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Conserved domains on  [gi|1720383787|ref|XP_030104299|]
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tensin-2 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 133-291 1.23e-110

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


The actual alignment was detected with superfamily member cd14562:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 159  Bit Score: 345.39  E-value: 1.23e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  133 DLTYVTERILAAAFPARPDEQRHRGHLRELAHVLQSKHRDKYLLFNLSEKRHDLTRLNPKVQDFGWPELHAPPLDKLCSI 212
Cdd:cd14562      1 DLTYITERIISVFFPPALEEQRYRGNLREVAQMLKSKHEDKYLLFNLSEKRHDITRLNPKVQDFGWPDLHAPPLDKICSI 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720383787  213 CKAMETWLSADPQHVVVLYCKGSKGKLGVIVSAYMHYSKISAGADQALATLTMRKFCEDKVATELQPSQRRYVSYFSGL 291
Cdd:cd14562     81 CKAMETWLNADPQHVVVLHCKGNKGKTGVIVAAYMHYSKISAGADQALSTLAMRKFCEDKVATSLQPSQRRYISYFGGL 159
PTB_tensin cd01213
Tensin Phosphotyrosine-binding (PTB) domain; Tensin is a a focal adhesion protein, which ...
 1272-1404 6.80e-80

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


:

Pssm-ID: 269924  Cd Length: 136  Bit Score: 258.71  E-value: 6.80e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1272 GAACSVLYLTSVETESLTGPQAVAKASSAALSCSPVPVPAIVHFKVSAQGITLTDNQRKLFFRRHYPVNSITFSSTDPQD 1351
Cdd:cd01213      1 GAACNVLYLGSVDTESLTGPQAVRKAVSETLERDPLPTPTVVHFKVSEQGITLTDNQRKLFFRRHYPLNTVSFCGMDPEN 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720383787 1352 RRWTNPD---GATSKIFGFVAKKPGSPWENVCHLFAELDPDQPASAIVTFITKVLL 1404
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. ...
 1135-1248 4.50e-68

Src homology 2 domain found in Tensin-like proteins; SH2 domain found in Tensin-like proteins. The Tensins are a family of intracellular proteins that interact with receptor tyrosine kinases (RTKs), integrins, and actin. They are thought act as signaling bridges between the extracellular space and the cytoskeleton. There are four homologues: Tensin1, Tensin2 (TENC1, C1-TEN), Tensin3 and Tensin4 (cten), all of which contain a C-terminal tandem SH2-PTB domain pairing, as well as actin-binding regions that may localize them to focal adhesions. The isoforms of Tensin2 and Tensin3 contain N-terminal C1 domains, which are atypical and not expected to bind to phorbol esters. Tensins 1-3 contain a phosphatase (PTPase) and C2 domain pairing which resembles PTEN (phosphatase and tensin homologue deleted on chromosome 10) protein. PTEN is a lipid phosphatase that dephosphorylates phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) to yield phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). As PtdIns(3,4,5)P3 is the product of phosphatidylinositol 3-kinase (PI3K) activity, PTEN is therefore a key negative regulator of the PI3K pathway. Because of their PTEN-like domains, the Tensins may also possess phosphoinositide-binding or phosphatase capabilities. However, only Tensin2 and Tensin3 have the potential to be phosphatases since only their PTPase domains contain a cysteine residue that is essential for catalytic activity. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


:

Pssm-ID: 198181 [Multi-domain]  Cd Length: 116  Bit Score: 224.23  E-value: 4.50e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1135 TSKFWYKPHLSRDQAIALLKDKDPGAFLIRDSHSFQGAYGLALKVATPPPSAQPW--KGDPSEQLVRHFLIETGPKGVKI 1212
Cdd:cd09927      1 TSKYWYKPNISRDQAIALLKDKPPGTFLVRDSTTYKGAYGLAVKVATPPPGVNPFeaKGDPESELVRHFLIEPSPKGVKL 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1720383787 1213 KGCPTEPYFGSLSALVSQHSISPISLPCCLRIPSKD 1248
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 ...
 298-425 1.64e-39

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: 143.19  E-value: 1.64e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  298 MNSSPLFLHYVFVPVLPAFEPNTGFQPFLKIYQSMQLV-YTSGVYRIAGPGPQQLCISLEP-ALLLKGDVMVTCYHKGGQ 375
Cdd:pfam10409    1 PPPKPLTLHSIILHGIPNFKSGGGCRPYIRIYQNKKKVfSTSGKYKKLKEYQQDDCVILFPkGIPVQGDVLVEFYHKGSD 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720383787  376 GTDRTLVFRVQFHTCTIHGSRLTFPKDQLDEAW---ADERFPFQASVEFVFSS 425
Cdd:pfam10409   81 LLSEEKMFRFWFNTSFIEDNTLTLPKNELDKADkdkKDKRFPKDFKVELLFSE 133
C1_TNS2 cd20887
protein kinase C conserved region 1 (C1 domain) found in tensin-2 and similar proteins; ...
 31-84 2.30e-24

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: 97.16  E-value: 2.30e-24
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720383787   31 EPHSFREKVFRKKtPVCAVCKVTIDGTGVSCRVCKVATHRKCEAKVTSSCQALP 84
Cdd:cd20887      1 EPHSFKEKTFKKK-RACAVCREPVGGQGLVCRVCKVASHKKCEAKVTSACQPPP 53
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 726-1124 5.34e-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: 64.57  E-value: 5.34e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  726 LLHPVRPGHPLPLLVPACGHHHAP--MPDYGCLKPPKVGEEGHEGC-SYAVCSEGRYGHSGYPALVTYGYG--------- 793
Cdd:PHA03247  2469 LLGELFPGAPVYRRPAEARFPFAAgaAPDPGGGGPPDPDAPPAPSRlAPAILPDEPVGEPVHPRMLTWIRGleelasdda 2548

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  794 GAVPSYCPAYGRAPHSCGSPSEGRGYPSPGAHSPRAGSVSPGSPPY-LQPRKLGyeisaeDGRDKYPLSGHLASTGPLAS 872
Cdd:PHA03247  2549 GDPPPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQsARPRAPV------DDRGDPRGPAPPSPLPPDTH 2622

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  873 TELFPPVSESPEPSWRDGSSGHSTLP-----RSPRDPQCSASSELSGPSTPLHTSSPVQG-------------KESNRRQ 934
Cdd:PHA03247  2623 APDPPPPSPSPAANEPDPHPPPTVPPperprDDPAPGRVSRPRRARRLGRAAQASSPPQRprrraarptvgslTSLADPP 2702

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  935 DTTRSPSLAPTQrLSPGEALPSVVQGVAEKTPELLTSSRPeqldPSPFSQTSAPGSPNGWPQERSPGGHTNSASPRSPVP 1014
Cdd:PHA03247  2703 PPPPTPEPAPHA-LVSATPLPPGPAAARQASPALPAAPAP----PAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAA 2777

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1015 TTLPGLRH--------------APWQG--------PRGTSDSPDGSPLTPVPTQMPWLVGSPEPPQSSPTPAFPLATSYD 1072
Cdd:PHA03247  2778 GPPRRLTRpavaslsesreslpSPWDPadppaavlAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVA 2857

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720383787 1073 ANGPIQPPLPEKRHLPGSGQQPSPPARS------TNQHVTFASPLPDVTQPPEHPLQE 1124
Cdd:PHA03247  2858 PGGDVRRRPPSRSPAAKPAAPARPPVRRlarpavSRSTESFALPPDQPERPPQPQAPP 2915
 
Name Accession Description Interval E-value
PTP_tensin-2 cd14562
protein tyrosine phosphatase-like domain of tensin-2; Tensin-2 (TNS2) is also called ...
 133-291 1.23e-110

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: 345.39  E-value: 1.23e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  133 DLTYVTERILAAAFPARPDEQRHRGHLRELAHVLQSKHRDKYLLFNLSEKRHDLTRLNPKVQDFGWPELHAPPLDKLCSI 212
Cdd:cd14562      1 DLTYITERIISVFFPPALEEQRYRGNLREVAQMLKSKHEDKYLLFNLSEKRHDITRLNPKVQDFGWPDLHAPPLDKICSI 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720383787  213 CKAMETWLSADPQHVVVLYCKGSKGKLGVIVSAYMHYSKISAGADQALATLTMRKFCEDKVATELQPSQRRYVSYFSGL 291
Cdd:cd14562     81 CKAMETWLNADPQHVVVLHCKGNKGKTGVIVAAYMHYSKISAGADQALSTLAMRKFCEDKVATSLQPSQRRYISYFGGL 159
PTB_tensin cd01213
Tensin Phosphotyrosine-binding (PTB) domain; Tensin is a a focal adhesion protein, which ...
 1272-1404 6.80e-80

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


Pssm-ID: 269924  Cd Length: 136  Bit Score: 258.71  E-value: 6.80e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1272 GAACSVLYLTSVETESLTGPQAVAKASSAALSCSPVPVPAIVHFKVSAQGITLTDNQRKLFFRRHYPVNSITFSSTDPQD 1351
Cdd:cd01213      1 GAACNVLYLGSVDTESLTGPQAVRKAVSETLERDPLPTPTVVHFKVSEQGITLTDNQRKLFFRRHYPLNTVSFCGMDPEN 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720383787 1352 RRWTNPD---GATSKIFGFVAKKPGSPWENVCHLFAELDPDQPASAIVTFITKVLL 1404
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. ...
 1135-1248 4.50e-68

Src homology 2 domain found in Tensin-like proteins; SH2 domain found in Tensin-like proteins. The Tensins are a family of intracellular proteins that interact with receptor tyrosine kinases (RTKs), integrins, and actin. They are thought act as signaling bridges between the extracellular space and the cytoskeleton. There are four homologues: Tensin1, Tensin2 (TENC1, C1-TEN), Tensin3 and Tensin4 (cten), all of which contain a C-terminal tandem SH2-PTB domain pairing, as well as actin-binding regions that may localize them to focal adhesions. The isoforms of Tensin2 and Tensin3 contain N-terminal C1 domains, which are atypical and not expected to bind to phorbol esters. Tensins 1-3 contain a phosphatase (PTPase) and C2 domain pairing which resembles PTEN (phosphatase and tensin homologue deleted on chromosome 10) protein. PTEN is a lipid phosphatase that dephosphorylates phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) to yield phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). As PtdIns(3,4,5)P3 is the product of phosphatidylinositol 3-kinase (PI3K) activity, PTEN is therefore a key negative regulator of the PI3K pathway. Because of their PTEN-like domains, the Tensins may also possess phosphoinositide-binding or phosphatase capabilities. However, only Tensin2 and Tensin3 have the potential to be phosphatases since only their PTPase domains contain a cysteine residue that is essential for catalytic activity. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198181 [Multi-domain]  Cd Length: 116  Bit Score: 224.23  E-value: 4.50e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1135 TSKFWYKPHLSRDQAIALLKDKDPGAFLIRDSHSFQGAYGLALKVATPPPSAQPW--KGDPSEQLVRHFLIETGPKGVKI 1212
Cdd:cd09927      1 TSKYWYKPNISRDQAIALLKDKPPGTFLVRDSTTYKGAYGLAVKVATPPPGVNPFeaKGDPESELVRHFLIEPSPKGVKL 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1720383787 1213 KGCPTEPYFGSLSALVSQHSISPISLPCCLRIPSKD 1248
Cdd:cd09927     81 KGCPNEPVFGSLSALVYQHSITPLALPCKLRIPDRD 116
PTB pfam08416
Phosphotyrosine-binding domain; The phosphotyrosine-binding domain (PTB, also ...
 1274-1408 3.08e-45

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: 159.43  E-value: 3.08e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1274 ACSVLYLTSVETESLTGPQAVAKAS--SAALSCSPVPVPAIVHFKVSAQGITLTDNQRKLFFrRHYPVNSITFSSTDPQD 1351
Cdd:pfam08416    1 QYRVEHLTTFELDSLTGLQAVEDAIrkLQLLDAQGRVWTQEMLLQVSDQGITLTDNETKEEL-ESYPLDSISHCQAVLND 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720383787 1352 RRWTNpdgatskIFGFVAKKPGSPWENVcHLFA--ELDPDQPASAIVTFITKVLLGQRK 1408
Cdd:pfam08416   80 GRYNS-------ILALVCQEPGQSKPDV-HLFQcdELGAELIAEDIESALSDVRLGKPK 130
PTEN_C2 pfam10409
C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key ...
 298-425 1.64e-39

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: 143.19  E-value: 1.64e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  298 MNSSPLFLHYVFVPVLPAFEPNTGFQPFLKIYQSMQLV-YTSGVYRIAGPGPQQLCISLEP-ALLLKGDVMVTCYHKGGQ 375
Cdd:pfam10409    1 PPPKPLTLHSIILHGIPNFKSGGGCRPYIRIYQNKKKVfSTSGKYKKLKEYQQDDCVILFPkGIPVQGDVLVEFYHKGSD 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720383787  376 GTDRTLVFRVQFHTCTIHGSRLTFPKDQLDEAW---ADERFPFQASVEFVFSS 425
Cdd:pfam10409   81 LLSEEKMFRFWFNTSFIEDNTLTLPKNELDKADkdkKDKRFPKDFKVELLFSE 133
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 1271-1408 1.80e-24

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: 100.08  E-value: 1.80e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  1271 QGAACSVLYLTSVETESLTGPQAVAKASS--AALSCSPVPVPAIVHFKVSAQGITLTDNQRKlFFRRHYPVNSITFSSTD 1348
Cdd:smart00462    2 SGVSFRVKYLGSVEVPEARGLQVVQEAIRklRAAQGSEKKEPQKVILSISSRGVKLIDEDTK-AVLHEHPLRRISFCAVG 80

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720383787  1349 PQDrrwtnpdgatSKIFGFVAKKPGSPWeNVCHLFAELDP--DQPASAIVTFITKVLLGQRK 1408
Cdd:smart00462   81 PDD----------LDVFGYIARDPGSSR-FACHVFRCEKAaeDIALAIGQAFQLAYELKLKA 131
C1_TNS2 cd20887
protein kinase C conserved region 1 (C1 domain) found in tensin-2 and similar proteins; ...
 31-84 2.30e-24

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: 97.16  E-value: 2.30e-24
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720383787   31 EPHSFREKVFRKKtPVCAVCKVTIDGTGVSCRVCKVATHRKCEAKVTSSCQALP 84
Cdd:cd20887      1 EPHSFKEKTFKKK-RACAVCREPVGGQGLVCRVCKVASHKKCEAKVTSACQPPP 53
SH2 smart00252
Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides ...
 1139-1237 3.39e-13

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


Pssm-ID: 214585 [Multi-domain]  Cd Length: 84  Bit Score: 66.10  E-value: 3.39e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  1139 WYKPHLSRDQAIALLKDKDPGAFLIRDSHSFQGAYGLALKVatpppsaqpwkgdpsEQLVRHFLIE-TGPKGVKIKGcpt 1217
Cdd:smart00252    3 WYHGFISREEAEKLLKNEGDGDFLVRDSESSPGDYVLSVRV---------------KGKVKHYRIRrNEDGKFYLEG--- 64

                            90       100
                    ....*....|....*....|
gi 1720383787  1218 EPYFGSLSALVSQHSISPIS 1237
Cdd:smart00252   65 GRKFPSLVELVEHYQKNSLG 84
SH2 pfam00017
SH2 domain;
1139-1231 1.93e-11

SH2 domain;


Pssm-ID: 425423 [Multi-domain]  Cd Length: 77  Bit Score: 61.08  E-value: 1.93e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1139 WYKPHLSRDQAIALLKDKDP-GAFLIRDSHSFQGAYGLALKvatpppsaqpWKGDpseqlVRHFLI-ETGPKGVKIKGcp 1216
Cdd:pfam00017    1 WYHGKISRQEAERLLLNGKPdGTFLVRESESTPGGYTLSVR----------DDGK-----VKHYKIqSTDNGGYYISG-- 63

                           90
                   ....*....|....*
gi 1720383787 1217 tEPYFGSLSALVSQH 1231
Cdd:pfam00017   64 -GVKFSSLAELVEHY 77
PHA03247 PHA03247
large tegument protein UL36; Provisional
 726-1124 5.34e-10

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 64.57  E-value: 5.34e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  726 LLHPVRPGHPLPLLVPACGHHHAP--MPDYGCLKPPKVGEEGHEGC-SYAVCSEGRYGHSGYPALVTYGYG--------- 793
Cdd:PHA03247  2469 LLGELFPGAPVYRRPAEARFPFAAgaAPDPGGGGPPDPDAPPAPSRlAPAILPDEPVGEPVHPRMLTWIRGleelasdda 2548

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  794 GAVPSYCPAYGRAPHSCGSPSEGRGYPSPGAHSPRAGSVSPGSPPY-LQPRKLGyeisaeDGRDKYPLSGHLASTGPLAS 872
Cdd:PHA03247  2549 GDPPPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQsARPRAPV------DDRGDPRGPAPPSPLPPDTH 2622

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  873 TELFPPVSESPEPSWRDGSSGHSTLP-----RSPRDPQCSASSELSGPSTPLHTSSPVQG-------------KESNRRQ 934
Cdd:PHA03247  2623 APDPPPPSPSPAANEPDPHPPPTVPPperprDDPAPGRVSRPRRARRLGRAAQASSPPQRprrraarptvgslTSLADPP 2702

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  935 DTTRSPSLAPTQrLSPGEALPSVVQGVAEKTPELLTSSRPeqldPSPFSQTSAPGSPNGWPQERSPGGHTNSASPRSPVP 1014
Cdd:PHA03247  2703 PPPPTPEPAPHA-LVSATPLPPGPAAARQASPALPAAPAP----PAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAA 2777

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1015 TTLPGLRH--------------APWQG--------PRGTSDSPDGSPLTPVPTQMPWLVGSPEPPQSSPTPAFPLATSYD 1072
Cdd:PHA03247  2778 GPPRRLTRpavaslsesreslpSPWDPadppaavlAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVA 2857

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720383787 1073 ANGPIQPPLPEKRHLPGSGQQPSPPARS------TNQHVTFASPLPDVTQPPEHPLQE 1124
Cdd:PHA03247  2858 PGGDVRRRPPSRSPAAKPAAPARPPVRRlarpavSRSTESFALPPDQPERPPQPQAPP 2915
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 33-80 9.36e-08

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


Pssm-ID: 197519  Cd Length: 50  Bit Score: 49.77  E-value: 9.36e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1720383787    33 HSFREKVFrKKTPVCAVCKVTIDG---TGVSCRVCKVATHRKCEAKVTSSC 80
Cdd:smart00109    1 HKHVFRTF-TKPTFCCVCRKSIWGsfkQGLRCSECKVKCHKKCADKVPKAC 50
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 930-1120 7.98e-07

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: 53.77  E-value: 7.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  930 SNRRQDTTRSPSLAPTqrlspGEALPSVVQGVAEKT--PELLTS--------SRPEQLDPSPFSQTSAPGSPNGWPQERS 999
Cdd:pfam05109  422 SKAPESTTTSPTLNTT-----GFAAPNTTTGLPSSThvPTNLTApastgptvSTADVTSPTPAGTTSGASPVTPSPSPRD 496

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1000 PGGHTNS---ASPRSPVPTTLPglrHAPWQGPRGTSDSPDGSPLTPVPTQMPWLVGSPEPPQSSPTPA---------FPL 1067
Cdd:pfam05109  497 NGTESKApdmTSPTSAVTTPTP---NATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAvttptpnatIPT 573

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720383787 1068 ATSYDANGPIQPPLPEKRHlPGSGQQpSPPARSTNQHVTFASPLPDVTQPPEH 1120
Cdd:pfam05109  574 LGKTSPTSAVTTPTPNATS-PTVGET-SPQANTTNHTLGGTSSTPVVTSPPKN 624
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
 877-1022 1.03e-04

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 47.19  E-value: 1.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  877 PPVSESPE----PSWRDGSSGHSTLPRSPRDPQCSASSELSGPST--PLHTSSPVQGKESNRRQDTTRSPSLA--PTQRL 948
Cdd:COG5422     49 GADNDIINseskESFGKYALGHQIFSSFSSSPKLFQRRNSAGPIThsPSATSSTSSLNSNDGDQFSPASDSLSfnPSSTQ 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  949 SPGEALPSVVQGVAEKTPELLTSSRpEQLDPSPFSQTSAPGSPNGWPQERS--------------PGGHTNSASPRSPV- 1013
Cdd:COG5422    129 SRKDSGPGDGSPVQKRKNPLLPSSS-THGTHPPIVFTDNNGSHAGAPNARSrkeipslgsqsmqlPSPHFRQKFSSSDTs 207

                          170
                   ....*....|
gi 1720383787 1014 -PTTLPGLRH 1022
Cdd:COG5422    208 nGFSYPSIRK 217
 
Name Accession Description Interval E-value
PTP_tensin-2 cd14562
protein tyrosine phosphatase-like domain of tensin-2; Tensin-2 (TNS2) is also called ...
 133-291 1.23e-110

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: 345.39  E-value: 1.23e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  133 DLTYVTERILAAAFPARPDEQRHRGHLRELAHVLQSKHRDKYLLFNLSEKRHDLTRLNPKVQDFGWPELHAPPLDKLCSI 212
Cdd:cd14562      1 DLTYITERIISVFFPPALEEQRYRGNLREVAQMLKSKHEDKYLLFNLSEKRHDITRLNPKVQDFGWPDLHAPPLDKICSI 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720383787  213 CKAMETWLSADPQHVVVLYCKGSKGKLGVIVSAYMHYSKISAGADQALATLTMRKFCEDKVATELQPSQRRYVSYFSGL 291
Cdd:cd14562     81 CKAMETWLNADPQHVVVLHCKGNKGKTGVIVAAYMHYSKISAGADQALSTLAMRKFCEDKVATSLQPSQRRYISYFGGL 159
PTP_tensin cd14508
protein tyrosine phosphatase-like domain of tensins; The tensin family of intracellular ...
 133-291 1.28e-94

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


Pssm-ID: 350358 [Multi-domain]  Cd Length: 159  Bit Score: 301.23  E-value: 1.28e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  133 DLTYVTERILAAAFPARPDEQRHRGHLRELAHVLQSKHRDKYLLFNLSEKRHDLTRLNPKVQDFGWPELHAPPLDKLCSI 212
Cdd:cd14508      1 DLTYITERIIALSFPSTCSEQTYRHNLREAAHLLQSKHGDNYMVFNLSERRHDLRSLNPKVLDFGWPELHAPPLEKLCSI 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720383787  213 CKAMETWLSADPQHVVVLYCKGSKGKLGVIVSAYMHYSKISAGADQALATLTMRKFCEDKVATELQPSQRRYVSYFSGL 291
Cdd:cd14508     81 CKNMDSWLNADPQNVVVLHCKGGKGRLGVVVSAYMHYSKISATADQALDRFAMKRFYDDKVGPLGQPSQKRYVGYFSGL 159
PTP_tensin-1 cd14560
protein tyrosine phosphatase-like domain of tensin-1; Tensin-1 (TNS1) is part of the tensin ...
 133-291 2.14e-80

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: 261.07  E-value: 2.14e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  133 DLTYVTERILAAAFPARPDEQRHRGHLRELAHVLQSKHRDKYLLFNLSEKRHDLTRLNPKVQDFGWPELHAPPLDKLCSI 212
Cdd:cd14560      1 DLVYITERIISVSFPSTAEEPSFRSNLKEVAQMLKSKHGDNYLLFNLSERRHDISKLHPKVLDFGWPDLHAPALEKICSI 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720383787  213 CKAMETWLSADPQHVVVLYCKGSKGKLGVIVSAYMHYSKISAGADQALATLTMRKFCEDKVATELQPSQRRYVSYFSGL 291
Cdd:cd14560     81 CKAMDTWLNADPHNVVVIHNKGNRGRTGVVIAAYMHYSNISASADQALDRFAMKRFYEDKVVPVGQPSQKRYVHYFSGL 159
PTB_tensin cd01213
Tensin Phosphotyrosine-binding (PTB) domain; Tensin is a a focal adhesion protein, which ...
 1272-1404 6.80e-80

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


Pssm-ID: 269924  Cd Length: 136  Bit Score: 258.71  E-value: 6.80e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1272 GAACSVLYLTSVETESLTGPQAVAKASSAALSCSPVPVPAIVHFKVSAQGITLTDNQRKLFFRRHYPVNSITFSSTDPQD 1351
Cdd:cd01213      1 GAACNVLYLGSVDTESLTGPQAVRKAVSETLERDPLPTPTVVHFKVSEQGITLTDNQRKLFFRRHYPLNTVSFCGMDPEN 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720383787 1352 RRWTNPD---GATSKIFGFVAKKPGSPWENVCHLFAELDPDQPASAIVTFITKVLL 1404
Cdd:cd01213     81 RKWQKYDlrgSKPSRIFGFVARKQGSSTENVCHLFAELDPEQPASAIVNFVNKVLL 136
PTP_tensin-3 cd14561
protein tyrosine phosphatase-like domain of tensin-3; Tensin-3 (TNS3) is also called ...
 133-291 6.81e-76

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: 248.32  E-value: 6.81e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  133 DLTYVTERILAAAFPARPDEQRHRGHLRELAHVLQSKHRDKYLLFNLSEKRHDLTRLNPKVQDFGWPELHAPPLDKLCSI 212
Cdd:cd14561      1 DLTYITERIIAVSFPADCSEETYLHNLQDVTRMLKSKHGDNYLVLNLSEKRYELTKLNPKIMDVGWPDLHAPPLDKMCTI 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720383787  213 CKAMETWLSADPQHVVVLYCKGSKGKLGVIVSAYMHYSKISAGADQALATLTMRKFCEDKVATELQPSQRRYVSYFSGL 291
Cdd:cd14561     81 CKAMESWLNSDPLHVVVIHCRGGKGRIGVVISSYMHFTNVSASADQALDRFAMKKFYDDKVSALMQPSQKRYVQFLSGL 159
SH2_Tensin_like cd09927
Src homology 2 domain found in Tensin-like proteins; SH2 domain found in Tensin-like proteins. ...
 1135-1248 4.50e-68

Src homology 2 domain found in Tensin-like proteins; SH2 domain found in Tensin-like proteins. The Tensins are a family of intracellular proteins that interact with receptor tyrosine kinases (RTKs), integrins, and actin. They are thought act as signaling bridges between the extracellular space and the cytoskeleton. There are four homologues: Tensin1, Tensin2 (TENC1, C1-TEN), Tensin3 and Tensin4 (cten), all of which contain a C-terminal tandem SH2-PTB domain pairing, as well as actin-binding regions that may localize them to focal adhesions. The isoforms of Tensin2 and Tensin3 contain N-terminal C1 domains, which are atypical and not expected to bind to phorbol esters. Tensins 1-3 contain a phosphatase (PTPase) and C2 domain pairing which resembles PTEN (phosphatase and tensin homologue deleted on chromosome 10) protein. PTEN is a lipid phosphatase that dephosphorylates phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) to yield phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). As PtdIns(3,4,5)P3 is the product of phosphatidylinositol 3-kinase (PI3K) activity, PTEN is therefore a key negative regulator of the PI3K pathway. Because of their PTEN-like domains, the Tensins may also possess phosphoinositide-binding or phosphatase capabilities. However, only Tensin2 and Tensin3 have the potential to be phosphatases since only their PTPase domains contain a cysteine residue that is essential for catalytic activity. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198181 [Multi-domain]  Cd Length: 116  Bit Score: 224.23  E-value: 4.50e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1135 TSKFWYKPHLSRDQAIALLKDKDPGAFLIRDSHSFQGAYGLALKVATPPPSAQPW--KGDPSEQLVRHFLIETGPKGVKI 1212
Cdd:cd09927      1 TSKYWYKPNISRDQAIALLKDKPPGTFLVRDSTTYKGAYGLAVKVATPPPGVNPFeaKGDPESELVRHFLIEPSPKGVKL 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1720383787 1213 KGCPTEPYFGSLSALVSQHSISPISLPCCLRIPSKD 1248
Cdd:cd09927     81 KGCPNEPVFGSLSALVYQHSITPLALPCKLRIPDRD 116
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 133-291 3.26e-53

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: 183.55  E-value: 3.26e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  133 DLTYVTERILAAAFPA-RPDEQRHRGHLRELAHVLQSKHRDKYLLFNLSEKRHDL-TRLNPKVQDFGWPELHAPPLDKLC 210
Cdd:cd14497      1 DLSYITPRIIAMSFPAtGYPESLYRNSIDDVANFLNTHHPDHYMIFNLSEEEYDDdSKFEGRVLHYGFPDHHPPPLGLLL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  211 SICKAMETWLSADPQHVVVLYCKGSKGKLGVIVSAYMHYSKISAGADQALATLTMRKFCEDKVATElQPSQRRYVSYFSG 290
Cdd:cd14497     81 EIVDDIDSWLSEDPNNVAVVHCKAGKGRTGTVICAYLLYYGQYSTADEALEYFAKKRFKEGLPGVT-IPSQLRYLQYFER 159


                   .
gi 1720383787  291 L 291
Cdd:cd14497    160 L 160
PTB pfam08416
Phosphotyrosine-binding domain; The phosphotyrosine-binding domain (PTB, also ...
 1274-1408 3.08e-45

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: 159.43  E-value: 3.08e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1274 ACSVLYLTSVETESLTGPQAVAKAS--SAALSCSPVPVPAIVHFKVSAQGITLTDNQRKLFFrRHYPVNSITFSSTDPQD 1351
Cdd:pfam08416    1 QYRVEHLTTFELDSLTGLQAVEDAIrkLQLLDAQGRVWTQEMLLQVSDQGITLTDNETKEEL-ESYPLDSISHCQAVLND 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720383787 1352 RRWTNpdgatskIFGFVAKKPGSPWENVcHLFA--ELDPDQPASAIVTFITKVLLGQRK 1408
Cdd:pfam08416   80 GRYNS-------ILALVCQEPGQSKPDV-HLFQcdELGAELIAEDIESALSDVRLGKPK 130
PTEN_C2 pfam10409
C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key ...
 298-425 1.64e-39

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: 143.19  E-value: 1.64e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  298 MNSSPLFLHYVFVPVLPAFEPNTGFQPFLKIYQSMQLV-YTSGVYRIAGPGPQQLCISLEP-ALLLKGDVMVTCYHKGGQ 375
Cdd:pfam10409    1 PPPKPLTLHSIILHGIPNFKSGGGCRPYIRIYQNKKKVfSTSGKYKKLKEYQQDDCVILFPkGIPVQGDVLVEFYHKGSD 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720383787  376 GTDRTLVFRVQFHTCTIHGSRLTFPKDQLDEAW---ADERFPFQASVEFVFSS 425
Cdd:pfam10409   81 LLSEEKMFRFWFNTSFIEDNTLTLPKNELDKADkdkKDKRFPKDFKVELLFSE 133
PTP_auxilin-like cd14511
protein tyrosine phosphatase-like domain of auxilin and similar proteins; This subfamily ...
 129-291 5.14e-37

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: 137.10  E-value: 5.14e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  129 RWDLDLTYVTERILAAAFPA-RPDEQRHRGHLRELAHVLQSKHRDKYLLFNLSEKRHDLTRLNPKVQDFGWPELHAPPLD 207
Cdd:cd14511      6 RNDLDISYITSRIIVMPFPAeGIESTYRKNNIEDVRAFLDSRHPQKYSVYNLSPRSYPTLRLPSRVVECSWPYRRAPSLH 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  208 KLCSICKAMETWLSADPQHVVVLYCKGSKGKLGVIVSAYMHYSKISAGADQALATLTMRKfCEDkvatELQPSQRRYVSY 287
Cdd:cd14511     86 ALYALCRDIYQWLNKDPKNVIVIHCTDGKAASATVVCALLVYCGLFKTPEDALQMFAVKR-CPP----GLSPSELRYLYY 160


                   ....
gi 1720383787  288 FSGL 291
Cdd:cd14511    161 FSDI 164
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 133-291 5.76e-36

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: 133.87  E-value: 5.76e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  133 DLTYVTERILAAAFPARPDEQRHRGHLRELAHVLQSKHRDKYLLFNL-SEKRHDLTRLNPKVQDFGWPELHAPPLDKLCS 211
Cdd:cd14509      1 DLTYITPNIIAMGFPAEGVEGVYRNPIDDVQRFLETKHKGHYKVYNLcSERSYDPSKFNGRVAEYPFDDHNPPPLELIKP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  212 ICKAMETWLSADPQHVVVLYCKGSKGKLGVIVSAYMHYSKISAGADQALATLTMRKfCEDKVATELqPSQRRYVSYFSGL 291
Cdd:cd14509     81 FCEDVDEWLKEDEKNVAAVHCKAGKGRTGVMICCYLLYLGKFPSAKEALDFYGAKR-TKNKKGVTI-PSQRRYVYYYSRL 158
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 131-291 5.83e-36

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: 134.80  E-value: 5.83e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  131 DLDLTYVTERILAAAFPARPDEQRHRGHLRELAHVLQSKHRDKYLLFNL-SEKRHDLTRLNPKVQDFGWPELHAPPLDKL 209
Cdd:cd14510     13 DLDLTYVTDRVIAMSFPSSGKQAFYRNPIEEVVRFLDTKHPDHYKVYNLcSERGYDPKYFHNRVERVPIDDHNVPTLDEM 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  210 CSICKAMETWLSADPQHVVVLYCKGSKGKLGVIVSAYMHYSKISAGADQALATLTMRKfcEDK-VATELQ----PSQRRY 284
Cdd:cd14510     93 LSFTAEVREWMAADPKNVVAIHCKGGKGRTGTMVCAWLIYSGQFESAKEALEYFGERR--TDKsVSSKFQgvetPSQSRY 170


                   ....*..
gi 1720383787  285 VSYFSGL 291
Cdd:cd14510    171 VGYFEKL 177
PTP_GAK cd14564
protein tyrosine phosphatase-like domain of cyclin-G-associated kinase; cyclin-G-associated ...
 129-287 1.11e-25

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: 104.60  E-value: 1.11e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  129 RWDLDLTYVTERILAAAFPARPDEQRHRGHLRELAHVLQSKHRDKYLLFNLSEKRHDLTRLNPKVQDFGWPELHAPPLDK 208
Cdd:cd14564      6 KGDLDISYITSRIAVMSFPAEGVESAIKNNIEDVRLFLDSRHPGHYAVYNLSQRTYRPSRFHNRVSECGWPARRAPNLQN 85

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720383787  209 LCSICKAMETWLSADPQHVVVLYCKGSKGKLGVIVSAYMHYSKISAGADQALATLTMRkfcedKVATELQPSQRRYVSY 287
Cdd:cd14564     86 LYSICKNMHLWLKQDQKNICIVHCLDGRAASAVVVCSFLCFCRLFTTAEAAVYMFSMK-----RCPPGIWPSHKRYIEY 159
PTP_auxilin_N cd14563
N-terminal protein tyrosine phosphatase-like domain of auxilin; Auxilin, also called auxilin-1 ...
 131-291 1.57e-24

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: 101.50  E-value: 1.57e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  131 DLDLTYVTERILAAAFPARPDEQRHRGHLRELAHVLQSKHRDKYLLFNLSEKRHDLTRLNPKVQDFGWPELHAPPLDKLC 210
Cdd:cd14563      8 ELDISYITSRIIVMSYPAEGVELGFRNHIEDVRSFLDSRHLDHYTVFNLSQKSYRSAKFHNRVSECSWPVRQAPSLHNLF 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  211 SICKAMETWLSADPQHVVVLYCKGSKGKLGVIVSAYMHYSKISAGADQALATLTMRkfcedKVATELQPSQRRYVSYFSG 290
Cdd:cd14563     88 AVCKNMHNWLQQNPKNVCVIHCMDGRAASAVLVSAMFCFCHLFSNPVPAMQLLNAK-----RPGIGLWPSHRRYIGYICD 162


                   .
gi 1720383787  291 L 291
Cdd:cd14563    163 L 163
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 1271-1408 1.80e-24

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: 100.08  E-value: 1.80e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  1271 QGAACSVLYLTSVETESLTGPQAVAKASS--AALSCSPVPVPAIVHFKVSAQGITLTDNQRKlFFRRHYPVNSITFSSTD 1348
Cdd:smart00462    2 SGVSFRVKYLGSVEVPEARGLQVVQEAIRklRAAQGSEKKEPQKVILSISSRGVKLIDEDTK-AVLHEHPLRRISFCAVG 80

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720383787  1349 PQDrrwtnpdgatSKIFGFVAKKPGSPWeNVCHLFAELDP--DQPASAIVTFITKVLLGQRK 1408
Cdd:smart00462   81 PDD----------LDVFGYIARDPGSSR-FACHVFRCEKAaeDIALAIGQAFQLAYELKLKA 131
C1_TNS2 cd20887
protein kinase C conserved region 1 (C1 domain) found in tensin-2 and similar proteins; ...
 31-84 2.30e-24

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: 97.16  E-value: 2.30e-24
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720383787   31 EPHSFREKVFRKKtPVCAVCKVTIDGTGVSCRVCKVATHRKCEAKVTSSCQALP 84
Cdd:cd20887      1 EPHSFKEKTFKKK-RACAVCREPVGGQGLVCRVCKVASHKKCEAKVTSACQPPP 53
C1_TNS2-like cd20826
protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; ...
 32-81 1.01e-19

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: 83.59  E-value: 1.01e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720383787   32 PHSFREKVFRKKtPVCAVCKVTIDGTGVSCRVCKVATHRKCEAKVTSSCQ 81
Cdd:cd20826      2 SHSFKEKSFRKP-RTCDVCKQIIWNEGSSCRVCKYACHRKCEPKVTAACS 50
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 1275-1401 6.23e-16

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: 75.24  E-value: 6.23e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1275 CSVLYLTSVETESLTGPQAV--AKASSAALSCSPVPVPAIVHFKVSAQGITLTDNQRKLFFRRHyPVNSITFSSTDPQDr 1352
Cdd:cd00934      3 FQVKYLGSVEVGSSRGVDVVeeALKALAAALKSSKRKPGPVLLEVSSKGVKLLDLDTKELLLRH-PLHRISYCGRDPDN- 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1720383787 1353 rwtnpdgatSKIFGFVAKKPGSpWENVCHLFAELDPDQpASAIVTFITK 1401
Cdd:cd00934     81 ---------PNVFAFIAGEEGG-SGFRCHVFQCEDEEE-AEEILQAIGQ 118
SH2 cd00173
Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they ...
 1139-1231 1.21e-15

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


Pssm-ID: 198173 [Multi-domain]  Cd Length: 79  Bit Score: 73.26  E-value: 1.21e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1139 WYKPHLSRDQAIALLKDKDPGAFLIRDSHSFQGAYGLALKVAtpppsaqpwkgdpsEQLVRHFLIETGPKGVKIKGCPtE 1218
Cdd:cd00173      2 WFHGSISREEAERLLRGKPDGTFLVRESSSEPGDYVLSVRSG--------------DGKVKHYLIERNEGGYYLLGGS-G 66

                           90
                   ....*....|...
gi 1720383787 1219 PYFGSLSALVSQH 1231
Cdd:cd00173     67 RTFPSLPELVEHY 79
C1_TNS3_v cd20889
protein kinase C conserved region 1 (C1 domain) found in tensin-3 (TNS3) variant and similar ...
 33-85 2.83e-14

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: 68.38  E-value: 2.83e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720383787   33 HSFREKVFrKKTPVCAVCKVTIDGTGVSCRVCKVATHRKCEAKVTSSCqaLPP 85
Cdd:cd20889      3 HTFKNKTF-KKPKVCSICKQVIDSQGISCRVCKYACHKKCEAKVVTPC--FPP 52
SH2 smart00252
Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides ...
 1139-1237 3.39e-13

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


Pssm-ID: 214585 [Multi-domain]  Cd Length: 84  Bit Score: 66.10  E-value: 3.39e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  1139 WYKPHLSRDQAIALLKDKDPGAFLIRDSHSFQGAYGLALKVatpppsaqpwkgdpsEQLVRHFLIE-TGPKGVKIKGcpt 1217
Cdd:smart00252    3 WYHGFISREEAEKLLKNEGDGDFLVRDSESSPGDYVLSVRV---------------KGKVKHYRIRrNEDGKFYLEG--- 64

                            90       100
                    ....*....|....*....|
gi 1720383787  1218 EPYFGSLSALVSQHSISPIS 1237
Cdd:smart00252   65 GRKFPSLVELVEHYQKNSLG 84
C1_TNS1_v cd20888
protein kinase C conserved region 1 (C1 domain) found in tensin-1 (TNS1) variant and similar ...
 33-81 3.94e-13

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: 65.28  E-value: 3.94e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1720383787   33 HSFREKVFRKKTPvCAVCKVTIDGTGVSCRVCKVATHRKCEAKVTSSCQ 81
Cdd:cd20888      6 HTFKVKTFKKVKS-CGICKQAITREGSTCRVCKLSCHKKCEAKVATPCV 53
SH2 pfam00017
SH2 domain;
1139-1231 1.93e-11

SH2 domain;


Pssm-ID: 425423 [Multi-domain]  Cd Length: 77  Bit Score: 61.08  E-value: 1.93e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1139 WYKPHLSRDQAIALLKDKDP-GAFLIRDSHSFQGAYGLALKvatpppsaqpWKGDpseqlVRHFLI-ETGPKGVKIKGcp 1216
Cdd:pfam00017    1 WYHGKISRQEAERLLLNGKPdGTFLVRESESTPGGYTLSVR----------DDGK-----VKHYKIqSTDNGGYYISG-- 63

                           90
                   ....*....|....*
gi 1720383787 1217 tEPYFGSLSALVSQH 1231
Cdd:pfam00017   64 -GVKFSSLAELVEHY 77
PHA03247 PHA03247
large tegument protein UL36; Provisional
 726-1124 5.34e-10

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 64.57  E-value: 5.34e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  726 LLHPVRPGHPLPLLVPACGHHHAP--MPDYGCLKPPKVGEEGHEGC-SYAVCSEGRYGHSGYPALVTYGYG--------- 793
Cdd:PHA03247  2469 LLGELFPGAPVYRRPAEARFPFAAgaAPDPGGGGPPDPDAPPAPSRlAPAILPDEPVGEPVHPRMLTWIRGleelasdda 2548

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  794 GAVPSYCPAYGRAPHSCGSPSEGRGYPSPGAHSPRAGSVSPGSPPY-LQPRKLGyeisaeDGRDKYPLSGHLASTGPLAS 872
Cdd:PHA03247  2549 GDPPPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQsARPRAPV------DDRGDPRGPAPPSPLPPDTH 2622

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  873 TELFPPVSESPEPSWRDGSSGHSTLP-----RSPRDPQCSASSELSGPSTPLHTSSPVQG-------------KESNRRQ 934
Cdd:PHA03247  2623 APDPPPPSPSPAANEPDPHPPPTVPPperprDDPAPGRVSRPRRARRLGRAAQASSPPQRprrraarptvgslTSLADPP 2702

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  935 DTTRSPSLAPTQrLSPGEALPSVVQGVAEKTPELLTSSRPeqldPSPFSQTSAPGSPNGWPQERSPGGHTNSASPRSPVP 1014
Cdd:PHA03247  2703 PPPPTPEPAPHA-LVSATPLPPGPAAARQASPALPAAPAP----PAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAA 2777

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1015 TTLPGLRH--------------APWQG--------PRGTSDSPDGSPLTPVPTQMPWLVGSPEPPQSSPTPAFPLATSYD 1072
Cdd:PHA03247  2778 GPPRRLTRpavaslsesreslpSPWDPadppaavlAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVA 2857

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720383787 1073 ANGPIQPPLPEKRHLPGSGQQPSPPARS------TNQHVTFASPLPDVTQPPEHPLQE 1124
Cdd:PHA03247  2858 PGGDVRRRPPSRSPAAKPAAPARPPVRRlarpavSRSTESFALPPDQPERPPQPQAPP 2915
PHA03247 PHA03247
large tegument protein UL36; Provisional
 801-1124 8.34e-10

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 63.80  E-value: 8.34e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  801 PAYGRAPHScGSPSEGRGYPSPGAHSPRAGSVSPGSPPYLQPRKLGYEISAEDGRDKYPLSGHLASTGPLASTELFPPVS 880
Cdd:PHA03247  2627 PPPSPSPAA-NEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPP 2705

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  881 ESPEPSWRDGSSG--HSTLPRSPRDPQCSASSELSGPSTPLHTSSPVQGKESNRRQDTT--------RSPSLAPTQRLSP 950
Cdd:PHA03247  2706 PTPEPAPHALVSAtpLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAgppapappAAPAAGPPRRLTR 2785

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  951 G---------EALPS------VVQGVAEKTPELLTSSRPEQLDPSPFS-QTSAPGSPNGWPQER-------SPGGH-TNS 1006
Cdd:PHA03247  2786 PavaslsesrESLPSpwdpadPPAAVLAPAAALPPAASPAGPLPPPTSaQPTAPPPPPGPPPPSlplggsvAPGGDvRRR 2865

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1007 ASPRSPVPT----TLPGLRHAPWQGPRGTSDSPDGSPLTPVPTQMPWLVGSPEPPQSSPTPAFPLATSYDANGPIQPPLP 1082
Cdd:PHA03247  2866 PPSRSPAAKpaapARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAP 2945

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1720383787 1083 EKRHLPGSGQQPSPPARSTNQHVTFASPLPDVTQPPEHPLQE 1124
Cdd:PHA03247  2946 TTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSRE 2987
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
 33-80 6.18e-09

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: 53.29  E-value: 6.18e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720383787   33 HSFREKVFRKKTpVCAVCKVTIDG---TGVSCRVCKVATHRKCEAKVTSSC 80
Cdd:cd00029      1 HRFVPTTFSSPT-FCDVCGKLIWGlfkQGLKCSDCGLVCHKKCLDKAPSPC 50
C1_Stac cd20817
protein kinase C conserved region 1 (C1 domain) found in the SH3 and cysteine-rich ...
 33-81 1.96e-08

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: 51.56  E-value: 1.96e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720383787   33 HSFREKVFRKKTPvCAVCKVTIDGT---GVSCRVCKVATHRKCEAKVtSSCQ 81
Cdd:cd20817      1 HSFQEHTFKKPTF-CDVCKELLVGLskqGLRCKNCKMNVHHKCQEGV-PDCS 50
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 33-80 9.36e-08

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


Pssm-ID: 197519  Cd Length: 50  Bit Score: 49.77  E-value: 9.36e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1720383787    33 HSFREKVFrKKTPVCAVCKVTIDG---TGVSCRVCKVATHRKCEAKVTSSC 80
Cdd:smart00109    1 HKHVFRTF-TKPTFCCVCRKSIWGsfkQGLRCSECKVKCHKKCADKVPKAC 50
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 801-1104 3.20e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 55.18  E-value: 3.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  801 PAYGRAPHSCGSPSEGRGYPSPGAHSPRAGSVSPGSPPYLQPRKLGYEISAEDGRDKYPLSGHLASTGPLASTELFPPVS 880
Cdd:PHA03307    97 PASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPL 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  881 ESPEPSWRDGSSGHSTLPRSPRDPQCSASSELSGPSTPLHTSSPVQGKESNRRQDTTRSPSLAPTQRLSPGEALPSVVQG 960
Cdd:PHA03307   177 SSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECP 256

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  961 VAEKTPELLTSSRPEQLDPSPFSQTSAPGSPNGWPQERSPgghtNSASPRSPVPTTLPGLRHAPWQGPRGTSDSPDGSPL 1040
Cdd:PHA03307   257 LPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSP----SPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSS 332

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720383787 1041 TPVPTQMPwlVGSPEPPQSSPTPAfplatsyDANGPIQPPLPEKRhlpgsgQQPSPPARSTNQH 1104
Cdd:PHA03307   333 SESSRGAA--VSPGPSPSRSPSPS-------RPPPPADPSSPRKR------PRPSRAPSSPAAS 381
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 930-1120 7.98e-07

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: 53.77  E-value: 7.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  930 SNRRQDTTRSPSLAPTqrlspGEALPSVVQGVAEKT--PELLTS--------SRPEQLDPSPFSQTSAPGSPNGWPQERS 999
Cdd:pfam05109  422 SKAPESTTTSPTLNTT-----GFAAPNTTTGLPSSThvPTNLTApastgptvSTADVTSPTPAGTTSGASPVTPSPSPRD 496

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1000 PGGHTNS---ASPRSPVPTTLPglrHAPWQGPRGTSDSPDGSPLTPVPTQMPWLVGSPEPPQSSPTPA---------FPL 1067
Cdd:pfam05109  497 NGTESKApdmTSPTSAVTTPTP---NATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAvttptpnatIPT 573

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720383787 1068 ATSYDANGPIQPPLPEKRHlPGSGQQpSPPARSTNQHVTFASPLPDVTQPPEH 1120
Cdd:pfam05109  574 LGKTSPTSAVTTPTPNATS-PTVGET-SPQANTTNHTLGGTSSTPVVTSPPKN 624
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 805-1086 9.13e-07

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 53.54  E-value: 9.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  805 RAPHSCGSPSEGRGYPS--PGAHSPRAGSVSP---GSPpylqprklGYEISAEDGRDKYPLSGHLASTGPLASTE-LFPP 878
Cdd:PTZ00449   512 EGPEASGLPPKAPGDKEgeEGEHEDSKESDEPkegGKP--------GETKEGEVGKKPGPAKEHKPSKIPTLSKKpEFPK 583

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  879 VS------ESPEPSWRDGSSGHSTLPRSPRDPQCS----ASSELSGPSTPLHTSSPvQGKESNRRQDTTRSPSlAPTQRL 948
Cdd:PTZ00449   584 DPkhpkdpEEPKKPKRPRSAQRPTRPKSPKLPELLdipkSPKRPESPKSPKRPPPP-QRPSSPERPEGPKIIK-SPKPPK 661

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  949 SPG--------EALPSVVQGVAEKTPELLTSSRPEQLDPSPFSQTsapgspngwpQERSPGGHTNSASPRSPVPTTLPGL 1020
Cdd:PTZ00449   662 SPKppfdpkfkEKFYDDYLDAAAKSKETKTTVVLDESFESILKET----------LPETPGTPFTTPRPLPPKLPRDEEF 731

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1021 RHAPWQGPrgTSDSPDGSPL-------------TPVPTQMPWLV-------------GSPEPPQSSP-TPafplaTSYDA 1073
Cdd:PTZ00449   732 PFEPIGDP--DAEQPDDIEFftppeeertffheTPADTPLPDILaeefkeedihaetGEPDEAMKRPdSP-----SEHED 804

                          330
                   ....*....|....
gi 1720383787 1074 NGP-IQPPLPEKRH 1086
Cdd:PTZ00449   805 KPPgDHPSLPKKRH 818
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 812-1133 1.40e-06

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: 53.23  E-value: 1.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  812 SPSEGRGYPSPGAHSPRAGSVSP---------GSPPYLQPRklgyeiSAEDGRDKYPLSGHLASTGPLASTELFPPVSES 882
Cdd:pfam03154  112 SPSEGEGESSDGRSVNDEGSSDPkdidqdnrsTSPSIPSPQ------DNESDSDSSAQQQILQTQPPVLQAQSGAASPPS 185

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  883 PEPSWRDGSSGHSTLPRSPRDPQCSASSELSGPSTPLHTSSPVQGKESNRRQDTTRSPSLAPTQRLSPGEALPSVVQGVA 962
Cdd:pfam03154  186 PPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQP 265

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  963 EKTPELLTSSRP--EQLDPSPfSQTSAPGSPNGWPQERSPGGHTNSASPRSPVPTTLPGLRHAPWQGPRGTSDSPD-GSP 1039
Cdd:pfam03154  266 LPQPSLHGQMPPmpHSLQTGP-SHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPrEQP 344

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1040 LTPVPTQMPWLvgspEPPQSSPTPAFPLATSY--------------DANGPIQPPL----------------PEKRHLPG 1089
Cdd:pfam03154  345 LPPAPLSMPHI----KPPPTTPIPQLPNPQSHkhpphlsgpspfqmNSNLPPPPALkplsslsthhppsahpPPLQLMPQ 420

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1720383787 1090 SGQQPSPPARSTNQHVTFASPLPDVTQPPEHPLQENQSNVKFVQ 1133
Cdd:pfam03154  421 SQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQ 464
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 872-1131 1.56e-06

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 52.77  E-value: 1.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  872 STELFPPVSEspepswrDGSSGHSTLPRSPrdpqcsassELSG--PSTPLHTSSpvqgkESNRRQDTTRSPSlaPTQRLS 949
Cdd:PTZ00449   492 SKKKLAPIEE-------EDSDKHDEPPEGP---------EASGlpPKAPGDKEG-----EEGEHEDSKESDE--PKEGGK 548

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  950 PGEALPSVVQ---GVAE-----KTPELltSSRPEqlDPSPFSQTSAPGSPNGWPQERSPGGHTNSASPRSPVPTTLPGLR 1021
Cdd:PTZ00449   549 PGETKEGEVGkkpGPAKehkpsKIPTL--SKKPE--FPKDPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSP 624

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1022 HAPWQGPRGTSDSPDGSPLTPVPTQMPWLVGSPEPPQSSPTPAFP-----LATSY------------------DANGPIQ 1078
Cdd:PTZ00449   625 KRPESPKSPKRPPPPQRPSSPERPEGPKIIKSPKPPKSPKPPFDPkfkekFYDDYldaaaksketkttvvldeSFESILK 704

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720383787 1079 PPLPEKRHLPGSGQQPSPPARSTNQHVTFasplpdvtQPPEHPLQENQSNVKF 1131
Cdd:PTZ00449   705 ETLPETPGTPFTTPRPLPPKLPRDEEFPF--------EPIGDPDAEQPDDIEF 749
SH2_Tec_family cd09934
Src homology 2 (SH2) domain found in Tec-like proteins; The Tec protein tyrosine kinase is the ...
 1139-1245 2.38e-06

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: 47.39  E-value: 2.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1139 WYKPHLSRDQAIALLKDKDP-GAFLIRDShSFQGAYGLALKVATPppsaqpwkGDPSeqlVRHFLIETGPKGVKI---KG 1214
Cdd:cd09934      8 WYVGDMSRQRAESLLKQEDKeGCFVVRNS-STKGLYTVSLFTKVP--------GSPH---VKHYHIKQNARSEFYlaeKH 75

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1720383787 1215 CptepyFGSLSALVSQHSISPISLPCCLRIP 1245
Cdd:cd09934     76 C-----FETIPELINYHQHNSGGLATRLKYP 101
C1_CeDKF1-like_rpt2 cd20798
second protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine ...
 32-83 4.01e-06

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


Pssm-ID: 410348  Cd Length: 54  Bit Score: 45.18  E-value: 4.01e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720383787   32 PHSFREKVFRKKTpVCAVCKVTIDG---TGVSCRVCKVATHRKCEAKVTSSCQAL 83
Cdd:cd20798      1 PHTLAEHNYKKPT-VCKVCDKLLVGlvrQGLKCRDCGVNVHKKCASLLPSNCRLS 54
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 822-1123 6.31e-06

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: 50.92  E-value: 6.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  822 PGAHSPRAGSVSPGSPPYLQPRKLGYEISAEDGrdkyPLSGHLASTGPLASTELFPPvsespEPSWRDGSSGHSTLPRSP 901
Cdd:pfam03154  243 PSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQM----PPMPHSLQTGPSHMQHPVPP-----QPFPLTPQSSQSQVPPGP 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  902 RDPQCSASSELsgPSTPLHTSSPVQGKESnRRQDTTRSPSLAPTQRLSPGEALPSVVQGVAEKTPelltssrPEQLDPSP 981
Cdd:pfam03154  314 SPAAPGQSQQR--IHTPPSQSQLQSQQPP-REQPLPPAPLSMPHIKPPPTTPIPQLPNPQSHKHP-------PHLSGPSP 383

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  982 FSQTSAPGSPNgwpqerspgghtnSASPRSPVPTtlpglRHAPWQGPRGTSDSPDGSPLTPVPTQMPWLVGSPE-PPQSS 1060
Cdd:pfam03154  384 FQMNSNLPPPP-------------ALKPLSSLST-----HHPPSAHPPPLQLMPQSQQLPPPPAQPPVLTQSQSlPPPAA 445

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720383787 1061 PTPafplATSYDANGPIQPPLPEKRHLPG--------SGQQPS-PPARSTNQHVTFAS-----PLPDVTQPPEHPLQ 1123
Cdd:pfam03154  446 SHP----PTSGLHQVPSQSPFPQHPFVPGgpppitppSGPPTStSSAMPGIQPPSSASvsssgPVPAAVSCPLPPVQ 518
C1_SpBZZ1-like cd20824
protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein ...
 32-80 7.32e-06

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: 44.61  E-value: 7.32e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720383787   32 PHSFREKVFRKKTPvCAVCKVTIDG---TGVSCRVCKVATHRKCEAKVTSSC 80
Cdd:cd20824      1 PHNFKPHSFSIPTK-CDYCGEKIWGlskKGLSCKDCGFNCHIKCELKVPPEC 51
C1_dGM13116p-like cd20831
protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and ...
 33-80 1.25e-05

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: 43.87  E-value: 1.25e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720383787   33 HSFREKVFrKKTPVCAVCKVTIDGT----GVSCRVCKVATHRKCEAKVTSSC 80
Cdd:cd20831      6 HTFVATHF-KGGPSCAVCNKLIPGRfgkqGYQCRDCGLICHKRCHVKVETHC 56
C1_Stac1 cd20880
protein kinase C conserved region 1 (C1 domain) found in SH3 and cysteine-rich ...
 33-72 1.26e-05

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


Pssm-ID: 410430  Cd Length: 57  Bit Score: 44.16  E-value: 1.26e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1720383787   33 HSFREKVFRKKTpVCAVCKVTIDGT----GVSCRVCKVATHRKC 72
Cdd:cd20880      3 HSFQEYIFKKPT-FCDVCNHMIVGTnakhGLRCKACKMSIHHKC 45
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
938-1119 1.56e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 49.49  E-value: 1.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  938 RSPSLAPTQRLSPGEALPSVVqgVAEKTPELLTSSRPEQLDPSPFSQTSAPGSPNGWP-------QERSPGGHTNSASPR 1010
Cdd:PRK12323   375 ATAAAAPVAQPAPAAAAPAAA--APAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPealaaarQASARGPGGAPAPAP 452

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1011 SPVPTTLPGLRHAPwQGPRGTSDSPDGSPLTPVPTQMPWLVGSPEPPQSSPTPAFPLATSYDANGPiqPPLPEKRHLPGS 1090
Cdd:PRK12323   453 APAAAPAAAARPAA-AGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAA--PAGWVAESIPDP 529

                          170       180
                   ....*....|....*....|....*....
gi 1720383787 1091 GQQPSPPARSTNQHVTFASPLPDVTQPPE 1119
Cdd:PRK12323   530 ATADPDDAFETLAPAPAAAPAPRAAAATE 558
SH2_Grb7_family cd09944
Src homology 2 (SH2) domain found in the growth factor receptor bound, subclass 7 (Grb7) ...
 1136-1243 2.01e-05

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: 45.10  E-value: 2.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1136 SKFWYKPHLSRDQAIALLKD---KDpGAFLIRDSHSFQGAYGLALKvatpppsaqpwkgdpSEQLVRHFLIETGPKGVKI 1212
Cdd:cd09944      4 SQPWFHGGISRDEAARLIRQqglVD-GVFLVRESQSNPGAFVLSLK---------------HGQKIKHYQIIPIEDEGQW 67

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1720383787 1213 -----KGcptEPYFGSLSALVSQHSISPISLPCCLR 1243
Cdd:cd09944     68 yftldDG---VTKFYDLLQLVEFYQLNAGSLPTRLK 100
PHA03378 PHA03378
EBNA-3B; Provisional
 907-1118 2.44e-05

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 48.91  E-value: 2.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  907 SASSELSGPSTPLHTSSPVQGKESNRRQDTTRSPSLAPTQrLSPGEALPSVVQGVAEKTPELLTSSRPEQLDPSPFSQTS 986
Cdd:PHA03378   588 SAPSYAQTPWPVPHPSQTPEPPTTQSHIPETSAPRQWPMP-LRPIPMRPLRMQPITFNVLVFPTPHQPPQVEITPYKPTW 666

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  987 ApgSPNGWPQERSPGGHTNS-----------ASPRSPVPTTLPGLRHAPWQGPRGTSDSPDGSPLTP--------VPTQM 1047
Cdd:PHA03378   667 T--QIGHIPYQPSPTGANTMlpiqwapgtmqPPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPgrarppaaAPGRA 744

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720383787 1048 PWLVGSP---EPPQSSPTPAFPLATSYDANGPIQPP----LPEKRhlPGSGQQPSPPARSTNQHVTFASPLPDVTQPP 1118
Cdd:PHA03378   745 RPPAAAPgraRPPAAAPGRARPPAAAPGAPTPQPPPqappAPQQR--PRGAPTPQPPPQAGPTSMQLMPRAAPGQQGP 820
PHA03247 PHA03247
large tegument protein UL36; Provisional
 911-1121 3.50e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 3.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  911 ELSGPSTPlhtssPVQGKESNRRQDTTR-SPSLAPTQRLSPGE---ALPSVVQGVAEKTPELLTSSRPEQLDPSPFSQTS 986
Cdd:PHA03247   251 DIAAPAPP-----PVVGEGADRAPETARgATGPPPPPEAAAPNgaaAPPDGVWGAALAGAPLALPAPPDPPPPAPAGDAE 325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  987 APG---------SPNGWPQERSPGGHTNSASPRSPVPTTLPGL---RHAPWQGP-----------------RGTSDSPDG 1037
Cdd:PHA03247   326 EEDdedgamevvSPLPRPRQHYPLGFPKRRRPTWTPPSSLEDLsagRHHPKRASlptrkrrsarhaatpfaRGPGGDDQT 405

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1038 SPLTPVPTQMPWLVGSPEPPQSSPTPAFPLATSydangpiQPPLPEKRHLPGSGQQPSPPARSTNQHVTFASPLP----D 1113
Cdd:PHA03247   406 RPAAPVPASVPTPAPTPVPASAPPPPATPLPSA-------EPGSDDGPAPPPERQPPAPATEPAPDDPDDATRKAldalR 478


                   ....*...
gi 1720383787 1114 VTQPPEHP 1121
Cdd:PHA03247   479 ERRPPEPP 486
C1_KSR cd20812
protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) ...
 33-80 3.65e-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: 3.65e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1720383787   33 HSFREKVFRKKTpvCAVCKVTIDGtGVSCRVCKVATHRKCEAKVTSSC 80
Cdd:cd20812      3 HRFSKKLFMRQT--CDYCHKQMFF-GLKCKDCKYKCHKKCAKKAPPSC 47
C1_nPKC_theta-like_rpt1 cd20834
first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
 33-80 4.31e-05

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


Pssm-ID: 410384  Cd Length: 61  Bit Score: 42.70  E-value: 4.31e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720383787   33 HSFREKVFRKKTpVCAVCKVTIDG---TGVSCRVCKVATHRKCEAKVTSSC 80
Cdd:cd20834      8 HEFIAKFFRQPT-FCSVCKEFLWGfnkQGYQCRQCNAAVHKKCHDKILGKC 57
PHA03247 PHA03247
large tegument protein UL36; Provisional
 870-1121 4.32e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.40  E-value: 4.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  870 LASTELFP--PVSESPePSWRDGSSghstlPRSPRDPQCSASSELSGPSTPLHTSspvqgkesnrrqdttrsPSLAPTQr 947
Cdd:PHA03247  2468 LLLGELFPgaPVYRRP-AEARFPFA-----AGAAPDPGGGGPPDPDAPPAPSRLA-----------------PAILPDE- 2523

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  948 lSPGEALP----SVVQGVAE--------KTPELLTSSRPEQLDPS-PFSQTSA-PGSPNGWPQERSPGGHTNSASPRSPV 1013
Cdd:PHA03247  2524 -PVGEPVHprmlTWIRGLEElasddagdPPPPLPPAAPPAAPDRSvPPPRPAPrPSEPAVTSRARRPDAPPQSARPRAPV 2602

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1014 pttlpglrhapwqgprgtsDSPDGSPLTPVPTQMPWLVGSPEPPQSSPTPAfplATSYDANGPIQPPLPEKRHLPGSGQQ 1093
Cdd:PHA03247  2603 -------------------DDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPA---ANEPDPHPPPTVPPPERPRDDPAPGR 2660

                          250       260
                   ....*....|....*....|....*...
gi 1720383787 1094 PSPPARSTNQhvtfaSPLPDVTQPPEHP 1121
Cdd:PHA03247  2661 VSRPRRARRL-----GRAAQASSPPQRP 2683
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 1279-1401 4.37e-05

Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK kinases catalyzes the transfer of the terminal phosphate of ATP to a specific tyrosine residue on its target protein. TK kinases play significant roles in development and cell division. Tyrosine-protein kinases can be divided into two subfamilies: receptor tyrosine kinases, which have an intracellular tyrosine kinase domain, a transmembrane domain and an extracellular ligand-binding domain; and non-receptor (cytoplasmic) tyrosine kinases, which are soluble, cytoplasmic kinases. In HMTK the conserved His-Arg-Asp sequence within the catalytic loop is replaced by a His-Met sequence. TM/HMTK have are 2-3 N-terminal PTB domains. PTB domains in TKs are thought to function analogously to the membrane targeting (PH, myristoylation) and pTyr binding (SH2) domains of Src subgroup kinases. 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: 269983  Cd Length: 120  Bit Score: 44.16  E-value: 4.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1279 YLTSVETESLTGPQAVAKASSAALSCSPVPVPAIVHfkVSAQGITL--TDNQRKLFFrrhYPVNSITFSSTDPQDRrwtn 1356
Cdd:cd13161      8 YLGSVPVKEPKGNDVVMAAVKRLKDLKLKPKPVVLV--VSSEGIRVveRLTGEVLTN---VPIKDISFVTVDPKDK---- 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1720383787 1357 pdgatsKIFGFVAKKP--GSpweNVCHLFaELDPDqpASAIVTFITK 1401
Cdd:cd13161     79 ------KLFAFISHDPrlGR---ITCHVF-RCKRG--AQEICDTIAE 113
C1_DGK_typeII_rpt1 cd20800
first protein kinase C conserved region 1 (C1 domain) found in type II diacylglycerol kinases; ...
 42-80 4.97e-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: 42.31  E-value: 4.97e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1720383787   42 KKTPVCAVCKVTIDG---TGVSCRVCKVATHRKCEAKVTSSC 80
Cdd:cd20800     13 ARPTYCNVCREALSGvtsHGLSCEVCKFKAHKRCAVKAPNNC 54
SH2_C-SH2_SHP_like cd09931
C-terminal Src homology 2 (C-SH2) domain found in SH2 domain Phosphatases (SHP) proteins; The ...
 1139-1236 5.54e-05

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: 43.42  E-value: 5.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1139 WYKPHLSRDQAIALLKDK-DPGAFLIRDSHSFQGAYGLALKVAtpppsaqpwkgdpsEQLVRHFLIETgpKGVKIKGCPT 1217
Cdd:cd09931      2 WFHGHLSGKEAEKLLLEKgKPGSFLVRESQSKPGDFVLSVRTD--------------DDKVTHIMIRC--QGGKYDVGGG 65

                           90
                   ....*....|....*....
gi 1720383787 1218 EPyFGSLSALVSQHSISPI 1236
Cdd:cd09931     66 EE-FDSLTDLVEHYKKNPM 83
C1_Stac2 cd20881
protein kinase C conserved region 1 (C1 domain) found in SH3 and cysteine-rich ...
 33-77 5.58e-05

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


Pssm-ID: 410431  Cd Length: 59  Bit Score: 42.13  E-value: 5.58e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1720383787   33 HSFREKVFRKKTPvCAVCKVTIDGT---GVSCRVCKVATHRKCEAKVT 77
Cdd:cd20881      6 HSFQEHVFKKPSP-CELCHQMIVGNskqGLRCKMCKVSVHLWCSEEVS 52
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 791-1124 5.62e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 47.67  E-value: 5.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  791 GYGGAVPSYCPAYGRAPHSCGSPSEGRGYPSPGAHSPRAGSVSPGSPPylQPRKLGYEISAEDGRDKYPLSGHLASTGPL 870
Cdd:PRK07764   386 GVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAP--APAPAPAPPSPAGNAPAGGAPSPPPAAAPS 463

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  871 ASTELFPPVSESPEPSWRDGSSGHSTLPRSPRDPQCSASSELSGPSTPLHTSSP-VQGKESNRRQDTTR----------- 938
Cdd:PRK07764   464 AQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAATLRERWPeILAAVPKRSRKTWAillpeatvlgv 543

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  939 ----------SPSLAptQRLSPGEALPSVVQGVAEKT-----------------PELLTSSRPEQLDPSPFSQTSAPGSP 991
Cdd:PRK07764   544 rgdtlvlgfsTGGLA--RRFASPGNAEVLVTALAEELggdwqveavvgpapgaaGGEGPPAPASSGPPEEAARPAAPAAP 621

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  992 NGWPQERSPGGHTNSASPRSPVPTTLPGLRHAPwqGPRGTSDSPDGSPLTPVPTQMPWLVGSPEPPQSSPTPA-FPLATS 1070
Cdd:PRK07764   622 AAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHP--KHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAApAGAAPA 699

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720383787 1071 YDANGPIQPPLPEkrhlPGSGQQPSPPARSTNQHVTFASPLPDVTQPPEHPLQE 1124
Cdd:PRK07764   700 QPAPAPAATPPAG----QADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPP 749
C1_MgcRacGAP cd20821
protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and ...
 32-80 5.87e-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: 42.01  E-value: 5.87e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720383787   32 PHSFREKVFRKKTpVCAVCKVTI-DGTGVS-CRVCKVATHRKCEAKVTSSC 80
Cdd:cd20821      2 PHRFVSKTVIKPE-TCVVCGKRIkFGKKALkCKDCRVVCHPDCKDKLPLPC 51
SH2_Grb2_like cd09941
Src homology 2 domain found in Growth factor receptor-bound protein 2 (Grb2) and similar ...
 1139-1237 7.70e-05

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: 43.03  E-value: 7.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1139 WYKPHLSRDQAIALL-KDKDPGAFLIRDSHSFQGAYGLALKVatpppsaqpwkgdpsEQLVRHFLIETGPKG------VK 1211
Cdd:cd09941      5 WFHGKISRAEAEEILmNQRPDGAFLIRESESSPGDFSLSVKF---------------GNDVQHFKVLRDGAGkyflwvVK 69

                           90       100
                   ....*....|....*....|....*.
gi 1720383787 1212 ikgcptepyFGSLSALVSQHSISPIS 1237
Cdd:cd09941     70 ---------FNSLNELVDYHRTTSVS 86
C1_cPKC_nPKC_rpt1 cd20792
first protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ...
 32-82 8.37e-05

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: 41.46  E-value: 8.37e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720383787   32 PHSFREKVFRKKTpVCAVCKVTIDG---TGVSCRVCKVATHRKCEAKVTSSCQA 82
Cdd:cd20792      1 GHKFVATFFKQPT-FCSHCKDFIWGlgkQGYQCQVCRFVVHKRCHEYVVFKCPG 53
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
951-1118 8.85e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 47.18  E-value: 8.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  951 GEALP--SVVQGVAEKTPellTSSRPEQLDPSPFSQTSAPGSPNGWPQERSPGGhtNSASPRSPVPTTLPGLRHAPWQGP 1028
Cdd:PRK12323   370 GGAGPatAAAAPVAQPAP---AAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVA--AAPARRSPAPEALAAARQASARGP 444

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1029 RGTSDSPDGSPLTPVPTQMPwLVGSPEPPQSSPTPAFPLATSYDANGPIQPPLPEKRHLPGSGQQPSP--PARSTNQHVT 1106
Cdd:PRK12323   445 GGAPAPAPAPAAAPAAAARP-AAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPaqPDAAPAGWVA 523

                          170
                   ....*....|..
gi 1720383787 1107 FASPLPDVTQPP 1118
Cdd:PRK12323   524 ESIPDPATADPD 535
SH2_ABL cd09935
Src homology 2 (SH2) domain found in Abelson murine lymphosarcoma virus (ABL) proteins; ...
 1139-1245 9.19e-05

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: 42.76  E-value: 9.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1139 WYKPHLSRDQAIALLKDKDPGAFLIRDSHSFQGAYGLALKvatpppsaqpwkgdpSEQLVRHFLIETGPKG-VKIKgcpT 1217
Cdd:cd09935      5 WYHGPISRNAAEYLLSSGINGSFLVRESESSPGQYSISLR---------------YDGRVYHYRISEDSDGkVYVT---Q 66

                           90       100
                   ....*....|....*....|....*...
gi 1720383787 1218 EPYFGSLSALVSQHSISPISLPCCLRIP 1245
Cdd:cd09935     67 EHRFNTLAELVHHHSKNADGLITTLRYP 94
PHA03247 PHA03247
large tegument protein UL36; Provisional
 801-1075 9.28e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 9.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  801 PAYGRAPHSCGSPSEGRGYPSP-GAHSPRAGSVSPGSPPYLQPRKLGYEISAEdgrdkyplsghlASTGPLASTELFPPV 879
Cdd:PHA03247  2742 PAVPAGPATPGGPARPARPPTTaGPPAPAPPAAPAAGPPRRLTRPAVASLSES------------RESLPSPWDPADPPA 2809

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  880 SESPEPSWRDGSSGHSTLPRSPRDPQCSASSELSGPS-TPLHTSSPVQGKESNRRQDTTRSPSLAPTQRLSP------GE 952
Cdd:PHA03247  2810 AVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPpPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPpvrrlaRP 2889

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  953 ALPSVVQGVAE--------KTPELLTSSRPEQLDPSPFSQTSAPGSPngwPQERSPgghtnsasprsPVPTTLPglrhAP 1024
Cdd:PHA03247  2890 AVSRSTESFALppdqperpPQPQAPPPPQPQPQPPPPPQPQPPPPPP---PRPQPP-----------LAPTTDP----AG 2951

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720383787 1025 WQGPRGTSDSPDGSPLTPVPTQMP-WLVGSPEPPQSSPTPAFPLATSYDANG 1075
Cdd:PHA03247  2952 AGEPSGAVPQPWLGALVPGRVAVPrFRVPQPAPSREAPASSTPPLTGHSLSR 3003
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
 877-1022 1.03e-04

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 47.19  E-value: 1.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  877 PPVSESPE----PSWRDGSSGHSTLPRSPRDPQCSASSELSGPST--PLHTSSPVQGKESNRRQDTTRSPSLA--PTQRL 948
Cdd:COG5422     49 GADNDIINseskESFGKYALGHQIFSSFSSSPKLFQRRNSAGPIThsPSATSSTSSLNSNDGDQFSPASDSLSfnPSSTQ 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  949 SPGEALPSVVQGVAEKTPELLTSSRpEQLDPSPFSQTSAPGSPNGWPQERS--------------PGGHTNSASPRSPV- 1013
Cdd:COG5422    129 SRKDSGPGDGSPVQKRKNPLLPSSS-THGTHPPIVFTDNNGSHAGAPNARSrkeipslgsqsmqlPSPHFRQKFSSSDTs 207

                          170
                   ....*....|
gi 1720383787 1014 -PTTLPGLRH 1022
Cdd:COG5422    208 nGFSYPSIRK 217
SH2_SOCS_family cd09923
Src homology 2 (SH2) domain found in suppressor of cytokine signaling (SOCS) family; SH2 ...
 1139-1166 1.42e-04

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: 41.80  E-value: 1.42e-04
                           10        20
                   ....*....|....*....|....*...
gi 1720383787 1139 WYKPHLSRDQAIALLKDKDPGAFLIRDS 1166
Cdd:cd09923      2 WYWGGITRYEAEELLAGKPEGTFLVRDS 29
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 877-1080 2.24e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.75  E-value: 2.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  877 PPVSESPEPSWRDGSSGHSTLP-RSPRDPQCSASSELSGPSTPLHTSSPVQGKESNRRQDTTRSPSLAPTQRLSPGEALP 955
Cdd:PRK07764   603 PASSGPPEEAARPAAPAAPAAPaAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPP 682

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  956 SVVQGVAEKTPellTSSRPEQLDPSPFSQTSAPGSPNGWPQERSPGghtNSASPRSPVPTTLPGLRHAPWQGPRGTSDSP 1035
Cdd:PRK07764   683 PAPAPAAPAAP---AGAAPAQPAPAPAATPPAGQADDPAAQPPQAA---QGASAPSPAADDPVPLPPEPDDPPDPAGAPA 756

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1720383787 1036 DGSPLTPVPTQMPWLVGSPEPPQSSPTPAFPLATSYDANGPIQPP 1080
Cdd:PRK07764   757 QPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRDA 801
C1_aPKC cd20794
protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) ...
 33-81 2.32e-04

protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) family; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. Members of this family contain one 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: 410344  Cd Length: 55  Bit Score: 40.33  E-value: 2.32e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720383787   33 HSFREKVFRKKTpVCAVCKVTIDG---TGVSCRVCKVATHRKCEAKVTSSCQ 81
Cdd:cd20794      3 HLFQAKRFNRRA-VCAYCSDRIWGlgrQGYKCINCKLLVHKKCHKLVKVACG 53
C1_cPKC_nPKC_rpt2 cd20793
second protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ...
 33-80 2.47e-04

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


Pssm-ID: 410343  Cd Length: 50  Bit Score: 39.95  E-value: 2.47e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720383787   33 HSFREKVFRKKTpVCAVCKVTIDG---TGVSCRVCKVATHRKCEAKVTSSC 80
Cdd:cd20793      1 HKFKVHTYYSPT-FCDHCGSLLYGlvrQGLKCKDCGMNVHHRCKENVPHLC 50
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
890-1100 2.50e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 45.64  E-value: 2.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  890 GSSGHSTLPRSPRDPQCSASSELSGPS--TPLHTSSPVQGKESNRRQDTTRSPSLAPTQRLSPGEALPSVVQ-----GVA 962
Cdd:PRK12323   367 QSGGGAGPATAAAAPVAQPAPAAAAPAaaAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQasargPGG 446

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  963 EKTPELLTSSRPEQLDPSPFSQTSAPGSPNGWPQERSpgghtNSASPRSPVPTTLPglrhaPWQGPRGTSDSPdgSPLTP 1042
Cdd:PRK12323   447 APAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARA-----APAAAPAPADDDPP-----PWEELPPEFASP--APAQP 514

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720383787 1043 VPTQMPW-LVGSPEPPQSSPTPAFPLAtsydANGPIQPPLPEKRHLPGSGQQPSPPARS 1100
Cdd:PRK12323   515 DAAPAGWvAESIPDPATADPDDAFETL----APAPAAAPAPRAAAATEPVVAPRPPRAS 569
C1_Myosin-IX cd20818
protein kinase C conserved region 1 (C1 domain) found in the unconventional myosin-IX family; ...
 33-81 2.59e-04

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: 40.36  E-value: 2.59e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720383787   33 HSFREKVFRKKTpVCAVCKVTIDGT--GVSCRVCKVATHRKCEAKVTSSCQ 81
Cdd:cd20818      4 HKFATVQFNIPT-YCEVCNSFIWLMekGLVCQVCKFTCHKKCYSKITAPCK 53
PHA03378 PHA03378
EBNA-3B; Provisional
 859-1106 2.97e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 45.44  E-value: 2.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  859 PLSGHLASTGP----------LASTELFPPVSESPEPSWRDGSSGHSTLPRSPRDPQCSASSELSGPSTPLHTSSPvqGK 928
Cdd:PHA03378   580 PTTSQLASSAPsyaqtpwpvpHPSQTPEPPTTQSHIPETSAPRQWPMPLRPIPMRPLRMQPITFNVLVFPTPHQPP--QV 657

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  929 ESNRRQDTTRSPSLAPTQRLSPGEA---LPSVVQGVAEKTPELLTSSRPEQLDPSPFSQTSAPGSPNGWPQERSPGGHTN 1005
Cdd:PHA03378   658 EITPYKPTWTQIGHIPYQPSPTGANtmlPIQWAPGTMQPPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPP 737

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1006 SASP-RSPVPTTLPGlRHAPWQGPRGTSDSPDGSPLTPVPTQMPWLVGSP-EPPQSSPTPAFPlatsydangPIQPPLPE 1083
Cdd:PHA03378   738 AAAPgRARPPAAAPG-RARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPqQRPRGAPTPQPP---------PQAGPTSM 807

                          250       260
                   ....*....|....*....|...
gi 1720383787 1084 KRHLPGSGQQPSPPARSTNQHVT 1106
Cdd:PHA03378   808 QLMPRAAPGQQGPTKQILRQLLT 830
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 795-1117 5.22e-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: 5.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  795 AVPSYCPAYGRAPHSCGSPSEGRGYPSPGAHSPRAGSVSPGSPPYLQPRKLgyeisaedgrdkYPLSG----HLASTGPL 870
Cdd:pfam17823  156 AAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSAPATL------------TPARGistaATATGHPA 223

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  871 ASTELFPPVSESPEPswRDGSSGHSTLPRSPRDPQCSASSELSGPSTPLHTSSPVQGKESNRRQDTTRSPSLAPTQRLSP 950
Cdd:pfam17823  224 AGTALAAVGNSSPAA--GTVTAAVGTVTPAALATLAAAAGTVASAAGTINMGDPHARRLSPAKHMPSDTMARNPAAPMGA 301

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  951 gEALPSVVQgVAEKTPELLTSSRPEqldPSPFSQTSAPGSPNGWPQERSPGGHTNSASPRSPVPTTLPGLRHApwQGPRG 1030
Cdd:pfam17823  302 -QAQGPIIQ-VSTDQPVHNTAGEPT---PSPSNTTLEPNTPKSVASTNLAVVTTTKAQAKEPSASPVPVLHTS--MIPEV 374

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1031 TSDSPDGSPLTPVPTQMPWLVGSPEPPQSSPTPAFPlatSYDANGPIqpplpekrhlPGSGQQPSPPARSTNQHVTFASP 1110
Cdd:pfam17823  375 EATSPTTQPSPLLPTQGAAGPGILLAPEQVATEATA---GTASAGPT----------PRSSGDPKTLAMASCQLSTQGQY 441


                   ....*..
gi 1720383787 1111 LPDVTQP 1117
Cdd:pfam17823  442 LVVTTDP 448
SH2_cSH2_p85_like cd09930
C-terminal Src homology 2 (cSH2) domain found in p85; Phosphoinositide 3-kinases (PI3Ks) are ...
 1139-1228 6.04e-04

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: 40.47  E-value: 6.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1139 WYKPHLSRDQAIALLKDKDPGAFLIRDShSFQGAYGLALKVatpppsaqpwkgdpsEQLVRHFLIETGPKGVKIkgcpTE 1218
Cdd:cd09930      8 WLVGDINRTQAEELLRGKPDGTFLIRES-STQGCYACSVVC---------------NGEVKHCVIYKTETGYGF----AE 67

                           90
                   ....*....|..
gi 1720383787 1219 PY--FGSLSALV 1228
Cdd:cd09930     68 PYnlYESLKELV 79
PHA03379 PHA03379
EBNA-3A; Provisional
 904-1120 6.76e-04

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 44.28  E-value: 6.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  904 PQCSASSE--LSGPStplHTSSPVQGKESNRRQDTTRSPSLAPTQ-----RLSPGEALPSVVQGVAEKTPELLTSSRPEQ 976
Cdd:PHA03379   544 PVCPAPPLiaMQGPG---ETSGIVRVRERWRPAPWTPNPPRSPSQmsvrdRLARLRAEAQPYQASVEVQPPQLTQVSPQQ 620

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  977 ldpspfsQTSAPGSPNGWPQERSPGGHTNSASPRSPVPTTLPGLRHAPWQGPRGTsdspdGSPLTPVPTQMpwlvgSPEP 1056
Cdd:PHA03379   621 -------PMEYPLEPEQQMFPGSPFSQVADVMRAGGVPAMQPQYFDLPLQQPISQ-----GAPLAPLRASM-----GPVP 683

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720383787 1057 PQSSPTPAF-------PLATSYDA-----NGPIQPPL-PEKRHLPGSG-QQPSPPARSTNQHvtFASPLpdvTQPPEH 1120
Cdd:PHA03379   684 PVPATQPQYfdipltePINQGASAahflpQQPMEGPLvPERWMFQGATlSQSVRPGVAQSQY--FDLPL---TQPINH 756
C1_PKD2_rpt2 cd20843
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and ...
 32-80 6.79e-04

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: 39.96  E-value: 6.79e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720383787   32 PHSFREKVFRKKTpVCAVCKVTIDG---TGVSCRVCKVATHRKCEAKVTSSC 80
Cdd:cd20843     11 PHTFVIHSYTRPT-VCQFCKKLLKGlfrQGLQCKDCKFNCHKRCATRVPNDC 61
SH2_C-SH2_PLC_gamma_like cd09932
C-terminal Src homology 2 (C-SH2) domain in Phospholipase C gamma; Phospholipase C gamma is a ...
 1136-1179 6.82e-04

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: 40.33  E-value: 6.82e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1720383787 1136 SKFWYKPHLSRDQAIALLK--DKDpGAFLIRDSHSFQGAYGLALKV 1179
Cdd:cd09932      3 SKEWFHANLTREQAEEMLMrvPRD-GAFLVRPSETDPNSFAISFRA 47
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 949-1121 7.94e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.01  E-value: 7.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  949 SPGEALPSVVQGvaeKTPELLTSSRPeqLDPSPFSQTSAPGSPNGWPQERSPGGHTNSASPRSPVPTTLPGLRHAPWQGP 1028
Cdd:PHA03307    27 TPGDAADDLLSG---SQGQLVSDSAE--LAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPA 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1029 RGTSDSPDGSPLTPVPTQMPWLVGSPEPPQSSPTPAFPLATSYDANGPIQPPLPEKRHLPG-----SGQQPSPPARSTNQ 1103
Cdd:PHA03307   102 REGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVasdaaSSRQAALPLSSPEE 181

                          170
                   ....*....|....*...
gi 1720383787 1104 HVTfASPLPDVTQPPEHP 1121
Cdd:PHA03307   182 TAR-APSSPPAEPPPSTP 198
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 849-1113 8.22e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.01  E-value: 8.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  849 ISAEDGRDKYPLSGH----LASTGPL-ASTELFPPVSESPEPSWRDGSSGHSTLPRSPRDpqcsasseLSGPSTPLHTSS 923
Cdd:PHA03307    25 PATPGDAADDLLSGSqgqlVSDSAELaAVTVVAGAAACDRFEPPTGPPPGPGTEAPANES--------RSTPTWSLSTLA 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  924 PVQGKESNRRQDTTRSPSLAPTQRLSPGEALPSVVQGVAEK-------TPELLTSSRPEQLDPSPFSQTSAPGSPNGWPQ 996
Cdd:PHA03307    97 PASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMlrpvgspGPPPAASPPAAGASPAAVASDAASSRQAALPL 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  997 ERSPGGHTNSASPRSPVPTTLPGLRHAPWQGPRGTSDSPDGSPLTPVPTQMPWLVGSPEPPQSSPTPAFPLATSYDANGP 1076
Cdd:PHA03307   177 SSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECP 256

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1720383787 1077 IqpPLPEKRHLPGSGQQPSPPARSTNQHVTFASPLPD 1113
Cdd:PHA03307   257 L--PRPAPITLPTRIWEASGWNGPSSRPGPASSSSSP 291
C1_Raf cd20811
protein kinase C conserved region 1 (C1 domain) found in the Raf (Rapidly Accelerated ...
 33-81 8.38e-04

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: 38.43  E-value: 8.38e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1720383787   33 HSFREKVFRKKTpVCAVCKVTIdGTGVSCRVCKVATHRKCEAKVTSSCQ 81
Cdd:cd20811      3 HNFVRKTFFTLA-FCDVCRKLL-FQGFRCQTCGFKFHQRCSDQVPALCE 49
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 866-1122 8.92e-04

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 43.76  E-value: 8.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  866 STGPLASTE--LFPPVSESPEPSWRDGSSGHSTLPRSPRDPQCSASSELSGPSTPLHTSS-PVqgkesnrrqdttrSPSL 942
Cdd:PLN03209   309 TTAPLTPMEelLAKIPSQRVPPKESDAADGPKPVPTKPVTPEAPSPPIEEEPPQPKAVVPrPL-------------SPYT 375

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  943 APTQRLSPGEALPSVVQGVAEKTPELLTSSRPEQLDPSPfsqtsAPGSPNGWPQERSPGGHTNSASPRSPV-------PT 1015
Cdd:PLN03209   376 AYEDLKPPTSPIPTPPSSSPASSKSVDAVAKPAEPDVVP-----SPGSASNVPEVEPAQVEAKKTRPLSPYaryedlkPP 450

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1016 TLPGLRHAPWQGPRGTSDSP-DGSPLTPVPTQMpwlVGSPEPPQSSPTPAFPLATSYDANGPIQPPLPEKRHLPGSGQQP 1094
Cdd:PLN03209   451 TSPSPTAPTGVSPSVSSTSSvPAVPDTAPATAA---TDAAAPPPANMRPLSPYAVYDDLKPPTSPSPAAPVGKVAPSSTN 527

                          250       260
                   ....*....|....*....|....*...
gi 1720383787 1095 SPPARSTNQHVTFASPLPDVTQPPEHPL 1122
Cdd:PLN03209   528 EVVKVGNSAPPTALADEQHHAQPKPRPL 555
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 782-1066 9.38e-04

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: 43.75  E-value: 9.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  782 SGYPALVTYGYGGAVPSYCP----AYGRAPhSCGSPSEGRGYPSPGAHSPRAGSVSPgSPPYLQPRklgyeisaedgrdk 857
Cdd:pfam05109  475 SPTPAGTTSGASPVTPSPSPrdngTESKAP-DMTSPTSAVTTPTPNATSPTPAVTTP-TPNATSPT-------------- 538

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  858 yplsghLASTGPLASTELFPPVSESPEPSWrdgssghSTLPRSPRDPQCSASSELSGPSTPL-HTSSPVQGKES---NRR 933
Cdd:pfam05109  539 ------LGKTSPTSAVTTPTPNATSPTPAV-------TTPTPNATIPTLGKTSPTSAVTTPTpNATSPTVGETSpqaNTT 605

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  934 QDTTRSPSLAPTQRLSPGEALPSVVQGVAEKTPellTSSRPEQLDPSPFSQTSAPGSPNGWPQERS------PGGHTN-- 1005
Cdd:pfam05109  606 NHTLGGTSSTPVVTSPPKNATSAVTTGQHNITS---SSTSSMSLRPSSISETLSPSTSDNSTSHMPlltsahPTGGENit 682

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720383787 1006 SASPRSPVPTTLPGLRHAPWQGPRGTSDSPDGSPLTPVPTQMPWLVGSpePPQSSPTPAFP 1066
Cdd:pfam05109  683 QVTPASTSTHHVSTSSPAPRPGTTSQASGPGNSSTSTKPGEVNVTKGT--PPKNATSPQAP 741
SH2_Cterm_shark_like cd10348
C-terminal Src homology 2 (SH2) domain found in SH2 domains, ANK, and kinase domain (shark) ...
 1139-1238 1.19e-03

C-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 its 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: 198211  Cd Length: 86  Bit Score: 39.33  E-value: 1.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1139 WYKPHLSRDQAIALLKDKD--PGAFLIRDSHSFQGAYGLALKvatpppsaqpwkgdpSEQLVRHFLIETgpKGVKIKGCP 1216
Cdd:cd10348      2 WLHGALDRNEAVEILKQKAdaDGSFLVRYSRRRPGGYVLTLV---------------YENHVYHFEIQN--RDDKWFYID 64

                           90       100
                   ....*....|....*....|..
gi 1720383787 1217 TEPYFGSLSALVSQHSISPISL 1238
Cdd:cd10348     65 DGPYFESLEHLIEHYTQFADGL 86
C1_nPKC_epsilon-like_rpt2 cd20838
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
 32-80 1.21e-03

second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) epsilon, eta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410388  Cd Length: 55  Bit Score: 38.41  E-value: 1.21e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720383787   32 PHSFREKVFRKKTpVCAVCKVTIDG---TGVSCRVCKVATHRKCEAKVTSSC 80
Cdd:cd20838      2 PHRFSVHNYKRPT-FCDHCGSLLYGlykQGLQCKVCKMNVHKRCQKNVANNC 52
PHA03377 PHA03377
EBNA-3C; Provisional
 745-972 1.27e-03

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 43.50  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  745 HHHAPMPDYGCLKPPKVGEEGhegcsYAVCSEGRYGHSGYPalvtyGYGGAVPSYcPAYGRAPHSCGSPSEGRGY-PSPG 823
Cdd:PHA03377   756 AQQAPYPGYWEPRPPQAPYLG-----YQEPQAQGVQVSSYP-----GYAGPWGLR-AQHPRYRHSWAYWSQYPGHgHPQG 824

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  824 AHSPRagsvspgsPPYLQPRKLGYEISAEDGRDKYPlsgHLAS-TGPlaSTELFPPVSESPEPSWRDGSSGHSTLPRSPR 902
Cdd:PHA03377   825 PWAPR--------PPHLPPQWDGSAGHGQDQVSQFP---HLQSeTGP--PRLQLSQVPQLPYSQTLVSSSAPSWSSPQPR 891

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  903 DPQCSASSELSGPSTPLHTSSPVQGKESNrrqdtTRSPSLAPTQRLSPGEALPSVVQGVAEKTPELLTSS 972
Cdd:PHA03377   892 APIRPIPTRFPPPPMPLQDSMAVGCDSSG-----TACPSMPFASDYSQGAFTPLDINAQTPKRPRVEESS 956
PHA03378 PHA03378
EBNA-3B; Provisional
 798-1123 1.31e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 43.52  E-value: 1.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  798 SYCPAYGRAPHSCGSPSEGRGYPSPGAHSPrAGSVSPGSPPYLQPRKLgyeisaedgrdkYPLSGHLASTGPLAstelFP 877
Cdd:PHA03378   587 SSAPSYAQTPWPVPHPSQTPEPPTTQSHIP-ETSAPRQWPMPLRPIPM------------RPLRMQPITFNVLV----FP 649

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  878 PVSESPEPSWRDGSSGHSTLPRSPRDPQCsasselSGPSTPLHTS-SPVQGKESNRRQDTTRSPSLAPTQRLSPGEAlps 956
Cdd:PHA03378   650 TPHQPPQVEITPYKPTWTQIGHIPYQPSP------TGANTMLPIQwAPGTMQPPPRAPTPMRPPAAPPGRAQRPAAA--- 720

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  957 vvQGVAEKTPELLTSSRPEQLDPSPFSQTSAPGSPNGWPQERSPGGHTNSASPRSPVPTTLPGLRHAPWQGPRG--TSDS 1034
Cdd:PHA03378   721 --TGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPRGapTPQP 798

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1035 PDGSPLTPVPTQMPWLVGSPEPPQSSPTpafPLATSYDANGPIQPPLPEK-RHLPGSGQQPSPPARSTNQHVTFASPLPD 1113
Cdd:PHA03378   799 PPQAGPTSMQLMPRAAPGQQGPTKQILR---QLLTGGVKRGRPSLKKPAAlERQAAAGPTPSPGSGTSDKIVQAPVFYPP 875

                          330
                   ....*....|
gi 1720383787 1114 VTQPPEHPLQ 1123
Cdd:PHA03378   876 VLQPIQVMRQ 885
SH2_Nck_family cd09943
Src homology 2 (SH2) domain found in the Nck family; Nck proteins are adaptors that modulate ...
 1139-1236 1.38e-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: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1139 WYKPHLSRDQAIALLKDKD-PGAFLIRDSHSFQGAYGLALKVATPPpsaqpwkgdpseqlvRHFLIETGPKGVKIkGCPT 1217
Cdd:cd09943      3 WYYGRITRHQAETLLNEHGhEGDFLIRDSESNPGDYSVSLKAPGRN---------------KHFKVQVVDNVYCI-GQRK 66

                           90
                   ....*....|....*....
gi 1720383787 1218 epyFGSLSALVSQHSISPI 1236
Cdd:cd09943     67 ---FHTMDELVEHYKKAPI 82
SH2_Nterm_shark_like cd10347
N-terminal Src homology 2 (SH2) domain found in SH2 domains, ANK, and kinase domain (shark) ...
 1139-1177 1.48e-03

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: 38.90  E-value: 1.48e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1720383787 1139 WYKPHLSRDQAIALL--KDKDPGAFLIRDSHSFQGAYGLAL 1177
Cdd:cd10347      3 WYHGKISREVAEALLlrEGGRDGLFLVRESTSAPGDYVLSL 43
SH2_SLAP cd10344
Src homology 2 domain found in Src-like adaptor proteins; SLAP belongs to the subfamily of ...
 1139-1242 1.77e-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: 39.40  E-value: 1.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1139 WYKPHLSRDQAIALLK--DKDPGAFLIRDSHSFQGAYGLALKVATPPPSAQpwkgdpseqlVRHFLIETGPKG-VKIKGC 1215
Cdd:cd10344     12 WLFEGLSREKAEELLMlpGNQVGSFLIRESETRRGCYSLSVRHRGSQSRDS----------VKHYRIFRLDNGwFYISPR 81

                           90       100
                   ....*....|....*....|....*..
gi 1720383787 1216 PTepyFGSLSALVSQHSISPISLpCCL 1242
Cdd:cd10344     82 LT---FQCLEDMVNHYSESADGL-CCV 104
SH2_Srm cd10360
Src homology 2 (SH2) domain found in Src-related kinase lacking C-terminal regulatory tyrosine ...
 1139-1181 1.93e-03

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: 38.40  E-value: 1.93e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1720383787 1139 WYKPHLSRDQAIALL--KDKDPGAFLIRDSHSFQGAYGLALKVAT 1181
Cdd:cd10360      2 WYFSGISRTQAQQLLlsPPNEPGAFLIRPSESSLGGYSLSVRAQA 46
C1_DGKtheta_typeV_rpt2 cd20804
second protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, ...
 32-80 1.94e-03

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


Pssm-ID: 410354  Cd Length: 57  Bit Score: 37.67  E-value: 1.94e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720383787   32 PHSFREKVFRKKTpVCAVC-KVTIDGTGVSCRVCKVATHRKCEAKVTSSC 80
Cdd:cd20804      5 AHCWSEPGHSKRK-FCNVCrKRLEDSPAFRCEVCEYYVHSDCQDFAVSDC 53
dnaA PRK14086
chromosomal replication initiator protein DnaA;
938-1135 2.21e-03

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 42.51  E-value: 2.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  938 RSPSLAPTQRLSPGEALPSVVQGVAEKTPELLTSSRPEQLDPSPFSQTSAPGSPNGWPQERsPGGHTNSASPRSPVPTTL 1017
Cdd:PRK14086    94 EPAPPPPHARRTSEPELPRPGRRPYEGYGGPRADDRPPGLPRQDQLPTARPAYPAYQQRPE-PGAWPRAADDYGWQQQRL 172

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1018 PGLRHAPWQGPrgTSDSPDGSPLTPVPTQMPWLVGSPEPPQSSPTPAFPLATSYDANGPIQPPLPEKRHLPGSGQQPSPP 1097
Cdd:PRK14086   173 GFPPRAPYASP--ASYAPEQERDREPYDAGRPEYDQRRRDYDHPRPDWDRPRRDRTDRPEPPPGAGHVHRGGPGPPERDD 250

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1720383787 1098 ARSTNQHVTFASPLPDVTQPPEHPLQENQS-NVKFVQDT 1135
Cdd:PRK14086   251 APVVPIRPSAPGPLAAQPAPAPGPGEPTARlNPKYTFDT 289
C1_DGK_typeI_like_rpt2 cd20851
second protein kinase C conserved region 1 (C1 domain) found in type I diacylglycerol kinases; ...
 47-80 2.73e-03

second 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 second 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: 410401  Cd Length: 52  Bit Score: 37.33  E-value: 2.73e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1720383787   47 CAVCKVTI----DGTGVSCRVCKVATHRKCEAKVTSSC 80
Cdd:cd20851     12 CDKCHKSIksyqGLTGLHCVWCHITLHNKCASHVKPEC 49
C1_DGKeta_rpt1 cd20848
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase eta (DAG ...
 47-81 2.79e-03

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


Pssm-ID: 410398  Cd Length: 86  Bit Score: 38.22  E-value: 2.79e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1720383787   47 CAVCKVTIDGT---GVSCRVCKVATHRKCEAKVTSSCQ 81
Cdd:cd20848     43 CNVCRESLSGVtshGLSCEVCKFKAHKRCAVRATNNCK 80
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 196-292 2.86e-03

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: 40.80  E-value: 2.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  196 FGWPELHAPPLDKLCSICKAMETWLsaDPQHVVVLYCKGSKGKLGVIVSAYMHYS-KISagADQALatltmrKFCEDKVA 274
Cdd:cd14506     82 FGWKDYGVPSLTTILDIVKVMAFAL--QEGGKVAVHCHAGLGRTGVLIACYLVYAlRMS--ADQAI------RLVRSKRP 151

                           90
                   ....*....|....*....
gi 1720383787  275 TELQPS-QRRYVSYFSGLL 292
Cdd:cd14506    152 NSIQTRgQVLCVREFAQFL 170
PHA03379 PHA03379
EBNA-3A; Provisional
 898-1127 3.18e-03

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 41.97  E-value: 3.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  898 PRsPRDPQCSASSELSGPST-----PLHTSS--PVQGKESNRRQDTTRSPSlAPTQRLSPGEALPSVVQ-GVAEKTPELL 969
Cdd:PHA03379   423 PR-PEVPQSLETATSHGSAQvpeppPVHDLEpgPLHDQHSMAPCPVAQLPP-GPLQDLEPGDQLPGVVQdGRPACAPVPA 500

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  970 TSS---RPEQLDPSPFS-QTSAPGSPNGWPQERSPGGHTNSASPRSPVPTTLPGLRHAPWQGPRGTSDSPDGSPLTPVPT 1045
Cdd:PHA03379   501 PAGpivRPWEASLSQVPgVAFAPVMPQPMPVEPVPVPTVALERPVCPAPPLIAMQGPGETSGIVRVRERWRPAPWTPNPP 580

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1046 QMPwlvgSPEPPQSSPTPAFPLATSYDANGPIQPP-LPEkrhlpGSGQQPSPPARSTNQHVTFASP---LPDVTQPPEHP 1121
Cdd:PHA03379   581 RSP----SQMSVRDRLARLRAEAQPYQASVEVQPPqLTQ-----VSPQQPMEYPLEPEQQMFPGSPfsqVADVMRAGGVP 651


                   ....*.
gi 1720383787 1122 LQENQS 1127
Cdd:PHA03379   652 AMQPQY 657
C1_nPKC_epsilon-like_rpt1 cd20835
first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
 33-80 3.19e-03

first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) epsilon, eta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410385  Cd Length: 64  Bit Score: 37.45  E-value: 3.19e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720383787   33 HSFREKVFRKKTpVCAVCKVTIDGT----GVSCRVCKVATHRKCEAKVTSSC 80
Cdd:cd20835     10 HKFMATYLRQPT-YCSHCKDFIWGVigkqGYQCQVCTCVVHKRCHQLVVTKC 60
C1_ScPKC1-like_rpt1 cd20822
first protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae ...
 47-80 3.43e-03

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: 36.88  E-value: 3.43e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1720383787   47 CAVCKVTIDGTGVSCRVCKVATHRKCEAKVTSSC 80
Cdd:cd20822     16 CAVCGEFLVNAGYQCEDCKYTCHKKCYEKVVTKC 49
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 971-1196 3.45e-03

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.06  E-value: 3.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  971 SSRPEQLDPSPFSQTSAPGSPNGWPQERSPGGHTNSASPRSPVPTTLPGLRHAPWQGPRGTSDSPDGSPLTPVPTQMPWL 1050
Cdd:pfam03154  131 SSDPKDIDQDNRSTSPSIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQG 210

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1051 VGSPEPPQSSPTPAFPLATSYDANGPIQPPLPEKRHLPGSGQQPSPPARSTNQHVTFASPLPDVTQPPEHPLQENQSNVK 1130
Cdd:pfam03154  211 SPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQ 290

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720383787 1131 FVQDTSKFWYKPHLSRDQAIALLKDKDPGaflirdsHSFQgayglalKVATPPPSAQPWKGDPSEQ 1196
Cdd:pfam03154  291 HPVPPQPFPLTPQSSQSQVPPGPSPAAPG-------QSQQ-------RIHTPPSQSQLQSQQPPRE 342
PHA03377 PHA03377
EBNA-3C; Provisional
 806-1127 4.24e-03

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 41.58  E-value: 4.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  806 APHSCGSPSEGRGYPSPGAHSPRAGSVSPGSPPYLQPRKLGyeisaedGRDKYPLSGHLASTGPlasTELFPPVS--ESP 883
Cdd:PHA03377   556 SPSDRGPPKASPPVMAPPSTGPRVMATPSTGPRDMAPPSTG-------PRQQAKCKDGPPASGP---HEKQPPSSapRDM 625

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  884 EPSWRDGSSGHSTLPRSP-RDPQC----SASSELSGpstplhtsspVQGKESNRRQDTTRSPSLAPTqRLSPGEALPSVV 958
Cdd:PHA03377   626 APSVVRMFLRERLLEQSTgPKPKSfwemRAGRDGSG----------IQQEPSSRRQPATQSTPPRPS-WLPSVFVLPSVD 694

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  959 QGVAEKTPEL----LTSSRP----EQL---DPSPFSQTSAPGSPNGWPQERSP-GGHTNSASPRSPVP---------TTL 1017
Cdd:PHA03377   695 AGRAQPSEEShlssMSPTQPisheEQPryeDPDDPLDLSLHPDQAPPPSHQAPySGHEEPQAQQAPYPgyweprppqAPY 774

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1018 PGLRHAPWQGPRGTSDSPDGSPLTPV--------------------PTQMPWLVGSPEPPQSSPTPAFPLATSYDANGPI 1077
Cdd:PHA03377   775 LGYQEPQAQGVQVSSYPGYAGPWGLRaqhpryrhswaywsqypghgHPQGPWAPRPPHLPPQWDGSAGHGQDQVSQFPHL 854

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720383787 1078 Q----PPLPEKRHLPGSGQQPSP-----PARSTNQHVTFASPLPDVTQPPEHPLQENQS 1127
Cdd:PHA03377   855 QsetgPPRLQLSQVPQLPYSQTLvsssaPSWSSPQPRAPIRPIPTRFPPPPMPLQDSMA 913
PTB_JIP cd01212
JNK-interacting protein-like (JIP) Phosphotyrosine-binding (PTB) domain; JIP is a ...
 1277-1383 4.26e-03

JNK-interacting protein-like (JIP) Phosphotyrosine-binding (PTB) domain; JIP is a mitogen-activated protein kinase scaffold protein. JIP consists of a C-terminal SH3 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: 269923  Cd Length: 149  Bit Score: 39.18  E-value: 4.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1277 VLYLTSVETESLTGP----QAVAKASSAALSCSPVPVPAIVHFKVSAQGITLTDNQRKLFFRR----HY--PVNSITFSS 1346
Cdd:cd01212      7 LGFLGSVEVPYHKGNdvlcQAMQKIATARRLTVHLRPPQSCILEISDRGLKMVDRSKPNKKDGkpciHYfySLKNISFCG 86

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1720383787 1347 TDPQDrrwtnpdgatSKIFGFVAKKPgSPWENVCHLF 1383
Cdd:cd01212     87 FHPRN----------SRYFGFITKHP-LLQRFACHVF 112
SH2_nSH2_p85_like cd09942
N-terminal Src homology 2 (nSH2) domain found in p85; Phosphoinositide 3-kinases (PI3Ks) are ...
 1139-1178 4.32e-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: 38.46  E-value: 4.32e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1720383787 1139 WYKPHLSRDQAIALLKDKDPGAFLIRDSHSFQGAYGLALK 1178
Cdd:cd09942      9 WYWGDISREEVNEKMRDTPDGTFLVRDASTMKGDYTLTLR 48
SH2_SHIP cd10343
Src homology 2 (SH2) domain found in SH2-containing inositol-5'-phosphatase (SHIP) and ...
 1139-1177 4.68e-03

Src homology 2 (SH2) domain found in SH2-containing inositol-5'-phosphatase (SHIP) and SLAM-associated protein (SAP); The SH2-containing inositol-5'-phosphatase, SHIP (also called SHIP1/SHIP1a), is a hematopoietic-restricted phosphatidylinositide phosphatase that translocates to the plasma membrane after extracellular stimulation and hydrolyzes the phosphatidylinositol-3-kinase (PI3K)-generated second messenger PI-3,4,5-P3 (PIP3) to PI-3,4-P2. As a result, SHIP dampens down PIP3 mediated signaling and represses the proliferation, differentiation, survival, activation, and migration of hematopoietic cells. PIP3 recruits lipid-binding pleckstrin homology(PH) domain-containing proteins to the inner wall of the plasma membrane and activates them. PH domain-containing downstream effectors include the survival/proliferation enhancing serine/threonine kinase, Akt (protein kinase B), the tyrosine kinase, Btk, the regulator of protein translation, S6K, and the Rac and cdc42 guanine nucleotide exchange factor, Vav. SHIP is believed to act as a tumor suppressor during leukemogenesis and lymphomagenesis, and may play a role in activating the immune system to combat cancer. SHIP contains an N-terminal SH2 domain, a centrally located phosphatase domain that specifically hydrolyzes the 5'-phosphate from PIP3, PI-4,5-P2 and inositol-1,3,4,5- tetrakisphosphate (IP4), a C2 domain, that is an allosteric activating site when bound by SHIP's enzymatic product, PI-3,4-P2; 2 NPXY motifs that bind proteins with a phosphotyrosine binding (Shc, Dok 1, Dok 2) or an SH2 (p85a, SHIP2) domain; and a proline-rich domain consisting of four PxxP motifs that bind a subset of SH3-containing proteins including Grb2, Src, Lyn, Hck, Abl, PLCg1, and PIAS1. The SH2 domain of SHIP binds to the tyrosine phosphorylated forms of Shc, SHP-2, Doks, Gabs, CD150, platelet-endothelial cell adhesion molecule, Cas, c-Cbl, immunoreceptor tyrosine-based inhibitory motifs (ITIMs), and immunoreceptor tyrosine-based activation motifs (ITAMs). The X-linked lymphoproliferative syndrome (XLP) gene encodes SAP (also called SH2D1A/DSHP) a protein that consists of a 5 residue N-terminus, a single SH2 domain, and a short 25 residue C-terminal tail. XLP is characterized by an extreme sensitivity to Epstein-Barr virus. Both T and natural killer (NK) cell dysfunctions have been seen in XLP patients. SAP binds the cytoplasmic tail of Signaling lymphocytic activation molecule (SLAM), 2B4, Ly-9, and CD84. SAP is believed to function as a signaling inhibitor, by blocking or regulating binding of other signaling proteins. SAP and the SAP-like protein EAT-2 recognize the sequence motif TIpYXX(V/I), which is found in the cytoplasmic domains of a restricted number of T, B, and NK cell surface receptors and are proposed to be natural inhibitors or regulators of the physiological role of a small family of receptors on the surface of these cells. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198206  Cd Length: 103  Bit Score: 38.19  E-value: 4.68e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1720383787 1139 WYKPHLSRDQAIALLKD--KDpGAFLIRDSHSFQGAYGLAL 1177
Cdd:cd10343      5 WYHGNITRSKAEELLSKagKD-GSFLVRDSESVSGAYALCV 44
C1_VAV cd20810
protein kinase C conserved region 1 (C1 domain) found in VAV proteins; VAV proteins function ...
 33-81 5.62e-03

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


Pssm-ID: 410360  Cd Length: 52  Bit Score: 36.47  E-value: 5.62e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720383787   33 HSFREKVFrKKTPVCAVCKVTIDGT---GVSCRVCKVATHRKCEAKVTsSCQ 81
Cdd:cd20810      3 HSFELTTF-KEPTTCSVCKKLLKGLffqGYKCSVCGAAVHKECIAKVK-RCG 52
SH2_a2chimerin_b2chimerin cd10352
Src homology 2 (SH2) domain found in alpha2-chimerin and beta2-chimerin proteins; Chimerins ...
 1144-1178 5.63e-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: 37.34  E-value: 5.63e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1720383787 1144 LSRDQAIALLKDKDPGAFLIRDSHSFQGAYGLALK 1178
Cdd:cd10352     13 ISREEAEQLLSGASDGSYLIRESSRDDGYYTLSLR 47
C1_PKD1_rpt2 cd20842
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and ...
 32-80 5.78e-03

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


Pssm-ID: 410392  Cd Length: 94  Bit Score: 37.69  E-value: 5.78e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720383787   32 PHSFREKVFRKKTpVCAVCKVTIDG---TGVSCRVCKVATHRKCEAKVTSSC 80
Cdd:cd20842     34 PHTFVIHSYTRPT-VCQYCKKLLKGlfrQGLQCKDCKFNCHKRCAPKVPNNC 84
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 796-1063 5.94e-03

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 41.29  E-value: 5.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  796 VPSYCPAYGRAPHSCGSPSEgRGYPSPGAHSPRAGSVSPGSPPYLQPrklgYEISAEDGRDKYPLSGHLASTGPLASTEL 875
Cdd:pfam03154  252 MTQPPPPSQVSPQPLPQPSL-HGQMPPMPHSLQTGPSHMQHPVPPQP----FPLTPQSSQSQVPPGPSPAAPGQSQQRIH 326

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  876 FPPVSESPEPSwrdGSSGHSTLPRSP------RDPQCSASSELSGPSTPLHTSSPVQGKESNRRQDTTRSPSLAPTQRLS 949
Cdd:pfam03154  327 TPPSQSQLQSQ---QPPREQPLPPAPlsmphiKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQMNSNLPPPPALKPLSSLS 403

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  950 ---PGEALPSVVQGVAEKT--------PELLTSSR----PEQLDPSPFSQTSAPGSPNGWPQERSPGGHTNSASPRSP-- 1012
Cdd:pfam03154  404 thhPPSAHPPPLQLMPQSQqlppppaqPPVLTQSQslppPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPpt 483

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1013 -VPTTLPGLRhAPWQGPRGTSDSPDGSPLTPVPT--------QMPWLVGSPEPPQSSPTP 1063
Cdd:pfam03154  484 sTSSAMPGIQ-PPSSASVSSSGPVPAAVSCPLPPvqikeealDEAEEPESPPPPPRSPSP 542
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 1276-1383 6.81e-03

Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins Phosphotyrosine-binding (PTB) PH-like fold; The null mutations in the LDL receptor adaptor protein 1 (LDLRAP1) gene, which serves as an adaptor for LDLR endocytosis in the liver, causes autosomal recessive hypercholesterolemia (ARH). LDLRAP1 contains a single 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 contains mammals, insects, and sponges.


Pssm-ID: 269981  Cd Length: 123  Bit Score: 38.08  E-value: 6.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1276 SVLYLTSVETESLTGPQAVAKASSAALSCSPV--PVPAIVHFKVSAQGITLTD---NQRKLffrrHYPVNSITFSSTDPQ 1350
Cdd:cd13159      6 YLKYLGSTLVEKPKGEGATAEAVKTIIAMAKAsgKKLQKVTLTVSPKGIKVTDsatNETIL----EVSIYRISYCTADAN 81

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1720383787 1351 DrrwtnpdgatSKIFGFVAKKPGSpwEN-VCHLF 1383
Cdd:cd13159     82 H----------DKVFAFIATNQDN--EKlECHAF 103
C1_DGK_typeI_rpt1 cd20799
first protein kinase C conserved region 1 (C1 domain) found in type I diacylglycerol kinases; ...
 33-80 7.05e-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: 36.20  E-value: 7.05e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720383787   33 HSFREKVFRKKTpVCAVCKVTIDG---TGVSCRVCKVATHRKCEAKVTSSC 80
Cdd:cd20799      6 HVWRLKHFNKPA-YCNVCENMLVGlrkQGLCCTFCKYTVHERCVSRAPASC 55
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 889-1118 8.59e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 8.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  889 DGSSGHSTLPRSPRDPQCSASSELSGPSTPLHTSSPVQGKesnrRQDTTRSPSLAPTQRLSPGEALPSVVQGVAEKTPEL 968
Cdd:PRK07764   589 GPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPA----PAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASD 664

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787  969 LTSSRPEQLDPSPFSQTSAPGSPNGWPQERSPGGHTNSASPRSPVPTTLPGLRHAPWQGPRGTSDSPDGSPLTPVPtqmp 1048
Cdd:PRK07764   665 GGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVP---- 740

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383787 1049 wlvgSPEPPQSSPTPAFPLATSYDANGPIQPPLPekrhlpgsgQQPSPPARSTNQHVTFASPLPDVTQPP 1118
Cdd:PRK07764   741 ----LPPEPDDPPDPAGAPAQPPPPPAPAPAAAP---------AAAPPPSPPSEEEEMAEDDAPSMDDED 797
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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