARLQSLRQSRGFQPS 963
Cdd:PHA03247 2774 APAAG---PPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPP-------AASPAGPLPPPTSAQPTAPPPPP 2843
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  964 PHWRRSASLSGVQArerqpaePPGPLRRRAASdgqyENQSPEATSPRSPGVRSPVQCVSPELALTIALNPGGRPKEPHLH 1043
Cdd:PHA03247 2844 GPPPPSLPLGGSVA-------PGGDVRRRPPS----RSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQ 2912
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1044 SYKEAFEEME---GTSPSSPPHSVARSPPGLAKTPLSALGLKPH----NPADILLHPTGVA--RRLIQPEEDEGEEVTKP 1114
Cdd:PHA03247 2913 APPPPQPQPQpppPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSgavpQPWLGALVPGRVAvpRFRVPQPAPSREAPASS 2992
                         490       500
                  ....*....|....*....|....*.
gi 568906148 1115 PEEPRSYVESvARTAVAGPRAQDVEP 1140
Cdd:PHA03247 2993 TPPLTGHSLS-RVSSWASSLALHEET 3017
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
155-251 1.12e-05

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 46.89  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  155 KVLEFGWPDLHTPALEKICSVCKAMDTWLNADpHNVVVlHNKGNRGRIGVVIAAYLHYSNIsaSADQALDRFAMKRfyeD 234
Cdd:COG2453    49 EYLHLPIPDFGAPDDEQLQEAVDFIDEALREG-KKVLV-HCRGGIGRTGTVAAAYLVLLGL--SAEEALARVRAAR---P 121
                          90
                  ....*....|....*..
gi 568906148  235 KIVPigQPSQRRYVHYF 251
Cdd:COG2453   122 GAVE--TPAQRAFLERF 136
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
1221-1544 3.11e-05

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 49.14  E-value: 3.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  1221 PAALSYQSSSPVPVGGSSYNSP-DYSLQPFSSSPESQGQPQYSAASVHMVPgSPQARHRTVGTNTPP----SPGFGRRAV 1295
Cdd:pfam05109  466 PTVSTADVTSPTPAGTTSGASPvTPSPSPRDNGTESKAPDMTSPTSAVTTP-TPNATSPTPAVTTPTpnatSPTLGKTSP 544
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  1296 NPTMAAPGSPSLSHR-QVMGPSGPGFHGNVVSGHPASAATTPG----SPSLGRHP----VGSHQVPGLHSSVVTTPGSPS 1366
Cdd:pfam05109  545 TSAVTTPTPNATSPTpAVTTPTPNATIPTLGKTSPTSAVTTPTpnatSPTVGETSpqanTTNHTLGGTSSTPVVTSPPKN 624
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  1367 LGRHPGAHQGNLASSLHSNAVISPGSPSLGRHLGGSGSVVPGSPSLDRHAAYGGYSTpedrrpTLSRQSSASGYQAPSTp 1446
Cdd:pfam05109  625 ATSAVTTGQHNITSSSTSSMSLRPSSISETLSPSTSDNSTSHMPLLTSAHPTGGENI------TQVTPASTSTHHVSTS- 697
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  1447 sfpvSPAYYPGLSSPATSPSPDSAAFRQG--SPTPALPEKRRMSVGDRAG---SLPNYATINGKVSSSPVANGMASGSST 1521
Cdd:pfam05109  698 ----SPAPRPGTTSQASGPGNSSTSTKPGevNVTKGTPPKNATSPQAPSGqktAVPTVTSTGGKANSTTGGKHTTGHGAR 773
                          330       340
                   ....*....|....*....|...
gi 568906148  1522 VSFSHTlpdfSKYSMPDNSPETR 1544
Cdd:pfam05109  774 TSTEPT----TDYGGDSTTPRTR 792
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
1256-1484 1.20e-03

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 43.59  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1256 QGQPQYSAASVHMVPGSPQARHRTVGTNTPPSPGFGrraVNPTMAAPGSPSLSHRQVMGPSGPGFHGNVVSGHPASAATT 1335
Cdd:COG3469    12 AGGASATAVTLLGAAATAASVTLTAATATTVVSTTG---SVVVAASGSAGSGTGTTAASSTAATSSTTSTTATATAAAAA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1336 PGSPSLGRHPVGSHQVPGLHSSVVTTPGSPslgrhpgahQGNLASSLHSNAVISPGSPSLGRHLGGSGSVVPGSPSLDrh 1415
Cdd:COG3469    89 ATSTSATLVATSTASGANTGTSTVTTTSTG---------AGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTE-- 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568906148 1416 AAYGGYSTPedrrptlsrqsSASGYQAPSTPSFPVSPAYYPGLSSPATSPSPDSAAFRQGSPTPALPEK 1484
Cdd:COG3469   158 TATGGTTTT-----------STTTTTTSASTTPSATTTATATTASGATTPSATTTATTTGPPTPGLPKH 215
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
751-1078 7.04e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 41.29  E-value: 7.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148   751 LQSLARSKPSPQLSAETPVAALPEFPRAASQQEIEQSIETLNMLmlDLEPASAAAPLHKSQSVPGAWPGASPLSSQPLLG 830
Cdd:pfam03154  174 LQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQP--PNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQP 251
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148   831 ---------SSRQSHPLTQSRSGYIPSGHSLGT-PELVSSGRPYSPYDYqlhPAGSNQSFHPKSPA--------SSTFLP 892
Cdd:pfam03154  252 mtqppppsqVSPQPLPQPSLHGQMPPMPHSLQTgPSHMQHPVPPQPFPL---TPQSSQSQVPPGPSpaapgqsqQRIHTP 328
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148   893 SPHSSAGPQEPPASLP---GLIAQPQLPPKETTSDP---------------SRTPEEEPLNLEGLVA----------HRV 944
Cdd:pfam03154  329 PSQSQLQSQQPPREQPlppAPLSMPHIKPPPTTPIPqlpnpqshkhpphlsGPSPFQMNSNLPPPPAlkplsslsthHPP 408
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148   945 AVYNARLQSLRQSRGFQPSPH----WRRSASL----------SGVQARERQPAEPPGPLRRRAASDGQYENQSPEATSPR 1010
Cdd:pfam03154  409 SAHPPPLQLMPQSQQLPPPPAqppvLTQSQSLpppaashpptSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPTSTSSA 488
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568906148  1011 SPGVRSPVQcVSPELALTIALNPGGrpKEPHLHSYKEAFEEMEGTSPSSPPHSVARSPPGLAKTPLSA 1078
Cdd:pfam03154  489 MPGIQPPSS-ASVSSSGPVPAAVSC--PLPPVQIKEEALDEAEEPESPPPPPRSPSPEPTVVNTPSHA 553
 
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 ...
96-254 4.05e-114

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: 357.75  E-value: 4.05e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148   96 DLVYVTERIIAVSFPSTANEENFRSNLREVAQMLKSKHGGNYLLFNLSEQRPDITKLHAKVLEFGWPDLHTPALEKICSV 175
Cdd:cd14560     1 DLVYITERIISVSFPSTAEEPSFRSNLKEVAQMLKSKHGDNYLLFNLSERRHDISKLHPKVLDFGWPDLHAPALEKICSI 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568906148  176 CKAMDTWLNADPHNVVVLHNKGNRGRIGVVIAAYLHYSNISASADQALDRFAMKRFYEDKIVPIGQPSQRRYVHYFSGL 254
Cdd:cd14560    81 CKAMDTWLNADPHNVVVIHNKGNRGRTGVVIAAYMHYSNISASADQALDRFAMKRFYEDKVVPVGQPSQKRYVHYFSGL 159
PTP_tensin cd14508
protein tyrosine phosphatase-like domain of tensins; The tensin family of intracellular ...
96-254 2.65e-94

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: 301.23  E-value: 2.65e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148   96 DLVYVTERIIAVSFPSTANEENFRSNLREVAQMLKSKHGGNYLLFNLSEQRPDITKLHAKVLEFGWPDLHTPALEKICSV 175
Cdd:cd14508     1 DLTYITERIIALSFPSTCSEQTYRHNLREAAHLLQSKHGDNYMVFNLSERRHDLRSLNPKVLDFGWPELHAPPLEKLCSI 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568906148  176 CKAMDTWLNADPHNVVVLHNKGNRGRIGVVIAAYLHYSNISASADQALDRFAMKRFYEDKIVPIGQPSQRRYVHYFSGL 254
Cdd:cd14508    81 CKNMDSWLNADPQNVVVLHCKGGKGRLGVVVSAYMHYSKISATADQALDRFAMKRFYDDKVGPLGQPSQKRYVGYFSGL 159
PTB_tensin cd01213
Tensin Phosphotyrosine-binding (PTB) domain; Tensin is a a focal adhesion protein, which ...
1690-1823 1.97e-86

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: 277.97  E-value: 1.97e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1690 GAACNVLFVNSVDMESLTGPQAISKATSETLAADPTPAATIVHFKVSAQGITLTDNQRKLFFRRHYPLNTVTFCDLDPQE 1769
Cdd:cd01213     1 GAACNVLYLGSVDTESLTGPQAVRKAVSETLERDPLPTPTVVHFKVSEQGITLTDNQRKLFFRRHYPLNTVSFCGMDPEN 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568906148 1770 RKWMKTE--GGAPAKLFGFVARKQGSTTDNACHLFAELDPNQPASAIVNFVSKVML 1823
Cdd:cd01213    81 RKWQKYDlrGSKPSRIFGFVARKQGSSTENVCHLFAELDPEQPASAIVNFVNKVLL 136
PTP_tensin-3 cd14561
protein tyrosine phosphatase-like domain of tensin-3; Tensin-3 (TNS3) is also called ...
96-254 4.15e-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: 4.15e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148   96 DLVYVTERIIAVSFPSTANEENFRSNLREVAQMLKSKHGGNYLLFNLSEQRPDITKLHAKVLEFGWPDLHTPALEKICSV 175
Cdd:cd14561     1 DLTYITERIIAVSFPADCSEETYLHNLQDVTRMLKSKHGDNYLVLNLSEKRYELTKLNPKIMDVGWPDLHAPPLDKMCTI 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568906148  176 CKAMDTWLNADPHNVVVLHNKGNRGRIGVVIAAYLHYSNISASADQALDRFAMKRFYEDKIVPIGQPSQRRYVHYFSGL 254
Cdd:cd14561    81 CKAMESWLNSDPLHVVVIHCRGGKGRIGVVISSYMHFTNVSASADQALDRFAMKKFYDDKVSALMQPSQKRYVQFLSGL 159
PTP_tensin-2 cd14562
protein tyrosine phosphatase-like domain of tensin-2; Tensin-2 (TNS2) is also called ...
96-254 4.20e-80

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: 260.65  E-value: 4.20e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148   96 DLVYVTERIIAVSFPSTANEENFRSNLREVAQMLKSKHGGNYLLFNLSEQRPDITKLHAKVLEFGWPDLHTPALEKICSV 175
Cdd:cd14562     1 DLTYITERIISVFFPPALEEQRYRGNLREVAQMLKSKHEDKYLLFNLSEKRHDITRLNPKVQDFGWPDLHAPPLDKICSI 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568906148  176 CKAMDTWLNADPHNVVVLHNKGNRGRIGVVIAAYLHYSNISASADQALDRFAMKRFYEDKIVPIGQPSQRRYVHYFSGL 254
Cdd:cd14562    81 CKAMETWLNADPQHVVVLHCKGNKGKTGVIVAAYMHYSKISAGADQALSTLAMRKFCEDKVATSLQPSQRRYISYFGGL 159
SH2_Tensin_like cd09927
Src homology 2 domain found in Tensin-like proteins; SH2 domain found in Tensin-like proteins. ...
1553-1668 2.66e-68

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: 225.38  E-value: 2.66e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1553 TSKYWYKPEISREQAIALLKDQEPGAFIIRDSHSFRGAYGLAMKVSSPPPTITQQGKKGDMTHELVRHFLIETGPRGVKL 1632
Cdd:cd09927     1 TSKYWYKPNISRDQAIALLKDKPPGTFLVRDSTTYKGAYGLAVKVATPPPGVNPFEAKGDPESELVRHFLIEPSPKGVKL 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568906148 1633 KGCPNEPNFGSLSALVYQHSVIPLALPCKLVIPSRD 1668
Cdd:cd09927    81 KGCPNEPVFGSLSALVYQHSITPLALPCKLRIPDRD 116
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
96-254 1.69e-64

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: 216.29  E-value: 1.69e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148   96 DLVYVTERIIAVSFPSTAN-EENFRSNLREVAQMLKSKHGGNYLLFNLSEQRPDI-TKLHAKVLEFGWPDLHTPALEKIC 173
Cdd:cd14497     1 DLSYITPRIIAMSFPATGYpESLYRNSIDDVANFLNTHHPDHYMIFNLSEEEYDDdSKFEGRVLHYGFPDHHPPPLGLLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  174 SVCKAMDTWLNADPHNVVVLHNKGNRGRIGVVIAAYLHYSNISASADQALDRFAMKRFYEdKIVPIGQPSQRRYVHYFSG 253
Cdd:cd14497    81 EIVDDIDSWLSEDPNNVAVVHCKAGKGRTGTVICAYLLYYGQYSTADEALEYFAKKRFKE-GLPGVTIPSQLRYLQYFER 159

                  .
gi 568906148  254 L 254
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 ...
261-387 7.40e-50

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: 173.23  E-value: 7.40e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148   261 MNNKPLFLHHVIMHGIPNFESKGGCRPFLRIYQAMQPV-YTSGIYNIPGDSQASICITIEP-GLLLKGDILLKCYHKKFR 338
Cdd:pfam10409    1 PPPKPLTLHSIILHGIPNFKSGGGCRPYIRIYQNKKKVfSTSGKYKKLKEYQQDDCVILFPkGIPVQGDVLVEFYHKGSD 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568906148   339 SPARDVIFRVQFHTCAIHDLGVVFGKEDLDEAFKD---DRFPDYGKVEFVFS 387
Cdd:pfam10409   81 LLSEEKMFRFWFNTSFIEDNTLTLPKNELDKADKDkkdKRFPKDFKVELLFS 132
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
96-254 3.82e-48

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: 169.31  E-value: 3.82e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148   96 DLVYVTERIIAVSFPSTANEENFRSNLREVAQMLKSKHGGNYLLFNL-SEQRPDITKLHAKVLEFGWPDLHTPALEKICS 174
Cdd:cd14509     1 DLTYITPNIIAMGFPAEGVEGVYRNPIDDVQRFLETKHKGHYKVYNLcSERSYDPSKFNGRVAEYPFDDHNPPPLELIKP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  175 VCKAMDTWLNADPHNVVVLHNKGNRGRIGVVIAAYLHYSNISASADQALDRFAMKRFYEDKIVPIgqPSQRRYVHYFSGL 254
Cdd:cd14509    81 FCEDVDEWLKEDEKNVAAVHCKAGKGRTGVMICCYLLYLGKFPSAKEALDFYGAKRTKNKKGVTI--PSQRRYVYYYSRL 158
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
87-254 6.91e-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: 149.05  E-value: 6.91e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148   87 RAMEDSCELDLVYVTERIIAVSFPSTANEENFRSNLREVAQMLKSKHGGNYLLFNL-SEQRPDITKLHAKVLEFGWPDLH 165
Cdd:cd14510     6 RYQKDGFDLDLTYVTDRVIAMSFPSSGKQAFYRNPIEEVVRFLDTKHPDHYKVYNLcSERGYDPKYFHNRVERVPIDDHN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  166 TPALEKICSVCKAMDTWLNADPHNVVVLHNKGNRGRIGVVIAAYLHYSNISASADQALDRFAMKRfyEDKIVP-----IG 240
Cdd:cd14510    86 VPTLDEMLSFTAEVREWMAADPKNVVAIHCKGGKGRTGTMVCAWLIYSGQFESAKEALEYFGERR--TDKSVSskfqgVE 163
                         170
                  ....*....|....
gi 568906148  241 QPSQRRYVHYFSGL 254
Cdd:cd14510   164 TPSQSRYVGYFEKL 177
PTP_auxilin-like cd14511
protein tyrosine phosphatase-like domain of auxilin and similar proteins; This subfamily ...
94-254 2.19e-39

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: 144.42  E-value: 2.19e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148   94 ELDLVYVTERIIAVSFPSTANEENFRSN-LREVAQMLKSKHGGNYLLFNLSEQRPDITKLHAKVLEFGWPDLHTPALEKI 172
Cdd:cd14511     8 DLDISYITSRIIVMPFPAEGIESTYRKNnIEDVRAFLDSRHPQKYSVYNLSPRSYPTLRLPSRVVECSWPYRRAPSLHAL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  173 CSVCKAMDTWLNADPHNVVVLHNKGNRGRIGVVIAAYLHYSNISASADQALDRFAMKRfyedkiVPIG-QPSQRRYVHYF 251
Cdd:cd14511    88 YALCRDIYQWLNKDPKNVIVIHCTDGKAASATVVCALLVYCGLFKTPEDALQMFAVKR------CPPGlSPSELRYLYYF 161

                  ...
gi 568906148  252 SGL 254
Cdd:cd14511   162 SDI 164
PTB pfam08416
Phosphotyrosine-binding domain; The phosphotyrosine-binding domain (PTB, also ...
1692-1828 2.30e-37

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: 137.48  E-value: 2.30e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  1692 ACNVLFVNSVDMESLTGPQAISKAT--SETLAADPTPAATIVHFKVSAQGITLTDNQRKLFFrRHYPLNTVTFCDLDPQE 1769
Cdd:pfam08416    1 QYRVEHLTTFELDSLTGLQAVEDAIrkLQLLDAQGRVWTQEMLLQVSDQGITLTDNETKEEL-ESYPLDSISHCQAVLND 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568906148  1770 RKWmkteggapAKLFGFVARKQGSTTDNAcHLFA--ELDPNQPASAIVNFVSKVMLSAGQK 1828
Cdd:pfam08416   80 GRY--------NSILALVCQEPGQSKPDV-HLFQcdELGAELIAEDIESALSDVRLGKPKK 131
PTP_GAK cd14564
protein tyrosine phosphatase-like domain of cyclin-G-associated kinase; cyclin-G-associated ...
94-250 1.85e-30

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: 118.85  E-value: 1.85e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148   94 ELDLVYVTERIIAVSFPSTANEENFRSNLREVAQMLKSKHGGNYLLFNLSEQRPDITKLHAKVLEFGWPDLHTPALEKIC 173
Cdd:cd14564     8 DLDISYITSRIAVMSFPAEGVESAIKNNIEDVRLFLDSRHPGHYAVYNLSQRTYRPSRFHNRVSECGWPARRAPNLQNLY 87
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568906148  174 SVCKAMDTWLNADPHNVVVLHNKGNRGRIGVVIAAYLHYSNISASADQALDRFAMKRfyedkiVPIG-QPSQRRYVHY 250
Cdd:cd14564    88 SICKNMHLWLKQDQKNICIVHCLDGRAASAVVVCSFLCFCRLFTTAEAAVYMFSMKR------CPPGiWPSHKRYIEY 159
PTP_auxilin_N cd14563
N-terminal protein tyrosine phosphatase-like domain of auxilin; Auxilin, also called auxilin-1 ...
94-254 1.22e-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: 104.96  E-value: 1.22e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148   94 ELDLVYVTERIIAVSFPSTANEENFRSNLREVAQMLKSKHGGNYLLFNLSEQRPDITKLHAKVLEFGWPDLHTPALEKIC 173
Cdd:cd14563     8 ELDISYITSRIIVMSYPAEGVELGFRNHIEDVRSFLDSRHLDHYTVFNLSQKSYRSAKFHNRVSECSWPVRQAPSLHNLF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  174 SVCKAMDTWLNADPHNVVVLHNKGNRGRIGVVIAAYLHYSNISASADQALDRFAMKRfyeDKIVPigQPSQRRYVHYFSG 253
Cdd:cd14563    88 AVCKNMHNWLQQNPKNVCVIHCMDGRAASAVLVSAMFCFCHLFSNPVPAMQLLNAKR---PGIGL--WPSHRRYIGYICD 162

                  .
gi 568906148  254 L 254
Cdd:cd14563   163 L 163
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
1689-1829 3.53e-22

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: 93.92  E-value: 3.53e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148   1689 QGAACNVLFVNSVDMESLTGPQAISKATSETLAADP--TPAATIVHFKVSAQGITLTDNQRKlFFRRHYPLNTVTFCDLD 1766
Cdd:smart00462    2 SGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAQGseKKEPQKVILSISSRGVKLIDEDTK-AVLHEHPLRRISFCAVG 80
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568906148   1767 PQErkwmkteggapAKLFGFVARKQGStTDNACHLFAELDP--NQPASAIVNFVSKVMLSAGQKR 1829
Cdd:smart00462   81 PDD-----------LDVFGYIARDPGS-SRFACHVFRCEKAaeDIALAIGQAFQLAYELKLKARS 133
SH2 cd00173
Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they ...
1557-1651 1.56e-15

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: 73.26  E-value: 1.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1557 WYKPEISREQAIALLKDQEPGAFIIRDSHSFRGAYGLAMKvssppptiTQQGKkgdmthelVRHFLIETGPRGVKLKGCP 1636
Cdd:cd00173     2 WFHGSISREEAERLLRGKPDGTFLVRESSSEPGDYVLSVR--------SGDGK--------VKHYLIERNEGGYYLLGGS 65
                          90
                  ....*....|....*
gi 568906148 1637 NEPnFGSLSALVYQH 1651
Cdd:cd00173    66 GRT-FPSLPELVEHY 79
SH2 smart00252
Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides ...
1557-1655 2.44e-12

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: 64.17  E-value: 2.44e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148   1557 WYKPEISREQAIALLKDQEPGAFIIRDSHSFRGAYGLAMKVssppptitqqgkkgdmtHELVRHFLIE-TGPRGVKLKGc 1635
Cdd:smart00252    3 WYHGFISREEAEKLLKNEGDGDFLVRDSESSPGDYVLSVRV-----------------KGKVKHYRIRrNEDGKFYLEG- 64
                            90       100
                    ....*....|....*....|..
gi 568906148   1636 pnEPNFGSLSALV--YQHSVIP 1655
Cdd:smart00252   65 --GRKFPSLVELVehYQKNSLG 84
PHA03247 PHA03247
large tegument protein UL36; Provisional
980-1556 1.68e-11

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 69.97  E-value: 1.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  980 RQPAEPPGPLRRRAASD-GQYENQSPEAtsPRSPGVRSPVqcvspelALTIAlnPGGRPKEPHLHSYKEAFEEMEGTSPS 1058
Cdd:PHA03247 2481 RRPAEARFPFAAGAAPDpGGGGPPDPDA--PPAPSRLAPA-------ILPDE--PVGEPVHPRMLTWIRGLEELASDDAG 2549
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1059 SPPHSVARSPPGLA---KTPLSALGLKPHNPAdillhPTGVARRLIQPEEdegeevTKPPEEPRSYVESVARTAVAGPRA 1135
Cdd:PHA03247 2550 DPPPPLPPAAPPAApdrSVPPPRPAPRPSEPA-----VTSRARRPDAPPQ------SARPRAPVDDRGDPRGPAPPSPLP 2618
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1136 QDVEPKSFSAPAAHAYGHETPLRNGTPGGSFVSPSPLSTSSPI-LSADSTSVGSFPSVVSSDQGPRTPFQPMLDSSIRSG 1214
Cdd:PHA03247 2619 PDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVsRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSL 2698
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1215 SL-----GQPSPAALSYQSSSPVPVGgssynsPDYSLQPFSSSPESQGQPQYSAASVhmVPGSPQARHRTVGTNTPPSPG 1289
Cdd:PHA03247 2699 ADpppppPTPEPAPHALVSATPLPPG------PAAARQASPALPAAPAPPAVPAGPA--TPGGPARPARPPTTAGPPAPA 2770
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1290 FGRRAVNP-----TMAAPGSPSLSHRQVMGPSGPGFHGNVVSGhPASAATTPGSPSlgrhpvgshqvPGLHSSVVTTPGS 1364
Cdd:PHA03247 2771 PPAAPAAGpprrlTRPAVASLSESRESLPSPWDPADPPAAVLA-PAAALPPAASPA-----------GPLPPPTSAQPTA 2838
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1365 PSLGRHPgahqgnLASSLHSNAVISPGSPSLGRHLGGSGSVVPGSPS------LDRHAAYGGYST--------------- 1423
Cdd:PHA03247 2839 PPPPPGP------PPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPArppvrrLARPAVSRSTESfalppdqperppqpq 2912
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1424 -PEDRRPTLSRQSSASGYQAPSTPSFPVSPAYYPGLSSPATSPSPDSAAFRQGSPTPALPEKRRMSVGDRAGSLPNYATI 1502
Cdd:PHA03247 2913 aPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASS 2992
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1503 NGKVSSSPVAnGMASGSSTVSFsHTLPDFSKYSM------PDNSPETRAKVKFVQDTSKY 1556
Cdd:PHA03247 2993 TPPLTGHSLS-RVSSWASSLAL-HEETDPPPVSLkqtlwpPDDTEDSDADSLFDSDSERS 3050
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
1693-1822 2.32e-10

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: 59.83  E-value: 2.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1693 CNVLFVNSVDMESLTGPQAISKATSETLAAD--PTPAATIVHFKVSAQGITLTDNQRKLFFRRHyPLNTVTFCDLDPQER 1770
Cdd:cd00934     3 FQVKYLGSVEVGSSRGVDVVEEALKALAAALksSKRKPGPVLLEVSSKGVKLLDLDTKELLLRH-PLHRISYCGRDPDNP 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568906148 1771 kwmkteggapaKLFGFVARKQGStTDNACHLFAELDPnQPASAIVNFVSKVM 1822
Cdd:cd00934    82 -----------NVFAFIAGEEGG-SGFRCHVFQCEDE-EEAEEILQAIGQAF 120
PHA03247 PHA03247
large tegument protein UL36; Provisional
853-1399 9.02e-10

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 64.19  E-value: 9.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  853 GTPELVS--SGRPYSPYDYQLHPAGSNQSFHPKSPASSTFLPSPHSSAgpqeppaslpgliAQPQLPPKETTSDPSRTPE 930
Cdd:PHA03247 2539 GLEELASddAGDPPPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRA-------------RRPDAPPQSARPRAPVDDR 2605
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  931 EEPlnleglvaHRVAVYNARLQSLRQSRGFQPSPHWRRSASLSGVQARERQPAEP---PGP----LRRRAASDGQYENQS 1003
Cdd:PHA03247 2606 GDP--------RGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPrddPAPgrvsRPRRARRLGRAAQAS 2677
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1004 PEATSPRSPGVRSPVQCVSpELAltialnpggRPKEPhlhsykeafeemeGTSPSSPPHSVARSPPgLAKTPLSALGLKP 1083
Cdd:PHA03247 2678 SPPQRPRRRAARPTVGSLT-SLA---------DPPPP-------------PPTPEPAPHALVSATP-LPPGPAAARQASP 2733
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1084 HNPADILLHPTGVArrliqPEEDEGEevtKPPEEPRSYVESVARTAVAGPRAQdvEPKSFSAPAAHAYGHETPLRNGTPG 1163
Cdd:PHA03247 2734 ALPAAPAPPAVPAG-----PATPGGP---ARPARPPTTAGPPAPAPPAAPAAG--PPRRLTRPAVASLSESRESLPSPWD 2803
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1164 GSFVSPSPLSTSSPILSADSTSVGSFPSVVSSDQGPRTPFQPMLDSSIRSGSLGQPSPAALSYQSSSPVPVGGSSYNSPD 1243
Cdd:PHA03247 2804 PADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPV 2883
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1244 YSLQ--PFSSSPESQGQPQYSAASvhmvPGSPQARHRTVGTNTPPSPGFGRRAVnPTMAAPGSPSLSHRQVMGPSGPgfh 1321
Cdd:PHA03247 2884 RRLArpAVSRSTESFALPPDQPER----PPQPQAPPPPQPQPQPPPPPQPQPPP-PPPPRPQPPLAPTTDPAGAGEP--- 2955
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568906148 1322 gnvvsgHPASAATTPGSPSLGRHPVGSHQVPGLHSSVVT-TPGSPSLGRHPGAHQGNLASSLHSNAVISPGSPSLGRHL 1399
Cdd:PHA03247 2956 ------SGAVPQPWLGALVPGRVAVPRFRVPQPAPSREApASSTPPLTGHSLSRVSSWASSLALHEETDPPPVSLKQTL 3028
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
159-274 1.21e-09

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 57.37  E-value: 1.21e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148    159 FGWPDLHTPAL-EKICSVCKAMDTWLNA-DPHNVVVLHNKGNRGRIGVVIAAYLHYSNISASAdqaldrfamkrfyedki 236
Cdd:smart00404    8 TGWPDHGVPESpDSILELLRAVKKNLNQsESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEA----------------- 70
                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 568906148    237 vpiGQPSQRRYVHYFSGLLSGSIKMNNKPLFLHHVIMH 274
Cdd:smart00404   71 ---GEVDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
159-274 1.21e-09

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: 57.37  E-value: 1.21e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148    159 FGWPDLHTPAL-EKICSVCKAMDTWLNA-DPHNVVVLHNKGNRGRIGVVIAAYLHYSNISASAdqaldrfamkrfyedki 236
Cdd:smart00012    8 TGWPDHGVPESpDSILELLRAVKKNLNQsESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEA----------------- 70
                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 568906148    237 vpiGQPSQRRYVHYFSGLLSGSIKMNNKPLFLHHVIMH 274
Cdd:smart00012   71 ---GEVDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
SH2 pfam00017
SH2 domain;
1557-1651 2.07e-08

SH2 domain;


Pssm-ID: 425423 [Multi-domain]  Cd Length: 77  Bit Score: 52.60  E-value: 2.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  1557 WYKPEISREQAIALLK-DQEPGAFIIRDSHSFRGAYGLAMKVssppptitqQGKkgdmthelVRHFLI-ETGPRGVKLKG 1634
Cdd:pfam00017    1 WYHGKISRQEAERLLLnGKPDGTFLVRESESTPGGYTLSVRD---------DGK--------VKHYKIqSTDNGGYYISG 63
                           90
                   ....*....|....*..
gi 568906148  1635 cpnEPNFGSLSALVYQH 1651
Cdd:pfam00017   64 ---GVKFSSLAELVEHY 77
C1_TNS1_v cd20888
protein kinase C conserved region 1 (C1 domain) found in tensin-1 (TNS1) variant and similar ...
2-23 7.79e-08

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: 50.64  E-value: 7.79e-08
                          10        20
                  ....*....|....*....|..
gi 568906148    2 VCSFSCHRKCQAKVAAPCVPPS 23
Cdd:cd20888    35 VCKLSCHKKCEAKVATPCVPAV 56
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
156-230 9.07e-08

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: 54.66  E-value: 9.07e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568906148  156 VLEFGWPDLHTPALEKICSVCKAMDTWLNaDPHNVVVlHNKGNRGRIGVVIAAYLHYSNiSASADQALDRFAMKR 230
Cdd:cd14506    79 FYNFGWKDYGVPSLTTILDIVKVMAFALQ-EGGKVAV-HCHAGLGRTGVLIACYLVYAL-RMSADQAIRLVRSKR 150
PHA03247 PHA03247
large tegument protein UL36; Provisional
644-1140 9.56e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 57.64  E-value: 9.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  644 PYEAANRVIPVHSSHSAPIRPSYSAQEGlagyqregpHPAWSQQVTSAHCGCDPSGLFRSQSFPDVEPQLPQAPTRGGSS 723
Cdd:PHA03247 2560 PPAAPDRSVPPPRPAPRPSEPAVTSRAR---------RPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPS 2630
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  724 REAVQRGLNSWQQQQPHPPPRQQERSPLQSLARSKPSPQLSAETPVAALPEFPRAASQQEIEQSIETLnmlmldlepASA 803
Cdd:PHA03247 2631 PSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSL---------ADP 2701
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  804 AAPLHKSQSVPGAWPGASPLSSQPllGSSRQSHPLTQSRSGYIPSGHSLGTPelVSSGRPYSPYDyqlhPAGSNQSFHPK 883
Cdd:PHA03247 2702 PPPPPTPEPAPHALVSATPLPPGP--AAARQASPALPAAPAPPAVPAGPATP--GGPARPARPPT----TAGPPAPAPPA 2773
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  884 SPASStflPSPHSSAGPQEPPASLPGLIAQPQLPPKETTSDPSRTPEEEPlnleglvAHRVAVYNARLQSLRQSRGFQPS 963
Cdd:PHA03247 2774 APAAG---PPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPP-------AASPAGPLPPPTSAQPTAPPPPP 2843
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  964 PHWRRSASLSGVQArerqpaePPGPLRRRAASdgqyENQSPEATSPRSPGVRSPVQCVSPELALTIALNPGGRPKEPHLH 1043
Cdd:PHA03247 2844 GPPPPSLPLGGSVA-------PGGDVRRRPPS----RSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQ 2912
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1044 SYKEAFEEME---GTSPSSPPHSVARSPPGLAKTPLSALGLKPH----NPADILLHPTGVA--RRLIQPEEDEGEEVTKP 1114
Cdd:PHA03247 2913 APPPPQPQPQpppPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSgavpQPWLGALVPGRVAvpRFRVPQPAPSREAPASS 2992
                         490       500
                  ....*....|....*....|....*.
gi 568906148 1115 PEEPRSYVESvARTAVAGPRAQDVEP 1140
Cdd:PHA03247 2993 TPPLTGHSLS-RVSSWASSLALHEET 3017
C1_TNS2-like cd20826
protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; ...
2-22 3.06e-06

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: 45.84  E-value: 3.06e-06
                          10        20
                  ....*....|....*....|.
gi 568906148    2 VCSFSCHRKCQAKVAAPCVPP 22
Cdd:cd20826    32 VCKYACHRKCEPKVTAACSPS 52
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1161-1486 4.87e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 51.71  E-value: 4.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1161 TPGGSFVSPSPLSTSSPILSADSTSVGSFPSVVSSDQGPRTPFQPMLDSSIRSGSLGQPSPAALSYQSSSPVPVGGSSYN 1240
Cdd:PHA03307   72 PPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAAS 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1241 SPDyslQPFSSSPESQGQPQYSAASVhmVPGSPQARHRTVGTNTPPSPGFGRRAVNPTMAAPGSPSLSHRQVMGPSGPGF 1320
Cdd:PHA03307  152 PPA---AGASPAAVASDAASSRQAAL--PLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGR 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1321 HGNVVSGHPASAATTPGSPSLGRHPVGshQVPGLHSSVVTTPGSPSLGrHPGAHQGNLASSLHSNAVISPGSPSLGRHLG 1400
Cdd:PHA03307  227 SAADDAGASSSDSSSSESSGCGWGPEN--ECPLPRPAPITLPTRIWEA-SGWNGPSSRPGPASSSSSPRERSPSPSPSSP 303
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1401 GSGSVVPGSPSLDRHAAYGGYSTPEDRRPTLSRQSSASGYQAPSTPSFPVSPAYYPGLSSPATSPSPDSAAFRQGSPTPA 1480
Cdd:PHA03307  304 GSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAG 383

                  ....*.
gi 568906148 1481 LPEKRR 1486
Cdd:PHA03307  384 RPTRRR 389
C1_TNS3_v cd20889
protein kinase C conserved region 1 (C1 domain) found in tensin-3 (TNS3) variant and similar ...
2-26 7.69e-06

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: 44.88  E-value: 7.69e-06
                          10        20
                  ....*....|....*....|....*
gi 568906148    2 VCSFSCHRKCQAKVAAPCVPPSSHE 26
Cdd:cd20889    32 VCKYACHKKCEAKVVTPCFPPVNYE 56
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
686-1076 1.09e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 50.55  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  686 QQVTSAHCGCDPSGLFRSQSFPDVEPqlPQAPTRGGSSREAVQR--GLNSWQQQQPHPPPRQQERSPLQSLARSK----- 758
Cdd:PHA03307   42 QLVSDSAELAAVTVVAGAAACDRFEP--PTGPPPGPGTEAPANEsrSTPTWSLSTLAPASPAREGSPTPPGPSSPdpppp 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  759 -PSPQLSAETPVAALPEFPRAASQQEIEQSIEtlnmlMLDLEPASAAAPLHKSQSVPGAWPGASPLSSQPLLGSSRQSHP 837
Cdd:PHA03307  120 tPPPASPPPSPAPDLSEMLRPVGSPGPPPAAS-----PPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPP 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  838 LTQSRSGYIPSGHSLGTPELVSSGRPYSpydyqlHPAGSNQSFHPKSPASSTFLPSPHSSAGPQ-EPPASLPGLIAQPQ- 915
Cdd:PHA03307  195 PSTPPAAASPRPPRRSSPISASASSPAP------APGRSAADDAGASSSDSSSSESSGCGWGPEnECPLPRPAPITLPTr 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  916 ----LPPKETTSDPSRTPEEEPLNLEGLVAHRVAVYNARLQSLRQSRGFQPSPHWRRSASLSGVQARERQPAEPPGPLRR 991
Cdd:PHA03307  269 iweaSGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPS 348
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  992 RAASDGqyenQSPEATSPRSPGVRSPVQCVSPELALTIA--LNPGGRPKEPHLHSYKEAFEEMEGT-SPSSPPHSVARSP 1068
Cdd:PHA03307  349 RSPSPS----RPPPPADPSSPRKRPRPSRAPSSPAASAGrpTRRRARAAVAGRARRRDATGRFPAGrPRPSPLDAGAASG 424

                  ....*...
gi 568906148 1069 PGLAKTPL 1076
Cdd:PHA03307  425 AFYARYPL 432
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
155-251 1.12e-05

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 46.89  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  155 KVLEFGWPDLHTPALEKICSVCKAMDTWLNADpHNVVVlHNKGNRGRIGVVIAAYLHYSNIsaSADQALDRFAMKRfyeD 234
Cdd:COG2453    49 EYLHLPIPDFGAPDDEQLQEAVDFIDEALREG-KKVLV-HCRGGIGRTGTVAAAYLVLLGL--SAEEALARVRAAR---P 121
                          90
                  ....*....|....*..
gi 568906148  235 KIVPigQPSQRRYVHYF 251
Cdd:COG2453   122 GAVE--TPAQRAFLERF 136
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
1221-1544 3.11e-05

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 49.14  E-value: 3.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  1221 PAALSYQSSSPVPVGGSSYNSP-DYSLQPFSSSPESQGQPQYSAASVHMVPgSPQARHRTVGTNTPP----SPGFGRRAV 1295
Cdd:pfam05109  466 PTVSTADVTSPTPAGTTSGASPvTPSPSPRDNGTESKAPDMTSPTSAVTTP-TPNATSPTPAVTTPTpnatSPTLGKTSP 544
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  1296 NPTMAAPGSPSLSHR-QVMGPSGPGFHGNVVSGHPASAATTPG----SPSLGRHP----VGSHQVPGLHSSVVTTPGSPS 1366
Cdd:pfam05109  545 TSAVTTPTPNATSPTpAVTTPTPNATIPTLGKTSPTSAVTTPTpnatSPTVGETSpqanTTNHTLGGTSSTPVVTSPPKN 624
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  1367 LGRHPGAHQGNLASSLHSNAVISPGSPSLGRHLGGSGSVVPGSPSLDRHAAYGGYSTpedrrpTLSRQSSASGYQAPSTp 1446
Cdd:pfam05109  625 ATSAVTTGQHNITSSSTSSMSLRPSSISETLSPSTSDNSTSHMPLLTSAHPTGGENI------TQVTPASTSTHHVSTS- 697
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  1447 sfpvSPAYYPGLSSPATSPSPDSAAFRQG--SPTPALPEKRRMSVGDRAG---SLPNYATINGKVSSSPVANGMASGSST 1521
Cdd:pfam05109  698 ----SPAPRPGTTSQASGPGNSSTSTKPGevNVTKGTPPKNATSPQAPSGqktAVPTVTSTGGKANSTTGGKHTTGHGAR 773
                          330       340
                   ....*....|....*....|...
gi 568906148  1522 VSFSHTlpdfSKYSMPDNSPETR 1544
Cdd:pfam05109  774 TSTEPT----TDYGGDSTTPRTR 792
SH2_Srm cd10360
Src homology 2 (SH2) domain found in Src-related kinase lacking C-terminal regulatory tyrosine ...
1557-1596 1.76e-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: 41.87  E-value: 1.76e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568906148 1557 WYKPEISREQAIALL--KDQEPGAFIIRDSHSFRGAYGLAMK 1596
Cdd:cd10360     2 WYFSGISRTQAQQLLlsPPNEPGAFLIRPSESSLGGYSLSVR 43
SH2_Tec_family cd09934
Src homology 2 (SH2) domain found in Tec-like proteins; The Tec protein tyrosine kinase is the ...
1555-1665 2.87e-04

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: 42.00  E-value: 2.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1555 KY-WYKPEISREQAIALLKDQ-EPGAFIIRDShSFRGAYGLA--MKVSSPPptitqqgkkgdmtheLVRHFLIETGPRG- 1629
Cdd:cd09934     5 KYeWYVGDMSRQRAESLLKQEdKEGCFVVRNS-STKGLYTVSlfTKVPGSP---------------HVKHYHIKQNARSe 68
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 568906148 1630 --VKLKGCpnepnFGSLSALVYQHSVIPLALPCKLVIP 1665
Cdd:cd09934    69 fyLAEKHC-----FETIPELINYHQHNSGGLATRLKYP 101
SH2_Grb2_like cd09941
Src homology 2 domain found in Growth factor receptor-bound protein 2 (Grb2) and similar ...
1557-1654 3.25e-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: 41.49  E-value: 3.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1557 WYKPEISREQAIALLKDQEP-GAFIIRDSHSFRGAYGLAMKVssppptitqqgkkgdmtHELVRHFLIETGPRG------ 1629
Cdd:cd09941     5 WFHGKISRAEAEEILMNQRPdGAFLIRESESSPGDFSLSVKF-----------------GNDVQHFKVLRDGAGkyflwv 67
                          90       100
                  ....*....|....*....|....*..
gi 568906148 1630 VKlkgcpnepnFGSLSALV--YQHSVI 1654
Cdd:cd09941    68 VK---------FNSLNELVdyHRTTSV 85
SH2_ABL cd09935
Src homology 2 (SH2) domain found in Abelson murine lymphosarcoma virus (ABL) proteins; ...
1557-1665 4.71e-04

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


Pssm-ID: 198189  Cd Length: 94  Bit Score: 40.83  E-value: 4.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1557 WYKPEISREQAIALLKDQEPGAFIIRDSHSFRGAYGLAMKVssppptitqqgkkgdmtHELVRHFLIETGPRGvKLKGCP 1636
Cdd:cd09935     5 WYHGPISRNAAEYLLSSGINGSFLVRESESSPGQYSISLRY-----------------DGRVYHYRISEDSDG-KVYVTQ 66
                          90       100
                  ....*....|....*....|....*....
gi 568906148 1637 NEPnFGSLSALVYQHSVIPLALPCKLVIP 1665
Cdd:cd09935    67 EHR-FNTLAELVHHHSKNADGLITTLRYP 94
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
134-250 5.26e-04

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: 41.57  E-value: 5.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  134 GGNYLLFNLSEQRPDitKLHAKVLEFGWPDLHTPALEKICSVCKAMDTWLNADPhnVVVLHNKGNRGRIGVVIAAYL-HY 212
Cdd:cd14494     6 PLRLIAGALPLSPLE--ADSRFLKQLGVTTIVDLTLAMVDRFLEVLDQAEKPGE--PVLVHCKAGVGRTGTLVACYLvLL 81
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 568906148  213 SNIsaSADQALDRfaMKRFYEDKIVPIgqPSQRRYVHY 250
Cdd:cd14494    82 GGM--SAEEAVRI--VRLIRPGGIPQT--IEQLDFLIK 113
SH2_Nterm_shark_like cd10347
N-terminal Src homology 2 (SH2) domain found in SH2 domains, ANK, and kinase domain (shark) ...
1557-1595 6.98e-04

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


Pssm-ID: 198210  Cd Length: 81  Bit Score: 40.05  E-value: 6.98e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568906148 1557 WYKPEISREQAIALLKDQEP--GAFIIRDSHSFRGAYGLAM 1595
Cdd:cd10347     3 WYHGKISREVAEALLLREGGrdGLFLVRESTSAPGDYVLSL 43
SH2_BLNK_SLP-76 cd09929
Src homology 2 (SH2) domain found in B-cell linker (BLNK) protein and SH2 domain-containing ...
1554-1673 7.04e-04

Src homology 2 (SH2) domain found in B-cell linker (BLNK) protein and SH2 domain-containing leukocyte protein of 76 kDa (SLP-76); BLNK (also known as SLP-65 or BASH) is an important adaptor protein expressed in B-lineage cells. BLNK consists of a N-terminal sterile alpha motif (SAM) domain and a C-terminal SH2 domain. BLNK is a cytoplasmic protein, but a part of it is bound to the plasma membrane through an N-terminal leucine zipper motif and transiently bound to a cytoplasmic domain of Iga through its C-terminal SH2 domain upon B cell antigen receptor (BCR)-stimulation. A non-ITAM phosphotyrosine in Iga is necessary for the binding with the BLNK SH2 domain and/or for normal BLNK function in signaling and B cell activation. Upon phosphorylation BLNK binds Btk and PLCgamma2 through their SH2 domains and mediates PLCgamma2 activation by Btk. BLNK also binds other signaling molecules such as Vav, Grb2, Syk, and HPK1. BLNK has been shown to be necessary for BCR-mediated Ca2+ mobilization, for the activation of mitogen-activated protein kinases such as ERK, JNK, and p38 in a chicken B cell line DT40, and for activation of transcription factors such as NF-AT and NF-kappaB in human or mouse B cells. BLNK is involved in B cell development, B cell survival, activation, proliferation, and T-independent immune responses. BLNK is structurally homologous to SLP-76. SLP-76 and (linker for activation of T cells) LAT are adaptor/linker proteins in T cell antigen receptor activation and T cell development. BLNK interacts with many downstream signaling proteins that interact directly with both SLP-76 and LAT. New data suggest functional complementation of SLP-76 and LAT in T cell antigen receptor function with BLNK in BCR 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: 198183  Cd Length: 121  Bit Score: 41.15  E-value: 7.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1554 SKYWYKPEISREQA-IALLKDQEPGAFIIRDS--HSFRGAYGLAM----KVSSPPptITQQGKKgdmthelvRHFLIETG 1626
Cdd:cd09929    10 PKEWYAGNIDRKEAeEALRRSNKDGTFLVRDSsgKDSSQPYTLMVlyndKVYNIQ--IRFLENT--------RQYALGTG 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 568906148 1627 PRGvklkgcpnEPNFGSLSALVYQHSVIPLALpcklvIPSRDPTDES 1673
Cdd:cd09929    80 LRG--------EETFSSVAEIIEHHQKTPLLL-----IDGKDNTKDS 113
PLN02217 PLN02217
probable pectinesterase/pectinesterase inhibitor
1315-1438 7.95e-04

probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 215130 [Multi-domain]  Cd Length: 670  Bit Score: 44.31  E-value: 7.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1315 PSGPGfhgnVVSGHPASAATTPGSPSLGRHPVGSHQVPglhSSVVTTPGSPslgrhPGAHQGNLASSlhSNAVISPGSPS 1394
Cdd:PLN02217  556 PYIPG----LFAGNPGSTNSTPTGSAASSNTTFSSDSP---STVVAPSTSP-----PAGHLGSPPAT--PSKIVSPSTSP 621
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 568906148 1395 LGRHLgGSGSVVPGSPSLDRHAAYGGYSTPEDRRPTLSRQSSAS 1438
Cdd:PLN02217  622 PASHL-GSPSTTPSSPESSIKVASTETASPESSIKVASTESSVS 664
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
1256-1484 1.20e-03

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 43.59  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1256 QGQPQYSAASVHMVPGSPQARHRTVGTNTPPSPGFGrraVNPTMAAPGSPSLSHRQVMGPSGPGFHGNVVSGHPASAATT 1335
Cdd:COG3469    12 AGGASATAVTLLGAAATAASVTLTAATATTVVSTTG---SVVVAASGSAGSGTGTTAASSTAATSSTTSTTATATAAAAA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1336 PGSPSLGRHPVGSHQVPGLHSSVVTTPGSPslgrhpgahQGNLASSLHSNAVISPGSPSLGRHLGGSGSVVPGSPSLDrh 1415
Cdd:COG3469    89 ATSTSATLVATSTASGANTGTSTVTTTSTG---------AGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTE-- 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568906148 1416 AAYGGYSTPedrrptlsrqsSASGYQAPSTPSFPVSPAYYPGLSSPATSPSPDSAAFRQGSPTPALPEK 1484
Cdd:COG3469   158 TATGGTTTT-----------STTTTTTSASTTPSATTTATATTASGATTPSATTTATTTGPPTPGLPKH 215
COG5099 COG5099
RNA-binding protein of the Puf family, translational repressor [Translation, ribosomal ...
1178-1574 1.24e-03

RNA-binding protein of the Puf family, translational repressor [Translation, ribosomal structure and biogenesis];


Pssm-ID: 227430 [Multi-domain]  Cd Length: 777  Bit Score: 43.58  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1178 ILSADSTSVGS--FPSVVSSDQGPRTPfqpmlDSSIRSGSLGQPSPAALSYQSSSP--VPVGGSSYNSPDYSLQPFSSSP 1253
Cdd:COG5099    46 IPSKASSSATFtlNLPINNSVNHKITS-----SSSSRRKPSGSWSVAISSSTSGSQslLMELPSSSFNPSTSSRNKSNSA 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1254 ESQGQPQYSAASVHmvpGSPQARHRTVGTNTPPSPGFGrraVNPTMAAPGSPSLSHrqvMGPSgPGFHGNVVSghPASAA 1333
Cdd:COG5099   121 LSSTQQGNANSSVT---LSSSTASSMFNSNKLPLPNPN---HSNSATTNQSGSSFI---NTPA-SSSSQPLTN--LVVSS 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1334 TTPGSPSLGRHPVGSHQVPGLhSSVVTTPGSPSLgrhpgahQGNLASSLHSNAVISPGSPSLGRH---LGGSGSVVPGSP 1410
Cdd:COG5099   189 IKRFPYLTSLSPFFNYLIDPS-SDSATASADTSP-------SFNPPPNLSPNNLFSTSDLSPLPDtqsVENNIILNSSSS 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1411 SLDRHAAYGGYSTPEDRRPT-------LSRQSSASGYQAPSTPsfPVSPAYYPGLSSPATSPSPDSA-AFRQGSPTPA-L 1481
Cdd:COG5099   261 INELTSIYGSVPSIRNLRGLnsalvsfLNVSSSSLAFSALNGK--EVSPTGSPSTRSFARVLPKSSPnNLLTEILTTGvN 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1482 PEKRRMSVGDRagSLPNYATIN-GKVSSSPVANGMASGSSTVSFSHTLPDFSKYSMPDNSPETRAKVKFVQDTskywYKP 1560
Cdd:COG5099   339 PPQSLPSLLNP--VFLSTSTGFsLTNLSGYLNPNKNLKKNTLSSLSNLGYSSNVPSPSSSESTRNILGNISPN----FKT 412
                         410
                  ....*....|....
gi 568906148 1561 EISREQAIALLKDQ 1574
Cdd:COG5099   413 SSNLTNLNSLLKEK 426
SH2_nSH2_p85_like cd09942
N-terminal Src homology 2 (nSH2) domain found in p85; Phosphoinositide 3-kinases (PI3Ks) are ...
1557-1596 1.46e-03

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: 40.00  E-value: 1.46e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 568906148 1557 WYKPEISREQAIALLKDQEPGAFIIRDSHSFRGAYGLAMK 1596
Cdd:cd09942     9 WYWGDISREEVNEKMRDTPDGTFLVRDASTMKGDYTLTLR 48
C1_MgcRacGAP cd20821
protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and ...
3-23 1.46e-03

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: 38.54  E-value: 1.46e-03
                          10        20
                  ....*....|....*....|.
gi 568906148    3 CSFSCHRKCQAKVAAPCVPPS 23
Cdd:cd20821    35 CRVVCHPDCKDKLPLPCVPTS 55
PTZ00395 PTZ00395
Sec24-related protein; Provisional
1209-1372 1.57e-03

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 43.53  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1209 SSIRSGSLGQpSPAALSYQSSSPVPVGGSSYNSPDYSLQPFSSSPESQ---GQPQYSAASVHMVPGSPQARHRTVGTNTP 1285
Cdd:PTZ00395  395 SNAAQSNAAQ-SNAGFSNAGYSNPGNSNPGYNNAPNSNTPYNNPPNSNtpySNPPNSNPPYSNLPYSNTPYSNAPLSNAP 473
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1286 PSPGFGRRAVNPTmaapgspSLSHRQVMGPSGPGFHGNVVSGHP--ASAATTPGSPSLGRhPVGSHQVPGLHSSVVTTPG 1363
Cdd:PTZ00395  474 PSSAKDHHSAYHA-------AYQHRAANQPAANLPTANQPAANNfhGAAGNSVGNPFASR-PFGSAPYGGNAATTADPNG 545

                  ....*....
gi 568906148 1364 SPSLGRHPG 1372
Cdd:PTZ00395  546 IAKREDHPE 554
SH2_CRK_like cd09926
Src homology 2 domain found in cancer-related signaling adaptor protein CRK; SH2 domain in the ...
1557-1599 2.12e-03

Src homology 2 domain found in cancer-related signaling adaptor protein CRK; SH2 domain in the CRK proteins. CRKI (SH2-SH3) and CRKII (SH2-SH3-SH3) are splicing isoforms of the oncoprotein CRK. CRKs regulate transcription and cytoskeletal reorganization for cell growth and motility by linking tyrosine kinases to small G proteins. The SH2 domain of CRK associates with tyrosine-phosphorylated receptors or components of focal adhesions, such as p130Cas and paxillin. CRK transmits signals to small G proteins through effectors that bind its SH3 domain, such as C3G, the guanine-nucleotide exchange factor (GEF) for Rap1 and R-Ras, and DOCK180, the GEF for Rac6. The binding of p130Cas to the CRK-C3G complex activates Rap1, leading to regulation of cell adhesion, and activates R-Ras, leading to JNK-mediated activation of cell proliferation, whereas the binding of CRK DOCK180 induces Rac1-mediated activation of cellular migration. The activity of the different splicing isoforms varies greatly with CRKI displaying substantial transforming activity, CRKII less so, and phosphorylated CRKII with no biological activity whatsoever. CRKII has a linker region with a phosphorylated Tyr and an additional C-terminal SH3 domain. The phosphorylated Tyr creates a binding site for its SH2 domain which disrupts the association between CRK and its SH2 target proteins. 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: 198180 [Multi-domain]  Cd Length: 106  Bit Score: 39.38  E-value: 2.12e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 568906148 1557 WYKPEISREQAIALLKDQEPGAFIIRDSHSFRGAYGLAMKVSS 1599
Cdd:cd09926     9 WYFGPMSRQEAQELLQGQRHGVFLVRDSSTIPGDYVLSVSENS 51
SH2_C-SH2_PLC_gamma_like cd09932
C-terminal Src homology 2 (C-SH2) domain in Phospholipase C gamma; Phospholipase C gamma is a ...
1554-1597 2.98e-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: 39.17  E-value: 2.98e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568906148 1554 SKYWYKPEISREQAIALLKD-QEPGAFIIRDSHSFRGAYGLAMKV 1597
Cdd:cd09932     3 SKEWFHANLTREQAEEMLMRvPRDGAFLVRPSETDPNSFAISFRA 47
SH2_Grb7_family cd09944
Src homology 2 (SH2) domain found in the growth factor receptor bound, subclass 7 (Grb7) ...
1554-1596 3.38e-03

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: 38.94  E-value: 3.38e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568906148 1554 SKYWYKPEISREQAIALLKDQ--EPGAFIIRDSHSFRGAYGLAMK 1596
Cdd:cd09944     4 SQPWFHGGISRDEAARLIRQQglVDGVFLVRESQSNPGAFVLSLK 48
SH2_csk_like cd09937
Src homology 2 (SH2) domain found in Carboxyl-Terminal Src Kinase (Csk); Both the C-terminal ...
1557-1595 3.57e-03

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


Pssm-ID: 198190  Cd Length: 98  Bit Score: 38.43  E-value: 3.57e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 568906148 1557 WYKPEISREQAIALLKDQEPGAFIIRDSHSFRGAYGLAM 1595
Cdd:cd09937     5 WFHGKISREEAERLLQPPEDGLFLVRESTNYPGDYTLCV 43
SH2_cSH2_p85_like cd09930
C-terminal Src homology 2 (cSH2) domain found in p85; Phosphoinositide 3-kinases (PI3Ks) are ...
1557-1652 3.93e-03

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: 38.55  E-value: 3.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1557 WYKPEISREQAIALLKDQEPGAFIIRDShSFRGAYGLAMKVSSppptitqqgkkgdmtheLVRHFLIETGPRGVKLKgcp 1636
Cdd:cd09930     8 WLVGDINRTQAEELLRGKPDGTFLIRES-STQGCYACSVVCNG-----------------EVKHCVIYKTETGYGFA--- 66
                          90       100
                  ....*....|....*....|
gi 568906148 1637 nEPN--FGSLSALV--YQHS 1652
Cdd:cd09930    67 -EPYnlYESLKELVlhYAHN 85
SH2_SOCS_family cd09923
Src homology 2 (SH2) domain found in suppressor of cytokine signaling (SOCS) family; SH2 ...
1557-1584 3.98e-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: 3.98e-03
                          10        20
                  ....*....|....*....|....*...
gi 568906148 1557 WYKPEISREQAIALLKDQEPGAFIIRDS 1584
Cdd:cd09923     2 WYWGGITRYEAEELLAGKPEGTFLVRDS 29
C1_Myosin-IX cd20818
protein kinase C conserved region 1 (C1 domain) found in the unconventional myosin-IX family; ...
2-19 4.32e-03

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: 37.28  E-value: 4.32e-03
                          10
                  ....*....|....*...
gi 568906148    2 VCSFSCHRKCQAKVAAPC 19
Cdd:cd20818    35 VCKFTCHKKCYSKITAPC 52
C1_TNS2 cd20887
protein kinase C conserved region 1 (C1 domain) found in tensin-2 and similar proteins; ...
2-22 5.11e-03

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: 36.68  E-value: 5.11e-03
                          10        20
                  ....*....|....*....|.
gi 568906148    2 VCSFSCHRKCQAKVAAPCVPP 22
Cdd:cd20887    32 VCKVASHKKCEAKVTSACQPP 52
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
751-1078 7.04e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 41.29  E-value: 7.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148   751 LQSLARSKPSPQLSAETPVAALPEFPRAASQQEIEQSIETLNMLmlDLEPASAAAPLHKSQSVPGAWPGASPLSSQPLLG 830
Cdd:pfam03154  174 LQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQP--PNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQP 251
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148   831 ---------SSRQSHPLTQSRSGYIPSGHSLGT-PELVSSGRPYSPYDYqlhPAGSNQSFHPKSPA--------SSTFLP 892
Cdd:pfam03154  252 mtqppppsqVSPQPLPQPSLHGQMPPMPHSLQTgPSHMQHPVPPQPFPL---TPQSSQSQVPPGPSpaapgqsqQRIHTP 328
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148   893 SPHSSAGPQEPPASLP---GLIAQPQLPPKETTSDP---------------SRTPEEEPLNLEGLVA----------HRV 944
Cdd:pfam03154  329 PSQSQLQSQQPPREQPlppAPLSMPHIKPPPTTPIPqlpnpqshkhpphlsGPSPFQMNSNLPPPPAlkplsslsthHPP 408
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148   945 AVYNARLQSLRQSRGFQPSPH----WRRSASL----------SGVQARERQPAEPPGPLRRRAASDGQYENQSPEATSPR 1010
Cdd:pfam03154  409 SAHPPPLQLMPQSQQLPPPPAqppvLTQSQSLpppaashpptSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPTSTSSA 488
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568906148  1011 SPGVRSPVQcVSPELALTIALNPGGrpKEPHLHSYKEAFEEMEGTSPSSPPHSVARSPPGLAKTPLSA 1078
Cdd:pfam03154  489 MPGIQPPSS-ASVSSSGPVPAAVSC--PLPPVQIKEEALDEAEEPESPPPPPRSPSPEPTVVNTPSHA 553
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
982-1376 7.12e-03

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 41.20  E-value: 7.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  982 PAEPPGPLRRRAASDGQYENQ---SPEATSPRSPGVRSPVQCVSPELALTIALNPGGRPKEPHLH-----SYKEAFEEME 1053
Cdd:COG5180    21 AARPVLSPELWAAANNDAVSQgdrSALASSPTRPYARKIFEPLDIKLALGKPQLPSVAEPEAYLDpappkSSPDTPEEQL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1054 GTSPSSPPHSVARSPPGLAKTPLSALGLKPHNPADI--------------------------LLHPTGVARRLIQPEEDE 1107
Cdd:COG5180   101 GAPAGDLLVLPAAKTPELAAGALPAPAAAAALPKAKvtreatsasagvalaaallqrsdpilAKDPDGDSASTLPPPAEK 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1108 GEEVTKPPEEP-RSYVESVARTAVAGPRAQDVEP-KSFSAPAAHAYGHETPLRNGTPGGS-FVSPSPLSTSSPILSADST 1184
Cdd:COG5180   181 LDKVLTEPRDAlKDSPEKLDRPKVEVKDEAQEEPpDLTGGADHPRPEAASSPKVDPPSTSeARSRPATVDAQPEMRPPAD 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1185 SVGSFPSVVSSDQGPRTPFQPMLDSSI--RSGSLGQPSPAALSYQSSSPVPVGGSSYNSPDYSLQPFSSSPEsqgQPQYS 1262
Cdd:COG5180   261 AKERRRAAIGDTPAAEPPGLPVLEAGSepQSDAPEAETARPIDVKGVASAPPATRPVRPPGGARDPGTPRPG---QPTER 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1263 AAsvhmvpGSPQArhrtvGTNTPPSPGFGRRAVNPTMAAPGSPSLSHRQVMGPSGPGFHGNvvSGHPASAATTPGSPS-- 1340
Cdd:COG5180   338 PA------GVPEA-----ASDAGQPPSAYPPAEEAVPGKPLEQGAPRPGSSGGDGAPFQPP--NGAPQPGLGRRGAPGpp 404
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 568906148 1341 --LGRHPVGSHQVPGLHSSVVTTPGSPsLGRHPGAHQG 1376
Cdd:COG5180   405 mgAGDLVQAALDGGGRETASLGGAAGG-AGQGPKADFV 441
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
798-1147 7.15e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.31  E-value: 7.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  798 LEPASAAAPLHKSQSVPGAWPGASPLS-SQPLLGSSrqSHPLTQ---------SRSGYIPSGHSLGTPELVSSGRPYSPY 867
Cdd:PHA03307   11 IEAAAEGGEFFPRPPATPGDAADDLLSgSQGQLVSD--SAELAAvtvvagaaaCDRFEPPTGPPPGPGTEAPANESRSTP 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  868 DYQLHPAGSNQSFHPKSP--ASSTFLPSPHSSAGPQEPPASlPGLIAQPQLPPKETTSDPSRTPEEEPLNLEGLVAHRVA 945
Cdd:PHA03307   89 TWSLSTLAPASPAREGSPtpPGPSSPDPPPPTPPPASPPPS-PAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148  946 vyNARLQSLRQSRGfQPSPHWRRSASLSGVQARERQPAEPPGPLRRRAASDGQYENQSPEATSPRSPGVRSPVQCVSPEL 1025
Cdd:PHA03307  168 --SSRQAALPLSSP-EETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSES 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906148 1026 ALTIA----LNPGGRPKEPHLHSYKEAFEEMEGTSPSSPPHSVARSPPGLAKTPLSALGLKP-------HNPADILLHPT 1094
Cdd:PHA03307  245 SGCGWgpenECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGpapssprASSSSSSSRES 324
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568906148 1095 GVARRLIQPEEDEGEEVTKPPEEPRSYVESVARTAVAGPRAQDVEPKSFSAPA 1147
Cdd:PHA03307  325 SSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSS 377
SH2_SLAP cd10344
Src homology 2 domain found in Src-like adaptor proteins; SLAP belongs to the subfamily of ...
1557-1600 7.43e-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: 7.43e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 568906148 1557 WYKPEISREQAIALLK--DQEPGAFIIRDSHSFRGAYGLAMKVSSP 1600
Cdd:cd10344    12 WLFEGLSREKAEELLMlpGNQVGSFLIRESETRRGCYSLSVRHRGS 57
SH2_Cterm_RasGAP cd10354
C-terminal Src homology 2 (SH2) domain found in Ras GTPase-activating protein 1 (GAP); RasGAP ...
1557-1629 8.08e-03

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: 37.02  E-value: 8.08e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568906148 1557 WYKPEISREQAIALL-KDQEPGAFIIRDSHSFRGAYGLAMKVSsppptitqqgkkgdmthELVRHFLIETGPRG 1629
Cdd:cd10354     2 WFHGKISREEAYNMLvKVGGPGSFLVRESDNTPGDYSLSFRVN-----------------EGIKHFKIIPTGNN 58
 
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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