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Conserved domains on  [gi|6755672|ref|NP_035618|]
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signal transducer and activator of transcription 5A isoform 1 [Mus musculus]

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List of domain hits

Name Accession Description Interval E-value
STAT_bind pfam02864
STAT protein, DNA binding domain; STAT proteins (Signal Transducers and Activators of ...
332-582 2.55e-139

STAT protein, DNA binding domain; STAT proteins (Signal Transducers and Activators of Transcription) are a family of transcription factors that are specifically activated to regulate gene transcription when cells encounter cytokines and growth factors. This family represents the DNA binding domain of STAT, which has an ig-like fold. STAT proteins also include an SH2 domain pfam00017.


:

Pssm-ID: 280939  Cd Length: 244  Bit Score: 413.93  E-value: 2.55e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672    332 FIIEKQPPQVLKTQTKFAATVRLLVGGKLNVHMNPPQVKATIISEQQAKSLLKN--ENTRNECSGEIlNNCCVMEYHQAT 409
Cdd:pfam02864   1 FVVEKQPPQVLKTQTKFSATVRLLVGDKLPEHNNPPKVKVSIDSEAQARALLKGflNMEESQNSGEI-NNTGAMEYHQAS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672    410 GTLSAHFRNMSLKRIKRADRRGAESVTEEKFTVLFESQFSVGsnELVFQVKTLSLPVVVIVHGSQDHNATATVLWDNAFA 489
Cdd:pfam02864  80 GQLSADFRNLQLKEIKRGGRKGNESVTEEKFALLFETQFTLG--GLVFDLQTLSLPVVVIVHGNQEPNAWATILWDNAFA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672    490 EPGRVPFAVPDKVLWPQLCEALNMKFKAevQSNRGLTKENLVFLAQKLFNISSNhledYNSMSVSWSQFNRENLPGWNYT 569
Cdd:pfam02864 158 EPKRVPFFVPPAVPWPQLAEALSWKFSS--GTGRGLSDEQLKYLAEKLFGDPVS----YSDSLVSWSQFCKENLPGRNFT 231
                         250
                  ....*....|...
gi 6755672    570 FWQWFDGVMEVLK 582
Cdd:pfam02864 232 FWEWFDGILDLIK 244
SH2_STAT5a cd10421
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) ...
573-712 1.05e-97

Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 5a proteins; STAT5 is a member of the STAT family of transcription factors. Two highly related proteins, STAT5a and STAT5b are encoded by separate genes, but are 90% identical at the amino acid level. Both STAT5a and STAT5b are ubiquitously expressed and functionally interchangeable. Mice lacking either STAT5a or STAT5b have mild defects in prolactin dependent mammary differentiation or sexually dimorphic growth hormone-dependent effects, respectively. Mice lacking both STAT5a and STAT5b exhibit a perinatal lethal phenotype and have multiple defects, including anemia and a virtual absence of B and T lymphocytes. STAT proteins mediate the signaling of cytokines and a number of growth factors from the receptors of these extracellular signaling molecules to the cell nucleus. STATs are specifically phosphorylated by receptor-associated Janus kinases, receptor tyrosine kinases, or cytoplasmic tyrosine kinases. The phosphorylated STAT molecules dimerize by reciprocal binding of their SH2 domains to the phosphotyrosine residues. These dimeric STATs translocate into the nucleus, bind to specific DNA sequences, and regulate the transcription of their target genes. However there are a number of unphosphorylated STATs that travel between the cytoplasm and nucleus and some STATs that exist as dimers in unstimulated cells that can exert biological functions independent of being activated. There are seven mammalian STAT family members which have been identified: STAT1, STAT2, STAT3, STAT4, STAT5 (STAT5A and STAT5B), and STAT6. There are 6 conserved domains in STAT: N-terminal domain (NTD), coiled-coil domain (CCD), DNA-binding domain (DBD), alpha-helical linker domain (LD), SH2 domain, and transactivation domain (TAD). NTD is involved in dimerization of unphosphorylated STATs monomers and for the tetramerization between STAT1, STAT3, STAT4 and STAT5 on promoters with two or more tandem STAT binding sites. It also plays a role in promoting interactions with transcriptional co-activators such as CREB binding protein (CBP)/p300, as well as being important for nuclear import and deactivation of STATs involving tyrosine de-phosphorylation. CCD interacts with other proteins, such as IFN regulatory protein 9 (IRF-9/p48) with STAT1 and c-JUN with STAT3 and is also thought to participate in the negative regulation of these proteins. Distinct genes are bound to STATs via their DBD domain. This domain is also involved in nuclear translocation of activated STAT1 and STAT3 phosphorylated dimers upon cytokine stimulation. LD links the DNA-binding and SH2 domains and is important for the transcriptional activation of STAT1 in response to IFN-gamma. It also plays a role in protein-protein interactions and has also been implicated in the constitutive nucleocytoplasmic shuttling of unphosphorylated STATs in resting cells. The SH2 domain is necessary for receptor association and tyrosine phosphodimer formation. Residues within this domain may be particularly important for some cellular functions mediated by the STATs as well as residues adjacent to this domain. The TAD interacts with several proteins, namely minichromosome maintenance complex component 5 (MCM5), breast cancer 1 (BRCA1) and CBP/p300. TAD also contains a modulatory phosphorylation site that regulates STAT activity and is necessary for maximal transcription of a number of target genes. The conserved tyrosine residue present in the C-terminus is crucial for dimerization via interaction with the SH2 domain upon the interaction of the ligand with the receptor. STAT activation by tyrosine phosphorylation also determines nuclear import and retention, DNA binding to specific DNA elements in the promoters of responsive genes, and transcriptional activation of STAT dimers. In addition to the SH2 domain there is a coiled-coil domain, a DNA binding domain, and a transactivation domain in the STAT proteins. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


:

Pssm-ID: 198284  Cd Length: 140  Bit Score: 301.96  E-value: 1.05e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672  573 WFDGVMEVLKKHHKPHWNDGAILGFVNKQQAHDLLINKPDGTFLLRFSDSEIGGITIAWKFDSPDRNLWNLKPFTTRDFS 652
Cdd:cd10421   1 WFDGVMEVLKKHHKPHWNDGAILGFVNKQQAHDLLINKPDGTFLLRFSDSEIGGITIAWKFDSPDRNLWNLKPFTTRDFS 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672  653 IRSLADRLGDLNYLIYVFPDRPKDEVFAKYYTPVLAKAVDGYVKPQIKQVVPEFVNASTD 712
Cdd:cd10421  81 IRSLADRLGDLNYLIYVFPDRPKDEVFSKYYTPVLAKAVDGYVKPQIKQVVPEFVSASAD 140
STAT_alpha pfam01017
STAT protein, all-alpha domain; STAT proteins (Signal Transducers and Activators of ...
141-330 2.04e-70

STAT protein, all-alpha domain; STAT proteins (Signal Transducers and Activators of Transcription) are a family of transcription factors that are specifically activated to regulate gene transcription when cells encounter cytokines and growth factors. STAT proteins also include an SH2 domain pfam00017.


:

Pssm-ID: 279369  Cd Length: 178  Bit Score: 230.56  E-value: 2.04e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672    141 HLQINQRFEELRLITQDTENELKKLQQTQEYFIIQYQESLRIQAQfaqlgqlnpqERMSRETALQQKQVSLetwLQREAQ 220
Cdd:pfam01017   1 QQEIEQRLQELRNRVQETEQDIRQLEDLQDEFDFKYKELQKLQEQ----------ERTSSEDKELKQQKEL---LQQMLN 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672    221 TLQQYRVELAEKHQKTLQLLRKQQTIILDDELIQWKRRQQLAGNGGPPEGSLDVLQSWCEKLAEIIWQNRQQIRRAEHLC 300
Cdd:pfam01017  68 ELDQKRKEVLDKLKELLNLLETLQELLLDEELIEWKRRQQLACIGAPPNSNLDQLQNWFTALAELLWQLRQQLKKLEELR 147
                         170       180       190
                  ....*....|....*....|....*....|.
gi 6755672    301 QQLPIPG-PVEEMLAEVNATITDIISALVTS 330
Cdd:pfam01017 148 QKLTYEGdPLTDQLPQLNARVTELLSSLVTS 178
STAT_int pfam02865
STAT protein, protein interaction domain; STAT proteins (Signal Transducers and Activators of ...
2-124 3.31e-53

STAT protein, protein interaction domain; STAT proteins (Signal Transducers and Activators of Transcription) are a family of transcription factors that are specifically activated to regulate gene transcription when cells encounter cytokines and growth factors. STAT proteins also include an SH2 domain pfam00017.


:

Pssm-ID: 280940  Cd Length: 122  Bit Score: 180.49  E-value: 3.31e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672      2 AGWIQAQQLQGDALRQMQVLYGQHFPIEVRHYLAQWIESQPWDAIDLDnPQDRGQATQLLEGLVQELQKKAEHQVGEDGF 81
Cdd:pfam02865   1 ALWAKLQQLPGDALEQVQQLYGDHFPIEVRHYLASWIESQDWEDIDPD-PQDESLATVLFHNLLQELQSQASRLSQEDNF 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 6755672     82 LLKIKLGHYATQLQNTYDRCPMELVRCIRHILYNEQRLVREAN 124
Cdd:pfam02865  80 LLKHKLREIARNFQNRYQENPLELARIIRNCLREEKRIVQQAE 122
 
Name Accession Description Interval E-value
STAT_bind pfam02864
STAT protein, DNA binding domain; STAT proteins (Signal Transducers and Activators of ...
332-582 2.55e-139

STAT protein, DNA binding domain; STAT proteins (Signal Transducers and Activators of Transcription) are a family of transcription factors that are specifically activated to regulate gene transcription when cells encounter cytokines and growth factors. This family represents the DNA binding domain of STAT, which has an ig-like fold. STAT proteins also include an SH2 domain pfam00017.


Pssm-ID: 280939  Cd Length: 244  Bit Score: 413.93  E-value: 2.55e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672    332 FIIEKQPPQVLKTQTKFAATVRLLVGGKLNVHMNPPQVKATIISEQQAKSLLKN--ENTRNECSGEIlNNCCVMEYHQAT 409
Cdd:pfam02864   1 FVVEKQPPQVLKTQTKFSATVRLLVGDKLPEHNNPPKVKVSIDSEAQARALLKGflNMEESQNSGEI-NNTGAMEYHQAS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672    410 GTLSAHFRNMSLKRIKRADRRGAESVTEEKFTVLFESQFSVGsnELVFQVKTLSLPVVVIVHGSQDHNATATVLWDNAFA 489
Cdd:pfam02864  80 GQLSADFRNLQLKEIKRGGRKGNESVTEEKFALLFETQFTLG--GLVFDLQTLSLPVVVIVHGNQEPNAWATILWDNAFA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672    490 EPGRVPFAVPDKVLWPQLCEALNMKFKAevQSNRGLTKENLVFLAQKLFNISSNhledYNSMSVSWSQFNRENLPGWNYT 569
Cdd:pfam02864 158 EPKRVPFFVPPAVPWPQLAEALSWKFSS--GTGRGLSDEQLKYLAEKLFGDPVS----YSDSLVSWSQFCKENLPGRNFT 231
                         250
                  ....*....|...
gi 6755672    570 FWQWFDGVMEVLK 582
Cdd:pfam02864 232 FWEWFDGILDLIK 244
SH2_STAT5a cd10421
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) ...
573-712 1.05e-97

Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 5a proteins; STAT5 is a member of the STAT family of transcription factors. Two highly related proteins, STAT5a and STAT5b are encoded by separate genes, but are 90% identical at the amino acid level. Both STAT5a and STAT5b are ubiquitously expressed and functionally interchangeable. Mice lacking either STAT5a or STAT5b have mild defects in prolactin dependent mammary differentiation or sexually dimorphic growth hormone-dependent effects, respectively. Mice lacking both STAT5a and STAT5b exhibit a perinatal lethal phenotype and have multiple defects, including anemia and a virtual absence of B and T lymphocytes. STAT proteins mediate the signaling of cytokines and a number of growth factors from the receptors of these extracellular signaling molecules to the cell nucleus. STATs are specifically phosphorylated by receptor-associated Janus kinases, receptor tyrosine kinases, or cytoplasmic tyrosine kinases. The phosphorylated STAT molecules dimerize by reciprocal binding of their SH2 domains to the phosphotyrosine residues. These dimeric STATs translocate into the nucleus, bind to specific DNA sequences, and regulate the transcription of their target genes. However there are a number of unphosphorylated STATs that travel between the cytoplasm and nucleus and some STATs that exist as dimers in unstimulated cells that can exert biological functions independent of being activated. There are seven mammalian STAT family members which have been identified: STAT1, STAT2, STAT3, STAT4, STAT5 (STAT5A and STAT5B), and STAT6. There are 6 conserved domains in STAT: N-terminal domain (NTD), coiled-coil domain (CCD), DNA-binding domain (DBD), alpha-helical linker domain (LD), SH2 domain, and transactivation domain (TAD). NTD is involved in dimerization of unphosphorylated STATs monomers and for the tetramerization between STAT1, STAT3, STAT4 and STAT5 on promoters with two or more tandem STAT binding sites. It also plays a role in promoting interactions with transcriptional co-activators such as CREB binding protein (CBP)/p300, as well as being important for nuclear import and deactivation of STATs involving tyrosine de-phosphorylation. CCD interacts with other proteins, such as IFN regulatory protein 9 (IRF-9/p48) with STAT1 and c-JUN with STAT3 and is also thought to participate in the negative regulation of these proteins. Distinct genes are bound to STATs via their DBD domain. This domain is also involved in nuclear translocation of activated STAT1 and STAT3 phosphorylated dimers upon cytokine stimulation. LD links the DNA-binding and SH2 domains and is important for the transcriptional activation of STAT1 in response to IFN-gamma. It also plays a role in protein-protein interactions and has also been implicated in the constitutive nucleocytoplasmic shuttling of unphosphorylated STATs in resting cells. The SH2 domain is necessary for receptor association and tyrosine phosphodimer formation. Residues within this domain may be particularly important for some cellular functions mediated by the STATs as well as residues adjacent to this domain. The TAD interacts with several proteins, namely minichromosome maintenance complex component 5 (MCM5), breast cancer 1 (BRCA1) and CBP/p300. TAD also contains a modulatory phosphorylation site that regulates STAT activity and is necessary for maximal transcription of a number of target genes. The conserved tyrosine residue present in the C-terminus is crucial for dimerization via interaction with the SH2 domain upon the interaction of the ligand with the receptor. STAT activation by tyrosine phosphorylation also determines nuclear import and retention, DNA binding to specific DNA elements in the promoters of responsive genes, and transcriptional activation of STAT dimers. In addition to the SH2 domain there is a coiled-coil domain, a DNA binding domain, and a transactivation domain in the STAT proteins. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198284  Cd Length: 140  Bit Score: 301.96  E-value: 1.05e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672  573 WFDGVMEVLKKHHKPHWNDGAILGFVNKQQAHDLLINKPDGTFLLRFSDSEIGGITIAWKFDSPDRNLWNLKPFTTRDFS 652
Cdd:cd10421   1 WFDGVMEVLKKHHKPHWNDGAILGFVNKQQAHDLLINKPDGTFLLRFSDSEIGGITIAWKFDSPDRNLWNLKPFTTRDFS 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672  653 IRSLADRLGDLNYLIYVFPDRPKDEVFAKYYTPVLAKAVDGYVKPQIKQVVPEFVNASTD 712
Cdd:cd10421  81 IRSLADRLGDLNYLIYVFPDRPKDEVFSKYYTPVLAKAVDGYVKPQIKQVVPEFVSASAD 140
STAT_alpha pfam01017
STAT protein, all-alpha domain; STAT proteins (Signal Transducers and Activators of ...
141-330 2.04e-70

STAT protein, all-alpha domain; STAT proteins (Signal Transducers and Activators of Transcription) are a family of transcription factors that are specifically activated to regulate gene transcription when cells encounter cytokines and growth factors. STAT proteins also include an SH2 domain pfam00017.


Pssm-ID: 279369  Cd Length: 178  Bit Score: 230.56  E-value: 2.04e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672    141 HLQINQRFEELRLITQDTENELKKLQQTQEYFIIQYQESLRIQAQfaqlgqlnpqERMSRETALQQKQVSLetwLQREAQ 220
Cdd:pfam01017   1 QQEIEQRLQELRNRVQETEQDIRQLEDLQDEFDFKYKELQKLQEQ----------ERTSSEDKELKQQKEL---LQQMLN 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672    221 TLQQYRVELAEKHQKTLQLLRKQQTIILDDELIQWKRRQQLAGNGGPPEGSLDVLQSWCEKLAEIIWQNRQQIRRAEHLC 300
Cdd:pfam01017  68 ELDQKRKEVLDKLKELLNLLETLQELLLDEELIEWKRRQQLACIGAPPNSNLDQLQNWFTALAELLWQLRQQLKKLEELR 147
                         170       180       190
                  ....*....|....*....|....*....|.
gi 6755672    301 QQLPIPG-PVEEMLAEVNATITDIISALVTS 330
Cdd:pfam01017 148 QKLTYEGdPLTDQLPQLNARVTELLSSLVTS 178
STAT_int pfam02865
STAT protein, protein interaction domain; STAT proteins (Signal Transducers and Activators of ...
2-124 3.31e-53

STAT protein, protein interaction domain; STAT proteins (Signal Transducers and Activators of Transcription) are a family of transcription factors that are specifically activated to regulate gene transcription when cells encounter cytokines and growth factors. STAT proteins also include an SH2 domain pfam00017.


Pssm-ID: 280940  Cd Length: 122  Bit Score: 180.49  E-value: 3.31e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672      2 AGWIQAQQLQGDALRQMQVLYGQHFPIEVRHYLAQWIESQPWDAIDLDnPQDRGQATQLLEGLVQELQKKAEHQVGEDGF 81
Cdd:pfam02865   1 ALWAKLQQLPGDALEQVQQLYGDHFPIEVRHYLASWIESQDWEDIDPD-PQDESLATVLFHNLLQELQSQASRLSQEDNF 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 6755672     82 LLKIKLGHYATQLQNTYDRCPMELVRCIRHILYNEQRLVREAN 124
Cdd:pfam02865  80 LLKHKLREIARNFQNRYQENPLELARIIRNCLREEKRIVQQAE 122
STAT_int smart00964
STAT protein, protein interaction domain; STAT proteins (Signal Transducers and Activators of ...
2-125 1.29e-47

STAT protein, protein interaction domain; STAT proteins (Signal Transducers and Activators of Transcription) are a family of transcription factors that are specifically activated to regulate gene transcription when cells encounter cytokines and growth factors. STAT proteins also include an SH2 domain.


Pssm-ID: 214942  Cd Length: 120  Bit Score: 164.77  E-value: 1.29e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672       2 AGWIQAQQLQGDALRQMQVLYGQHFPIEVRHYLAQWIESQPWDAIDLDNPqdrgQATQLLEGLVQELQKKAEHQVGEDGF 81
Cdd:smart00964   1 SQWAQLQQLDSKFLEQVQQLYGDNFPMELRHYLADWIESQDWELAANDEA----QATRLFHNLLEQLDQQLSRFSQESNF 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 6755672      82 LLKIKLGHYATQLQNTYDRCPMELVRCIRHILYNEQRLVREANN 125
Cdd:smart00964  77 LLKHNLRHIKSNLQSLYQENPLELARIIRNILQEERRILAEASR 120
SH2 pfam00017
SH2 domain;
589-668 4.66e-14

SH2 domain;


Pssm-ID: 278446  Cd Length: 77  Bit Score: 68.78  E-value: 4.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672    589 WNDGAIlgfvNKQQAHDLLIN-KPDGTFLLRFSDSEIGGITIAWKFDspDRNLWNLKPFTTRDFSIRSLADRLGDLNYLI 667
Cdd:pfam00017   1 WYHGKI----SREEAERLLLNgKPDGTFLVRESESTPGGYTLSVRDD--GKVKHYKIQSTDNGGYYISGGVKFSSLAELV 74

                  .
gi 6755672    668 Y 668
Cdd:pfam00017  75 E 75
SH2 smart00252
Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides ...
596-634 4.50e-10

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


Pssm-ID: 214585  Cd Length: 84  Bit Score: 57.24  E-value: 4.50e-10
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 6755672     596 GFVNKQQAHDLLINKPDGTFLLRFSDSEIGGITIAWKFD 634
Cdd:smart00252   6 GFISREEAEKLLKNEGDGDFLVRDSESSPGDYVLSVRVK 44
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
141-303 1.06e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.11  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672     141 HLQINQRFEELRLITQDTE------NELKKLQQTQEYFIIQYQESLRI-QAQFAQLGQLNpQERMSRETALQQKQVSLET 213
Cdd:TIGR00618  193 HGKAELLTLRSQLLTLCTPcmpdtyHERKQVLEKELKHLREALQQTQQsHAYLTQKREAQ-EEQLKKQQLLKQLRARIEE 271
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672     214 WLQREAQ-TLQQYRVELAEK------HQKTLQLLRKQQTII----------LDDELIQWKRRQQLAGNGGPPEGSLDVLQ 276
Cdd:TIGR00618  272 LRAQEAVlEETQERINRARKaaplaaHIKAVTQIEQQAQRIhtelqskmrsRAKLLMKRAAHVKQQSSIEEQRRLLQTLH 351
                          170       180
                   ....*....|....*....|....*..
gi 6755672     277 SWCEKLAEiiwQNRQQIRRAEHLCQQL 303
Cdd:TIGR00618  352 SQEIHIRD---AHEVATSIREISCQQH 375
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
142-262 4.38e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 292337 [Multi-domain]  Cd Length: 516  Bit Score: 39.11  E-value: 4.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672    142 LQINQRFEELRLITQDTENElkklQQTQEyfiiqyqESLRIQAQfaqlgqlnpQERMSRETALQQKQVSLETW--LQREA 219
Cdd:pfam15709 374 LEQQRRAEEIRLRKQRLEEE----RQRQE-------EEERKQRL---------QLQAAQERARQQQEEFRRKLqeLQRKK 433
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 6755672    220 QTLQQYRVELAEKHQKTL--QLLRKQQTI--ILDDELIQWKRRQQLA 262
Cdd:pfam15709 434 QQEEAERAEAEKQRQKELemQLAEEQKRLmeMAEEERLEYQRQKQEA 480
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
139-247 5.41e-03

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 38.97  E-value: 5.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672  139 QKHLQINQRFEELRLITQDTENELKKLQQTQEYFI-----IQYQESLR--IQAQFAQLGQLNPQ--ERMSRETALQQKQV 209
Cdd:COG0419 274 EELRELERLLEELEEKIERLEELEREIEELEEELEglralLEELEELLekLKSLEERLEKLEEKleKLESELEELAEEKN 353
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 6755672  210 SLETWLQREAQTLQQYRVELAEKHQKTLQLLRKQQTII 247
Cdd:COG0419 354 ELAKLLEERLKELEERLEELEKELEKALERLKQLEEAI 391
 
Name Accession Description Interval E-value
STAT_bind pfam02864
STAT protein, DNA binding domain; STAT proteins (Signal Transducers and Activators of ...
332-582 2.55e-139

STAT protein, DNA binding domain; STAT proteins (Signal Transducers and Activators of Transcription) are a family of transcription factors that are specifically activated to regulate gene transcription when cells encounter cytokines and growth factors. This family represents the DNA binding domain of STAT, which has an ig-like fold. STAT proteins also include an SH2 domain pfam00017.


Pssm-ID: 280939  Cd Length: 244  Bit Score: 413.93  E-value: 2.55e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672    332 FIIEKQPPQVLKTQTKFAATVRLLVGGKLNVHMNPPQVKATIISEQQAKSLLKN--ENTRNECSGEIlNNCCVMEYHQAT 409
Cdd:pfam02864   1 FVVEKQPPQVLKTQTKFSATVRLLVGDKLPEHNNPPKVKVSIDSEAQARALLKGflNMEESQNSGEI-NNTGAMEYHQAS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672    410 GTLSAHFRNMSLKRIKRADRRGAESVTEEKFTVLFESQFSVGsnELVFQVKTLSLPVVVIVHGSQDHNATATVLWDNAFA 489
Cdd:pfam02864  80 GQLSADFRNLQLKEIKRGGRKGNESVTEEKFALLFETQFTLG--GLVFDLQTLSLPVVVIVHGNQEPNAWATILWDNAFA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672    490 EPGRVPFAVPDKVLWPQLCEALNMKFKAevQSNRGLTKENLVFLAQKLFNISSNhledYNSMSVSWSQFNRENLPGWNYT 569
Cdd:pfam02864 158 EPKRVPFFVPPAVPWPQLAEALSWKFSS--GTGRGLSDEQLKYLAEKLFGDPVS----YSDSLVSWSQFCKENLPGRNFT 231
                         250
                  ....*....|...
gi 6755672    570 FWQWFDGVMEVLK 582
Cdd:pfam02864 232 FWEWFDGILDLIK 244
SH2_STAT5a cd10421
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) ...
573-712 1.05e-97

Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 5a proteins; STAT5 is a member of the STAT family of transcription factors. Two highly related proteins, STAT5a and STAT5b are encoded by separate genes, but are 90% identical at the amino acid level. Both STAT5a and STAT5b are ubiquitously expressed and functionally interchangeable. Mice lacking either STAT5a or STAT5b have mild defects in prolactin dependent mammary differentiation or sexually dimorphic growth hormone-dependent effects, respectively. Mice lacking both STAT5a and STAT5b exhibit a perinatal lethal phenotype and have multiple defects, including anemia and a virtual absence of B and T lymphocytes. STAT proteins mediate the signaling of cytokines and a number of growth factors from the receptors of these extracellular signaling molecules to the cell nucleus. STATs are specifically phosphorylated by receptor-associated Janus kinases, receptor tyrosine kinases, or cytoplasmic tyrosine kinases. The phosphorylated STAT molecules dimerize by reciprocal binding of their SH2 domains to the phosphotyrosine residues. These dimeric STATs translocate into the nucleus, bind to specific DNA sequences, and regulate the transcription of their target genes. However there are a number of unphosphorylated STATs that travel between the cytoplasm and nucleus and some STATs that exist as dimers in unstimulated cells that can exert biological functions independent of being activated. There are seven mammalian STAT family members which have been identified: STAT1, STAT2, STAT3, STAT4, STAT5 (STAT5A and STAT5B), and STAT6. There are 6 conserved domains in STAT: N-terminal domain (NTD), coiled-coil domain (CCD), DNA-binding domain (DBD), alpha-helical linker domain (LD), SH2 domain, and transactivation domain (TAD). NTD is involved in dimerization of unphosphorylated STATs monomers and for the tetramerization between STAT1, STAT3, STAT4 and STAT5 on promoters with two or more tandem STAT binding sites. It also plays a role in promoting interactions with transcriptional co-activators such as CREB binding protein (CBP)/p300, as well as being important for nuclear import and deactivation of STATs involving tyrosine de-phosphorylation. CCD interacts with other proteins, such as IFN regulatory protein 9 (IRF-9/p48) with STAT1 and c-JUN with STAT3 and is also thought to participate in the negative regulation of these proteins. Distinct genes are bound to STATs via their DBD domain. This domain is also involved in nuclear translocation of activated STAT1 and STAT3 phosphorylated dimers upon cytokine stimulation. LD links the DNA-binding and SH2 domains and is important for the transcriptional activation of STAT1 in response to IFN-gamma. It also plays a role in protein-protein interactions and has also been implicated in the constitutive nucleocytoplasmic shuttling of unphosphorylated STATs in resting cells. The SH2 domain is necessary for receptor association and tyrosine phosphodimer formation. Residues within this domain may be particularly important for some cellular functions mediated by the STATs as well as residues adjacent to this domain. The TAD interacts with several proteins, namely minichromosome maintenance complex component 5 (MCM5), breast cancer 1 (BRCA1) and CBP/p300. TAD also contains a modulatory phosphorylation site that regulates STAT activity and is necessary for maximal transcription of a number of target genes. The conserved tyrosine residue present in the C-terminus is crucial for dimerization via interaction with the SH2 domain upon the interaction of the ligand with the receptor. STAT activation by tyrosine phosphorylation also determines nuclear import and retention, DNA binding to specific DNA elements in the promoters of responsive genes, and transcriptional activation of STAT dimers. In addition to the SH2 domain there is a coiled-coil domain, a DNA binding domain, and a transactivation domain in the STAT proteins. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198284  Cd Length: 140  Bit Score: 301.96  E-value: 1.05e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672  573 WFDGVMEVLKKHHKPHWNDGAILGFVNKQQAHDLLINKPDGTFLLRFSDSEIGGITIAWKFDSPDRNLWNLKPFTTRDFS 652
Cdd:cd10421   1 WFDGVMEVLKKHHKPHWNDGAILGFVNKQQAHDLLINKPDGTFLLRFSDSEIGGITIAWKFDSPDRNLWNLKPFTTRDFS 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672  653 IRSLADRLGDLNYLIYVFPDRPKDEVFAKYYTPVLAKAVDGYVKPQIKQVVPEFVNASTD 712
Cdd:cd10421  81 IRSLADRLGDLNYLIYVFPDRPKDEVFSKYYTPVLAKAVDGYVKPQIKQVVPEFVSASAD 140
SH2_STAT5 cd10376
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 5 ...
573-707 1.31e-94

Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 5 proteins; STAT5 is a member of the STAT family of transcription factors. Two highly related proteins, STAT5a and STAT5b are encoded by separate genes, but are 90% identical at the amino acid level. Both STAT5a and STAT5b are ubiquitously expressed and functionally interchangeable. Mice lacking either STAT5a or STAT5b have mild defects in prolactin dependent mammary differentiation or sexually dimorphic growth hormone-dependent effects, respectively. Mice lacking both STAT5a and STAT5b exhibit a perinatal lethal phenotype and have multiple defects, including anemia and a virtual absence of B and T lymphocytes. STAT proteins mediate the signaling of cytokines and a number of growth factors from the receptors of these extracellular signaling molecules to the cell nucleus. STATs are specifically phosphorylated by receptor-associated Janus kinases, receptor tyrosine kinases, or cytoplasmic tyrosine kinases. The phosphorylated STAT molecules dimerize by reciprocal binding of their SH2 domains to the phosphotyrosine residues. These dimeric STATs translocate into the nucleus, bind to specific DNA sequences, and regulate the transcription of their target genes. However there are a number of unphosphorylated STATs that travel between the cytoplasm and nucleus and some STATs that exist as dimers in unstimulated cells that can exert biological functions independent of being activated. There are seven mammalian STAT family members which have been identified: STAT1, STAT2, STAT3, STAT4, STAT5 (STAT5A and STAT5B), and STAT6. There are 6 conserved domains in STAT: N-terminal domain (NTD), coiled-coil domain (CCD), DNA-binding domain (DBD), alpha-helical linker domain (LD), SH2 domain, and transactivation domain (TAD). NTD is involved in dimerization of unphosphorylated STATs monomers and for the tetramerization between STAT1, STAT3, STAT4 and STAT5 on promoters with two or more tandem STAT binding sites. It also plays a role in promoting interactions with transcriptional co-activators such as CREB binding protein (CBP)/p300, as well as being important for nuclear import and deactivation of STATs involving tyrosine de-phosphorylation. CCD interacts with other proteins, such as IFN regulatory protein 9 (IRF-9/p48) with STAT1 and c-JUN with STAT3 and is also thought to participate in the negative regulation of these proteins. Distinct genes are bound to STATs via their DBD domain. This domain is also involved in nuclear translocation of activated STAT1 and STAT3 phosphorylated dimers upon cytokine stimulation. LD links the DNA-binding and SH2 domains and is important for the transcriptional activation of STAT1 in response to IFN-gamma. It also plays a role in protein-protein interactions and has also been implicated in the constitutive nucleocytoplasmic shuttling of unphosphorylated STATs in resting cells. The SH2 domain is necessary for receptor association and tyrosine phosphodimer formation. Residues within this domain may be particularly important for some cellular functions mediated by the STATs as well as residues adjacent to this domain. The TAD interacts with several proteins, namely minichromosome maintenance complex component 5 (MCM5), breast cancer 1 (BRCA1) and CBP/p300. TAD also contains a modulatory phosphorylation site that regulates STAT activity and is necessary for maximal transcription of a number of target genes. The conserved tyrosine residue present in the C-terminus is crucial for dimerization via interaction with the SH2 domain upon the interaction of the ligand with the receptor. STAT activation by tyrosine phosphorylation also determines nuclear import and retention, DNA binding to specific DNA elements in the promoters of responsive genes, and transcriptional activation of STAT dimers. In addition to the SH2 domain there is a coiled-coil domain, a DNA binding domain, and a transactivation domain in the STAT proteins.


Pssm-ID: 198239  Cd Length: 137  Bit Score: 293.81  E-value: 1.31e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672  573 WFDGVMEVLKKHHKPHWNDGAILGFVNKQQAHDLLINKPDGTFLLRFSDSEIGGITIAWKFDSPDRNLWNLKPFTTRDFS 652
Cdd:cd10376   1 WFDGVMEVLKKHLKPHWNDGAILGFVNKQQAHDLLINKPDGTFLLRFSDSEIGGITIAWKFDSPDRALWNLMPFTTRDFS 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6755672  653 IRSLADRLGDLNYLIYVFPDRPKDEVFAKYYTPVLAK--AVDGYVKPQIKQVVPEFV 707
Cdd:cd10376  81 IRSLADRLGDLNYLIYVFPDRPKDEVFSKYYTPVLCNpsAVDGYVKPQIKQVVPEFV 137
SH2_STAT5b cd10420
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) ...
573-712 3.22e-88

Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 5b proteins; STAT5 is a member of the STAT family of transcription factors. Two highly related proteins, STAT5a and STAT5b are encoded by separate genes, but are 90% identical at the amino acid level. Both STAT5a and STAT5b are ubiquitously expressed and functionally interchangeable. Mice lacking either STAT5a or STAT5b have mild defects in prolactin dependent mammary differentiation or sexually dimorphic growth hormone-dependent effects, respectively. Mice lacking both STAT5a and STAT5b exhibit a perinatal lethal phenotype and have multiple defects, including anemia and a virtual absence of B and T lymphocytes. STAT proteins mediate the signaling of cytokines and a number of growth factors from the receptors of these extracellular signaling molecules to the cell nucleus. STATs are specifically phosphorylated by receptor-associated Janus kinases, receptor tyrosine kinases, or cytoplasmic tyrosine kinases. The phosphorylated STAT molecules dimerize by reciprocal binding of their SH2 domains to the phosphotyrosine residues. These dimeric STATs translocate into the nucleus, bind to specific DNA sequences, and regulate the transcription of their target genes. However there are a number of unphosphorylated STATs that travel between the cytoplasm and nucleus and some STATs that exist as dimers in unstimulated cells that can exert biological functions independent of being activated. There are seven mammalian STAT family members which have been identified: STAT1, STAT2, STAT3, STAT4, STAT5 (STAT5A and STAT5B), and STAT6. There are 6 conserved domains in STAT: N-terminal domain (NTD), coiled-coil domain (CCD), DNA-binding domain (DBD), alpha-helical linker domain (LD), SH2 domain, and transactivation domain (TAD). NTD is involved in dimerization of unphosphorylated STATs monomers and for the tetramerization between STAT1, STAT3, STAT4 and STAT5 on promoters with two or more tandem STAT binding sites. It also plays a role in promoting interactions with transcriptional co-activators such as CREB binding protein (CBP)/p300, as well as being important for nuclear import and deactivation of STATs involving tyrosine de-phosphorylation. CCD interacts with other proteins, such as IFN regulatory protein 9 (IRF-9/p48) with STAT1 and c-JUN with STAT3 and is also thought to participate in the negative regulation of these proteins. Distinct genes are bound to STATs via their DBD domain. This domain is also involved in nuclear translocation of activated STAT1 and STAT3 phosphorylated dimers upon cytokine stimulation. LD links the DNA-binding and SH2 domains and is important for the transcriptional activation of STAT1 in response to IFN-gamma. It also plays a role in protein-protein interactions and has also been implicated in the constitutive nucleocytoplasmic shuttling of unphosphorylated STATs in resting cells. The SH2 domain is necessary for receptor association and tyrosine phosphodimer formation. Residues within this domain may be particularly important for some cellular functions mediated by the STATs as well as residues adjacent to this domain. The TAD interacts with several proteins, namely minichromosome maintenance complex component 5 (MCM5), breast cancer 1 (BRCA1) and CBP/p300. TAD also contains a modulatory phosphorylation site that regulates STAT activity and is necessary for maximal transcription of a number of target genes. The conserved tyrosine residue present in the C-terminus is crucial for dimerization via interaction with the SH2 domain upon the interaction of the ligand with the receptor. STAT activation by tyrosine phosphorylation also determines nuclear import and retention, DNA binding to specific DNA elements in the promoters of responsive genes, and transcriptional activation of STAT dimers. In addition to the SH2 domain there is a coiled-coil domain, a DNA binding domain, and a transactivation domain in the STAT proteins. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198283  Cd Length: 145  Bit Score: 276.96  E-value: 3.22e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672  573 WFDGVMEVLKKHHKPHWNDGAILGFVNKQQAHDLLINKPDGTFLLRFSDSEIGGITIAWKFDSPDRNLWNLKPFTTRDFS 652
Cdd:cd10420   1 WFDGVMEVLKKHLKPHWNDGAILGFVNKQQAHDLLINKPDGTFLLRFSDSEIGGITIAWKFDSQERMFWNLMPFTTRDFS 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6755672  653 IRSLADRLGDLNYLIYVFPDRPKDEVFAKYYTPV-----LAKAVDGYVKPQIKQVVPEFVNASTD 712
Cdd:cd10420  81 IRSLADRLGDLNYLIYVFPDRPKDEVYSKYYTPVpcepaTAKAVDGYVKPQIKQVVPEFVSASAD 145
STAT_alpha pfam01017
STAT protein, all-alpha domain; STAT proteins (Signal Transducers and Activators of ...
141-330 2.04e-70

STAT protein, all-alpha domain; STAT proteins (Signal Transducers and Activators of Transcription) are a family of transcription factors that are specifically activated to regulate gene transcription when cells encounter cytokines and growth factors. STAT proteins also include an SH2 domain pfam00017.


Pssm-ID: 279369  Cd Length: 178  Bit Score: 230.56  E-value: 2.04e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672    141 HLQINQRFEELRLITQDTENELKKLQQTQEYFIIQYQESLRIQAQfaqlgqlnpqERMSRETALQQKQVSLetwLQREAQ 220
Cdd:pfam01017   1 QQEIEQRLQELRNRVQETEQDIRQLEDLQDEFDFKYKELQKLQEQ----------ERTSSEDKELKQQKEL---LQQMLN 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672    221 TLQQYRVELAEKHQKTLQLLRKQQTIILDDELIQWKRRQQLAGNGGPPEGSLDVLQSWCEKLAEIIWQNRQQIRRAEHLC 300
Cdd:pfam01017  68 ELDQKRKEVLDKLKELLNLLETLQELLLDEELIEWKRRQQLACIGAPPNSNLDQLQNWFTALAELLWQLRQQLKKLEELR 147
                         170       180       190
                  ....*....|....*....|....*....|.
gi 6755672    301 QQLPIPG-PVEEMLAEVNATITDIISALVTS 330
Cdd:pfam01017 148 QKLTYEGdPLTDQLPQLNARVTELLSSLVTS 178
SH2_STAT_family cd09919
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) ...
573-685 8.63e-56

Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) family; STAT proteins mediate the signaling of cytokines and a number of growth factors from the receptors of these extracellular signaling molecules to the cell nucleus. STATs are specifically phosphorylated by receptor-associated Janus kinases, receptor tyrosine kinases, or cytoplasmic tyrosine kinases. The phosphorylated STAT molecules dimerize by reciprocal binding of their SH2 domains to the phosphotyrosine residues. These dimeric STATs translocate into the nucleus, bind to specific DNA sequences, and regulate the transcription of their target genes. However there are a number of unphosphorylated STATs that travel between the cytoplasm and nucleus and some STATs that exist as dimers in unstimulated cells that can exert biological functions independent of being activated by a receptor. There are seven mammalian STAT family members which have been identified: STAT1, STAT2, STAT3, STAT4, STAT5 (STAT5A and STAT5B), and STAT6. There are 6 conserved domains in STAT: N-terminal domain (NTD), coiled-coil domain (CCD), DNA-binding domain (DBD), alpha-helical linker domain (LD), SH2 domain, and transactivation domain (TAD). NTD is involved in dimerization of unphosphorylated STATs monomers and for the tetramerization between STAT1, STAT3, STAT4 and STAT5 on promoters with two or more tandem STAT binding sites. It also plays a role in promoting interactions with transcriptional co-activators such as CREB binding protein (CBP)/p300, as well as being important for nuclear import and deactivation of STATs involving tyrosine de-phosphorylation. The CCD interacts with other proteins, such as IFN regulatory protein 9 (IRF-9/p48) with STAT1 and c-JUN with STAT3 and is also thought to participate in the negative regulation of these proteins. Distinct genes are bound to STATs via their DBD domain. This domain is also involved in nuclear translocation of activated STAT1 and STAT3 phosphorylated dimers upon cytokine stimulation. LD links the DNA-binding and SH2 domains and is important for the transcriptional activation of STAT1 in response to IFN-gamma. It also plays a role in protein-protein interactions and has also been implicated in the constitutive nucleocytoplasmic shuttling of unphosphorylated STATs in resting cells. The SH2 domain is necessary for receptor association and tyrosine phosphodimer formation. Residues within this domain may be particularly important for some cellular functions mediated by the STATs as well as residues adjacent to this domain. The TAD interacts with several proteins, namely minichromosome maintenance complex component 5 (MCM5), breast cancer 1 (BRCA1) and CBP/p300. TAD also contains a modulatory phosphorylation site that regulates STAT activity and is necessary for maximal transcription of a number of target genes. The conserved tyrosine residue present in the C-terminus is crucial for dimerization via interaction with the SH2 domain upon the interaction of the ligand with the receptor. STAT activation by tyrosine phosphorylation also determines nuclear import and retention, DNA binding to specific DNA elements in the promoters of responsive genes, and transcriptional activation of STAT dimers. In addition to the SH2 domain there is a coiled-coil domain, a DNA binding domain, and a transactivation domain in the STAT proteins. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198175  Cd Length: 115  Bit Score: 187.41  E-value: 8.63e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672  573 WFDGVMEVLKKHHKPHWNDGAILGFVNKQQAHDLLINKPDGTFLLRFSDSEIGGITIAWKFDSPD--RNLWNLKPFTTRD 650
Cdd:cd09919   1 WFFAIMLLTKRHLLKLWQDGLIMGFISKEEAEDLLKKKPPGTFLLRFSDSELGGITIAWVNEDPDgqSQVIHLQPYTKKD 80
                        90       100       110
                ....*....|....*....|....*....|....*
gi 6755672  651 FSIRSLADRLGDLNYLIYVFPDRPKDEVFAKYYTP 685
Cdd:cd09919  81 LDIRSLADRIRDLPQLVYLYPDIPKDEAFGKYYSP 115
STAT_int pfam02865
STAT protein, protein interaction domain; STAT proteins (Signal Transducers and Activators of ...
2-124 3.31e-53

STAT protein, protein interaction domain; STAT proteins (Signal Transducers and Activators of Transcription) are a family of transcription factors that are specifically activated to regulate gene transcription when cells encounter cytokines and growth factors. STAT proteins also include an SH2 domain pfam00017.


Pssm-ID: 280940  Cd Length: 122  Bit Score: 180.49  E-value: 3.31e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672      2 AGWIQAQQLQGDALRQMQVLYGQHFPIEVRHYLAQWIESQPWDAIDLDnPQDRGQATQLLEGLVQELQKKAEHQVGEDGF 81
Cdd:pfam02865   1 ALWAKLQQLPGDALEQVQQLYGDHFPIEVRHYLASWIESQDWEDIDPD-PQDESLATVLFHNLLQELQSQASRLSQEDNF 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 6755672     82 LLKIKLGHYATQLQNTYDRCPMELVRCIRHILYNEQRLVREAN 124
Cdd:pfam02865  80 LLKHKLREIARNFQNRYQENPLELARIIRNCLREEKRIVQQAE 122
SH2_STAT6 cd10377
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 6 ...
573-695 4.55e-50

Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 6 proteins; STAT6 mediate signals from the IL-4 receptor. Unlike the other STAT proteins which bind an IFNgamma Activating Sequence (GAS), STAT6 stands out as having a unique binding site preference. This site consists of a palindromic sequence separated by a 3 bp spacer (TTCNNNG-AA)(N3 site). STAT6 is able to bind the GAS site but only at a low affinity. STAT6 may be an important regulator of mitogenesis when cells respond normally to IL-4. There is speculation that the inappropriate activation of STAT6 is involved in uncontrolled cell growth in an oncogenic state. IFNgamma is a negative regulator of STAT6 dependent transcription of target genes. Bcl-6 is another negative regulator of STAT6 activity. Bcl-6 is a transcriptional repressor normally expressed in germinal center B cells and some T cells. IL-4 signaling via STAT6 initially occurs unopposed, but is then dampened by a negative feedback mechanism through the IL-4/Stat6 dependent induction of SOCS1 expression. The IL-4 dependent aspect of Th2 differentiation requires the activation of STAT6. IL-4 signaling and STAT6 appear to play an important role in the immune response. Recently, it was shown that large scale chromatin remodeling of the IL-4 gene occurs as cells differentiate into Th2 effectors is STAT6 dependent. STAT proteins mediate the signaling of cytokines and a number of growth factors from the receptors of these extracellular signaling molecules to the cell nucleus. STATs are specifically phosphorylated by receptor-associated Janus kinases, receptor tyrosine kinases, or cytoplasmic tyrosine kinases. The phosphorylated STAT molecules dimerize by reciprocal binding of their SH2 domains to the phosphotyrosine residues. These dimeric STATs translocate into the nucleus, bind to specific DNA sequences, and regulate the transcription of their target genes. However there are a number of unphosphorylated STATs that travel between the cytoplasm and nucleus and some STATs that exist as dimers in unstimulated cells that can exert biological functions independent of being activated. There are seven mammalian STAT family members which have been identified: STAT1, STAT2, STAT3, STAT4, STAT5 (STAT5A and STAT5B), and STAT6. There are 6 conserved domains in STAT: N-terminal domain (NTD), coiled-coil domain (CCD), DNA-binding domain (DBD), alpha-helical linker domain (LD), SH2 domain, and transactivation domain (TAD). NTD is involved in dimerization of unphosphorylated STATs monomers and for the tetramerization between STAT1, STAT3, STAT4 and STAT5 on promoters with two or more tandem STAT binding sites. It also plays a role in promoting interactions with transcriptional co-activators such as CREB binding protein (CBP)/p300, as well as being important for nuclear import and deactivation of STATs involving tyrosine de-phosphorylation. CCD interacts with other proteins, such as IFN regulatory protein 9 (IRF-9/p48) with STAT1 and c-JUN with STAT3 and is also thought to participate in the negative regulation of these proteins. Distinct genes are bound to STATs via their DBD domain. This domain is also involved in nuclear translocation of activated STAT1 and STAT3 phosphorylated dimers upon cytokine stimulation. LD links the DNA-binding and SH2 domains and is important for the transcriptional activation of STAT1 in response to IFN-gamma. It also plays a role in protein-protein interactions and has also been implicated in the constitutive nucleocytoplasmic shuttling of unphosphorylated STATs in resting cells. The SH2 domain is necessary for receptor association and tyrosine phosphodimer formation. Residues within this domain may be particularly important for some cellular functions mediated by the STATs as well as residues adjacent to this domain. The TAD interacts with several proteins, namely minichromosome maintenance complex component 5 (MCM5), breast cancer 1 (BRCA1) and CBP/p300. TAD also contains a modulatory phosphorylation site that regulates STAT activity and is necessary for maximal transcription of a number of target genes. The conserved tyrosine residue present in the C-terminus is crucial for dimerization via interaction with the SH2 domain upon the interaction of the ligand with the receptor. STAT activation by tyrosine phosphorylation also determines nuclear import and retention, DNA binding to specific DNA elements in the promoters of responsive genes, and transcriptional activation of STAT dimers. In addition to the SH2 domain there is a coiled-coil domain, a DNA binding domain, and a transactivation domain in the STAT proteins. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198240  Cd Length: 129  Bit Score: 171.90  E-value: 4.55e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672  573 WFDGVMEVLKKHHKPHWNDGAILGFVNKQQAHDLLINKPDGTFLLRFSDSEIGGITIAW--KFDSPDRNLWNLKPFTTRD 650
Cdd:cd10377   1 WFDGVLDLTKRCLRSYWSDRLIIGFISKQYVTSLLLNEPDGTFLLRFSDSEIGGITIAHviRGQDGSPQIENIQPFSAKD 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 6755672  651 FSIRSLADRLGDLNYLIYVFPDRPKDEVFAKYYTPVLAKAVDGYV 695
Cdd:cd10377  81 LSIRSLGDRIRDLAQLKNLYPKKPKDEAFRSHYKPEQMKDGRGYV 125
STAT_int smart00964
STAT protein, protein interaction domain; STAT proteins (Signal Transducers and Activators of ...
2-125 1.29e-47

STAT protein, protein interaction domain; STAT proteins (Signal Transducers and Activators of Transcription) are a family of transcription factors that are specifically activated to regulate gene transcription when cells encounter cytokines and growth factors. STAT proteins also include an SH2 domain.


Pssm-ID: 214942  Cd Length: 120  Bit Score: 164.77  E-value: 1.29e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672       2 AGWIQAQQLQGDALRQMQVLYGQHFPIEVRHYLAQWIESQPWDAIDLDNPqdrgQATQLLEGLVQELQKKAEHQVGEDGF 81
Cdd:smart00964   1 SQWAQLQQLDSKFLEQVQQLYGDNFPMELRHYLADWIESQDWELAANDEA----QATRLFHNLLEQLDQQLSRFSQESNF 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 6755672      82 LLKIKLGHYATQLQNTYDRCPMELVRCIRHILYNEQRLVREANN 125
Cdd:smart00964  77 LLKHNLRHIKSNLQSLYQENPLELARIIRNILQEERRILAEASR 120
SH2_STAT4 cd10375
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) ...
573-684 4.27e-25

Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 4proteins; STAT4 mediate signals from the IL-12 receptors. STAT4 is mainly phosphorylated by IL-12-mediated signaling pathway in T cells. STAT4 expression is restricted in myeloid cells, thymus and testis. L-12 is the major cytokine that can activate STAT4, resulting in its tyrosine phosphorylation. The IL-12 receptor has two chains, termed IL-12R 1 and IL-12R 2, and ligand binding results in heterodimer formation and activation of the receptor associated JAK kinases, Jak2 and Tyk2. Phosphorylated STAT4 homo-dimerizes via its SH2 domain, and translocates into nucleus where it can recognize traditional N3 STAT target sequences in IL-12 responsive genes. STAT4 can also be phosphorylated in response to IFN-gamma stimulation through activation of Jak1 and Tyk2 in human. IL-17 can also activate STAT4 in human monocytic leukemia cell lines and IL-2 can induce Jak2 and Stat4 activation in NK cells but not in T cells. T helper 1 (Th1) cells produce IL-2 and IFNgamma, whereas Th2 cells secrete IL-4, IL-5, IL-6 and IL-13. Th1 cells are responsible for cell-mediated/inflammatory immunity and can enhance defenses against infectious agents and cancer, while Th2 cells are essential for humoral immunity and the clearance of parasitic antigens. The most potent factors that can promote Th1 and Th2 differentiation are the cytokines IL-12 and IL-4 respectively Although STAT4 is expressed both in Th1 and Th2 cells, STAT4 can only be phosphorylated by IL-12 which suggests that STAT4 plays an important role in Th1 cell function or development. STAT4 activation leads to Th1 differentiation, including the target genes of STAT4 such as ERM, a transcription factor that belongs to the Ets family of transcription factors. The expression of ERM is specifically induced by IL-12 in wild-type Th1 cells, but not in STAT4-deficient T cells. STAT proteins mediate the signaling of cytokines and a number of growth factors from the receptors of these extracellular signaling molecules to the cell nucleus. STATs are specifically phosphorylated by receptor-associated Janus kinases, receptor tyrosine kinases, or cytoplasmic tyrosine kinases. The phosphorylated STAT molecules dimerize by reciprocal binding of their SH2 domains to the phosphotyrosine residues. These dimeric STATs translocate into the nucleus, bind to specific DNA sequences, and regulate the transcription of their target genes. However there are a number of unphosphorylated STATs that travel between the cytoplasm and nucleus and some STATs that exist as dimers in unstimulated cells that can exert biological functions independent of being activated. There are seven mammalian STAT family members which have been identified: STAT1, STAT2, STAT3, STAT4, STAT5 (STAT5A and STAT5B), and STAT6. There are 6 conserved domains in STAT: N-terminal domain (NTD), coiled-coil domain (CCD), DNA-binding domain (DBD), alpha-helical linker domain (LD), SH2 domain, and transactivation domain (TAD). NTD is involved in dimerization of unphosphorylated STATs monomers and for the tetramerization between STAT1, STAT3, STAT4 and STAT5 on promoters with two or more tandem STAT binding sites. It also plays a role in promoting interactions with transcriptional co-activators such as CREB binding protein (CBP)/p300, as well as being important for nuclear import and deactivation of STATs involving tyrosine de-phosphorylation. CCD interacts with other proteins, such as IFN regulatory protein 9 (IRF-9/p48) with STAT1 and c-JUN with STAT3 and is also thought to participate in the negative regulation of these proteins. Distinct genes are bound to STATs via their DBD domain. This domain is also involved in nuclear translocation of activated STAT1 and STAT3 phosphorylated dimers upon cytokine stimulation. LD links the DNA-binding and SH2 domains and is important for the transcriptional activation of STAT1 in response to IFN-gamma. It also plays a role in protein-protein interactions and has also been implicated in the constitutive nucleocytoplasmic shuttling of unphosphorylated STATs in resting cells. The SH2 domain is necessary for receptor association and tyrosine phosphodimer formation. Residues within this domain may be particularly important for some cellular functions mediated by the STATs as well as residues adjacent to this domain. The TAD interacts with several proteins, namely minichromosome maintenance complex component 5 (MCM5), breast cancer 1 (BRCA1) and CBP/p300. TAD also contains a modulatory phosphorylation site that regulates STAT activity and is necessary for maximal transcription of a number of target genes. The conserved tyrosine residue present in the C-terminus is crucial for dimerization via interaction with the SH2 domain upon the interaction of the ligand with the receptor. STAT activation by tyrosine phosphorylation also determines nuclear import and retention, DNA binding to specific DNA elements in the promoters of responsive genes, and transcriptional activation of STAT dimers. In addition to the SH2 domain there is a coiled-coil domain, a DNA binding domain, and a transactivation domain in the STAT proteins. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198238  Cd Length: 148  Bit Score: 102.65  E-value: 4.27e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672  573 WFDGVMEVLKKHHKPHWNDGAILGFVNKQQAHDLLINKPDGTFLLRFSDSEIGGITIAW--KFDSPDRNLWNLKPFTTRD 650
Cdd:cd10375   1 WLEAILDLIKKHILPLWIDGYIMGFVSKEKERLLLKDKMPGTFLLRFSESHLGGITFTWvdQSENGEVRFHSVEPYNKGR 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 6755672  651 FSIRSLADRLGDL----------NYLIYVFPDRPKDEVFAKYYT 684
Cdd:cd10375  81 LSALPFADILRDYkvimaenipeNPLKYLYPDIPKDKAFGKHYS 124
SH2_STAT3 cd10374
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 3 ...
563-685 2.17e-24

Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 3 proteins; STAT3 encoded by this gene is a member of the STAT protein family. STAT3 mediates the expression of a variety of genes in response to cell stimuli, and plays a key role in many cellular processes such as cell growth and apoptosis. The small GTPase Rac1 regulates the activity of STAT3 and PIAS3 inhibits it. Three alternatively spliced transcript variants encoding distinct isoforms have been described. STAT 3 activation is required for self-renewal of embryonic stem cells (ESCs) and is essential for the differentiation of the TH17 helper T cells. Mutations in the STAT3 gene result in Hyperimmunoglobulin E syndrome and human cancers. STAT3 has been shown to interact with Androgen receptor, C-jun, ELP2, EP300, Epidermal growth factor receptor, Glucocorticoid receptor, HIF1A, Janus kinase 1, KHDRBS1, Mammalian target of rapamycin, MyoD, NDUFA13, NFKB1, Nuclear receptor coactivator 1, Promyelocytic leukemia protein, RAC1, RELA, RET proto-oncogene, RPA2, Src, STAT1, and TRIP10. STAT proteins mediate the signaling of cytokines and a number of growth factors from the receptors of these extracellular signaling molecules to the cell nucleus. STATs are specifically phosphorylated by receptor-associated Janus kinases, receptor tyrosine kinases, or cytoplasmic tyrosine kinases. The phosphorylated STAT molecules dimerize by reciprocal binding of their SH2 domains to the phosphotyrosine residues. These dimeric STATs translocate into the nucleus, bind to specific DNA sequences, and regulate the transcription of their target genes. However there are a number of unphosphorylated STATs that travel between the cytoplasm and nucleus and some STATs that exist as dimers in unstimulated cells that can exert biological functions independent of being activated. There are seven mammalian STAT family members which have been identified: STAT1, STAT2, STAT3, STAT4, STAT5 (STAT5A and STAT5B), and STAT6. There are 6 conserved domains in STAT: N-terminal domain (NTD), coiled-coil domain (CCD), DNA-binding domain (DBD), alpha-helical linker domain (LD), SH2 domain, and transactivation domain (TAD). NTD is involved in dimerization of unphosphorylated STATs monomers and for the tetramerization between STAT1, STAT3, STAT4 and STAT5 on promoters with two or more tandem STAT binding sites. It also plays a role in promoting interactions with transcriptional co-activators such as CREB binding protein (CBP)/p300, as well as being important for nuclear import and deactivation of STATs involving tyrosine de-phosphorylation. CCD interacts with other proteins, such as IFN regulatory protein 9 (IRF-9/p48) with STAT1 and c-JUN with STAT3 and is also thought to participate in the negative regulation of these proteins. Distinct genes are bound to STATs via their DBD domain. This domain is also involved in nuclear translocation of activated STAT1 and STAT3 phosphorylated dimers upon cytokine stimulation. LD links the DNA-binding and SH2 domains and is important for the transcriptional activation of STAT1 in response to IFN-gamma. It also plays a role in protein-protein interactions and has also been implicated in the constitutive nucleocytoplasmic shuttling of unphosphorylated STATs in resting cells. The SH2 domain is necessary for receptor association and tyrosine phosphodimer formation. Residues within this domain may be particularly important for some cellular functions mediated by the STATs as well as residues adjacent to this domain. The TAD interacts with several proteins, namely minichromosome maintenance complex component 5 (MCM5), breast cancer 1 (BRCA1) and CBP/p300. TAD also contains a modulatory phosphorylation site that regulates STAT activity and is necessary for maximal transcription of a number of target genes. The conserved tyrosine residue present in the C-terminus is crucial for dimerization via interaction with the SH2 domain upon the interaction of the ligand with the receptor. STAT activation by tyrosine phosphorylation also determines nuclear import and retention, DNA binding to specific DNA elements in the promoters of responsive genes, and transcriptional activation of STAT dimers. In addition to the SH2 domain there is a coiled-coil domain, a DNA binding domain, and a transactivation domain in the STAT proteins. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198237  Cd Length: 162  Bit Score: 101.26  E-value: 2.17e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672  563 LPGWNYTFWQWFDGVMEVLKKHHKPHWNDGAILGFVNKQQAHDLLINKPDGTFLLRFSD-SEIGGITIAW--KFDSPDRN 639
Cdd:cd10374   1 MAGKGFSFWVWLDNIIDLVKKYILALWNEGYIMGFISKERERAILSTKPPGTFLLRFSEsSKEGGVTFTWveKDISGKTQ 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6755672  640 LWNLKPFTTRDFSIRSLAD-----RLGD-----LNYLIYVFPDRPKDEVFAKYYTP 685
Cdd:cd10374  81 IQSVEPYTKQQLNNMSFAEiimgyKIMDatnilVSPLVYLYPDIPKEEAFGKYCRP 136
SH2_STAT1 cd10372
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 1 ...
573-699 5.94e-22

Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 1 proteins; STAT1 is a member of the STAT family of transcription factors. STAT1 is involved in upregulating genes due to a signal by interferons. STAT1 forms homodimers or heterodimers with STAT3 that bind to the Interferon-Gamma Activated Sequence (GAS) promoter element in response to IFN-gamma stimulation. STAT1 forms a heterodimer with STAT2 that can bind Interferon Stimulated Response Element (ISRE) promoter element in response to either IFN-alpha or IFN-beta stimulation. Binding in both cases leads to an increased expression of ISG (Interferon Stimulated Genes). STAT1 has been shown to interact with protein kinase R, Src, IRF1, STAT3, MCM5, STAT2, CD117, Fanconi anemia, complementation group C, CREB-binding protein, Interleukin 27 receptor, alpha subunit, PIAS1, BRCA1, Epidermal growth factor receptor, PTK2, Mammalian target of rapamycin, IFNAR2, PRKCD, TRADD, C-jun, Calcitriol receptor, ISGF3G, and GNB2L1. STAT proteins mediate the signaling of cytokines and a number of growth factors from the receptors of these extracellular signaling molecules to the cell nucleus. STATs are specifically phosphorylated by receptor-associated Janus kinases, receptor tyrosine kinases, or cytoplasmic tyrosine kinases. The phosphorylated STAT molecules dimerize by reciprocal binding of their SH2 domains to the phosphotyrosine residues. These dimeric STATs translocate into the nucleus, bind to specific DNA sequences, and regulate the transcription of their target genes. However there are a number of unphosphorylated STATs that travel between the cytoplasm and nucleus and some STATs that exist as dimers in unstimulated cells that can exert biological functions independent of being activated. There are seven mammalian STAT family members which have been identified: STAT1, STAT2, STAT3, STAT4, STAT5 (STAT5A and STAT5B), and STAT6. There are 6 conserved domains in STAT: N-terminal domain (NTD), coiled-coil domain (CCD), DNA-binding domain (DBD), alpha-helical linker domain (LD), SH2 domain, and transactivation domain (TAD). NTD is involved in dimerization of unphosphorylated STATs monomers and for the tetramerization between STAT1, STAT3, STAT4 and STAT5 on promoters with two or more tandem STAT binding sites. It also plays a role in promoting interactions with transcriptional co-activators such as CREB binding protein (CBP)/p300, as well as being important for nuclear import and deactivation of STATs involving tyrosine de-phosphorylation. CCD interacts with other proteins, such as IFN regulatory protein 9 (IRF-9/p48) with STAT1 and c-JUN with STAT3 and is also thought to participate in the negative regulation of these proteins. Distinct genes are bound to STATs via their DBD domain. This domain is also involved in nuclear translocation of activated STAT1 and STAT3 phosphorylated dimers upon cytokine stimulation. LD links the DNA-binding and SH2 domains and is important for the transcriptional activation of STAT1 in response to IFN-gamma. It also plays a role in protein-protein interactions and has also been implicated in the constitutive nucleocytoplasmic shuttling of unphosphorylated STATs in resting cells. The SH2 domain is necessary for receptor association and tyrosine phosphodimer formation. Residues within this domain may be particularly important for some cellular functions mediated by the STATs as well as residues adjacent to this domain. The TAD interacts with several proteins, namely minichromosome maintenance complex component 5 (MCM5), breast cancer 1 (BRCA1) and CBP/p300. TAD also contains a modulatory phosphorylation site that regulates STAT activity and is necessary for maximal transcription of a number of target genes. The conserved tyrosine residue present in the C-terminus is crucial for dimerization via interaction with the SH2 domain upon the interaction of the ligand with the receptor. STAT activation by tyrosine phosphorylation also determines nuclear import and retention, DNA binding to specific DNA elements in the promoters of responsive genes, and transcriptional activation of STAT dimers. In addition to the SH2 domain there is a coiled-coil domain, a DNA binding domain, and a transactivation domain in the STAT proteins. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198235  Cd Length: 151  Bit Score: 93.82  E-value: 5.94e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672  573 WFDGVMEVLKKHHKPHWNDGAILGFVNKQQAHDLLINKPDGTFLLRFSDSEI-GGITIAWKFDS---PDRNLWNLKPFTT 648
Cdd:cd10372   1 WIESILELIKKHLLSLWNDGCIMGFISKERERALLKDQQPGTFLLRFSESSReGAITFTWVERSqngGEPDFHAVEPYTK 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672  649 RDFSIRSLADRLGDL----------NYLIYVFPDRPKDEVFAKYYT---------PVLAKAVDGYVKPQI 699
Cdd:cd10372  81 KELSAVTFPDIIRNYkvmaaenipeNPLKYLYPNIDKDHAFGKYYSrpkeapepmELDGPKGTGYIKTEL 150
SH2_STAT2 cd10373
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 2 ...
573-683 3.25e-18

Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 2 proteins; STAT2 is a member of the STAT protein family. In response to interferon, STAT2 forms a complex with STAT1 and IFN regulatory factor family protein p48 (ISGF3G), in which this protein acts as a transactivator, but lacks the ability to bind DNA directly. Transcription adaptor P300/CBP (EP300/CREBBP) has been shown to interact specifically with STAT2, which is thought to be involved in the process of blocking IFN-alpha response by adenovirus. STAT2 has been shown to interact with MED14, CREB-binding protein, SMARCA4, STAT1, IFNAR2, IFNAR1, and ISGF3G. STAT proteins mediate the signaling of cytokines and a number of growth factors from the receptors of these extracellular signaling molecules to the cell nucleus. STATs are specifically phosphorylated by receptor-associated Janus kinases, receptor tyrosine kinases, or cytoplasmic tyrosine kinases. The phosphorylated STAT molecules dimerize by reciprocal binding of their SH2 domains to the phosphotyrosine residues. These dimeric STATs translocate into the nucleus, bind to specific DNA sequences, and regulate the transcription of their target genes. However there are a number of unphosphorylated STATs that travel between the cytoplasm and nucleus and some STATs that exist as dimers in unstimulated cells that can exert biological functions independent of being activated. There are seven mammalian STAT family members which have been identified: STAT1, STAT2, STAT3, STAT4, STAT5 (STAT5A and STAT5B), and STAT6. There are 6 conserved domains in STAT: N-terminal domain (NTD), coiled-coil domain (CCD), DNA-binding domain (DBD), alpha-helical linker domain (LD), SH2 domain, and transactivation domain (TAD). NTD is involved in dimerization of unphosphorylated STATs monomers and for the tetramerization between STAT1, STAT3, STAT4 and STAT5 on promoters with two or more tandem STAT binding sites. It also plays a role in promoting interactions with transcriptional co-activators such as CREB binding protein (CBP)/p300, as well as being important for nuclear import and deactivation of STATs involving tyrosine de-phosphorylation. CCD interacts with other proteins, such as IFN regulatory protein 9 (IRF-9/p48) with STAT1 and c-JUN with STAT3 and is also thought to participate in the negative regulation of these proteins. Distinct genes are bound to STATs via their DBD domain. This domain is also involved in nuclear translocation of activated STAT1 and STAT3 phosphorylated dimers upon cytokine stimulation. LD links the DNA-binding and SH2 domains and is important for the transcriptional activation of STAT1 in response to IFN-gamma. It also plays a role in protein-protein interactions and has also been implicated in the constitutive nucleocytoplasmic shuttling of unphosphorylated STATs in resting cells. The SH2 domain is necessary for receptor association and tyrosine phosphodimer formation. Residues within this domain may be particularly important for some cellular functions mediated by the STATs as well as residues adjacent to this domain. The TAD interacts with several proteins, namely minichromosome maintenance complex component 5 (MCM5), breast cancer 1 (BRCA1) and CBP/p300. TAD also contains a modulatory phosphorylation site that regulates STAT activity and is necessary for maximal transcription of a number of target genes. The conserved tyrosine residue present in the C-terminus is crucial for dimerization via interaction with the SH2 domain upon the interaction of the ligand with the receptor. STAT activation by tyrosine phosphorylation also determines nuclear import and retention, DNA binding to specific DNA elements in the promoters of responsive genes, and transcriptional activation of STAT dimers. In addition to the SH2 domain there is a coiled-coil domain, a DNA binding domain, and a transactivation domain in the STAT proteins. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198236  Cd Length: 151  Bit Score: 83.02  E-value: 3.25e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672  573 WFDGVMEVLKKHHKPHWNDGAILGFVNKQQAHDLLINKPDGTFLLRFSDSEIGGITIAW--KFDSPDRNLWNLKPFTTRD 650
Cdd:cd10373   1 WLDKILELVHDHLKDLWKDGRIMGFVSRNQERRLLKKTISGTFLLRFSETSEGGITCSWveHQDDDKVLIYSVQPYTKEV 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 6755672  651 FS-------IRS---LADRLGDLNYLIYVFPDRPKDEVFAKYY 683
Cdd:cd10373  81 LQslplteiIRHyqlLTEENIPENPLRFLYPRIPRDEAFGCYY 123
SH2 pfam00017
SH2 domain;
589-668 4.66e-14

SH2 domain;


Pssm-ID: 278446  Cd Length: 77  Bit Score: 68.78  E-value: 4.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672    589 WNDGAIlgfvNKQQAHDLLIN-KPDGTFLLRFSDSEIGGITIAWKFDspDRNLWNLKPFTTRDFSIRSLADRLGDLNYLI 667
Cdd:pfam00017   1 WYHGKI----SREEAERLLLNgKPDGTFLVRESESTPGGYTLSVRDD--GKVKHYKIQSTDNGGYYISGGVKFSSLAELV 74

                  .
gi 6755672    668 Y 668
Cdd:pfam00017  75 E 75
SH2 smart00252
Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides ...
596-634 4.50e-10

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


Pssm-ID: 214585  Cd Length: 84  Bit Score: 57.24  E-value: 4.50e-10
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 6755672     596 GFVNKQQAHDLLINKPDGTFLLRFSDSEIGGITIAWKFD 634
Cdd:smart00252   6 GFISREEAEKLLKNEGDGDFLVRDSESSPGDYVLSVRVK 44
SH2 cd00173
Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they ...
596-635 9.52e-08

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  Cd Length: 79  Bit Score: 50.53  E-value: 9.52e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 6755672  596 GFVNKQQAHDLLINKPDGTFLLRFSDSEIGGITIAWKFDS 635
Cdd:cd00173   5 GSISREEAERLLRGKPDGTFLVRESSSEPGDYVLSVRSGD 44
SH2_SH2D2A_SH2D7 cd10349
Src homology 2 domain found in the SH2 domain containing protein 2A and 7 (SH2D2A and SH2D7); ...
596-627 2.36e-04

Src homology 2 domain found in the SH2 domain containing protein 2A and 7 (SH2D2A and SH2D7); SH2D2A and SH7 both contain a single SH2 domain. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 199830  Cd Length: 77  Bit Score: 40.20  E-value: 2.36e-04
                        10        20        30
                ....*....|....*....|....*....|..
gi 6755672  596 GFVNKQQAHDLLINKPDGTFLLRFSDSEIGGI 627
Cdd:cd10349   5 GFITRREAERLLEPKPQGCYLVRFSESAVTFV 36
SH2_Vav_family cd09940
Src homology 2 (SH2) domain found in the Vav family; Vav proteins are involved in several ...
568-634 8.52e-04

Src homology 2 (SH2) domain found in the Vav family; Vav proteins are involved in several processes that require cytoskeletal reorganization, such as the formation of the immunological synapse (IS), phagocytosis, platelet aggregation, spreading, and transformation. Vavs function as guanine nucleotide exchange factors (GEFs) for the Rho/Rac family of GTPases. Vav family members have several conserved motifs/domains including: a leucine-rich region, a leucine-zipper, a calponin homology (CH) domain, an acidic domain, a Dbl-homology (DH) domain, a pleckstrin homology (PH) domain, a cysteine-rich domain, 2 SH3 domains, a proline-rich region, and a SH2 domain. Vavs are the only known Rho GEFs that have both the DH/PH motifs and SH2/SH3 domains in the same protein. The leucine-rich helix-loop-helix (HLH) domain is thought to be involved in protein heterodimerization with other HLH proteins and it may function as a negative regulator by forming inactive heterodimers. The CH domain is usually involved in the association with filamentous actin, but in Vav it controls NFAT stimulation, Ca2+ mobilization, and its transforming activity. Acidic domains are involved in protein-protein interactions and contain regulatory tyrosines. The DH domain is a GDP-GTP exchange factor on Rho/Rac GTPases. The PH domain in involved in interactions with GTP-binding proteins, lipids and/or phosphorylated serine/threonine residues. The SH3 domain is involved in localization of proteins to specific sites within the cell interacting with protein with proline-rich sequences. The SH2 domain mediates a high affinity interaction with tyrosine phosphorylated proteins. There are three Vav mammalian family members: Vav1 which is expressed in the hematopoietic system, Vav2 and Vav3 are more ubiquitously expressed. The members here include insect and amphibian Vavs. 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: 198193  Cd Length: 102  Bit Score: 38.43  E-value: 8.52e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6755672  568 YTFWQWFDGVMEvlkkhhkphwndgailgfvnKQQAHDLLINKPDGTFLLRFSDSEIGGITIAWKFD 634
Cdd:cd09940   2 LSEFLWFVGEME--------------------RDTAENRLENRPDGTYLVRVRPQGETQYALSIKYN 48
SH2_SH2D7 cd10417
Src homology 2 domain found in the SH2 domain containing protein 7 (SH2D7); SH2D7 contains a ...
596-627 2.42e-03

Src homology 2 domain found in the SH2 domain containing protein 7 (SH2D7); SH2D7 contains a single SH2 domain. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 199832  Cd Length: 102  Bit Score: 37.18  E-value: 2.42e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 6755672  596 GFVNKQQAHDLLINKPDGTFLLRFSDSEIGGI 627
Cdd:cd10417  12 GFITRKQTEQLLRDKALGSFLIRLSDRATGYI 43
SH2_SOCS_family cd09923
Src homology 2 (SH2) domain found in suppressor of cytokine signaling (SOCS) family; SH2 ...
596-623 4.16e-03

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


Pssm-ID: 198178  Cd Length: 81  Bit Score: 36.41  E-value: 4.16e-03
                        10        20
                ....*....|....*....|....*...
gi 6755672  596 GFVNKQQAHDLLINKPDGTFLLRfsDSE 623
Cdd:cd09923   5 GGITRYEAEELLAGKPEGTFLVR--DSS 30
SH2_SH2D4B cd10351
Src homology 2 domain found in the SH2 domain containing protein 4B (SH2D4B); SH2D4B contains ...
596-635 6.29e-03

Src homology 2 domain found in the SH2 domain containing protein 4B (SH2D4B); SH2D4B contains a single SH2 domain. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198214  Cd Length: 103  Bit Score: 36.02  E-value: 6.29e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 6755672  596 GFVNKQQAHDLLINKPDGTFLLRFSDsEIGGITIAWKFDS 635
Cdd:cd10351  12 GIISREEAEALLMNATEGSFLVRVSE-KIWGYTLSYRLQS 50
SH2_cSH2_p85_like cd09930
C-terminal Src homology 2 (cSH2) domain found in p85; Phosphoinositide 3-kinases (PI3Ks) are ...
587-622 8.16e-03

C-terminal Src homology 2 (cSH2) domain found in p85; Phosphoinositide 3-kinases (PI3Ks) are essential for cell growth, migration, and survival. p110, the catalytic subunit, is composed of an adaptor-binding domain, a Ras-binding domain, a C2 domain, a helical domain, and a kinase domain. The regulatory unit is called p85 and is composed of an SH3 domain, a RhoGap domain, a N-terminal SH2 (nSH2) domain, a inter SH2 (iSH2) domain, and C-terminal (cSH2) domain. There are 2 inhibitory interactions between p110alpha and p85 of P13K: 1) p85 nSH2 domain with the C2, helical, and kinase domains of p110alpha and 2) p85 iSH2 domain with C2 domain of p110alpha. There are 3 inhibitory interactions between p110beta and p85 of P13K: 1) p85 nSH2 domain with the C2, helical, and kinase domains of p110beta, 2) p85 iSH2 domain with C2 domain of p110alpha, and 3) p85 cSH2 domain with the kinase domain of p110alpha. It is interesting to note that p110beta is oncogenic as a wild type protein while p110alpha lacks this ability. One explanation is the idea that the regulation of p110beta by p85 is unique because of the addition of inhibitory contacts from the cSH2 domain and the loss of contacts in the iSH2 domain. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198184  Cd Length: 104  Bit Score: 35.47  E-value: 8.16e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 6755672  587 PH-----WNDGAIlgfvNKQQAHDLLINKPDGTFLLRFSDS 622
Cdd:cd09930   1 PHhdertWLVGDI----NRTQAEELLRGKPDGTFLIRESST 37
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
141-303 1.06e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.11  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672     141 HLQINQRFEELRLITQDTE------NELKKLQQTQEYFIIQYQESLRI-QAQFAQLGQLNpQERMSRETALQQKQVSLET 213
Cdd:TIGR00618  193 HGKAELLTLRSQLLTLCTPcmpdtyHERKQVLEKELKHLREALQQTQQsHAYLTQKREAQ-EEQLKKQQLLKQLRARIEE 271
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672     214 WLQREAQ-TLQQYRVELAEK------HQKTLQLLRKQQTII----------LDDELIQWKRRQQLAGNGGPPEGSLDVLQ 276
Cdd:TIGR00618  272 LRAQEAVlEETQERINRARKaaplaaHIKAVTQIEQQAQRIhtelqskmrsRAKLLMKRAAHVKQQSSIEEQRRLLQTLH 351
                          170       180
                   ....*....|....*....|....*..
gi 6755672     277 SWCEKLAEiiwQNRQQIRRAEHLCQQL 303
Cdd:TIGR00618  352 SQEIHIRD---AHEVATSIREISCQQH 375
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
58-243 1.24e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.11  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672      58 TQLLEGLVQELQKKAEHQVGEDGFLLKIKLGHYATQLQN-----TYDRcPM-----ELVRCIRHILYNEQRLVREANNCS 127
Cdd:TIGR00618  649 HALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSekeqlTYWK-EMlaqcqTLLRELETHIEEYDREFNEIENAS 727
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672     128 SPAGVLVDAMSQKHLQINQRFEELR------------------LITQDTENELKKLQQTQEYFIIQYQESlriqaqFAQL 189
Cdd:TIGR00618  728 SSLGSDLAAREDALNQSLKELMHQArtvlkarteahfnnneevTAALQTGAELSHLAAEIQFFNRLREED------THLL 801
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 6755672     190 GQLNPQERMSRETALQQKQVSLETWLQREAQTLQQyrveLAEKHQKTLQLLRKQ 243
Cdd:TIGR00618  802 KTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSR----LEEKSATLGEITHQL 851
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
142-262 4.38e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 292337 [Multi-domain]  Cd Length: 516  Bit Score: 39.11  E-value: 4.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672    142 LQINQRFEELRLITQDTENElkklQQTQEyfiiqyqESLRIQAQfaqlgqlnpQERMSRETALQQKQVSLETW--LQREA 219
Cdd:pfam15709 374 LEQQRRAEEIRLRKQRLEEE----RQRQE-------EEERKQRL---------QLQAAQERARQQQEEFRRKLqeLQRKK 433
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 6755672    220 QTLQQYRVELAEKHQKTL--QLLRKQQTI--ILDDELIQWKRRQQLA 262
Cdd:pfam15709 434 QQEEAERAEAEKQRQKELemQLAEEQKRLmeMAEEERLEYQRQKQEA 480
Activator_LAG-3 pfam11498
Transcriptional activator LAG-3; The C.elegans Notch pathway, involved in the control of ...
122-243 5.20e-03

Transcriptional activator LAG-3; The C.elegans Notch pathway, involved in the control of growth, differentiation and patterning in animal development, relies on either of the receptors GLP-1 or LIN-12. Both these receptors promote signalling by the recruitment of LAG-3 to target promoters, where it then acts as a transcriptional activator. LAG-3 works as a ternary complex together with the DNA binding protein, LAG-1.


Pssm-ID: 151935 [Multi-domain]  Cd Length: 476  Bit Score: 38.79  E-value: 5.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672    122 EANNCSSPAGVLVDAMSQKHLQ-----------INQRFEELRLITQDTENELKKLQQTQEYFIIQYQESLRIQAQfaQLG 190
Cdd:pfam11498 302 EAGGDRMPQSAPPPAMNPQHIAqlaqqqnkmrlLQQQEMEMQRIEQQRQQQIMHQHQQQQQQEHQQQQMLLQQQQ--QMH 379
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 6755672    191 QLNPQERMSR----ETALQQKQVSLETWLQREAQTLQQYRVELAEKHQKTLQLLRKQ 243
Cdd:pfam11498 380 QLQQHHQMNGggqfATQAHQHAAYLQQMQHMRLQEQIQHQQQQAQHHQQAQQQHQQP 436
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
139-247 5.41e-03

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 38.97  E-value: 5.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755672  139 QKHLQINQRFEELRLITQDTENELKKLQQTQEYFI-----IQYQESLR--IQAQFAQLGQLNPQ--ERMSRETALQQKQV 209
Cdd:COG0419 274 EELRELERLLEELEEKIERLEELEREIEELEEELEglralLEELEELLekLKSLEERLEKLEEKleKLESELEELAEEKN 353
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 6755672  210 SLETWLQREAQTLQQYRVELAEKHQKTLQLLRKQQTII 247
Cdd:COG0419 354 ELAKLLEERLKELEERLEELEKELEKALERLKQLEEAI 391
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.15
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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