NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2217330555|ref|XP_047301593|]
View 

tensin-1 isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 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 ...
 180-338 1.14e-115

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


:

Pssm-ID: 350408 [Multi-domain]  Cd Length: 159  Bit Score: 362.76  E-value: 1.14e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  180 DLVYVTERIIAVSFPSTANEENFRSNLREVAQMLKSKHGGNYLLFNLSERRPDITKLHAKVLEFGWPDLHTPALEKICSI 259
Cdd:cd14560      1 DLVYITERIISVSFPSTAEEPSFRSNLKEVAQMLKSKHGDNYLLFNLSERRHDISKLHPKVLDFGWPDLHAPALEKICSI 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217330555  260 CKAMDTWLNADPHNVVVLHNKGNRGRIGVVIAAYMHYSNISASADQALDRFAMKRFYEDKIVPIGQPSQRRYVHYFSGL 338
Cdd:cd14560     81 CKAMDTWLNADPHNVVVIHNKGNRGRTGVVIAAYMHYSNISASADQALDRFAMKRFYEDKVVPVGQPSQKRYVHYFSGL 159
PTB_tensin cd01213
Tensin Phosphotyrosine-binding (PTB) domain; Tensin is a a focal adhesion protein, which ...
 1907-2040 5.89e-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: 276.82  E-value: 5.89e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1907 GAACNVLFVNSVDMESLTGPQAISKATSETLAADPTPAATIVHFKVSAQGITLTDNQRKLFFRRHYPLNTVTFCDLDPQE 1986
Cdd:cd01213      1 GAACNVLYLGSVDTESLTGPQAVRKAVSETLERDPLPTPTVVHFKVSEQGITLTDNQRKLFFRRHYPLNTVSFCGMDPEN 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217330555 1987 RKWMKTE--GGAPAKLFGFVARKQGSTTDNACHLFAELDPNQPASAIVNFVSKVML 2040
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. ...
 1770-1885 2.70e-69

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: 228.08  E-value: 2.70e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1770 TSKYWYKPEISREQAIALLKDQEPGAFIIRDSHSFRGAYGLAMKVSSPPPTIMQQNKKGDMTHELVRHFLIETGPRGVKL 1849
Cdd:cd09927      1 TSKYWYKPNISRDQAIALLKDKPPGTFLVRDSTTYKGAYGLAVKVATPPPGVNPFEAKGDPESELVRHFLIEPSPKGVKL 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2217330555 1850 KGCPNEPNFGSLSALVYQHSIIPLALPCKLVIPNRD 1885
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 ...
 345-471 8.31e-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: 8.31e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  345 MNNKPLFLHHVIMHGIPNFESKGGCRPFLRIYQAMQPV-YTSGIYNIPGDSQTSVCITIEP-GLLLKGDILLKCYHKKFR 422
Cdd:pfam10409    1 PPPKPLTLHSIILHGIPNFKSGGGCRPYIRIYQNKKKVfSTSGKYKKLKEYQQDDCVILFPkGIPVQGDVLVEFYHKGSD 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2217330555  423 SPARDVIFRVQFHTCAIHDLGVVFGKEDLDDAFKD---DRFPEYGKVEFVFS 471
Cdd:pfam10409   81 LLSEEKMFRFWFNTSFIEDNTLTLPKNELDKADKDkkdKRFPKDFKVELLFS 132
C1_TNS1_v cd20888
protein kinase C conserved region 1 (C1 domain) found in tensin-1 (TNS1) variant and similar ...
 57-113 8.52e-24

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: 96.09  E-value: 8.52e-24
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217330555   57 EAPKTHRFKVKTFKKVKPCGICRQVITQEGCTCKVCSFSCHRKCQAKVAAPCVPPSN 113
Cdd:cd20888      1 EAPHTHTFKVKTFKKVKSCGICKQAITREGSTCRVCKLSCHKKCEAKVATPCVPAVN 57
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 793-1208 3.72e-10

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 65.73  E-value: 3.72e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  793 NGGGYPYESASRAGPAHAGHTAPMRPSYSAQEGLAGYQREGPHPAWPQPvTTSHYAHDPSGMFRSQSFSEAEPQLPPAPV 872
Cdd:PHA03247  2547 DAGDPPPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQS-ARPRAPVDDRGDPRGPAPPSPLPPDTHAPD 2625

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  873 RGGSSREAVQRGLNSWQQQQQQQQQPRPPPRQQERAHLeSLVASRPSPQPLAETPipslPEFPRAASQQEIEQSIETLnm 952
Cdd:PHA03247  2626 PPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSR-PRRARRLGRAAQASSP----PQRPRRRAARPTVGSLTSL-- 2698

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  953 lmldlepASAAAPLHKSQSVPGAWPGASPLSSQPLSGSSRQSHPLTQSRSGYIPSGHSL-GTPEPAPRASLESVPP---- 1027
Cdd:PHA03247  2699 -------ADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATpGGPARPARPPTTAGPPapap 2771

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1028 --GRSYSPYDYQPCLAGPNQDFHSKSPASSSLPAFLPTTHSPPGPQQPPASLPGLTAQPLLSPKEATSDPSRTPEEEPLN 1105
Cdd:PHA03247  2772 paAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLP 2851

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1106 LEGLVA--HRVAAYNARLQGIGHSGSFPPPPLHRLQSSSLSGVQAREKQPAEPPAPLRRRAASDGQYENQSPEATSPRSP 1183
Cdd:PHA03247  2852 LGGSVApgGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQP 2931

                          410       420
                   ....*....|....*....|....*
gi 2217330555 1184 GVRSPVQCVSPeLALTIALNPGGRP 1208
Cdd:PHA03247  2932 PPPPPPRPQPP-LAPTTDPAGAGEP 2955
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 1302-1701 1.37e-06

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.79  E-value: 1.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1302 PFFPASPSSHLSSRLPSEEDEGKVVVRLSEEPRsyvesvaRTAVAGPRAQDSEPKSFSAPATQAYGHEIPLRNGTLGGSF 1381
Cdd:PHA03247  2577 PSEPAVTSRARRPDAPPQSARPRAPVDDRGDPR-------GPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPP 2649

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1382 VSPSPLSTSSPI-LSADSTSVGSFPSGESSDQGPRTPTQPLLESGFrsGSLGQPSPsaQRNYQSSSPLPTVGSSYSSPDY 1460
Cdd:PHA03247  2650 ERPRDDPAPGRVsRPRRARRLGRAAQASSPPQRPRRRAARPTVGSL--TSLADPPP--PPPTPEPAPHALVSATPLPPGP 2725

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1461 SLQHFSSSPESQARAQFSVAGVHTVPGSPQARHRTVGTNTPPSPGfgwrainPSMAAPSSPSLSHHQMMGPPGTGFHGST 1540
Cdd:PHA03247  2726 AAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPA-------PPAAPAAGPPRRLTRPAVASLSESRESL 2798

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1541 VSSPQSSAATTPGSPSLCRHPAGVYQVSGLHNKVATTPGSPSLGRHPgahqgnLASGLHSNAIASPGSPSLGRHLGGSGS 1620
Cdd:PHA03247  2799 PSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGP------PPPSLPLGGSVAPGGDVRRRPPSRSPA 2872

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1621 VVPGSPcldRHVAYGGYSTPEDRRPTLSRQSSASGYQAPSTPSFPVSPAYY---------------PGLSSPATSPSPDS 1685
Cdd:PHA03247  2873 AKPAAP---ARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQpqpppppqpqpppppPPRPQPPLAPTTDP 2949

                          410
                   ....*....|....*.
gi 2217330555 1686 AAfrQGSPTPALPEKR 1701
Cdd:PHA03247  2950 AG--AGEPSGAVPQPW 2963
 
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 ...
 180-338 1.14e-115

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


Pssm-ID: 350408 [Multi-domain]  Cd Length: 159  Bit Score: 362.76  E-value: 1.14e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  180 DLVYVTERIIAVSFPSTANEENFRSNLREVAQMLKSKHGGNYLLFNLSERRPDITKLHAKVLEFGWPDLHTPALEKICSI 259
Cdd:cd14560      1 DLVYITERIISVSFPSTAEEPSFRSNLKEVAQMLKSKHGDNYLLFNLSERRHDISKLHPKVLDFGWPDLHAPALEKICSI 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217330555  260 CKAMDTWLNADPHNVVVLHNKGNRGRIGVVIAAYMHYSNISASADQALDRFAMKRFYEDKIVPIGQPSQRRYVHYFSGL 338
Cdd:cd14560     81 CKAMDTWLNADPHNVVVIHNKGNRGRTGVVIAAYMHYSNISASADQALDRFAMKRFYEDKVVPVGQPSQKRYVHYFSGL 159
PTB_tensin cd01213
Tensin Phosphotyrosine-binding (PTB) domain; Tensin is a a focal adhesion protein, which ...
 1907-2040 5.89e-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: 276.82  E-value: 5.89e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1907 GAACNVLFVNSVDMESLTGPQAISKATSETLAADPTPAATIVHFKVSAQGITLTDNQRKLFFRRHYPLNTVTFCDLDPQE 1986
Cdd:cd01213      1 GAACNVLYLGSVDTESLTGPQAVRKAVSETLERDPLPTPTVVHFKVSEQGITLTDNQRKLFFRRHYPLNTVSFCGMDPEN 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217330555 1987 RKWMKTE--GGAPAKLFGFVARKQGSTTDNACHLFAELDPNQPASAIVNFVSKVML 2040
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. ...
 1770-1885 2.70e-69

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: 228.08  E-value: 2.70e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1770 TSKYWYKPEISREQAIALLKDQEPGAFIIRDSHSFRGAYGLAMKVSSPPPTIMQQNKKGDMTHELVRHFLIETGPRGVKL 1849
Cdd:cd09927      1 TSKYWYKPNISRDQAIALLKDKPPGTFLVRDSTTYKGAYGLAVKVATPPPGVNPFEAKGDPESELVRHFLIEPSPKGVKL 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2217330555 1850 KGCPNEPNFGSLSALVYQHSIIPLALPCKLVIPNRD 1885
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 ...
 345-471 8.31e-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: 8.31e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  345 MNNKPLFLHHVIMHGIPNFESKGGCRPFLRIYQAMQPV-YTSGIYNIPGDSQTSVCITIEP-GLLLKGDILLKCYHKKFR 422
Cdd:pfam10409    1 PPPKPLTLHSIILHGIPNFKSGGGCRPYIRIYQNKKKVfSTSGKYKKLKEYQQDDCVILFPkGIPVQGDVLVEFYHKGSD 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2217330555  423 SPARDVIFRVQFHTCAIHDLGVVFGKEDLDDAFKD---DRFPEYGKVEFVFS 471
Cdd:pfam10409   81 LLSEEKMFRFWFNTSFIEDNTLTLPKNELDKADKDkkdKRFPKDFKVELLFS 132
PTB pfam08416
Phosphotyrosine-binding domain; The phosphotyrosine-binding domain (PTB, also ...
 1909-2045 4.87e-38

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: 139.40  E-value: 4.87e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1909 ACNVLFVNSVDMESLTGPQAISKAT--SETLAADPTPAATIVHFKVSAQGITLTDNQRKLFFrRHYPLNTVTFCDLDPQE 1986
Cdd:pfam08416    1 QYRVEHLTTFELDSLTGLQAVEDAIrkLQLLDAQGRVWTQEMLLQVSDQGITLTDNETKEEL-ESYPLDSISHCQAVLND 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217330555 1987 RKWmkteggapAKLFGFVARKQGSTTDNAcHLFA--ELDPNQPASAIVNFVSKVMLNAGQK 2045
Cdd:pfam08416   80 GRY--------NSILALVCQEPGQSKPDV-HLFQcdELGAELIAEDIESALSDVRLGKPKK 131
C1_TNS1_v cd20888
protein kinase C conserved region 1 (C1 domain) found in tensin-1 (TNS1) variant and similar ...
 57-113 8.52e-24

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: 96.09  E-value: 8.52e-24
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217330555   57 EAPKTHRFKVKTFKKVKPCGICRQVITQEGCTCKVCSFSCHRKCQAKVAAPCVPPSN 113
Cdd:cd20888      1 EAPHTHTFKVKTFKKVKSCGICKQAITREGSTCRVCKLSCHKKCEAKVATPCVPAVN 57
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 1906-2046 8.53e-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: 93.15  E-value: 8.53e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  1906 QGAACNVLFVNSVDMESLTGPQAISKATSETLAADP--TPAATIVHFKVSAQGITLTDNQRKlFFRRHYPLNTVTFCDLD 1983
Cdd:smart00462    2 SGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAQGseKKEPQKVILSISSRGVKLIDEDTK-AVLHEHPLRRISFCAVG 80

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217330555  1984 PQErkwmkteggapAKLFGFVARKQGStTDNACHLFAELDP--NQPASAIVNFVSKVMLNAGQKR 2046
Cdd:smart00462   81 PDD-----------LDVFGYIARDPGS-SRFACHVFRCEKAaeDIALAIGQAFQLAYELKLKARS 133
SH2 smart00252
Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides ...
 1774-1868 6.03e-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: 63.02  E-value: 6.03e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  1774 WYKPEISREQAIALLKDQEPGAFIIRDSHSFRGAYGLAMKVssppptimqqnkkgdmtHELVRHFLIE-TGPRGVKLKGc 1852
Cdd:smart00252    3 WYHGFISREEAEKLLKNEGDGDFLVRDSESSPGDYVLSVRV-----------------KGKVKHYRIRrNEDGKFYLEG- 64

                            90
                    ....*....|....*...
gi 2217330555  1853 pnEPNFGSLSALV--YQH 1868
Cdd:smart00252   65 --GRKFPSLVELVehYQK 80
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 243-358 2.49e-10

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: 59.29  E-value: 2.49e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555   243 FGWPDLHTPAL-EKICSICKAMDTWLNA-DPHNVVVLHNKGNRGRIGVVIAAYMHYSNISASAdqaldrfamkrfyedki 320
Cdd:smart00012    8 TGWPDHGVPESpDSILELLRAVKKNLNQsESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEA----------------- 70

                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 2217330555   321 vpiGQPSQRRYVHYFSGLLSGSIKMNNKPLFLHHVIMH 358
Cdd:smart00012   71 ---GEVDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
PHA03247 PHA03247
large tegument protein UL36; Provisional
 793-1208 3.72e-10

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 65.73  E-value: 3.72e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  793 NGGGYPYESASRAGPAHAGHTAPMRPSYSAQEGLAGYQREGPHPAWPQPvTTSHYAHDPSGMFRSQSFSEAEPQLPPAPV 872
Cdd:PHA03247  2547 DAGDPPPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQS-ARPRAPVDDRGDPRGPAPPSPLPPDTHAPD 2625

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  873 RGGSSREAVQRGLNSWQQQQQQQQQPRPPPRQQERAHLeSLVASRPSPQPLAETPipslPEFPRAASQQEIEQSIETLnm 952
Cdd:PHA03247  2626 PPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSR-PRRARRLGRAAQASSP----PQRPRRRAARPTVGSLTSL-- 2698

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  953 lmldlepASAAAPLHKSQSVPGAWPGASPLSSQPLSGSSRQSHPLTQSRSGYIPSGHSL-GTPEPAPRASLESVPP---- 1027
Cdd:PHA03247  2699 -------ADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATpGGPARPARPPTTAGPPapap 2771

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1028 --GRSYSPYDYQPCLAGPNQDFHSKSPASSSLPAFLPTTHSPPGPQQPPASLPGLTAQPLLSPKEATSDPSRTPEEEPLN 1105
Cdd:PHA03247  2772 paAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLP 2851

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1106 LEGLVA--HRVAAYNARLQGIGHSGSFPPPPLHRLQSSSLSGVQAREKQPAEPPAPLRRRAASDGQYENQSPEATSPRSP 1183
Cdd:PHA03247  2852 LGGSVApgGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQP 2931

                          410       420
                   ....*....|....*....|....*
gi 2217330555 1184 GVRSPVQCVSPeLALTIALNPGGRP 1208
Cdd:PHA03247  2932 PPPPPPRPQPP-LAPTTDPAGAGEP 2955
SH2 pfam00017
SH2 domain;
1774-1868 3.36e-08

SH2 domain;


Pssm-ID: 425423 [Multi-domain]  Cd Length: 77  Bit Score: 52.22  E-value: 3.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1774 WYKPEISREQAIALLK-DQEPGAFIIRDSHSFRGAYGLAMKVSSppptimqqnkkgdmtheLVRHFLI-ETGPRGVKLKG 1851
Cdd:pfam00017    1 WYHGKISRQEAERLLLnGKPDGTFLVRESESTPGGYTLSVRDDG-----------------KVKHYKIqSTDNGGYYISG 63

                           90
                   ....*....|....*..
gi 2217330555 1852 cpnEPNFGSLSALVYQH 1868
Cdd:pfam00017   64 ---GVKFSSLAELVEHY 77
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1302-1701 1.37e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.79  E-value: 1.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1302 PFFPASPSSHLSSRLPSEEDEGKVVVRLSEEPRsyvesvaRTAVAGPRAQDSEPKSFSAPATQAYGHEIPLRNGTLGGSF 1381
Cdd:PHA03247  2577 PSEPAVTSRARRPDAPPQSARPRAPVDDRGDPR-------GPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPP 2649

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1382 VSPSPLSTSSPI-LSADSTSVGSFPSGESSDQGPRTPTQPLLESGFrsGSLGQPSPsaQRNYQSSSPLPTVGSSYSSPDY 1460
Cdd:PHA03247  2650 ERPRDDPAPGRVsRPRRARRLGRAAQASSPPQRPRRRAARPTVGSL--TSLADPPP--PPPTPEPAPHALVSATPLPPGP 2725

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1461 SLQHFSSSPESQARAQFSVAGVHTVPGSPQARHRTVGTNTPPSPGfgwrainPSMAAPSSPSLSHHQMMGPPGTGFHGST 1540
Cdd:PHA03247  2726 AAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPA-------PPAAPAAGPPRRLTRPAVASLSESRESL 2798

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1541 VSSPQSSAATTPGSPSLCRHPAGVYQVSGLHNKVATTPGSPSLGRHPgahqgnLASGLHSNAIASPGSPSLGRHLGGSGS 1620
Cdd:PHA03247  2799 PSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGP------PPPSLPLGGSVAPGGDVRRRPPSRSPA 2872

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1621 VVPGSPcldRHVAYGGYSTPEDRRPTLSRQSSASGYQAPSTPSFPVSPAYY---------------PGLSSPATSPSPDS 1685
Cdd:PHA03247  2873 AKPAAP---ARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQpqpppppqpqpppppPPRPQPPLAPTTDP 2949

                          410
                   ....*....|....*.
gi 2217330555 1686 AAfrQGSPTPALPEKR 1701
Cdd:PHA03247  2950 AG--AGEPSGAVPQPW 2963
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 1294-1689 9.73e-06

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: 51.07  E-value: 9.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1294 ALPHLHHLPFFPASPSS--------HLSSRLPSEEDEGKVVVRLSEEPRSYVESVARTAVAGPRAQDSEPKSFSAPATQA 1365
Cdd:pfam05109  447 GLPSSTHVPTNLTAPAStgptvstaDVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATSPTPA 526

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1366 YGHEIP-LRNGTLGGSfvspsplstsspilSADSTSVGSFPSGESSDQGPRTPTQ----PLLESGFRSGSLGQPSPSA-- 1438
Cdd:pfam05109  527 VTTPTPnATSPTLGKT--------------SPTSAVTTPTPNATSPTPAVTTPTPnatiPTLGKTSPTSAVTTPTPNAts 592

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1439 ----QRNYQSSSPLPTVGSSYSSPdyslqhFSSSPESQARAQFSVaGVHTVPGSPQA----RHRTVGTNTPPSPGFGWRA 1510
Cdd:pfam05109  593 ptvgETSPQANTTNHTLGGTSSTP------VVTSPPKNATSAVTT-GQHNITSSSTSsmslRPSSISETLSPSTSDNSTS 665

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1511 INPSMAAPSSPSLSHHQMMGPPGTGFHGSTVSSP-----QSSAATTPGSPSLCRHPAGVYQVSGLHNKVATTPGSPSlGR 1585
Cdd:pfam05109  666 HMPLLTSAHPTGGENITQVTPASTSTHHVSTSSPaprpgTTSQASGPGNSSTSTKPGEVNVTKGTPPKNATSPQAPS-GQ 744

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1586 HPGAHQGNLASGlhsnaiaSPGSPSLGRHLGGSGSVVPGSPCLDrhvaYGGYSTpedrrpTLSRQSSASGYQAPSTPSfP 1665
Cdd:pfam05109  745 KTAVPTVTSTGG-------KANSTTGGKHTTGHGARTSTEPTTD----YGGDST------TPRTRYNATTYLPPSTSS-K 806

                          410       420
                   ....*....|....*....|....*...
gi 2217330555 1666 VSPAYY----PGLSSPATSPSPDSAAFR 1689
Cdd:pfam05109  807 LRPRWTftspPVTTAQATVPVPPTSQPR 834
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
239-335 1.83e-05

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 46.50  E-value: 1.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  239 KVLEFGWPDLHTPALEKICSICKAMDTWLNADpHNVVVlHNKGNRGRIGVVIAAYMHYSNIsaSADQALDRFAMKRfyeD 318
Cdd:COG2453     49 EYLHLPIPDFGAPDDEQLQEAVDFIDEALREG-KKVLV-HCRGGIGRTGTVAAAYLVLLGL--SAEEALARVRAAR---P 121

                           90
                   ....*....|....*..
gi 2217330555  319 KIVPigQPSQRRYVHYF 335
Cdd:COG2453    122 GAVE--TPAQRAFLERF 136
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 75-108 3.06e-04

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


Pssm-ID: 197519  Cd Length: 50  Bit Score: 40.14  E-value: 3.06e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2217330555    75 CGICRQVI---TQEGCTCKVCSFSCHRKCQAKVAAPC 108
Cdd:smart00109   14 CCVCRKSIwgsFKQGLRCSECKVKCHKKCADKVPKAC 50
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 919-1104 3.83e-04

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: 45.53  E-value: 3.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  919 SPQPLAETPIPSLPEFPRAASQQEIEQSIETLNMLMLDLEPASAAAPLHKSQSVPGAWPGA-------SPLSSQPLSGSS 991
Cdd:pfam03154  143 STSPSIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSApsvppqgSPATSQPPNQTQ 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  992 RQSHPLTQSRSG------YIPSGHS----LGTPEPAPRASLESVPPGRSYSPYDY--QPCLAGPNQDFHSKSPASSSLPA 1059
Cdd:pfam03154  223 STAAPHTLIQQTptlhpqRLPSPHPplqpMTQPPPPSQVSPQPLPQPSLHGQMPPmpHSLQTGPSHMQHPVPPQPFPLTP 302

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2217330555 1060 FLPTTHSPPGPQqppASLPGLTAQ-PLLSPKEATSDPSRTPEEEPL 1104
Cdd:pfam03154  303 QSSQSQVPPGPS---PAAPGQSQQrIHTPPSQSQLQSQQPPREQPL 345
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
1478-1700 6.67e-03

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 41.28  E-value: 6.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1478 SVAGVHTVPGSPQArhrTVGTNTPPSPGFGWraiNPSMAAPSSPSLSHHQMMGPPGTGFHGSTVSSPQSSAATTPGSPSL 1557
Cdd:COG3469     21 TLLGAAATAASVTL---TAATATTVVSTTGS---VVVAASGSAGSGTGTTAASSTAATSSTTSTTATATAAAAAATSTSA 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1558 CRHPAGVYQVSGLHNKVATTPGSPslgrhpgahQGNLASGLHSNAIASPGSPSLGRHLGGSGSVVPGSPcldrhvAYGGY 1637
Cdd:COG3469     95 TLVATSTASGANTGTSTVTTTSTG---------AGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVS------GTETA 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217330555 1638 STPedrrptlSRQSSASGYQAPSTPSFPVSPAYYPGLSSPATSPSPDSAAFRQGSPTPALPEK 1700
Cdd:COG3469    160 TGG-------TTTTSTTTTTTSASTTPSATTTATATTASGATTPSATTTATTTGPPTPGLPKH 215
 
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 ...
 180-338 1.14e-115

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


Pssm-ID: 350408 [Multi-domain]  Cd Length: 159  Bit Score: 362.76  E-value: 1.14e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  180 DLVYVTERIIAVSFPSTANEENFRSNLREVAQMLKSKHGGNYLLFNLSERRPDITKLHAKVLEFGWPDLHTPALEKICSI 259
Cdd:cd14560      1 DLVYITERIISVSFPSTAEEPSFRSNLKEVAQMLKSKHGDNYLLFNLSERRHDISKLHPKVLDFGWPDLHAPALEKICSI 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217330555  260 CKAMDTWLNADPHNVVVLHNKGNRGRIGVVIAAYMHYSNISASADQALDRFAMKRFYEDKIVPIGQPSQRRYVHYFSGL 338
Cdd:cd14560     81 CKAMDTWLNADPHNVVVIHNKGNRGRTGVVIAAYMHYSNISASADQALDRFAMKRFYEDKVVPVGQPSQKRYVHYFSGL 159
PTP_tensin cd14508
protein tyrosine phosphatase-like domain of tensins; The tensin family of intracellular ...
 180-338 4.47e-96

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: 306.62  E-value: 4.47e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  180 DLVYVTERIIAVSFPSTANEENFRSNLREVAQMLKSKHGGNYLLFNLSERRPDITKLHAKVLEFGWPDLHTPALEKICSI 259
Cdd:cd14508      1 DLTYITERIIALSFPSTCSEQTYRHNLREAAHLLQSKHGDNYMVFNLSERRHDLRSLNPKVLDFGWPELHAPPLEKLCSI 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217330555  260 CKAMDTWLNADPHNVVVLHNKGNRGRIGVVIAAYMHYSNISASADQALDRFAMKRFYEDKIVPIGQPSQRRYVHYFSGL 338
Cdd:cd14508     81 CKNMDSWLNADPQNVVVLHCKGGKGRLGVVVSAYMHYSKISATADQALDRFAMKRFYDDKVGPLGQPSQKRYVGYFSGL 159
PTB_tensin cd01213
Tensin Phosphotyrosine-binding (PTB) domain; Tensin is a a focal adhesion protein, which ...
 1907-2040 5.89e-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: 276.82  E-value: 5.89e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1907 GAACNVLFVNSVDMESLTGPQAISKATSETLAADPTPAATIVHFKVSAQGITLTDNQRKLFFRRHYPLNTVTFCDLDPQE 1986
Cdd:cd01213      1 GAACNVLYLGSVDTESLTGPQAVRKAVSETLERDPLPTPTVVHFKVSEQGITLTDNQRKLFFRRHYPLNTVSFCGMDPEN 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217330555 1987 RKWMKTE--GGAPAKLFGFVARKQGSTTDNACHLFAELDPNQPASAIVNFVSKVML 2040
Cdd:cd01213     81 RKWQKYDlrGSKPSRIFGFVARKQGSSTENVCHLFAELDPEQPASAIVNFVNKVLL 136
PTP_tensin-3 cd14561
protein tyrosine phosphatase-like domain of tensin-3; Tensin-3 (TNS3) is also called ...
 180-338 1.36e-82

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: 267.97  E-value: 1.36e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  180 DLVYVTERIIAVSFPSTANEENFRSNLREVAQMLKSKHGGNYLLFNLSERRPDITKLHAKVLEFGWPDLHTPALEKICSI 259
Cdd:cd14561      1 DLTYITERIIAVSFPADCSEETYLHNLQDVTRMLKSKHGDNYLVLNLSEKRYELTKLNPKIMDVGWPDLHAPPLDKMCTI 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217330555  260 CKAMDTWLNADPHNVVVLHNKGNRGRIGVVIAAYMHYSNISASADQALDRFAMKRFYEDKIVPIGQPSQRRYVHYFSGL 338
Cdd:cd14561     81 CKAMESWLNSDPLHVVVIHCRGGKGRIGVVISSYMHFTNVSASADQALDRFAMKKFYDDKVSALMQPSQKRYVQFLSGL 159
PTP_tensin-2 cd14562
protein tyrosine phosphatase-like domain of tensin-2; Tensin-2 (TNS2) is also called ...
 180-338 2.19e-81

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: 264.50  E-value: 2.19e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  180 DLVYVTERIIAVSFPSTANEENFRSNLREVAQMLKSKHGGNYLLFNLSERRPDITKLHAKVLEFGWPDLHTPALEKICSI 259
Cdd:cd14562      1 DLTYITERIISVFFPPALEEQRYRGNLREVAQMLKSKHEDKYLLFNLSEKRHDITRLNPKVQDFGWPDLHAPPLDKICSI 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217330555  260 CKAMDTWLNADPHNVVVLHNKGNRGRIGVVIAAYMHYSNISASADQALDRFAMKRFYEDKIVPIGQPSQRRYVHYFSGL 338
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. ...
 1770-1885 2.70e-69

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: 228.08  E-value: 2.70e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1770 TSKYWYKPEISREQAIALLKDQEPGAFIIRDSHSFRGAYGLAMKVSSPPPTIMQQNKKGDMTHELVRHFLIETGPRGVKL 1849
Cdd:cd09927      1 TSKYWYKPNISRDQAIALLKDKPPGTFLVRDSTTYKGAYGLAVKVATPPPGVNPFEAKGDPESELVRHFLIEPSPKGVKL 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2217330555 1850 KGCPNEPNFGSLSALVYQHSIIPLALPCKLVIPNRD 1885
Cdd:cd09927     81 KGCPNEPVFGSLSALVYQHSITPLALPCKLRIPDRD 116
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 180-338 1.44e-65

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: 219.37  E-value: 1.44e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  180 DLVYVTERIIAVSFPSTAN-EENFRSNLREVAQMLKSKHGGNYLLFNLSERRPDI-TKLHAKVLEFGWPDLHTPALEKIC 257
Cdd:cd14497      1 DLSYITPRIIAMSFPATGYpESLYRNSIDDVANFLNTHHPDHYMIFNLSEEEYDDdSKFEGRVLHYGFPDHHPPPLGLLL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  258 SICKAMDTWLNADPHNVVVLHNKGNRGRIGVVIAAYMHYSNISASADQALDRFAMKRFYEdKIVPIGQPSQRRYVHYFSG 337
Cdd:cd14497     81 EIVDDIDSWLSEDPNNVAVVHCKAGKGRTGTVICAYLLYYGQYSTADEALEYFAKKRFKE-GLPGVTIPSQLRYLQYFER 159


                   .
gi 2217330555  338 L 338
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 ...
 345-471 8.31e-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: 8.31e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  345 MNNKPLFLHHVIMHGIPNFESKGGCRPFLRIYQAMQPV-YTSGIYNIPGDSQTSVCITIEP-GLLLKGDILLKCYHKKFR 422
Cdd:pfam10409    1 PPPKPLTLHSIILHGIPNFKSGGGCRPYIRIYQNKKKVfSTSGKYKKLKEYQQDDCVILFPkGIPVQGDVLVEFYHKGSD 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2217330555  423 SPARDVIFRVQFHTCAIHDLGVVFGKEDLDDAFKD---DRFPEYGKVEFVFS 471
Cdd:pfam10409   81 LLSEEKMFRFWFNTSFIEDNTLTLPKNELDKADKDkkdKRFPKDFKVELLFS 132
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 180-338 4.86e-49

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: 172.00  E-value: 4.86e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  180 DLVYVTERIIAVSFPSTANEENFRSNLREVAQMLKSKHGGNYLLFNL-SERRPDITKLHAKVLEFGWPDLHTPALEKICS 258
Cdd:cd14509      1 DLTYITPNIIAMGFPAEGVEGVYRNPIDDVQRFLETKHKGHYKVYNLcSERSYDPSKFNGRVAEYPFDDHNPPPLELIKP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  259 ICKAMDTWLNADPHNVVVLHNKGNRGRIGVVIAAYMHYSNISASADQALDRFAMKRFYEDKIVPIgqPSQRRYVHYFSGL 338
Cdd:cd14509     81 FCEDVDEWLKEDEKNVAAVHCKAGKGRTGVMICCYLLYLGKFPSAKEALDFYGAKRTKNKKGVTI--PSQRRYVYYYSRL 158
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 171-338 1.05e-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: 151.75  E-value: 1.05e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  171 RTMEDSCELDLVYVTERIIAVSFPSTANEENFRSNLREVAQMLKSKHGGNYLLFNL-SERRPDITKLHAKVLEFGWPDLH 249
Cdd:cd14510      6 RYQKDGFDLDLTYVTDRVIAMSFPSSGKQAFYRNPIEEVVRFLDTKHPDHYKVYNLcSERGYDPKYFHNRVERVPIDDHN 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  250 TPALEKICSICKAMDTWLNADPHNVVVLHNKGNRGRIGVVIAAYMHYSNISASADQALDRFAMKRfyEDKIVP-----IG 324
Cdd:cd14510     86 VPTLDEMLSFTAEVREWMAADPKNVVAIHCKGGKGRTGTMVCAWLIYSGQFESAKEALEYFGERR--TDKSVSskfqgVE 163

                          170
                   ....*....|....
gi 2217330555  325 QPSQRRYVHYFSGL 338
Cdd:cd14510    164 TPSQSRYVGYFEKL 177
PTP_auxilin-like cd14511
protein tyrosine phosphatase-like domain of auxilin and similar proteins; This subfamily ...
 178-338 1.72e-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: 144.80  E-value: 1.72e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  178 ELDLVYVTERIIAVSFPSTANEENFRSN-LREVAQMLKSKHGGNYLLFNLSERRPDITKLHAKVLEFGWPDLHTPALEKI 256
Cdd:cd14511      8 DLDISYITSRIIVMPFPAEGIESTYRKNnIEDVRAFLDSRHPQKYSVYNLSPRSYPTLRLPSRVVECSWPYRRAPSLHAL 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  257 CSICKAMDTWLNADPHNVVVLHNKGNRGRIGVVIAAYMHYSNISASADQALDRFAMKRfyedkiVPIG-QPSQRRYVHYF 335
Cdd:cd14511     88 YALCRDIYQWLNKDPKNVIVIHCTDGKAASATVVCALLVYCGLFKTPEDALQMFAVKR------CPPGlSPSELRYLYYF 161


                   ...
gi 2217330555  336 SGL 338
Cdd:cd14511    162 SDI 164
PTB pfam08416
Phosphotyrosine-binding domain; The phosphotyrosine-binding domain (PTB, also ...
 1909-2045 4.87e-38

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: 139.40  E-value: 4.87e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1909 ACNVLFVNSVDMESLTGPQAISKAT--SETLAADPTPAATIVHFKVSAQGITLTDNQRKLFFrRHYPLNTVTFCDLDPQE 1986
Cdd:pfam08416    1 QYRVEHLTTFELDSLTGLQAVEDAIrkLQLLDAQGRVWTQEMLLQVSDQGITLTDNETKEEL-ESYPLDSISHCQAVLND 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217330555 1987 RKWmkteggapAKLFGFVARKQGSTTDNAcHLFA--ELDPNQPASAIVNFVSKVMLNAGQK 2045
Cdd:pfam08416   80 GRY--------NSILALVCQEPGQSKPDV-HLFQcdELGAELIAEDIESALSDVRLGKPKK 131
PTP_GAK cd14564
protein tyrosine phosphatase-like domain of cyclin-G-associated kinase; cyclin-G-associated ...
 178-334 7.84e-31

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: 120.01  E-value: 7.84e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  178 ELDLVYVTERIIAVSFPSTANEENFRSNLREVAQMLKSKHGGNYLLFNLSERRPDITKLHAKVLEFGWPDLHTPALEKIC 257
Cdd:cd14564      8 DLDISYITSRIAVMSFPAEGVESAIKNNIEDVRLFLDSRHPGHYAVYNLSQRTYRPSRFHNRVSECGWPARRAPNLQNLY 87

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217330555  258 SICKAMDTWLNADPHNVVVLHNKGNRGRIGVVIAAYMHYSNISASADQALDRFAMKRfyedkiVPIG-QPSQRRYVHY 334
Cdd:cd14564     88 SICKNMHLWLKQDQKNICIVHCLDGRAASAVVVCSFLCFCRLFTTAEAAVYMFSMKR------CPPGiWPSHKRYIEY 159
PTP_auxilin_N cd14563
N-terminal protein tyrosine phosphatase-like domain of auxilin; Auxilin, also called auxilin-1 ...
 178-338 2.65e-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: 104.19  E-value: 2.65e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  178 ELDLVYVTERIIAVSFPSTANEENFRSNLREVAQMLKSKHGGNYLLFNLSERRPDITKLHAKVLEFGWPDLHTPALEKIC 257
Cdd:cd14563      8 ELDISYITSRIIVMSYPAEGVELGFRNHIEDVRSFLDSRHLDHYTVFNLSQKSYRSAKFHNRVSECSWPVRQAPSLHNLF 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  258 SICKAMDTWLNADPHNVVVLHNKGNRGRIGVVIAAYMHYSNISASADQALDRFAMKRfyeDKIVPigQPSQRRYVHYFSG 337
Cdd:cd14563     88 AVCKNMHNWLQQNPKNVCVIHCMDGRAASAVLVSAMFCFCHLFSNPVPAMQLLNAKR---PGIGL--WPSHRRYIGYICD 162


                   .
gi 2217330555  338 L 338
Cdd:cd14563    163 L 163
C1_TNS1_v cd20888
protein kinase C conserved region 1 (C1 domain) found in tensin-1 (TNS1) variant and similar ...
 57-113 8.52e-24

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: 96.09  E-value: 8.52e-24
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217330555   57 EAPKTHRFKVKTFKKVKPCGICRQVITQEGCTCKVCSFSCHRKCQAKVAAPCVPPSN 113
Cdd:cd20888      1 EAPHTHTFKVKTFKKVKSCGICKQAITREGSTCRVCKLSCHKKCEAKVATPCVPAVN 57
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 1906-2046 8.53e-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: 93.15  E-value: 8.53e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  1906 QGAACNVLFVNSVDMESLTGPQAISKATSETLAADP--TPAATIVHFKVSAQGITLTDNQRKlFFRRHYPLNTVTFCDLD 1983
Cdd:smart00462    2 SGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAQGseKKEPQKVILSISSRGVKLIDEDTK-AVLHEHPLRRISFCAVG 80

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217330555  1984 PQErkwmkteggapAKLFGFVARKQGStTDNACHLFAELDP--NQPASAIVNFVSKVMLNAGQKR 2046
Cdd:smart00462   81 PDD-----------LDVFGYIARDPGS-SRFACHVFRCEKAaeDIALAIGQAFQLAYELKLKARS 133
C1_TNS2-like cd20826
protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; ...
 74-111 2.46e-16

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: 74.73  E-value: 2.46e-16
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2217330555   74 PCGICRQVITQEGCTCKVCSFSCHRKCQAKVAAPCVPP 111
Cdd:cd20826     15 TCDVCKQIIWNEGSSCRVCKYACHRKCEPKVTAACSPS 52
C1_TNS3_v cd20889
protein kinase C conserved region 1 (C1 domain) found in tensin-3 (TNS3) variant and similar ...
 74-115 5.05e-16

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: 73.77  E-value: 5.05e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2217330555   74 PCGICRQVITQEGCTCKVCSFSCHRKCQAKVAAPCVPPSNHE 115
Cdd:cd20889     15 VCSICKQVIDSQGISCRVCKYACHKKCEAKVVTPCFPPVNYE 56
SH2 cd00173
Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they ...
 1774-1868 3.29e-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: 72.49  E-value: 3.29e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1774 WYKPEISREQAIALLKDQEPGAFIIRDSHSFRGAYGLAMKVSSPpptimqqnkkgdmtheLVRHFLIETGPRGVKLKGCP 1853
Cdd:cd00173      2 WFHGSISREEAERLLRGKPDGTFLVRESSSEPGDYVLSVRSGDG----------------KVKHYLIERNEGGYYLLGGS 65

                           90
                   ....*....|....*
gi 2217330555 1854 NEPnFGSLSALVYQH 1868
Cdd:cd00173     66 GRT-FPSLPELVEHY 79
SH2 smart00252
Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides ...
 1774-1868 6.03e-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: 63.02  E-value: 6.03e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  1774 WYKPEISREQAIALLKDQEPGAFIIRDSHSFRGAYGLAMKVssppptimqqnkkgdmtHELVRHFLIE-TGPRGVKLKGc 1852
Cdd:smart00252    3 WYHGFISREEAEKLLKNEGDGDFLVRDSESSPGDYVLSVRV-----------------KGKVKHYRIRrNEDGKFYLEG- 64

                            90
                    ....*....|....*...
gi 2217330555  1853 pnEPNFGSLSALV--YQH 1868
Cdd:smart00252   65 --GRKFPSLVELVehYQK 80
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 243-358 2.49e-10

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: 59.29  E-value: 2.49e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555   243 FGWPDLHTPAL-EKICSICKAMDTWLNA-DPHNVVVLHNKGNRGRIGVVIAAYMHYSNISASAdqaldrfamkrfyedki 320
Cdd:smart00012    8 TGWPDHGVPESpDSILELLRAVKKNLNQsESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEA----------------- 70

                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 2217330555   321 vpiGQPSQRRYVHYFSGLLSGSIKMNNKPLFLHHVIMH 358
Cdd:smart00012   71 ---GEVDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
243-358 2.49e-10

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 59.29  E-value: 2.49e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555   243 FGWPDLHTPAL-EKICSICKAMDTWLNA-DPHNVVVLHNKGNRGRIGVVIAAYMHYSNISASAdqaldrfamkrfyedki 320
Cdd:smart00404    8 TGWPDHGVPESpDSILELLRAVKKNLNQsESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEA----------------- 70

                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 2217330555   321 vpiGQPSQRRYVHYFSGLLSGSIKMNNKPLFLHHVIMH 358
Cdd:smart00404   71 ---GEVDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 1910-2039 2.61e-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: 2.61e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1910 CNVLFVNSVDMESLTGPQAISKATSETLAAD--PTPAATIVHFKVSAQGITLTDNQRKLFFRRHyPLNTVTFCDLDPQER 1987
Cdd:cd00934      3 FQVKYLGSVEVGSSRGVDVVEEALKALAAALksSKRKPGPVLLEVSSKGVKLLDLDTKELLLRH-PLHRISYCGRDPDNP 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2217330555 1988 kwmkteggapaKLFGFVARKQGStTDNACHLFAELDPnQPASAIVNFVSKVM 2039
Cdd:cd00934     82 -----------NVFAFIAGEEGG-SGFRCHVFQCEDE-EEAEEILQAIGQAF 120
PHA03247 PHA03247
large tegument protein UL36; Provisional
 793-1208 3.72e-10

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 65.73  E-value: 3.72e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  793 NGGGYPYESASRAGPAHAGHTAPMRPSYSAQEGLAGYQREGPHPAWPQPvTTSHYAHDPSGMFRSQSFSEAEPQLPPAPV 872
Cdd:PHA03247  2547 DAGDPPPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQS-ARPRAPVDDRGDPRGPAPPSPLPPDTHAPD 2625

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  873 RGGSSREAVQRGLNSWQQQQQQQQQPRPPPRQQERAHLeSLVASRPSPQPLAETPipslPEFPRAASQQEIEQSIETLnm 952
Cdd:PHA03247  2626 PPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSR-PRRARRLGRAAQASSP----PQRPRRRAARPTVGSLTSL-- 2698

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  953 lmldlepASAAAPLHKSQSVPGAWPGASPLSSQPLSGSSRQSHPLTQSRSGYIPSGHSL-GTPEPAPRASLESVPP---- 1027
Cdd:PHA03247  2699 -------ADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATpGGPARPARPPTTAGPPapap 2771

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1028 --GRSYSPYDYQPCLAGPNQDFHSKSPASSSLPAFLPTTHSPPGPQQPPASLPGLTAQPLLSPKEATSDPSRTPEEEPLN 1105
Cdd:PHA03247  2772 paAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLP 2851

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1106 LEGLVA--HRVAAYNARLQGIGHSGSFPPPPLHRLQSSSLSGVQAREKQPAEPPAPLRRRAASDGQYENQSPEATSPRSP 1183
Cdd:PHA03247  2852 LGGSVApgGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQP 2931

                          410       420
                   ....*....|....*....|....*
gi 2217330555 1184 GVRSPVQCVSPeLALTIALNPGGRP 1208
Cdd:PHA03247  2932 PPPPPPRPQPP-LAPTTDPAGAGEP 2955
C1_TNS2 cd20887
protein kinase C conserved region 1 (C1 domain) found in tensin-2 and similar proteins; ...
 74-111 5.24e-09

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: 54.02  E-value: 5.24e-09
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2217330555   74 PCGICRQVITQEGCTCKVCSFSCHRKCQAKVAAPCVPP 111
Cdd:cd20887     15 ACAVCREPVGGQGLVCRVCKVASHKKCEAKVTSACQPP 52
PHA03247 PHA03247
large tegument protein UL36; Provisional
 834-1211 1.74e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 60.34  E-value: 1.74e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  834 PHPAWPQPVTTSHYAHDPSGmfRSQSFSEAEPQLPPAPVRGGSSREavQRGlnswqqqqqqqqqprppprqqerahlESL 913
Cdd:PHA03247  2560 PPAAPDRSVPPPRPAPRPSE--PAVTSRARRPDAPPQSARPRAPVD--DRG--------------------------DPR 2609

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  914 VASRPSPQPLAETPIPSLPEFPR-AASQQEIEQSIETLNMLMLDLEPASAAAPLHKSQSVPGAWPGASPLSSQPLSGSSR 992
Cdd:PHA03247  2610 GPAPPSPLPPDTHAPDPPPPSPSpAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAAR 2689

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  993 QS-HPLTQSRSGYIPSghslGTPEPAPRASLESVP--PGRSYSPYDYQPCLAGPNQDFHSKSPASSSLPAFLPTTHSPPG 1069
Cdd:PHA03247  2690 PTvGSLTSLADPPPPP----PTPEPAPHALVSATPlpPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAG 2765

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1070 PQQP-PASLPGLTAQPLLS-PKEATSDPSRTPEEEPLNLEGLVAHRVAAYNARLQGIGHSGSFPPPPLHRLQSSSLSGVQ 1147
Cdd:PHA03247  2766 PPAPaPPAAPAAGPPRRLTrPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGP 2845

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217330555 1148 AREKQPAE----PPAPLRRRAASdgqyENQSPEATSPRSPGVRSPVQCVSPELALTIALNPGGRPKEP 1211
Cdd:PHA03247  2846 PPPSLPLGgsvaPGGDVRRRPPS----RSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPP 2909
SH2 pfam00017
SH2 domain;
1774-1868 3.36e-08

SH2 domain;


Pssm-ID: 425423 [Multi-domain]  Cd Length: 77  Bit Score: 52.22  E-value: 3.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1774 WYKPEISREQAIALLK-DQEPGAFIIRDSHSFRGAYGLAMKVSSppptimqqnkkgdmtheLVRHFLI-ETGPRGVKLKG 1851
Cdd:pfam00017    1 WYHGKISRQEAERLLLnGKPDGTFLVRESESTPGGYTLSVRDDG-----------------KVKHYKIqSTDNGGYYISG 63

                           90
                   ....*....|....*..
gi 2217330555 1852 cpnEPNFGSLSALVYQH 1868
Cdd:pfam00017   64 ---GVKFSSLAELVEHY 77
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 240-314 5.51e-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: 55.43  E-value: 5.51e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217330555  240 VLEFGWPDLHTPALEKICSICKAMDTWLNaDPHNVVVlHNKGNRGRIGVVIAAYMHYSNiSASADQALDRFAMKR 314
Cdd:cd14506     79 FYNFGWKDYGVPSLTTILDIVKVMAFALQ-EGGKVAV-HCHAGLGRTGVLIACYLVYAL-RMSADQAIRLVRSKR 150
PHA03247 PHA03247
large tegument protein UL36; Provisional
 772-1162 1.39e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 57.26  E-value: 1.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  772 PEALSPLTNGLDKSYPmepmvngggyPYESASRAGPAHAGHTAPMRPSYSAQEGLAGYQREGPHPAWPQPVTTSHYAHDP 851
Cdd:PHA03247  2689 RPTVGSLTSLADPPPP----------PPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPA 2758

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  852 SGMFRSQSFSEAEPQLPPAPVRGGSSREAVqrglnswqqqqqqqqqprppprqqerAHLESLVASRPSPQPLAETPIPSL 931
Cdd:PHA03247  2759 RPPTTAGPPAPAPPAAPAAGPPRRLTRPAV--------------------------ASLSESRESLPSPWDPADPPAAVL 2812

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  932 PEFPRAASQQeieqsietlnmlmldlEPASAAAPLHKSQSVPGAWPGASPLSSQPLSGSSRQSHPLtqSRSGyiPSGHSL 1011
Cdd:PHA03247  2813 APAAALPPAA----------------SPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDV--RRRP--PSRSPA 2872

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1012 GTPEPAPRASLESVP-PGRSYSPydyQPCLAGPNQDFHSKSPASSSLPAFLPTTHSPPGPQQPPASlPGLTAQPLLSPKE 1090
Cdd:PHA03247  2873 AKPAAPARPPVRRLArPAVSRST---ESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPP-PPRPQPPLAPTTD 2948

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217330555 1091 ATSDPSRTPEEEPLNLEGLVAHRVAAYNARLQGIGHSGSFPPPPLHRLQSSSLSGVQ------AREKQPAEPPAPLRR 1162
Cdd:PHA03247  2949 PAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSswasslALHEETDPPPVSLKQ 3026
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
 75-108 2.32e-07

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


Pssm-ID: 410341  Cd Length: 50  Bit Score: 49.05  E-value: 2.32e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2217330555   75 CGICRQVIT---QEGCTCKVCSFSCHRKCQAKVAAPC 108
Cdd:cd00029     14 CDVCGKLIWglfKQGLKCSDCGLVCHKKCLDKAPSPC 50
C1_SpBZZ1-like cd20824
protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein ...
 74-108 5.56e-07

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


Pssm-ID: 410374  Cd Length: 53  Bit Score: 48.08  E-value: 5.56e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2217330555   74 PCGICRQVI---TQEGCTCKVCSFSCHRKCQAKVAAPC 108
Cdd:cd20824     14 KCDYCGEKIwglSKKGLSCKDCGFNCHIKCELKVPPEC 51
PHA03247 PHA03247
large tegument protein UL36; Provisional
 927-1211 9.17e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.56  E-value: 9.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  927 PIPSLPEFPRAASQqeiEQSIETlnmlmldlePASAAAPLHKSQSVPGAWPGASPLSSQPLS-GSSRQSHPLTQSRSGYI 1005
Cdd:PHA03247  2551 PPPPLPPAAPPAAP---DRSVPP---------PRPAPRPSEPAVTSRARRPDAPPQSARPRApVDDRGDPRGPAPPSPLP 2618

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1006 PSGHSLGTPEPAPRASLESVPPGRSYSPYDyqpclagPNQDFHSKSPASSSLPAFLPTTHSPPGPQQPPASLPGLTAQPL 1085
Cdd:PHA03247  2619 PDTHAPDPPPPSPSPAANEPDPHPPPTVPP-------PERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPT 2691

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1086 LSPKEATSDP---SRTPEEEPLNLEGLVAHRVAAYNARlqgighsGSFPPPPLHRLQSSSLSGV--------QAREKQPA 1154
Cdd:PHA03247  2692 VGSLTSLADPpppPPTPEPAPHALVSATPLPPGPAAAR-------QASPALPAAPAPPAVPAGPatpggparPARPPTTA 2764

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217330555 1155 EPPAPLRRRAASDGQYENQSPEATSPRS------PGVRSPVQCVSPELALTIALNPGGRPKEP 1211
Cdd:PHA03247  2765 GPPAPAPPAAPAAGPPRRLTRPAVASLSesreslPSPWDPADPPAAVLAPAAALPPAASPAGP 2827
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1302-1701 1.37e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.79  E-value: 1.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1302 PFFPASPSSHLSSRLPSEEDEGKVVVRLSEEPRsyvesvaRTAVAGPRAQDSEPKSFSAPATQAYGHEIPLRNGTLGGSF 1381
Cdd:PHA03247  2577 PSEPAVTSRARRPDAPPQSARPRAPVDDRGDPR-------GPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPP 2649

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1382 VSPSPLSTSSPI-LSADSTSVGSFPSGESSDQGPRTPTQPLLESGFrsGSLGQPSPsaQRNYQSSSPLPTVGSSYSSPDY 1460
Cdd:PHA03247  2650 ERPRDDPAPGRVsRPRRARRLGRAAQASSPPQRPRRRAARPTVGSL--TSLADPPP--PPPTPEPAPHALVSATPLPPGP 2725

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1461 SLQHFSSSPESQARAQFSVAGVHTVPGSPQARHRTVGTNTPPSPGfgwrainPSMAAPSSPSLSHHQMMGPPGTGFHGST 1540
Cdd:PHA03247  2726 AAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPA-------PPAAPAAGPPRRLTRPAVASLSESRESL 2798

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1541 VSSPQSSAATTPGSPSLCRHPAGVYQVSGLHNKVATTPGSPSLGRHPgahqgnLASGLHSNAIASPGSPSLGRHLGGSGS 1620
Cdd:PHA03247  2799 PSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGP------PPPSLPLGGSVAPGGDVRRRPPSRSPA 2872

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1621 VVPGSPcldRHVAYGGYSTPEDRRPTLSRQSSASGYQAPSTPSFPVSPAYY---------------PGLSSPATSPSPDS 1685
Cdd:PHA03247  2873 AKPAAP---ARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQpqpppppqpqpppppPPRPQPPLAPTTDP 2949

                          410
                   ....*....|....*.
gi 2217330555 1686 AAfrQGSPTPALPEKR 1701
Cdd:PHA03247  2950 AG--AGEPSGAVPQPW 2963
C1_cPKC_nPKC_rpt1 cd20792
first protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ...
 75-108 3.07e-06

first protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) protein kinase C (cPKC), novel protein kinase C (nPKC), and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. nPKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs (aPKCs) only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. This family includes classical PKCs (cPKCs) and novel PKCs (nPKCs). There are four cPKC isoforms (named alpha, betaI, betaII, and gamma) and four nPKC isoforms (delta, epsilon, eta, and theta). Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410342  Cd Length: 53  Bit Score: 46.08  E-value: 3.07e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2217330555   75 CGICRQVI---TQEGCTCKVCSFSCHRKCQAKVAAPC 108
Cdd:cd20792     15 CSHCKDFIwglGKQGYQCQVCRFVVHKRCHEYVVFKC 51
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1012-1557 3.45e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.63  E-value: 3.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1012 GTPEPAPRASLESVPPGRSYSPYDYQPCLAGPNQDFHSKSPASSSLPAFLPTTHSPPGP---QQPPASLPGLTAQPLLSP 1088
Cdd:PHA03247  2549 GDPPPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDprgPAPPSPLPPDTHAPDPPP 2628

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1089 KEATSDPSRTPEEEPLNLEGLVAHRVAAYNARLQgighsgsfppppLHRLQSSslsgvQAREKQPAEPPAPLRRRAAsdg 1168
Cdd:PHA03247  2629 PSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVS------------RPRRARR-----LGRAAQASSPPQRPRRRAA--- 2688

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1169 qyenqsPEATSPRSPGVRSPVQCVSPELALTIALNpgGRPKEPHLHSYKEAFEEMEGTSPSSPPPSGVRSPPGLAKTPLS 1248
Cdd:PHA03247  2689 ------RPTVGSLTSLADPPPPPPTPEPAPHALVS--ATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARP 2760

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1249 ALGLKPHNPADILLHPTGVTRRRIQPDSLSqeiipvnlfLSFSFFALPhlhhLPFFPASPSSHLSSRLPSEEDegkvvvr 1328
Cdd:PHA03247  2761 PTTAGPPAPAPPAAPAAGPPRRLTRPAVAS---------LSESRESLP----SPWDPADPPAAVLAPAAALPP------- 2820

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1329 lSEEPRSYVESVARTAVAGPraqdSEPKSFSAPATQAYGHEIPlrngtlGGSFVSPSPLSTSSPILSAD----------- 1397
Cdd:PHA03247  2821 -AASPAGPLPPPTSAQPTAP----PPPPGPPPPSLPLGGSVAP------GGDVRRRPPSRSPAAKPAAParppvrrlarp 2889

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1398 --STSVGSFPSGESSDQGPRTPTQPllesgfrsgSLGQPSPSAQRNYQSSSPLPTVGSSYSSPDYSLQHfSSSPESQARA 1475
Cdd:PHA03247  2890 avSRSTESFALPPDQPERPPQPQAP---------PPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDP-AGAGEPSGAV 2959

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1476 QFSVAGvHTVPGSPQARHRTVGTNTPPSPgfgwrainpsMAAPSSPSLSHHQMmgppgtgfhgSTVSSPQSSAA----TT 1551
Cdd:PHA03247  2960 PQPWLG-ALVPGRVAVPRFRVPQPAPSRE----------APASSTPPLTGHSL----------SRVSSWASSLAlheeTD 3018


                   ....*.
gi 2217330555 1552 PGSPSL 1557
Cdd:PHA03247  3019 PPPVSL 3024
PHA03378 PHA03378
EBNA-3B; Provisional
 937-1196 3.52e-06

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 52.38  E-value: 3.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  937 AASQQEIEQSIETLNMLMLDLEPASAAAPLHKSQSVPG----AWPGASPlsSQPLSGSSRQSH----------------- 995
Cdd:PHA03378   554 ASTEPVHDQLLPAPGLGPLQIQPLTSPTTSQLASSAPSyaqtPWPVPHP--SQTPEPPTTQSHipetsaprqwpmplrpi 631

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  996 PLTQSRSGYIPSGHSLG-TPEPAPRASLESVPPGRSYSPY-DYQPCLAGPNQDFH-SKSPASSSLPAFLPTTHSPP---- 1068
Cdd:PHA03378   632 PMRPLRMQPITFNVLVFpTPHQPPQVEITPYKPTWTQIGHiPYQPSPTGANTMLPiQWAPGTMQPPPRAPTPMRPPaapp 711

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1069 GPQQPPASLPGLTAQPLLSPKEAtsdpsRTPEEEPlnleGLVAHRVAAYNARLQGIGHSGSFPPPplhrlqsSSLSGVQA 1148
Cdd:PHA03378   712 GRAQRPAAATGRARPPAAAPGRA-----RPPAAAP----GRARPPAAAPGRARPPAAAPGRARPP-------AAAPGAPT 775

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2217330555 1149 REKQPAEPPAPLRR-RAASDGQYENQSPEAT---SPRS-PGVRSPVQCVSPEL 1196
Cdd:PHA03378   776 PQPPPQAPPAPQQRpRGAPTPQPPPQAGPTSmqlMPRAaPGQQGPTKQILRQL 828
C1_Myosin-IX cd20818
protein kinase C conserved region 1 (C1 domain) found in the unconventional myosin-IX family; ...
 75-108 6.59e-06

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: 44.98  E-value: 6.59e-06
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2217330555   75 CGICRQVI--TQEGCTCKVCSFSCHRKCQAKVAAPC 108
Cdd:cd20818     17 CEVCNSFIwlMEKGLVCQVCKFTCHKKCYSKITAPC 52
C1_MRCKalpha cd20864
protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related ...
 60-111 7.68e-06

protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related Cdc42-binding kinase alpha (MRCK alpha) and similar proteins; MRCK alpha, also called Cdc42-binding protein kinase alpha, DMPK-like alpha, or myotonic dystrophy protein kinase-like alpha, is a serine/threonine-protein kinase expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK alpha is an important downstream effector of Cdc42 and plays a role in the regulation of cytoskeleton reorganization and cell migration. 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: 410414  Cd Length: 60  Bit Score: 45.01  E-value: 7.68e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217330555   60 KTHRFKVKTFKKVKPCGICRQVIT---QEGCTCKVCSFSCHRKCQAKVAAPC-VPP 111
Cdd:cd20864      1 KAHQFVVKSFTTPTKCNQCTSLMVgliRQGCTCEVCGFSCHVTCADKAPSVCpIPP 56
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 1294-1689 9.73e-06

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: 51.07  E-value: 9.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1294 ALPHLHHLPFFPASPSS--------HLSSRLPSEEDEGKVVVRLSEEPRSYVESVARTAVAGPRAQDSEPKSFSAPATQA 1365
Cdd:pfam05109  447 GLPSSTHVPTNLTAPAStgptvstaDVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATSPTPA 526

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1366 YGHEIP-LRNGTLGGSfvspsplstsspilSADSTSVGSFPSGESSDQGPRTPTQ----PLLESGFRSGSLGQPSPSA-- 1438
Cdd:pfam05109  527 VTTPTPnATSPTLGKT--------------SPTSAVTTPTPNATSPTPAVTTPTPnatiPTLGKTSPTSAVTTPTPNAts 592

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1439 ----QRNYQSSSPLPTVGSSYSSPdyslqhFSSSPESQARAQFSVaGVHTVPGSPQA----RHRTVGTNTPPSPGFGWRA 1510
Cdd:pfam05109  593 ptvgETSPQANTTNHTLGGTSSTP------VVTSPPKNATSAVTT-GQHNITSSSTSsmslRPSSISETLSPSTSDNSTS 665

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1511 INPSMAAPSSPSLSHHQMMGPPGTGFHGSTVSSP-----QSSAATTPGSPSLCRHPAGVYQVSGLHNKVATTPGSPSlGR 1585
Cdd:pfam05109  666 HMPLLTSAHPTGGENITQVTPASTSTHHVSTSSPaprpgTTSQASGPGNSSTSTKPGEVNVTKGTPPKNATSPQAPS-GQ 744

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1586 HPGAHQGNLASGlhsnaiaSPGSPSLGRHLGGSGSVVPGSPCLDrhvaYGGYSTpedrrpTLSRQSSASGYQAPSTPSfP 1665
Cdd:pfam05109  745 KTAVPTVTSTGG-------KANSTTGGKHTTGHGARTSTEPTTD----YGGDST------TPRTRYNATTYLPPSTSS-K 806

                          410       420
                   ....*....|....*....|....*...
gi 2217330555 1666 VSPAYY----PGLSSPATSPSPDSAAFR 1689
Cdd:pfam05109  807 LRPRWTftspPVTTAQATVPVPPTSQPR 834
C1_MgcRacGAP cd20821
protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and ...
 75-112 1.32e-05

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: 44.32  E-value: 1.32e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2217330555   75 CGICRQVIT-QEGCT-CKVCSFSCHRKCQAKVAAPCVPPS 112
Cdd:cd20821     16 CVVCGKRIKfGKKALkCKDCRVVCHPDCKDKLPLPCVPTS 55
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
239-335 1.83e-05

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 46.50  E-value: 1.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  239 KVLEFGWPDLHTPALEKICSICKAMDTWLNADpHNVVVlHNKGNRGRIGVVIAAYMHYSNIsaSADQALDRFAMKRfyeD 318
Cdd:COG2453     49 EYLHLPIPDFGAPDDEQLQEAVDFIDEALREG-KKVLV-HCRGGIGRTGTVAAAYLVLLGL--SAEEALARVRAAR---P 121

                           90
                   ....*....|....*..
gi 2217330555  319 KIVPigQPSQRRYVHYF 335
Cdd:COG2453    122 GAVE--TPAQRAFLERF 136
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1156-1725 3.01e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 3.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1156 PPAPLRRRAAsdgqyENQSPEATSP-RSPGVRSPVQCVSP----ELALTIALN-PGGRPKEPHLHSYKEAFEEMEGTSPS 1229
Cdd:PHA03247  2475 PGAPVYRRPA-----EARFPFAAGAaPDPGGGGPPDPDAPpapsRLAPAILPDePVGEPVHPRMLTWIRGLEELASDDAG 2549

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1230 SPPPSGVRSPPGLA---KTPLSALGLKPHNPAdillhptgVTRRRIQPDSLSQeiipvnlflsfsffalphlhhlpffPA 1306
Cdd:PHA03247  2550 DPPPPLPPAAPPAApdrSVPPPRPAPRPSEPA--------VTSRARRPDAPPQ-------------------------SA 2596

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1307 SPSShlssrlpseedegkvvvrlseePRSYVESVARTAVAGPRAQDSEPKSFSAPATQAYGHEIPLRNGTLGGSFVSPSP 1386
Cdd:PHA03247  2597 RPRA----------------------PVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRD 2654

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1387 LSTSSPI-LSADSTSVGSFPSGESSDQGPRTPTQPLLESGFrsGSLGQPSPsaQRNYQSSSPLPTVGSSYSSPDYSLQHF 1465
Cdd:PHA03247  2655 DPAPGRVsRPRRARRLGRAAQASSPPQRPRRRAARPTVGSL--TSLADPPP--PPPTPEPAPHALVSATPLPPGPAAARQ 2730

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1466 SSSPESQARAQFSVAGVHTVPGSPQARHRTVGTNTPPSPGfgwrainPSMAAPSSPSLSHHQMMGPPGTGFHGSTVSSPQ 1545
Cdd:PHA03247  2731 ASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPA-------PPAAPAAGPPRRLTRPAVASLSESRESLPSPWD 2803

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1546 SSAATTPGSPSLCRHPAGVYQVSGLHNKVATTPGSPSLGRHPgahqgnLASGLHSNAIASPGSPSLGRHLGGSGSVVPGS 1625
Cdd:PHA03247  2804 PADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGP------PPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAA 2877

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1626 PcldRHVAYGGYSTPEDRRPTLSRQSSASGYQAPSTPSFPVSPAYYPGLSSPatsPSPDSAAFRQGSPTPAL-PEKRRMS 1704
Cdd:PHA03247  2878 P---ARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPP---PQPQPPPPPPPRPQPPLaPTTDPAG 2951

                          570       580
                   ....*....|....*....|....
gi 2217330555 1705 VGDRAGSLPNY---ATINGKVSSP 1725
Cdd:PHA03247  2952 AGEPSGAVPQPwlgALVPGRVAVP 2975
C1_DGK_typeII_rpt1 cd20800
first protein kinase C conserved region 1 (C1 domain) found in type II diacylglycerol kinases; ...
 75-108 6.01e-05

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


Pssm-ID: 410350  Cd Length: 60  Bit Score: 42.69  E-value: 6.01e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2217330555   75 CGICRQVI---TQEGCTCKVCSFSCHRKCQAKVAAPC 108
Cdd:cd20800     18 CNVCREALsgvTSHGLSCEVCKFKAHKRCAVKAPNNC 54
C1_KSR cd20812
protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) ...
 74-108 6.22e-05

protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) family; KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. KSR proteins contain a SAM-like domain, a zinc finger cysteine-rich domain (C1), and a pseudokinase domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410362  Cd Length: 48  Bit Score: 42.31  E-value: 6.22e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2217330555   74 PCGICRQVItQEGCTCKVCSFSCHRKCQAKVAAPC 108
Cdd:cd20812     14 TCDYCHKQM-FFGLKCKDCKYKCHKKCAKKAPPSC 47
C1_ScPKC1-like_rpt1 cd20822
first protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae ...
 75-108 7.93e-05

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


Pssm-ID: 410372  Cd Length: 52  Bit Score: 41.89  E-value: 7.93e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2217330555   75 CGICRQVITQEGCTCKVCSFSCHRKCQAKVAAPC 108
Cdd:cd20822     16 CAVCGEFLVNAGYQCEDCKYTCHKKCYEKVVTKC 49
SH2_Srm cd10360
Src homology 2 (SH2) domain found in Src-related kinase lacking C-terminal regulatory tyrosine ...
 1774-1813 1.67e-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: 1.67e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2217330555 1774 WYKPEISREQAIALL--KDQEPGAFIIRDSHSFRGAYGLAMK 1813
Cdd:cd10360      2 WYFSGISRTQAQQLLlsPPNEPGAFLIRPSESSLGGYSLSVR 43
C1_PKD_rpt2 cd20796
second protein kinase C conserved region 1 (C1 domain) found in the family of protein kinase D ...
 76-108 1.73e-04

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


Pssm-ID: 410346  Cd Length: 54  Bit Score: 41.12  E-value: 1.73e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2217330555   76 GICRQvitqeGCTCKVCSFSCHRKCQAKVAAPC 108
Cdd:cd20796     24 GLFRQ-----GLQCKDCKFNCHKKCAEKVPKDC 51
C1_MRCK cd20809
protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related ...
 75-111 2.53e-04

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


Pssm-ID: 410359  Cd Length: 53  Bit Score: 40.72  E-value: 2.53e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2217330555   75 CGICRQV---ITQEGCTCKVCSFSCHRKCQAKVAAPCVPP 111
Cdd:cd20809     14 CNHCTSLmvgLVRQGLVCEVCGYACHVSCADKAPQVCPVP 53
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 75-108 3.06e-04

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


Pssm-ID: 197519  Cd Length: 50  Bit Score: 40.14  E-value: 3.06e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2217330555    75 CGICRQVI---TQEGCTCKVCSFSCHRKCQAKVAAPC 108
Cdd:smart00109   14 CCVCRKSIwgsFKQGLRCSECKVKCHKKCADKVPKAC 50
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1011-1680 3.33e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 3.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1011 LGTPEPAPRASLESVP--PGRSYSPYDYQPCLAGPNQDfhskspassslpaflPTTHSPPGPQQPPAslPGLTAqPLLSP 1088
Cdd:PHA03247  2460 LGAPFSLSLLLGELFPgaPVYRRPAEARFPFAAGAAPD---------------PGGGGPPDPDAPPA--PSRLA-PAILP 2521

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1089 KEATSDPsrtpeeeplnleglVAHRVAAYNARLQGIGHSGSF-PPPPLHRLQSS----------------SLSGVQAREK 1151
Cdd:PHA03247  2522 DEPVGEP--------------VHPRMLTWIRGLEELASDDAGdPPPPLPPAAPPaapdrsvppprpaprpSEPAVTSRAR 2587

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1152 QPAEPPAPLRRRAASDGQYENQSPEATSPRSPGVRSPvqcvSPElaltialNPGGRPKephlhsykeAFEEMEGTSPSSP 1231
Cdd:PHA03247  2588 RPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAP----DPP-------PPSPSPA---------ANEPDPHPPPTVP 2647

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1232 PPSGVRSPPGLAKTPLSALGLKPHNPADILLHPTGVTRRRIQPdslsqeiiPVNlflSFSFFALPHLHhlPFFPASPSSH 1311
Cdd:PHA03247  2648 PPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARP--------TVG---SLTSLADPPPP--PPTPEPAPHA 2714

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1312 LSSRLPSeedegkvvvrlseeprSYVESVARTAVAGPRAQDSEPKSFSAPATQAYGHEIPLRNGTLGgsfvspsplstss 1391
Cdd:PHA03247  2715 LVSATPL----------------PPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAG------------- 2765

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1392 pilsadstsvgsfPSGESSDQGPRTPTQPLLesgfrsgslgqPSPSAQRNYQSSSPLPTVGSSYSSPDYSLQHFSSSPES 1471
Cdd:PHA03247  2766 -------------PPAPAPPAAPAAGPPRRL-----------TRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPA 2821

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1472 QARAQFSVAGVHTVPGSPQARHRTVGTNTPP----SPGFGWRAINPSMAAPSSPSLSHHqmmgPPGTGFHGSTVSSPQSS 1547
Cdd:PHA03247  2822 ASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLggsvAPGGDVRRRPPSRSPAAKPAAPAR----PPVRRLARPAVSRSTES 2897

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1548 AATTPGSPSLCRHPAGVYQVSGLHNKVATTPGSPSLgRHPGAHQGNLASglhSNAIASPGSPSLGRHLGGSGSVVPGSPC 1627
Cdd:PHA03247  2898 FALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPP-PPPPRPQPPLAP---TTDPAGAGEPSGAVPQPWLGALVPGRVA 2973

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2217330555 1628 LDRHVAyggySTPEDRRPTlsrqssasgyQAPSTPSFPVSPAyyPGLSSPATS 1680
Cdd:PHA03247  2974 VPRFRV----PQPAPSREA----------PASSTPPLTGHSL--SRVSSWASS 3010
SH2_Tec_family cd09934
Src homology 2 (SH2) domain found in Tec-like proteins; The Tec protein tyrosine kinase is the ...
 1772-1882 3.35e-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: 3.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1772 KY-WYKPEISREQAIALLKDQ-EPGAFIIRDShSFRGAYGLA--MKVSSPPptimqqnkkgdmtheLVRHFLIETGPRG- 1846
Cdd:cd09934      5 KYeWYVGDMSRQRAESLLKQEdKEGCFVVRNS-STKGLYTVSlfTKVPGSP---------------HVKHYHIKQNARSe 68

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2217330555 1847 --VKLKGCpnepnFGSLSALVYQHSIIPLALPCKLVIP 1882
Cdd:cd09934     69 fyLAEKHC-----FETIPELINYHQHNSGGLATRLKYP 101
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 919-1104 3.83e-04

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: 45.53  E-value: 3.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  919 SPQPLAETPIPSLPEFPRAASQQEIEQSIETLNMLMLDLEPASAAAPLHKSQSVPGAWPGA-------SPLSSQPLSGSS 991
Cdd:pfam03154  143 STSPSIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSApsvppqgSPATSQPPNQTQ 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  992 RQSHPLTQSRSG------YIPSGHS----LGTPEPAPRASLESVPPGRSYSPYDY--QPCLAGPNQDFHSKSPASSSLPA 1059
Cdd:pfam03154  223 STAAPHTLIQQTptlhpqRLPSPHPplqpMTQPPPPSQVSPQPLPQPSLHGQMPPmpHSLQTGPSHMQHPVPPQPFPLTP 302

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2217330555 1060 FLPTTHSPPGPQqppASLPGLTAQ-PLLSPKEATSDPSRTPEEEPL 1104
Cdd:pfam03154  303 QSSQSQVPPGPS---PAAPGQSQQrIHTPPSQSQLQSQQPPREQPL 345
SH2_Grb2_like cd09941
Src homology 2 domain found in Growth factor receptor-bound protein 2 (Grb2) and similar ...
 1774-1871 4.52e-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: 41.10  E-value: 4.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1774 WYKPEISREQAIALLKDQEP-GAFIIRDSHSFRGAYGLAMKVssppptimqqnkkgdmtHELVRHFLIETGPRG------ 1846
Cdd:cd09941      5 WFHGKISRAEAEEILMNQRPdGAFLIRESESSPGDFSLSVKF-----------------GNDVQHFKVLRDGAGkyflwv 67

                           90       100
                   ....*....|....*....|....*..
gi 2217330555 1847 VKlkgcpnepnFGSLSALV--YQHSII 1871
Cdd:cd09941     68 VK---------FNSLNELVdyHRTTSV 85
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 1405-1709 5.64e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.16  E-value: 5.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1405 PSGESSDQGPRTPTQPLLESGFRSGSLGQPSPSAQ----RNYQSSSPLPTVGSSYSSPdyslqhFSSSPESQARAQFSVA 1480
Cdd:PHA03307    80 PANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPdpppPTPPPASPPPSPAPDLSEM------LRPVGSPGPPPAASPP 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1481 GVHTVPGSPQARHRTVGTNTPPSPgfgwraINPSMAAPSSPSLSHHQMMGPPGTGFHGSTVSSPQSSAATTPGSPSLCRH 1560
Cdd:PHA03307   154 AAGASPAAVASDAASSRQAALPLS------SPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRS 227

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1561 PAG------------VYQVSGLHNKVATTPGSPSLGRHPG----AHQGNLASGLHSNAIASPGSPSLGRHLGGSGSVVPG 1624
Cdd:PHA03307   228 AADdagasssdssssESSGCGWGPENECPLPRPAPITLPTriweASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGP 307

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1625 SPCLDRHVAYGGYSTPEDRRPTLSRQSSASGYQAPSTPSFPVSPAYYPGLSSPATSPSPDSAAFRQGSPTPA------LP 1698
Cdd:PHA03307   308 APSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAasagrpTR 387

                          330
                   ....*....|.
gi 2217330555 1699 EKRRMSVGDRA 1709
Cdd:PHA03307   388 RRARAAVAGRA 398
SH2_Nterm_shark_like cd10347
N-terminal Src homology 2 (SH2) domain found in SH2 domains, ANK, and kinase domain (shark) ...
 1774-1840 6.18e-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: 40.44  E-value: 6.18e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217330555 1774 WYKPEISREQAIALLKDQEP--GAFIIRDSHSFRGAYGLAMkvssppptiMQQNKkgdmthelVRHFLI 1840
Cdd:cd10347      3 WYHGKISREVAEALLLREGGrdGLFLVRESTSAPGDYVLSL---------LAQGE--------VLHYQI 54
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 918-1187 7.51e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.78  E-value: 7.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  918 PSPQPLAETPIPSLPEFPRAASQQEIEQSietlnMLMLDLEPASAAAPlhksqsvpgawpgASPLSSQPLSGSSRQSHPL 997
Cdd:PHA03307   144 PGPPPAASPPAAGASPAAVASDAASSRQA-----ALPLSSPEETARAP-------------SSPPAEPPPSTPPAAASPR 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  998 TQSRSGYIPSGHSLGTPEPAPRASLESVPPGRSYSPYDYQPCLAGPNQDFHSKSPASSSLPAFLPTTHSP------PGPQ 1071
Cdd:PHA03307   206 PPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWngpssrPGPA 285

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1072 QPPASLPGLTAQPllSPKEATSDPSRTPEEEPLNLEGLVAHRVAAYNARLQGIGHSGSFPPPPLHRLQSSSlsgvqarEK 1151
Cdd:PHA03307   286 SSSSSPRERSPSP--SPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPS-------RP 356

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 2217330555 1152 QPAEPPAPLRRRAASDGQYENQSPEATSPRSPGVRS 1187
Cdd:PHA03307   357 PPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARA 392
C1_PIK3R-like_rpt2 cd20830
second protein kinase C conserved region 1 (C1 domain) found in uncharacterized ...
 75-108 7.75e-04

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


Pssm-ID: 410380  Cd Length: 52  Bit Score: 39.16  E-value: 7.75e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2217330555   75 CGICRQV---ITQEGCTCKVCSFSCHRKCQAKVAAPC 108
Cdd:cd20830     14 CDKCGKFlfgLVHQGLQCQDCGLVCHRTCAATGLPKC 50
PRK12727 PRK12727
flagellar biosynthesis protein FlhF;
914-1111 8.18e-04

flagellar biosynthesis protein FlhF;


Pssm-ID: 237182 [Multi-domain]  Cd Length: 559  Bit Score: 44.21  E-value: 8.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  914 VASRPSPQPLAETPIPSLPEFPRAASQQEIEQSIETLNMlmldlEPASAAAPLHKSQSVPGAWPGASPL--SSQPLSGSS 991
Cdd:PRK12727    67 AAPAPAPQAPTKPAAPVHAPLKLSANANMSQRQRVASAA-----EDMIAAMALRQPVSVPRQAPAAAPVraASIPSPAAQ 141

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  992 RQSHPLTQSRSGyiPSGHSLGT-PEPAPRASLESVPPGRsyspydyqPCLAGPNQDFHSKSPA-SSSLPAFLPTT----- 1064
Cdd:PRK12727   142 ALAHAAAVRTAP--RQEHALSAvPEQLFADFLTTAPVPR--------APVQAPVVAAPAPVPAiAAALAAHAAYAqddde 211

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217330555 1065 ---------HSPPGPQQPPASLPGLT---AQPLLSPKEATSDPSRTPEEEPLNLEGLVA 1111
Cdd:PRK12727   212 qldddgfdlDDALPQILPPAALPPIVvapAAPAALAAVAAAAPAPQNDEELKQLRGELA 270
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 184-334 8.21e-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: 40.80  E-value: 8.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  184 VTERIIAVSFPStaneenfrSNLREVAQMLKSKhgGNYLLFNLserrpditklhakvlefgwpdlhtpALEKICSICKAM 263
Cdd:cd14494      5 DPLRLIAGALPL--------SPLEADSRFLKQL--GVTTIVDL-------------------------TLAMVDRFLEVL 49

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217330555  264 DTWLNADPhnVVVLHNKGNRGRIGVVIAAY-MHYSNIsaSADQALDRfaMKRFYEDKIVPIgqPSQRRYVHY 334
Cdd:cd14494     50 DQAEKPGE--PVLVHCKAGVGRTGTLVACYlVLLGGM--SAEEAVRI--VRLIRPGGIPQT--IEQLDFLIK 113
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 1434-1700 8.45e-04

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 44.18  E-value: 8.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1434 PSPSAQRNYQSSSPLPTVgsSYSSPDYSLqhfSSSPESQARAQFSVAGVHTVPGSPQARHRTVGTNTPPSPGFGWRAIN- 1512
Cdd:pfam17823  123 PSSAAQSLPAAIAALPSE--AFSAPRAAA---CRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTt 197

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1513 -----PSMAAPSSPSLSHHQMMGPPGTGFHGSTVSSpQSSAATTPGSPSLCRHPAGVYQVSGLHNKVATTPGSPSLGrHP 1587
Cdd:pfam17823  198 aassaPATLTPARGISTAATATGHPAAGTALAAVGN-SSPAAGTVTAAVGTVTPAALATLAAAAGTVASAAGTINMG-DP 275

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1588 GAHQGNLASGLHSNAIASPGSPSLGRHLGGSGSVVP---------GSPCLDRHVAYGGYSTPEDRRPTLSRQSSASGYQA 1658
Cdd:pfam17823  276 HARRLSPAKHMPSDTMARNPAAPMGAQAQGPIIQVStdqpvhntaGEPTPSPSNTTLEPNTPKSVASTNLAVVTTTKAQA 355

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2217330555 1659 --PSTPSFPVSP-AYYPGL--SSPATSPSPDSAAFRQGSP-TPALPEK 1700
Cdd:pfam17823  356 kePSASPVPVLHtSMIPEVeaTSPTTQPSPLLPTQGAAGPgILLAPEQ 403
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 807-1103 8.63e-04

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: 44.37  E-value: 8.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  807 PAHAGHTAPMRPSYSAQEGLAGYQREGPHPAWPQPVTT--SHYAHDPSGMFRSQSFSEAEPQLPPAPvrggssreavqrg 884
Cdd:pfam03154  247 PPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTgpSHMQHPVPPQPFPLTPQSSQSQVPPGP------------- 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  885 lnswqqqqqqqqQPRPPPRQQERAHLESLVASRPSPQPLAETPIP---------------SLPEFPRAASQQEIEQSIET 949
Cdd:pfam03154  314 ------------SPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPpaplsmphikpppttPIPQLPNPQSHKHPPHLSGP 381

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  950 LNMLM-LDLEPASAAAPLHK--SQSVPGAWPGASPL--SSQPLSGSSRQSHPLTQSRSgyipsgHSLGTPEPAPRASLES 1024
Cdd:pfam03154  382 SPFQMnSNLPPPPALKPLSSlsTHHPPSAHPPPLQLmpQSQQLPPPPAQPPVLTQSQS------LPPPAASHPPTSGLHQ 455

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1025 VPPGRSYSPYDY----QPCLAGPNQDFHSKSPASSSL--PAFLPTTHSPPGPQQPPASLPG--LTAQPLLSPKEATS--D 1094
Cdd:pfam03154  456 VPSQSPFPQHPFvpggPPPITPPSGPPTSTSSAMPGIqpPSSASVSSSGPVPAAVSCPLPPvqIKEEALDEAEEPESppP 535


                   ....*....
gi 2217330555 1095 PSRTPEEEP 1103
Cdd:pfam03154  536 PPRSPSPEP 544
SH2_ABL cd09935
Src homology 2 (SH2) domain found in Abelson murine lymphosarcoma virus (ABL) proteins; ...
 1774-1882 1.14e-03

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: 40.06  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1774 WYKPEISREQAIALLKDQEPGAFIIRDSHSFRGAYGLAMKVssppptimqqnkkgdmtHELVRHFLIETGPRGvKLKGCP 1853
Cdd:cd09935      5 WYHGPISRNAAEYLLSSGINGSFLVRESESSPGQYSISLRY-----------------DGRVYHYRISEDSDG-KVYVTQ 66

                           90       100
                   ....*....|....*....|....*....
gi 2217330555 1854 NEPnFGSLSALVYQHSIIPLALPCKLVIP 1882
Cdd:cd09935     67 EHR-FNTLAELVHHHSKNADGLITTLRYP 94
SH2_BLNK_SLP-76 cd09929
Src homology 2 (SH2) domain found in B-cell linker (BLNK) protein and SH2 domain-containing ...
 1771-1875 1.47e-03

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: 40.37  E-value: 1.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1771 SKYWYKPEISREQA-IALLKDQEPGAFIIRDS--HSFRGAYGLAM----KVSSPPPTIMQQNkkgdmthelvRHFLIETG 1843
Cdd:cd09929     10 PKEWYAGNIDRKEAeEALRRSNKDGTFLVRDSsgKDSSQPYTLMVlyndKVYNIQIRFLENT----------RQYALGTG 79

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2217330555 1844 PRGvklkgcpnEPNFGSLSALVYQHSIIPLAL 1875
Cdd:cd09929     80 LRG--------EETFSSVAEIIEHHQKTPLLL 103
C1_RASSF5 cd20886
protein kinase C conserved region 1 (C1 domain) found in Ras association domain-containing ...
 75-108 1.55e-03

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


Pssm-ID: 410436  Cd Length: 50  Bit Score: 38.13  E-value: 1.55e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2217330555   75 CGICRQVITQEGCTCKVCSFSCHRKCQAKVAAPC 108
Cdd:cd20886     16 CDLCGRYILSQALRCTNCKYTCHSECRDLVQLDC 49
SH2_nSH2_p85_like cd09942
N-terminal Src homology 2 (nSH2) domain found in p85; Phosphoinositide 3-kinases (PI3Ks) are ...
 1774-1813 1.64e-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: 1.64e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2217330555 1774 WYKPEISREQAIALLKDQEPGAFIIRDSHSFRGAYGLAMK 1813
Cdd:cd09942      9 WYWGDISREEVNEKMRDTPDGTFLVRDASTMKGDYTLTLR 48
C1_PKD2_rpt2 cd20843
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and ...
 75-122 1.65e-03

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


Pssm-ID: 410393  Cd Length: 79  Bit Score: 39.19  E-value: 1.65e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2217330555   75 CGICRQVIT---QEGCTCKVCSFSCHRKCQAKVAAPCVPPS--NHELVPITTE 122
Cdd:cd20843     25 CQFCKKLLKglfRQGLQCKDCKFNCHKRCATRVPNDCLGETlfNGDLVPMEAA 77
SH2_CRK_like cd09926
Src homology 2 domain found in cancer-related signaling adaptor protein CRK; SH2 domain in the ...
 1774-1816 1.84e-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: 39.76  E-value: 1.84e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2217330555 1774 WYKPEISREQAIALLKDQEPGAFIIRDSHSFRGAYGLAMKVSS 1816
Cdd:cd09926      9 WYFGPMSRQEAQELLQGQRHGVFLVRDSSTIPGDYVLSVSENS 51
SH2_Nck_family cd09943
Src homology 2 (SH2) domain found in the Nck family; Nck proteins are adaptors that modulate ...
 1774-1849 2.02e-03

Src homology 2 (SH2) domain found in the Nck family; Nck proteins are adaptors that modulate actin cytoskeleton dynamics by linking proline-rich effector molecules to tyrosine kinases or phosphorylated signaling intermediates. There are two members known in this family: Nck1 (Nckalpha) and Nck2 (Nckbeta and Growth factor receptor-bound protein 4 (Grb4)). They are characterized by having 3 SH3 domains and a C-terminal SH2 domain. Nck1 and Nck2 have overlapping functions as determined by gene knockouts. Both bind receptor tyrosine kinases and other tyrosine-phosphorylated proteins through their SH2 domains. In addition they also bind distinct targets. Neuronal signaling proteins: EphrinB1, EphrinB2, and Disabled-1 (Dab-1) all bind to Nck-2 exclusively. And in the case of PDGFR, Tyr(P)751 binds to Nck1 while Tyr(P)1009 binds to Nck2. Nck1 and Nck2 have a role in the infection process of enteropathogenic Escherichia coli (EPEC). Their SH3 domains are involved in recruiting and activating the N-WASP/Arp2/3 complex inducing actin polymerization resulting in the production of pedestals, dynamic bacteria-presenting protrusions of the plasma membrane. A similar thing occurs in the vaccinia virus where motile plasma membrane projections are formed beneath the virus. Recently it has been shown that the SH2 domains of both Nck1 and Nck2 bind the G-protein coupled receptor kinase-interacting protein 1 (GIT1) in a phosphorylation-dependent manner. 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: 198196  Cd Length: 93  Bit Score: 39.42  E-value: 2.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1774 WYKPEISREQAIALLKDQ-EPGAFIIRDSHSFRGAYGLAMKVSSPPPTIMQQNKKG----------DMtHELVRHFL--- 1839
Cdd:cd09943      3 WYYGRITRHQAETLLNEHgHEGDFLIRDSESNPGDYSVSLKAPGRNKHFKVQVVDNvycigqrkfhTM-DELVEHYKkap 81

                           90
                   ....*....|
gi 2217330555 1840 IETGPRGVKL 1849
Cdd:cd09943     82 IFTSEQGEKL 91
C1_Myosin-IXa cd20883
protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXa and similar ...
 75-108 2.07e-03

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


Pssm-ID: 410433  Cd Length: 58  Bit Score: 38.41  E-value: 2.07e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2217330555   75 CGICRQVI--TQEGCTCKVCSFSCHRKCQAKVAAPC 108
Cdd:cd20883     19 CEYCSSLIwmMDRAYVCKLCRYACHKKCCLKTTTKC 54
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 1344-1725 2.46e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.24  E-value: 2.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1344 AVAGPRAQDSEPKSFSAPATQAYGHEIPLRNGTLGGSFVSPSPLSTSSPILSADSTSVGSFPSGESSDQGPRTPTQPLLE 1423
Cdd:PHA03307    75 PGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPA 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1424 SGFRSGSLGQPSPSAQrnyQSSSPLPTVGSSYSSPDYSLQHFSSSPESQARaqfsvagvhtvPGSPQARHRTVGTNTP-- 1501
Cdd:PHA03307   155 AGASPAAVASDAASSR---QAALPLSSPEETARAPSSPPAEPPPSTPPAAA-----------SPRPPRRSSPISASASsp 220

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1502 -PSPGFGWRAINPSMAAPSSPSLSHHQMMGPPGT--GFHGSTVSSPQSSAATTPGSPSLCRHPAGVYQVSGLHNKVATTP 1578
Cdd:PHA03307   221 aPAPGRSAADDAGASSSDSSSSESSGCGWGPENEcpLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSP 300

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1579 GSPSLGRHPGAHQGNLASGLHSNAIASPGSPSlgrHLGGSGSVVPGSPCLDRHVAYGGYSTPEDRRPTLSRQSSASGYQA 1658
Cdd:PHA03307   301 SSPGSGPAPSSPRASSSSSSSRESSSSSTSSS---SESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSS 377

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217330555 1659 PSTPSfpvspayyPGLSSPATSPSPDSAAFRQGSPtPALPEKRRMSVGDRAGSLPNYATINGKVSSP 1725
Cdd:PHA03307   378 PAASA--------GRPTRRRARAAVAGRARRRDAT-GRFPAGRPRPSPLDAGAASGAFYARYPLLTP 435
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 915-1103 3.07e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.67  E-value: 3.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  915 ASRPSPQPLAETPIPSLPEFPRAASQQEIEQSietlnmlmldlePASAAAPLHKSQSVPGAWPGASPLSSQPLSGSSRQS 994
Cdd:PRK07764   612 AARPAAPAAPAAPAAPAPAGAAAAPAEASAAP------------APGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPA 679

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555  995 HPLTQSRSGYIPSGHSLGTPEPAPRASLESvPPGRSYSPYDYQPclaGPNQDFHSKSPASSSLPAFLPTTHSPPGPQQPP 1074
Cdd:PRK07764   680 APPPAPAPAAPAAPAGAAPAQPAPAPAATP-PAGQADDPAAQPP---QAAQGASAPSPAADDPVPLPPEPDDPPDPAGAP 755

                          170       180
                   ....*....|....*....|....*....
gi 2217330555 1075 ASLPGLTAQPLLSPKEATSDPSRTPEEEP 1103
Cdd:PRK07764   756 AQPPPPPAPAPAAAPAAAPPPSPPSEEEE 784
SH2_C-SH2_PLC_gamma_like cd09932
C-terminal Src homology 2 (C-SH2) domain in Phospholipase C gamma; Phospholipase C gamma is a ...
 1771-1814 3.35e-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: 3.35e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2217330555 1771 SKYWYKPEISREQAIALLKD-QEPGAFIIRDSHSFRGAYGLAMKV 1814
Cdd:cd09932      3 SKEWFHANLTREQAEEMLMRvPRDGAFLVRPSETDPNSFAISFRA 47
SH2_Grb7_family cd09944
Src homology 2 (SH2) domain found in the growth factor receptor bound, subclass 7 (Grb7) ...
 1771-1813 3.79e-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: 3.79e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2217330555 1771 SKYWYKPEISREQAIALLKDQ--EPGAFIIRDSHSFRGAYGLAMK 1813
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 ...
 1774-1812 4.00e-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: 4.00e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217330555 1774 WYKPEISREQAIALLKDQEPGAFIIRDSHSFRGAYGLAM 1812
Cdd:cd09937      5 WFHGKISREEAERLLQPPEDGLFLVRESTNYPGDYTLCV 43
C1_DGK_typeI_rpt1 cd20799
first protein kinase C conserved region 1 (C1 domain) found in type I diacylglycerol kinases; ...
 75-109 4.20e-03

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


Pssm-ID: 410349  Cd Length: 62  Bit Score: 37.35  E-value: 4.20e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2217330555   75 CGICRQVIT---QEGCTCKVCSFSCHRKCQAKVAAPCV 109
Cdd:cd20799     19 CNVCENMLVglrKQGLCCTFCKYTVHERCVSRAPASCI 56
SH2_SOCS_family cd09923
Src homology 2 (SH2) domain found in suppressor of cytokine signaling (SOCS) family; SH2 ...
 1774-1801 4.46e-03

Src homology 2 (SH2) domain found in suppressor of cytokine signaling (SOCS) family; SH2 domain found in SOCS proteins. SOCS was first recognized as a group of cytokine-inducible SH2 (CIS) domain proteins comprising eight family members in human (CIS and SOCS1-SOCS7). In addition to the SH2 domain, SOCS proteins have a variable N-terminal domain and a conserved SOCS box in the C-terminal domain. SOCS proteins bind to a substrate via their SH2 domain. The prototypical members, CIS and SOCS1-SOCS3, have been shown to regulate growth hormone signaling in vitro and in a classic negative feedback response compete for binding at phosphotyrosine sites in JAK kinase and receptor pathways to displace effector proteins and target bound receptors for proteasomal degradation. Loss of SOCS activity results in excessive cytokine signaling associated with a variety of hematopoietic, autoimmune, and inflammatory diseases and certain cancers. Members (SOCS4-SOCS7) were identified by their conserved SOCS box, an adapter motif of 3 helices that associates substrate binding domains, such as the SOCS SH2 domain, ankryin, and WD40 with ubiquitin ligase components. These show limited cytokine induction. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198178  Cd Length: 81  Bit Score: 37.95  E-value: 4.46e-03
                           10        20
                   ....*....|....*....|....*...
gi 2217330555 1774 WYKPEISREQAIALLKDQEPGAFIIRDS 1801
Cdd:cd09923      2 WYWGGITRYEAEELLAGKPEGTFLVRDS 29
C1_nPKC_theta-like_rpt2 cd20837
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
 76-108 4.97e-03

second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) theta, delta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410387  Cd Length: 50  Bit Score: 37.03  E-value: 4.97e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2217330555   76 GICRQvitqeGCTCKVCSFSCHRKCQAKVAAPC 108
Cdd:cd20837     23 GLFRQ-----GLKCEECGMNVHHKCQKKVANLC 50
C1_PDZD8 cd20825
protein kinase C conserved region 1 (C1 domain) found in PDZ domain-containing protein 8 ...
 75-103 5.18e-03

protein kinase C conserved region 1 (C1 domain) found in PDZ domain-containing protein 8 (PDZD8) and similar proteins; PDZD8, also called Sarcoma antigen NY-SAR-84/NY-SAR-104, is a molecular tethering protein that connects endoplasmic reticulum (ER) and mitochondrial membranes. PDZD8-dependent ER-mitochondria membrane tethering is essential for ER-mitochondria Ca2+ transfer. In neurons, it is involved in the regulation of dendritic Ca2+ dynamics by regulating mitochondrial Ca2+ uptake. PDZD8 also plays an indirect role in the regulation of cell morphology and cytoskeletal organization. It contains a PDZ domain and a C1 domain. This model describes the C1 domain, a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410375  Cd Length: 55  Bit Score: 36.87  E-value: 5.18e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2217330555   75 CGIC-RQVITQEGCTCKVCSFSCHRKCQAK 103
Cdd:cd20825     17 CDFCkKKIWLKEAFQCRLCGMICHKKCLDK 46
SH2_cSH2_p85_like cd09930
C-terminal Src homology 2 (cSH2) domain found in p85; Phosphoinositide 3-kinases (PI3Ks) are ...
 1774-1869 5.25e-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: 5.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1774 WYKPEISREQAIALLKDQEPGAFIIRDShSFRGAYGLAMKVSSppptimqqnkkgdmtheLVRHFLIETGPRGVKLKgcp 1853
Cdd:cd09930      8 WLVGDINRTQAEELLRGKPDGTFLIRES-STQGCYACSVVCNG-----------------EVKHCVIYKTETGYGFA--- 66

                           90       100
                   ....*....|....*....|
gi 2217330555 1854 nEPN--FGSLSALV--YQHS 1869
Cdd:cd09930     67 -EPYnlYESLKELVlhYAHN 85
C1_Raf cd20811
protein kinase C conserved region 1 (C1 domain) found in the Raf (Rapidly Accelerated ...
 75-109 5.29e-03

protein kinase C conserved region 1 (C1 domain) found in the Raf (Rapidly Accelerated Fibrosarcoma) kinase family; Raf kinases are serine/threonine kinases (STKs) that catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. They act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain (C1), and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410361  Cd Length: 49  Bit Score: 36.89  E-value: 5.29e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2217330555   75 CGICRQVITQeGCTCKVCSFSCHRKCQAKVAAPCV 109
Cdd:cd20811     16 CDVCRKLLFQ-GFRCQTCGFKFHQRCSDQVPALCE 49
SH2_C-SH2_SHP_like cd09931
C-terminal Src homology 2 (C-SH2) domain found in SH2 domain Phosphatases (SHP) proteins; The ...
 1774-1850 6.03e-03

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


Pssm-ID: 198185  Cd Length: 99  Bit Score: 38.03  E-value: 6.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1774 WYKPEISREQAIALLKDQ-EPGAFIIRDSHSFRGAYGLAMKVSSPPPT---IMQQNKK---------GDMThELVRHF-- 1838
Cdd:cd09931      2 WFHGHLSGKEAEKLLLEKgKPGSFLVRESQSKPGDFVLSVRTDDDKVThimIRCQGGKydvgggeefDSLT-DLVEHYkk 80

                           90
                   ....*....|....
gi 2217330555 1839 --LIETGPRGVKLK 1850
Cdd:cd09931     81 npMVETSGTVVHLK 94
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
1478-1700 6.67e-03

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 41.28  E-value: 6.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1478 SVAGVHTVPGSPQArhrTVGTNTPPSPGFGWraiNPSMAAPSSPSLSHHQMMGPPGTGFHGSTVSSPQSSAATTPGSPSL 1557
Cdd:COG3469     21 TLLGAAATAASVTL---TAATATTVVSTTGS---VVVAASGSAGSGTGTTAASSTAATSSTTSTTATATAAAAAATSTSA 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330555 1558 CRHPAGVYQVSGLHNKVATTPGSPslgrhpgahQGNLASGLHSNAIASPGSPSLGRHLGGSGSVVPGSPcldrhvAYGGY 1637
Cdd:COG3469     95 TLVATSTASGANTGTSTVTTTSTG---------AGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVS------GTETA 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217330555 1638 STPedrrptlSRQSSASGYQAPSTPSFPVSPAYYPGLSSPATSPSPDSAAFRQGSPTPALPEK 1700
Cdd:COG3469    160 TGG-------TTTTSTTTTTTSASTTPSATTTATATTASGATTPSATTTATTTGPPTPGLPKH 215
SH2_a2chimerin_b2chimerin cd10352
Src homology 2 (SH2) domain found in alpha2-chimerin and beta2-chimerin proteins; Chimerins ...
 1779-1842 6.92e-03

Src homology 2 (SH2) domain found in alpha2-chimerin and beta2-chimerin proteins; Chimerins are a family of phorbol ester- and diacylglycerol-responsive GTPase-activating proteins. Alpha1-chimerin (formerly known as n-chimerin) and alpha2-chimerin are alternatively spliced products of a single gene, as are beta1- and beta2-chimerin. alpha1- and beta1-chimerin have a relatively short N-terminal region that does not encode any recognizable domains, whereas alpha2- and beta2-chimerin both include a functional SH2 domain that can bind to phosphotyrosine motifs within receptors. All of the isoforms contain a GAP domain with specificity in vitro for Rac1 and a diacylglycerol (DAG)-binding C1 domain which allows them to translocate to membranes in response to DAG signaling and anchors them in close proximity to activated Rac. Other C1 domain-containing diacylglycerol receptors including: PKC, Munc-13 proteins, phorbol ester binding scaffolding proteins involved in Ca2+-stimulated exocytosis, and RasGRPs, diacylglycerol-activated guanine-nucleotide exchange factors (GEFs) for Ras and Rap1. 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: 198215  Cd Length: 91  Bit Score: 37.73  E-value: 6.92e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217330555 1779 ISREQAIALLKDQEPGAFIIRDSHSFRGAYGLAMKVSSPP--------PTIMQQN---KKGDMTHELVR----HFLIET 1842
Cdd:cd10352     13 ISREEAEQLLSGASDGSYLIRESSRDDGYYTLSLRFNGKVknyklyydGKNHYHYvgeKRFDTIHDLVAdgliTLYMET 91
C1_dGM13116p-like cd20831
protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and ...
 75-108 7.78e-03

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


Pssm-ID: 410381  Cd Length: 58  Bit Score: 36.55  E-value: 7.78e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2217330555   75 CGICRQVIT----QEGCTCKVCSFSCHRKCQAKVAAPC 108
Cdd:cd20831     19 CAVCNKLIPgrfgKQGYQCRDCGLICHKRCHVKVETHC 56
C1_Stac cd20817
protein kinase C conserved region 1 (C1 domain) found in the SH3 and cysteine-rich ...
 74-110 8.65e-03

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


Pssm-ID: 410367  Cd Length: 51  Bit Score: 36.15  E-value: 8.65e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2217330555   74 PCGICRQVI---TQEGCTCKVCSFSCHRKCQAKVaAPCVP 110
Cdd:cd20817     13 FCDVCKELLvglSKQGLRCKNCKMNVHHKCQEGV-PDCSG 51
SH2_SLAP cd10344
Src homology 2 domain found in Src-like adaptor proteins; SLAP belongs to the subfamily of ...
 1774-1817 8.83e-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: 8.83e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2217330555 1774 WYKPEISREQAIALLK--DQEPGAFIIRDSHSFRGAYGLAMKVSSP 1817
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 ...
 1774-1846 9.05e-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: 9.05e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217330555 1774 WYKPEISREQAIALL-KDQEPGAFIIRDSHSFRGAYGLAMKVSsppptimqqnkkgdmthELVRHFLIETGPRG 1846
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH