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Conserved domains on  [gi|402886468|ref|XP_003906651|]
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PREDICTED: signal transducer and activator of transcription 2 [Papio anubis]

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List of domain hits

Name Accession Description Interval E-value
SH2_STAT2 cd10373
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 2 ...
556-706 1.28e-103

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: 319.15  E-value: 1.28e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468 556 WLDKILELVHDHLKDLWNDGRIMGFVSRSQERRLLKKTISGTFLLRFSESSEGGITCSWVEHQDDDKVLIYSVQPYTKEV 635
Cdd:cd10373    1 WLDKILELVHDHLKDLWKDGRIMGFVSRNQERRLLKKTISGTFLLRFSETSEGGITCSWVEHQDDDKVLIYSVQPYTKEV 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 402886468 636 LQSLPLTEIIRHYQLLTEENIPENPLRFLYPRIPRDEAFGCYYQEKVNLQERRKYLKHRLIVVSNRQVDEL 706
Cdd:cd10373   81 LQSLPLTEIIRHYQLLTEENIPENPLRFLYPRIPRDEAFGCYYQEKVNLEEREKYLKHKLIVVSNRQVDEL 151
STAT_bind super family cl03748
STAT protein, DNA binding domain; STAT proteins (Signal Transducers and Activators of ...
316-566 1.13e-115

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.


The actual alignment was detected with superfamily member pfam02864:

Pssm-ID: 145817  Cd Length: 254  Bit Score: 354.86  E-value: 1.13e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468  316 FVVETQPCMPQTPHRPLILKTGSKFTVRTRLLVRLQEGNESLTVEVSIDRNPPQLQ---GFRKFNILTSNQKTLTPEKGQ 392
Cdd:pfam02864   1 FVVERQPCMPTHPQRPLVLKTGTQFTAKVRLLVKLQELNYQLKPKVVIDKIVSEKQaqrGFRKFNILGTNTKILNMEESM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468  393 SQGLIWDFGYLTLVEQRSGGSGKGSNKGPLGVTEELHIISFTVKYTYQGLKQELKTDTLPVVIISNMNQLSIAWASVLWF 472
Cdd:pfam02864  81 NGSLAAEFRHLTLREQRLKKGKRANRKGPLSVTEELHAILFETQFTVQGLKIDLETLSLPVVVISNGNQLPNAWASILWY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468  473 NLLSPNLQNQQFFSNPRKAPWSLLGPALSWQFSSYVGRGLNSDQLSMLRNKLFGQNCRTEDPLLSWADFTKRESPPGKLP 552
Cdd:pfam02864 161 NALTEDPRNLVFFLVPPRVTWAQLSEVLSWQFSSEVGRGLNIEQLGFLAEKLFGQNSSYSGGSISWSQFCKENLPGKSFT 240
                         250
                  ....*....|....
gi 402886468  553 FWTWLDKILELVHD 566
Cdd:pfam02864 241 FWQWFDAILDLVKK 254
STAT_alpha pfam01017
STAT protein, all-alpha domain; STAT proteins (Signal Transducers and Activators of ...
139-314 7.35e-58

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: 250297  Cd Length: 182  Bit Score: 195.99  E-value: 7.35e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468  139 ESQQHEIESRILDLRAMMEKLVKSISQLKDQQDVFSFRYK-IQAKGKTP----SLDSHQKKEQQILQETLNELDKRRKEV 213
Cdd:pfam01017   1 SEKQLEIDSKVEDLRNSVQDTEQDIKQLEDLQDEFDFRYKtLQSLIETPangtSLKEHLKQEKLTLQQMLNKLDQKRKEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468  214 LDASKALLGRLTTLI-ELLLPKLEEWKAQQQKACIRAPIDHGLEQLEKWFTAGAKLLFHLRQLLKELKGLSCLVSYQDDP 292
Cdd:pfam01017  81 ADKHQETLGLLEALQnALLDEELIEWKRRQQLACIGGPPEGCLDQLQNWFTALAESLFQLRQQLKKLEELRQKLTYEGDP 160
                         170       180
                  ....*....|....*....|..
gi 402886468  293 LIKGVDLRNAQVTELLQRLLHR 314
Cdd:pfam01017 161 ITKGRPQLNERVTELLKNLVTS 182
STAT_int smart00964
STAT protein, protein interaction domain; STAT proteins (Signal Transducers and Activators of ...
2-124 1.56e-43

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: 154.37  E-value: 1.56e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468     2 AQWEMLQNLDSPFQDQLHQLYSrSLLPVDIRQYLAVWIEDQNWQEAvlGNDDSKATMLFFHFLHQLNYECGRCSQDpDSL 81
Cdd:smart00964   1 SQWAQLQQLDSKFLEQVQQLYG-DNFPMELRHYLADWIESQDWELA--ANDEAQATRLFHNLLEQLDQQLSRFSQE-SNF 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 402886468    82 LLKHNLRKFCRDIQAFSQG-PTQLAEMIFNLLLEEKRILIQAQR 124
Cdd:smart00964  77 LLKHNLRHIKSNLQSLYQEnPLELARIIRNILQEERRILAEASR 120
STAT2_C pfam12188
Signal transducer and activator of transcription 2 C terminal; This domain family is found in ...
783-838 2.80e-31

Signal transducer and activator of transcription 2 C terminal; This domain family is found in eukaryotes, and is approximately 60 amino acids in length. The family is found in association with pfam02865, pfam00017, pfam01017, pfam02864. There is a conserved DLP sequence motif. STATs are involved in transcriptional regulation and are the only regulators known to be modulated by tyrosine phosphorylation. STAT2 forms a trimeric complex with STAT1 and IRF-9 (Interferon Regulatory Factor 9), on activation of the cell by interferon, which is called ISGF3 (Interferon-stimulated gene factor 3). The C terminal domain of STAT2 contains a nuclear export signal (NES) which allows export of STAT2 into the cytoplasm along with any complexed molecules.


:

Pssm-ID: 152623  Cd Length: 56  Bit Score: 117.64  E-value: 2.80e-31
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 402886468  783 SQPVPEPDLPCDLRHLNTEPMEIFRNCVKIEEVMPNGDPLLAGQNTVDEAYVSRPS 838
Cdd:pfam12188   1 SQPVPEPDLPHDLQQLNTEEMEIFRNNINIEEIMPNGDPLLAGQNTVDEAYVSCPS 56
 
Name Accession Description Interval E-value
SH2_STAT2 cd10373
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 2 ...
556-706 1.28e-103

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: 319.15  E-value: 1.28e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468 556 WLDKILELVHDHLKDLWNDGRIMGFVSRSQERRLLKKTISGTFLLRFSESSEGGITCSWVEHQDDDKVLIYSVQPYTKEV 635
Cdd:cd10373    1 WLDKILELVHDHLKDLWKDGRIMGFVSRNQERRLLKKTISGTFLLRFSETSEGGITCSWVEHQDDDKVLIYSVQPYTKEV 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 402886468 636 LQSLPLTEIIRHYQLLTEENIPENPLRFLYPRIPRDEAFGCYYQEKVNLQERRKYLKHRLIVVSNRQVDEL 706
Cdd:cd10373   81 LQSLPLTEIIRHYQLLTEENIPENPLRFLYPRIPRDEAFGCYYQEKVNLEEREKYLKHKLIVVSNRQVDEL 151
STAT_bind pfam02864
STAT protein, DNA binding domain; STAT proteins (Signal Transducers and Activators of ...
316-566 1.13e-115

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: 145817  Cd Length: 254  Bit Score: 354.86  E-value: 1.13e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468  316 FVVETQPCMPQTPHRPLILKTGSKFTVRTRLLVRLQEGNESLTVEVSIDRNPPQLQ---GFRKFNILTSNQKTLTPEKGQ 392
Cdd:pfam02864   1 FVVERQPCMPTHPQRPLVLKTGTQFTAKVRLLVKLQELNYQLKPKVVIDKIVSEKQaqrGFRKFNILGTNTKILNMEESM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468  393 SQGLIWDFGYLTLVEQRSGGSGKGSNKGPLGVTEELHIISFTVKYTYQGLKQELKTDTLPVVIISNMNQLSIAWASVLWF 472
Cdd:pfam02864  81 NGSLAAEFRHLTLREQRLKKGKRANRKGPLSVTEELHAILFETQFTVQGLKIDLETLSLPVVVISNGNQLPNAWASILWY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468  473 NLLSPNLQNQQFFSNPRKAPWSLLGPALSWQFSSYVGRGLNSDQLSMLRNKLFGQNCRTEDPLLSWADFTKRESPPGKLP 552
Cdd:pfam02864 161 NALTEDPRNLVFFLVPPRVTWAQLSEVLSWQFSSEVGRGLNIEQLGFLAEKLFGQNSSYSGGSISWSQFCKENLPGKSFT 240
                         250
                  ....*....|....
gi 402886468  553 FWTWLDKILELVHD 566
Cdd:pfam02864 241 FWQWFDAILDLVKK 254
STAT_alpha pfam01017
STAT protein, all-alpha domain; STAT proteins (Signal Transducers and Activators of ...
139-314 7.35e-58

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: 250297  Cd Length: 182  Bit Score: 195.99  E-value: 7.35e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468  139 ESQQHEIESRILDLRAMMEKLVKSISQLKDQQDVFSFRYK-IQAKGKTP----SLDSHQKKEQQILQETLNELDKRRKEV 213
Cdd:pfam01017   1 SEKQLEIDSKVEDLRNSVQDTEQDIKQLEDLQDEFDFRYKtLQSLIETPangtSLKEHLKQEKLTLQQMLNKLDQKRKEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468  214 LDASKALLGRLTTLI-ELLLPKLEEWKAQQQKACIRAPIDHGLEQLEKWFTAGAKLLFHLRQLLKELKGLSCLVSYQDDP 292
Cdd:pfam01017  81 ADKHQETLGLLEALQnALLDEELIEWKRRQQLACIGGPPEGCLDQLQNWFTALAESLFQLRQQLKKLEELRQKLTYEGDP 160
                         170       180
                  ....*....|....*....|..
gi 402886468  293 LIKGVDLRNAQVTELLQRLLHR 314
Cdd:pfam01017 161 ITKGRPQLNERVTELLKNLVTS 182
STAT_int smart00964
STAT protein, protein interaction domain; STAT proteins (Signal Transducers and Activators of ...
2-124 1.56e-43

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: 154.37  E-value: 1.56e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468     2 AQWEMLQNLDSPFQDQLHQLYSrSLLPVDIRQYLAVWIEDQNWQEAvlGNDDSKATMLFFHFLHQLNYECGRCSQDpDSL 81
Cdd:smart00964   1 SQWAQLQQLDSKFLEQVQQLYG-DNFPMELRHYLADWIESQDWELA--ANDEAQATRLFHNLLEQLDQQLSRFSQE-SNF 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 402886468    82 LLKHNLRKFCRDIQAFSQG-PTQLAEMIFNLLLEEKRILIQAQR 124
Cdd:smart00964  77 LLKHNLRHIKSNLQSLYQEnPLELARIIRNILQEERRILAEASR 120
STAT_int pfam02865
STAT protein, protein interaction domain; STAT proteins (Signal Transducers and Activators of ...
2-125 6.37e-41

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: 251576  Cd Length: 125  Bit Score: 147.05  E-value: 6.37e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468    2 AQWEMLQNLDSPFQDQLHQLYSRSLlPVDIRQYLAVWIEDQNWQEAVLGN--DDSKATMLFFHFLHQLNYECGRCSQDpD 79
Cdd:pfam02865   1 SLWKQLQQLDPEFLEQVQQLYGDNF-PIEVRHYLAQWIESQDWEEAALDNpqDESQATVLFHNLLQELQRQASRLSQE-D 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 402886468   80 SLLLKHNLRKFCRDIQA-FSQGPTQLAEMIFNLLLEEKRILIQAQRA 125
Cdd:pfam02865  79 NFLLRHNLREIARNLQNrYQHNPLELARIIRNCLQEERRIVQEASRA 125
STAT2_C pfam12188
Signal transducer and activator of transcription 2 C terminal; This domain family is found in ...
783-838 2.80e-31

Signal transducer and activator of transcription 2 C terminal; This domain family is found in eukaryotes, and is approximately 60 amino acids in length. The family is found in association with pfam02865, pfam00017, pfam01017, pfam02864. There is a conserved DLP sequence motif. STATs are involved in transcriptional regulation and are the only regulators known to be modulated by tyrosine phosphorylation. STAT2 forms a trimeric complex with STAT1 and IRF-9 (Interferon Regulatory Factor 9), on activation of the cell by interferon, which is called ISGF3 (Interferon-stimulated gene factor 3). The C terminal domain of STAT2 contains a nuclear export signal (NES) which allows export of STAT2 into the cytoplasm along with any complexed molecules.


Pssm-ID: 152623  Cd Length: 56  Bit Score: 117.64  E-value: 2.80e-31
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 402886468  783 SQPVPEPDLPCDLRHLNTEPMEIFRNCVKIEEVMPNGDPLLAGQNTVDEAYVSRPS 838
Cdd:pfam12188   1 SQPVPEPDLPHDLQQLNTEEMEIFRNNINIEEIMPNGDPLLAGQNTVDEAYVSCPS 56
SH2 pfam00017
SH2 domain;
577-648 1.28e-11

SH2 domain;


Pssm-ID: 249511  Cd Length: 77  Bit Score: 61.82  E-value: 1.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468  577 IMGFVSRSQ-ERRLLKKTISGTFLLRFSESSEGGITCSWVehqDDDKVLIYSVQP--------YTKEVLQSLPltEIIRH 647
Cdd:pfam00017   2 YHGKISREEaERLLLNGKPDGTFLVRESESKPGDYTLSVR---DDGRVKHYRIQSldnggyyiSGGVTFNSLP--ELVEH 76

                  .
gi 402886468  648 Y 648
Cdd:pfam00017  77 Y 77
SH2 smart00252
Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides ...
578-649 2.13e-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: 58.39  E-value: 2.13e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 402886468   578 MGFVSRSQERRLLKKTISGTFLLRFSESSEGGITCSWVehqDDDKVLIYSVQP------YTKEVLQSLPLTEIIRHYQ 649
Cdd:smart00252   5 HGFISREEAEKLLKNEGDGDFLVRDSESSPGDYVLSVR---VKGKVKHYRIRRnedgkfYLEGGRKFPSLVELVEHYQ 79
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
115-283 1.69e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins].


Pssm-ID: 233758 [Multi-domain]  Cd Length: 1164  Bit Score: 47.37  E-value: 1.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468   115 EKRILIQAQRAQPEQGEpalVTPVESQQHEIESRILDLRAMMEKLVKSISQLkdQQDVFSFRYKIQakgktpslDSHQKK 194
Cdd:TIGR02169  722 EKEIEQLEQEEEKLKER---LEELEEDLSSLEQEIENVKSELKELEARIEEL--EEDLHKLEEALN--------DLEARL 788
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468   195 EQQILQETLNELDKRRKEVLDASKAL------LGRLTTLIELLLPKLEEWKAQQ-----QKACIRAPIDHGLEQLEKWFT 263
Cdd:TIGR02169  789 SHSRIPEIQAELSKLEEEVSRIEARLreieqkLNRLTLEKEYLEKEIQELQEQRidlkeQIKSIEKEIENLNGKKEELEE 868
                          170       180
                   ....*....|....*....|
gi 402886468   264 AGAKLLFHLRQLLKELKGLS 283
Cdd:TIGR02169  869 ELEELEAALRDLESRLGDLK 888
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
120-263 4.23e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 256862 [Multi-domain]  Cd Length: 1198  Bit Score: 39.29  E-value: 4.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468   120 IQAQRAQPEQGEPALVT---PVESQQHEIESRILDLRAMMEKLvksiSQLKDQQDVFSFRYKIQakgktpsldshQKKEQ 196
Cdd:pfam12128  616 LQSAVAKQKQAEEQLVQanaELEEQKRAEAEARTALKQARLDL----QRLQNEQQSLKDKLELA-----------IAERK 680
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468   197 QILQETLNELDKRRKEVLDASKALLGRL-TTLIELLLPKLEEWKA------------QQQKACIRAPIDHGLEQLEKWFT 263
Cdd:pfam12128  681 QQAETQLRQLDAQLKQLLEQQQAFLEALkDDFRELRTERLAKWQVvegeldnqlaqlSAAIEAARTQAKARLKELKKQYD 760
COG4942 COG4942
Membrane-bound metallopeptidase [Cell division and chromosome partitioning]
83-243 9.09e-03

Membrane-bound metallopeptidase [Cell division and chromosome partitioning]


Pssm-ID: 227278 [Multi-domain]  Cd Length: 420  Bit Score: 37.78  E-value: 9.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468  83 LKHNLRKFCRDIQAFSQgptQLAEMIFNL--LLEEKR--------ILIQAQRAQPEQGEPALVTPVESQQheiESRIL-- 150
Cdd:COG4942   78 LEAQLIETADDLKKLRK---QIADLNARLnaLEVQEReqrrrlaeQLAALQRSGRNPPPALLVSPEDAQR---SVRLAiy 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468 151 ------DLRAMMEKLVKSISQLKDQqdvfsfRYKIQAKGKT-PSLDSHQKKEQQILQETLNELDKrrkevldaskaLLGR 223
Cdd:COG4942  152 ygalnpARAERIDALKATLKQLAAV------RAEIAAEQAElTTLLSEQRAQQAKLAQLLEERKK-----------TLAQ 214
                        170       180
                 ....*....|....*....|
gi 402886468 224 LTTLIELLLPKLEEWKAQQQ 243
Cdd:COG4942  215 LNSELSADQKKLEELRANES 234
 
Name Accession Description Interval E-value
SH2_STAT2 cd10373
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 2 ...
556-706 1.28e-103

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: 319.15  E-value: 1.28e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468 556 WLDKILELVHDHLKDLWNDGRIMGFVSRSQERRLLKKTISGTFLLRFSESSEGGITCSWVEHQDDDKVLIYSVQPYTKEV 635
Cdd:cd10373    1 WLDKILELVHDHLKDLWKDGRIMGFVSRNQERRLLKKTISGTFLLRFSETSEGGITCSWVEHQDDDKVLIYSVQPYTKEV 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 402886468 636 LQSLPLTEIIRHYQLLTEENIPENPLRFLYPRIPRDEAFGCYYQEKVNLQERRKYLKHRLIVVSNRQVDEL 706
Cdd:cd10373   81 LQSLPLTEIIRHYQLLTEENIPENPLRFLYPRIPRDEAFGCYYQEKVNLEEREKYLKHKLIVVSNRQVDEL 151
STAT_bind pfam02864
STAT protein, DNA binding domain; STAT proteins (Signal Transducers and Activators of ...
316-566 1.13e-115

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: 145817  Cd Length: 254  Bit Score: 354.86  E-value: 1.13e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468  316 FVVETQPCMPQTPHRPLILKTGSKFTVRTRLLVRLQEGNESLTVEVSIDRNPPQLQ---GFRKFNILTSNQKTLTPEKGQ 392
Cdd:pfam02864   1 FVVERQPCMPTHPQRPLVLKTGTQFTAKVRLLVKLQELNYQLKPKVVIDKIVSEKQaqrGFRKFNILGTNTKILNMEESM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468  393 SQGLIWDFGYLTLVEQRSGGSGKGSNKGPLGVTEELHIISFTVKYTYQGLKQELKTDTLPVVIISNMNQLSIAWASVLWF 472
Cdd:pfam02864  81 NGSLAAEFRHLTLREQRLKKGKRANRKGPLSVTEELHAILFETQFTVQGLKIDLETLSLPVVVISNGNQLPNAWASILWY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468  473 NLLSPNLQNQQFFSNPRKAPWSLLGPALSWQFSSYVGRGLNSDQLSMLRNKLFGQNCRTEDPLLSWADFTKRESPPGKLP 552
Cdd:pfam02864 161 NALTEDPRNLVFFLVPPRVTWAQLSEVLSWQFSSEVGRGLNIEQLGFLAEKLFGQNSSYSGGSISWSQFCKENLPGKSFT 240
                         250
                  ....*....|....
gi 402886468  553 FWTWLDKILELVHD 566
Cdd:pfam02864 241 FWQWFDAILDLVKK 254
STAT_alpha pfam01017
STAT protein, all-alpha domain; STAT proteins (Signal Transducers and Activators of ...
139-314 7.35e-58

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: 250297  Cd Length: 182  Bit Score: 195.99  E-value: 7.35e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468  139 ESQQHEIESRILDLRAMMEKLVKSISQLKDQQDVFSFRYK-IQAKGKTP----SLDSHQKKEQQILQETLNELDKRRKEV 213
Cdd:pfam01017   1 SEKQLEIDSKVEDLRNSVQDTEQDIKQLEDLQDEFDFRYKtLQSLIETPangtSLKEHLKQEKLTLQQMLNKLDQKRKEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468  214 LDASKALLGRLTTLI-ELLLPKLEEWKAQQQKACIRAPIDHGLEQLEKWFTAGAKLLFHLRQLLKELKGLSCLVSYQDDP 292
Cdd:pfam01017  81 ADKHQETLGLLEALQnALLDEELIEWKRRQQLACIGGPPEGCLDQLQNWFTALAESLFQLRQQLKKLEELRQKLTYEGDP 160
                         170       180
                  ....*....|....*....|..
gi 402886468  293 LIKGVDLRNAQVTELLQRLLHR 314
Cdd:pfam01017 161 ITKGRPQLNERVTELLKNLVTS 182
SH2_STAT4 cd10375
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) ...
556-683 6.32e-48

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: 167.37  E-value: 6.32e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468 556 WLDKILELVHDHLKDLWNDGRIMGFVSRSQERRLLKKTISGTFLLRFSESSEGGITCSWVEHQDDDKVLIYSVQPYTKEV 635
Cdd:cd10375    1 WLEAILDLIKKHILPLWIDGYIMGFVSKEKERLLLKDKMPGTFLLRFSESHLGGITFTWVDQSENGEVRFHSVEPYNKGR 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 402886468 636 LQSLPLTEIIRHYQLLTEENIPENPLRFLYPRIPRDEAFGCYYQEKVN 683
Cdd:cd10375   81 LSALPFADILRDYKVIMAENIPENPLKYLYPDIPKDKAFGKHYSSQPC 128
SH2_STAT1 cd10372
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 1 ...
556-686 3.50e-47

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: 165.47  E-value: 3.50e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468 556 WLDKILELVHDHLKDLWNDGRIMGFVSRSQERRLLKKTISGTFLLRFSESS-EGGITCSWVEH-QDDDKVLIYSVQPYTK 633
Cdd:cd10372    1 WIESILELIKKHLLSLWNDGCIMGFISKERERALLKDQQPGTFLLRFSESSrEGAITFTWVERsQNGGEPDFHAVEPYTK 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 402886468 634 EVLQSLPLTEIIRHYQLLTEENIPENPLRFLYPRIPRDEAFGCYYQEKVNLQE 686
Cdd:cd10372   81 KELSAVTFPDIIRNYKVMAAENIPENPLKYLYPNIDKDHAFGKYYSRPKEAPE 133
SH2_STAT_family cd09919
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) ...
556-680 4.67e-45

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: 158.13  E-value: 4.67e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468 556 WLDKILELVHDHLKDLWNDGRIMGFVSRSQERRLLKKTISGTFLLRFSESSEGGITCSWVEHQDDDKVLIYSVQPYTKEV 635
Cdd:cd09919    1 WFFAIMLLTKRHLLKLWQDGLIMGFISKEEAEDLLKKKPPGTFLLRFSDSELGGITIAWVNEDPDGQSQVIHLQPYTKKD 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 402886468 636 LQSLPLTEIIRHYQllteenipenPLRFLYPRIPRDEAFGCYYQE 680
Cdd:cd09919   81 LDIRSLADRIRDLP----------QLVYLYPDIPKDEAFGKYYSP 115
STAT_int smart00964
STAT protein, protein interaction domain; STAT proteins (Signal Transducers and Activators of ...
2-124 1.56e-43

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: 154.37  E-value: 1.56e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468     2 AQWEMLQNLDSPFQDQLHQLYSrSLLPVDIRQYLAVWIEDQNWQEAvlGNDDSKATMLFFHFLHQLNYECGRCSQDpDSL 81
Cdd:smart00964   1 SQWAQLQQLDSKFLEQVQQLYG-DNFPMELRHYLADWIESQDWELA--ANDEAQATRLFHNLLEQLDQQLSRFSQE-SNF 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 402886468    82 LLKHNLRKFCRDIQAFSQG-PTQLAEMIFNLLLEEKRILIQAQR 124
Cdd:smart00964  77 LLKHNLRHIKSNLQSLYQEnPLELARIIRNILQEERRILAEASR 120
SH2_STAT3 cd10374
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 3 ...
553-699 5.27e-42

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: 151.34  E-value: 5.27e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468 553 FWTWLDKILELVHDHLKDLWNDGRIMGFVSRSQERRLLKKTISGTFLLRFSESS-EGGITCSWVEHQDDDKVLIYSVQPY 631
Cdd:cd10374    8 FWVWLDNIIDLVKKYILALWNEGYIMGFISKERERAILSTKPPGTFLLRFSESSkEGGVTFTWVEKDISGKTQIQSVEPY 87
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 402886468 632 TKEVLQSLPLTEIIRHYQLLTEENIPENPLRFLYPRIPRDEAFGCYYQEKVNLQER------RKYLKHRLIVVS 699
Cdd:cd10374   88 TKQQLNNMSFAEIIMGYKIMDATNILVSPLVYLYPDIPKEEAFGKYCRPESQEHPEadpgsaAPYLKTKFICVT 161
STAT_int pfam02865
STAT protein, protein interaction domain; STAT proteins (Signal Transducers and Activators of ...
2-125 6.37e-41

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: 251576  Cd Length: 125  Bit Score: 147.05  E-value: 6.37e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468    2 AQWEMLQNLDSPFQDQLHQLYSRSLlPVDIRQYLAVWIEDQNWQEAVLGN--DDSKATMLFFHFLHQLNYECGRCSQDpD 79
Cdd:pfam02865   1 SLWKQLQQLDPEFLEQVQQLYGDNF-PIEVRHYLAQWIESQDWEEAALDNpqDESQATVLFHNLLQELQRQASRLSQE-D 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 402886468   80 SLLLKHNLRKFCRDIQA-FSQGPTQLAEMIFNLLLEEKRILIQAQRA 125
Cdd:pfam02865  79 NFLLRHNLREIARNLQNrYQHNPLELARIIRNCLQEERRIVQEASRA 125
STAT2_C pfam12188
Signal transducer and activator of transcription 2 C terminal; This domain family is found in ...
783-838 2.80e-31

Signal transducer and activator of transcription 2 C terminal; This domain family is found in eukaryotes, and is approximately 60 amino acids in length. The family is found in association with pfam02865, pfam00017, pfam01017, pfam02864. There is a conserved DLP sequence motif. STATs are involved in transcriptional regulation and are the only regulators known to be modulated by tyrosine phosphorylation. STAT2 forms a trimeric complex with STAT1 and IRF-9 (Interferon Regulatory Factor 9), on activation of the cell by interferon, which is called ISGF3 (Interferon-stimulated gene factor 3). The C terminal domain of STAT2 contains a nuclear export signal (NES) which allows export of STAT2 into the cytoplasm along with any complexed molecules.


Pssm-ID: 152623  Cd Length: 56  Bit Score: 117.64  E-value: 2.80e-31
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 402886468  783 SQPVPEPDLPCDLRHLNTEPMEIFRNCVKIEEVMPNGDPLLAGQNTVDEAYVSRPS 838
Cdd:pfam12188   1 SQPVPEPDLPHDLQQLNTEEMEIFRNNINIEEIMPNGDPLLAGQNTVDEAYVSCPS 56
SH2_STAT6 cd10377
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 6 ...
556-681 2.62e-25

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: 102.94  E-value: 2.62e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468 556 WLDKILELVHDHLKDLWNDGRIMGFVSRSQERRLLKKTISGTFLLRFSESSEGGITCSWVEHQDDDKVLIYSVQPYTKEV 635
Cdd:cd10377    1 WFDGVLDLTKRCLRSYWSDRLIIGFISKQYVTSLLLNEPDGTFLLRFSDSEIGGITIAHVIRGQDGSPQIENIQPFSAKD 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 402886468 636 LQSLPLTEIIRhyqllteeNIPEnpLRFLYPRIPRDEAFGCYYQEK 681
Cdd:cd10377   81 LSIRSLGDRIR--------DLAQ--LKNLYPKKPKDEAFRSHYKPE 116
SH2_STAT5b cd10420
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) ...
556-678 2.82e-17

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: 80.12  E-value: 2.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468 556 WLDKILELVHDHLKDLWNDGRIMGFVSRSQERRLLKKTISGTFLLRFSESSEGGITCSWveHQDDDKVLIYSVQPYTKEV 635
Cdd:cd10420    1 WFDGVMEVLKKHLKPHWNDGAILGFVNKQQAHDLLINKPDGTFLLRFSDSEIGGITIAW--KFDSQERMFWNLMPFTTRD 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 402886468 636 LQSLPLTEIIRHYQLLTeenipenplrFLYPRIPRDEAFGCYY 678
Cdd:cd10420   79 FSIRSLADRLGDLNYLI----------YVFPDRPKDEVYSKYY 111
SH2_STAT5 cd10376
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 5 ...
556-678 2.93e-17

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: 80.02  E-value: 2.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468 556 WLDKILELVHDHLKDLWNDGRIMGFVSRSQERRLLKKTISGTFLLRFSESSEGGITCSWvEHQDDDKVLiYSVQPYTKEV 635
Cdd:cd10376    1 WFDGVMEVLKKHLKPHWNDGAILGFVNKQQAHDLLINKPDGTFLLRFSDSEIGGITIAW-KFDSPDRAL-WNLMPFTTRD 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 402886468 636 LQSLPLTEIIRHYqllteenipeNPLRFLYPRIPRDEAFGCYY 678
Cdd:cd10376   79 FSIRSLADRLGDL----------NYLIYVFPDRPKDEVFSKYY 111
SH2_STAT5a cd10421
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) ...
556-678 2.04e-16

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: 77.39  E-value: 2.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468 556 WLDKILELVHDHLKDLWNDGRIMGFVSRSQERRLLKKTISGTFLLRFSESSEGGITCSWVEHQDDDKvlIYSVQPYTKEV 635
Cdd:cd10421    1 WFDGVMEVLKKHHKPHWNDGAILGFVNKQQAHDLLINKPDGTFLLRFSDSEIGGITIAWKFDSPDRN--LWNLKPFTTRD 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 402886468 636 LQSLPLTEIIRHYqllteenipeNPLRFLYPRIPRDEAFGCYY 678
Cdd:cd10421   79 FSIRSLADRLGDL----------NYLIYVFPDRPKDEVFSKYY 111
SH2 pfam00017
SH2 domain;
577-648 1.28e-11

SH2 domain;


Pssm-ID: 249511  Cd Length: 77  Bit Score: 61.82  E-value: 1.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468  577 IMGFVSRSQ-ERRLLKKTISGTFLLRFSESSEGGITCSWVehqDDDKVLIYSVQP--------YTKEVLQSLPltEIIRH 647
Cdd:pfam00017   2 YHGKISREEaERLLLNGKPDGTFLVRESESKPGDYTLSVR---DDGRVKHYRIQSldnggyyiSGGVTFNSLP--ELVEH 76

                  .
gi 402886468  648 Y 648
Cdd:pfam00017  77 Y 77
SH2 smart00252
Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides ...
578-649 2.13e-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: 58.39  E-value: 2.13e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 402886468   578 MGFVSRSQERRLLKKTISGTFLLRFSESSEGGITCSWVehqDDDKVLIYSVQP------YTKEVLQSLPLTEIIRHYQ 649
Cdd:smart00252   5 HGFISREEAEKLLKNEGDGDFLVRDSESSPGDYVLSVR---VKGKVKHYRIRRnedgkfYLEGGRKFPSLVELVEHYQ 79
SH2 cd00173
Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they ...
579-648 5.69e-06

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: 45.14  E-value: 5.69e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 402886468 579 GFVSRSQERRLLKKTISGTFLLRFSESSEGGITCSWVEHQDDDK-VLIYSVQPYTKEVLQSLP----LTEIIRHY 648
Cdd:cd00173    5 GSISREEAERLLRGKPDGTFLVRESSSEPGDYVLSVRSGDGKVKhYLIERNEGGYYLLGGSGRtfpsLPELVEHY 79
SH2_ABL cd09935
Src homology 2 (SH2) domain found in Abelson murine lymphosarcoma virus (ABL) proteins; ...
579-629 1.07e-03

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


Pssm-ID: 198189  Cd Length: 94  Bit Score: 38.14  E-value: 1.07e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 402886468 579 GFVSRSQERRLLKKTISGTFLLRFSESSEGGITCSwVEHqdDDKVLIYSVQ 629
Cdd:cd09935    8 GPISRNAAEYLLSSGINGSFLVRESESSPGQYSIS-LRY--DGRVYHYRIS 55
SH2_SH2D2A_SH2D7 cd10349
Src homology 2 domain found in the SH2 domain containing protein 2A and 7 (SH2D2A and SH2D7); ...
579-610 5.32e-03

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: 35.96  E-value: 5.32e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 402886468 579 GFVSRSQERRLLKKTISGTFLLRFSESSEGGI 610
Cdd:cd10349    5 GFITRREAERLLEPKPQGCYLVRFSESAVTFV 36
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
115-283 1.69e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins].


Pssm-ID: 233758 [Multi-domain]  Cd Length: 1164  Bit Score: 47.37  E-value: 1.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468   115 EKRILIQAQRAQPEQGEpalVTPVESQQHEIESRILDLRAMMEKLVKSISQLkdQQDVFSFRYKIQakgktpslDSHQKK 194
Cdd:TIGR02169  722 EKEIEQLEQEEEKLKER---LEELEEDLSSLEQEIENVKSELKELEARIEEL--EEDLHKLEEALN--------DLEARL 788
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468   195 EQQILQETLNELDKRRKEVLDASKAL------LGRLTTLIELLLPKLEEWKAQQ-----QKACIRAPIDHGLEQLEKWFT 263
Cdd:TIGR02169  789 SHSRIPEIQAELSKLEEEVSRIEARLreieqkLNRLTLEKEYLEKEIQELQEQRidlkeQIKSIEKEIENLNGKKEELEE 868
                          170       180
                   ....*....|....*....|
gi 402886468   264 AGAKLLFHLRQLLKELKGLS 283
Cdd:TIGR02169  869 ELEELEAALRDLESRLGDLK 888
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
120-263 4.23e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 256862 [Multi-domain]  Cd Length: 1198  Bit Score: 39.29  E-value: 4.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468   120 IQAQRAQPEQGEPALVT---PVESQQHEIESRILDLRAMMEKLvksiSQLKDQQDVFSFRYKIQakgktpsldshQKKEQ 196
Cdd:pfam12128  616 LQSAVAKQKQAEEQLVQanaELEEQKRAEAEARTALKQARLDL----QRLQNEQQSLKDKLELA-----------IAERK 680
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468   197 QILQETLNELDKRRKEVLDASKALLGRL-TTLIELLLPKLEEWKA------------QQQKACIRAPIDHGLEQLEKWFT 263
Cdd:pfam12128  681 QQAETQLRQLDAQLKQLLEQQQAFLEALkDDFRELRTERLAKWQVvegeldnqlaqlSAAIEAARTQAKARLKELKKQYD 760
COG4942 COG4942
Membrane-bound metallopeptidase [Cell division and chromosome partitioning]
83-243 9.09e-03

Membrane-bound metallopeptidase [Cell division and chromosome partitioning]


Pssm-ID: 227278 [Multi-domain]  Cd Length: 420  Bit Score: 37.78  E-value: 9.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468  83 LKHNLRKFCRDIQAFSQgptQLAEMIFNL--LLEEKR--------ILIQAQRAQPEQGEPALVTPVESQQheiESRIL-- 150
Cdd:COG4942   78 LEAQLIETADDLKKLRK---QIADLNARLnaLEVQEReqrrrlaeQLAALQRSGRNPPPALLVSPEDAQR---SVRLAiy 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468 151 ------DLRAMMEKLVKSISQLKDQqdvfsfRYKIQAKGKT-PSLDSHQKKEQQILQETLNELDKrrkevldaskaLLGR 223
Cdd:COG4942  152 ygalnpARAERIDALKATLKQLAAV------RAEIAAEQAElTTLLSEQRAQQAKLAQLLEERKK-----------TLAQ 214
                        170       180
                 ....*....|....*....|
gi 402886468 224 LTTLIELLLPKLEEWKAQQQ 243
Cdd:COG4942  215 LNSELSADQKKLEELRANES 234
COG1579 COG1579
Zn-ribbon protein, possibly nucleic acid-binding [General function prediction only]
111-260 9.59e-03

Zn-ribbon protein, possibly nucleic acid-binding [General function prediction only]


Pssm-ID: 224495 [Multi-domain]  Cd Length: 239  Bit Score: 37.35  E-value: 9.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402886468 111 LLLEEKRILIQAQRAQPEQGE-PALVTPVESQQHEIESRILDLRAMMEKLVKSISQLkdQQDVFSFRYKI------QAKG 183
Cdd:COG1579    8 SLLAIQKLDLEKDRLEPRIKEiRKALKKAKAELEALNKALEALEIELEDLENQVSQL--ESEIQEIRERIkraeekLSAV 85
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 402886468 184 KTPSLDSHQKKEQQILQETLNELDKRRKEVLDAskalLGRLTTLIELLLPKLEewKAQQQKACIRAPIDHGLEQLEK 260
Cdd:COG1579   86 KDERELRALNIEIQIAKERINSLEDELAELMEE----IEKLEKEIEDLKERLE--RLEKNLAEAEARLEEEVAEIRE 156
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • 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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