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Conserved domains on  [gi|9910572|ref|NP_064347|]
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signal transducer and activator of transcription 2 [Mus musculus]

Protein Classification

STAT_bind and SH2_STAT2 domain-containing protein (domain architecture ID 12223530)

protein containing domains STAT_int, STAT_alpha, STAT_bind, and SH2_STAT2

Graphical summary

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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 ...
554-704 6.58e-102

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: 317.22  E-value: 6.58e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572  554 WLDKILELVHDHLKDLWKDGRIMGFVSRNQERRLLKKMLSGTFLLRFSETSEGGITCSWVEHQDDDKVEIYSVQPYTKEV 633
Cdd:cd10373   1 WLDKILELVHDHLKDLWKDGRIMGFVSRNQERRLLKKTISGTFLLRFSETSEGGITCSWVEHQDDDKVLIYSVQPYTKEV 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9910572  634 LQSLPLTEIIRHYQVLAEENIPENPLRFLYPRIPRDEAFGCYYQEKVNFEEQRKYLKHKLIVISNRQVDEL 704
Cdd:cd10373  81 LQSLPLTEIIRHYQLLTEENIPENPLRFLYPRIPRDEAFGCYYQEKVNLEEREKYLKHKLIVVSNRQVDEL 151
STAT_bind pfam02864
STAT protein, DNA binding domain; STAT proteins (Signal Transducers and Activators of ...
316-563 5.24e-83

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: 308483  Cd Length: 246  Bit Score: 270.24  E-value: 5.24e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572    316 FVVETQPcmpqtlhrPLILKTGNKFTVRTRLLV--RLQEGSESLKAEVSVDRNSD----LPGFRKFNILTS-------NQ 382
Cdd:pfam02864   1 FVVEKQP--------PQVLKTQTKFSATVRLLVggKLPEHNNPPKVKVSIDSESQaralLKGFTKVNMEESqnsgeinNT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572    383 KTLTPEEGQRQgLIWDFGFLTLVEQRAvgagKGNKGPLAVTEELHVISFVVEYVYQGLKMKLQTDTLPVVIISNMNQLSI 462
Cdd:pfam02864  73 GALEYHQTSGQ-LSADFRNLQLKEIKR----GGRKGTESVTEEKFALLFQTQFTLGELVFDLQTLSLPVVVIVHGNQEPN 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572    463 AWASILWFNMlSPNPKNQQFFCqAPKAPWSLLGPVLSWQFSSYVGRGLDSEQLGMLRTKLFGKSCKMEDALLSWVDFCKR 542
Cdd:pfam02864 148 AWATILWDNA-FAEPGRVPFFV-PPKVPWPQLAEALSWKFSSGTGRGLSDEQLNYLAEKLFGDPSSYPDSLVSWSQFCKE 225
                         250       260
                  ....*....|....*....|.
gi 9910572    543 ESPPGKIPFWTWLDKILELVH 563
Cdd:pfam02864 226 NLPGRNFTFWEWFDGILDLIK 246
STAT_alpha pfam01017
STAT protein, all-alpha domain; STAT proteins (Signal Transducers and Activators of ...
141-314 5.93e-54

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: 307245  Cd Length: 177  Bit Score: 186.64  E-value: 5.93e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572    141 QLEIENRIQGLHVDIEFLVRSIRQLKDEQDVFSFRYTVFSLKKT---SSSDPHQSQQAQLVQATANKVDRMRKEVLDISK 217
Cdd:pfam01017   1 QQEIEQRLQELRNRVQETEQDIRQLEDLQDEFDFKYKELQKLEAqnnDSEEKELKQEKELLQQMLNELDQKRKEVLDKLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572    218 GLVGRLTTLVDLLL-PKLDEWKVQQQKSCIGAPPPELqLEQLEQWLTAGAKFLFHLRQLLKQLKEMSHMLRYKGDMFGQG 296
Cdd:pfam01017  81 ELLNLLETLQELLLdEELIEWKRRQQLACIGAPPNSC-LDQLQNWFTALAELLWQLRQQLKKLEELRQKLTYEGDPLTDG 159
                         170
                  ....*....|....*...
gi 9910572    297 VDLQNAQVMELLQRLLQR 314
Cdd:pfam01017 160 LPQLNARVTELLSSLVTS 177
STAT_int smart00964
STAT protein, protein interaction domain; STAT proteins (Signal Transducers and Activators of ...
2-123 4.08e-40

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: 145.90  E-value: 4.08e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572       2 AQWEMLQNLDSLFLDQLHQVYSQSiLPMDVRQHLATWIEDQNWREAALgsDDAKANMLYFSILDQL-NQWDHYSSDSNhF 80
Cdd:smart00964   1 SQWAQLQQLDSKFLEQVQQLYGDN-FPMELRHYLADWIESQDWELAAN--DEAQATRLFHNLLEQLdQQLSRFSQESN-F 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 9910572      81 LLQHNLRKFSRDIQTFPNG-PTQLAEMIFNLLLEEQRILNQAQR 123
Cdd:smart00964  77 LLKHNLRHIKSNLQSLYQEnPLELARIIRNILQEERRILAEASR 120
STAT2_C pfam12188
Signal transducer and activator of transcription 2 C terminal; This domain family is found in ...
853-907 5.83e-20

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: 314971  Cd Length: 56  Bit Score: 86.74  E-value: 5.83e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 9910572    853 LQQPSESDLPEDLQQISVEDLKKLSNP-STEYITTNENPMLAGESSGDETSIPYHS 907
Cdd:pfam12188   1 SQPVPEPDLPHDLQHLNTEDMEIFRNSiNIEEIMPNGDPLLAGQNTGDEAYISCPS 56
Trypan_PARP super family cl25865
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ...
742-820 9.19e-08

Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei procyclic acidic repetitive protein (PARP) like sequences. The procyclic acidic repetitive protein (parp) genes of Trypanosoma brucei encode a small family of abundant surface proteins whose expression is restricted to the procyclic form of the parasite. They are found at two unlinked loci, parpA and parpB; transcription of both loci is developmentally regulated.


The actual alignment was detected with superfamily member pfam05887:

Pssm-ID: 330686  Cd Length: 145  Bit Score: 52.65  E-value: 9.19e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9910572    742 GTELKVDPILSTAPQVLLEPAPQVLLEPAPQVPLEPAPQVLLEPAPQVLLEPAPQVLLEPAPqvllEPAPQVQLEPAPQ 820
Cdd:pfam05887  47 GTKVGADDTNGTDPDDEPEEEEEPEPEEEGEEEPEPEEEGEEEPEPEETGEEEPEPEPEPEP----EPEPEPEPEPEPE 121
 
Name Accession Description Interval E-value
SH2_STAT2 cd10373
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 2 ...
554-704 6.58e-102

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: 317.22  E-value: 6.58e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572  554 WLDKILELVHDHLKDLWKDGRIMGFVSRNQERRLLKKMLSGTFLLRFSETSEGGITCSWVEHQDDDKVEIYSVQPYTKEV 633
Cdd:cd10373   1 WLDKILELVHDHLKDLWKDGRIMGFVSRNQERRLLKKTISGTFLLRFSETSEGGITCSWVEHQDDDKVLIYSVQPYTKEV 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9910572  634 LQSLPLTEIIRHYQVLAEENIPENPLRFLYPRIPRDEAFGCYYQEKVNFEEQRKYLKHKLIVISNRQVDEL 704
Cdd:cd10373  81 LQSLPLTEIIRHYQLLTEENIPENPLRFLYPRIPRDEAFGCYYQEKVNLEEREKYLKHKLIVVSNRQVDEL 151
STAT_bind pfam02864
STAT protein, DNA binding domain; STAT proteins (Signal Transducers and Activators of ...
316-563 5.24e-83

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: 308483  Cd Length: 246  Bit Score: 270.24  E-value: 5.24e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572    316 FVVETQPcmpqtlhrPLILKTGNKFTVRTRLLV--RLQEGSESLKAEVSVDRNSD----LPGFRKFNILTS-------NQ 382
Cdd:pfam02864   1 FVVEKQP--------PQVLKTQTKFSATVRLLVggKLPEHNNPPKVKVSIDSESQaralLKGFTKVNMEESqnsgeinNT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572    383 KTLTPEEGQRQgLIWDFGFLTLVEQRAvgagKGNKGPLAVTEELHVISFVVEYVYQGLKMKLQTDTLPVVIISNMNQLSI 462
Cdd:pfam02864  73 GALEYHQTSGQ-LSADFRNLQLKEIKR----GGRKGTESVTEEKFALLFQTQFTLGELVFDLQTLSLPVVVIVHGNQEPN 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572    463 AWASILWFNMlSPNPKNQQFFCqAPKAPWSLLGPVLSWQFSSYVGRGLDSEQLGMLRTKLFGKSCKMEDALLSWVDFCKR 542
Cdd:pfam02864 148 AWATILWDNA-FAEPGRVPFFV-PPKVPWPQLAEALSWKFSSGTGRGLSDEQLNYLAEKLFGDPSSYPDSLVSWSQFCKE 225
                         250       260
                  ....*....|....*....|.
gi 9910572    543 ESPPGKIPFWTWLDKILELVH 563
Cdd:pfam02864 226 NLPGRNFTFWEWFDGILDLIK 246
STAT_alpha pfam01017
STAT protein, all-alpha domain; STAT proteins (Signal Transducers and Activators of ...
141-314 5.93e-54

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: 307245  Cd Length: 177  Bit Score: 186.64  E-value: 5.93e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572    141 QLEIENRIQGLHVDIEFLVRSIRQLKDEQDVFSFRYTVFSLKKT---SSSDPHQSQQAQLVQATANKVDRMRKEVLDISK 217
Cdd:pfam01017   1 QQEIEQRLQELRNRVQETEQDIRQLEDLQDEFDFKYKELQKLEAqnnDSEEKELKQEKELLQQMLNELDQKRKEVLDKLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572    218 GLVGRLTTLVDLLL-PKLDEWKVQQQKSCIGAPPPELqLEQLEQWLTAGAKFLFHLRQLLKQLKEMSHMLRYKGDMFGQG 296
Cdd:pfam01017  81 ELLNLLETLQELLLdEELIEWKRRQQLACIGAPPNSC-LDQLQNWFTALAELLWQLRQQLKKLEELRQKLTYEGDPLTDG 159
                         170
                  ....*....|....*...
gi 9910572    297 VDLQNAQVMELLQRLLQR 314
Cdd:pfam01017 160 LPQLNARVTELLSSLVTS 177
STAT_int smart00964
STAT protein, protein interaction domain; STAT proteins (Signal Transducers and Activators of ...
2-123 4.08e-40

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: 145.90  E-value: 4.08e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572       2 AQWEMLQNLDSLFLDQLHQVYSQSiLPMDVRQHLATWIEDQNWREAALgsDDAKANMLYFSILDQL-NQWDHYSSDSNhF 80
Cdd:smart00964   1 SQWAQLQQLDSKFLEQVQQLYGDN-FPMELRHYLADWIESQDWELAAN--DEAQATRLFHNLLEQLdQQLSRFSQESN-F 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 9910572      81 LLQHNLRKFSRDIQTFPNG-PTQLAEMIFNLLLEEQRILNQAQR 123
Cdd:smart00964  77 LLKHNLRHIKSNLQSLYQEnPLELARIIRNILQEERRILAEASR 120
STAT_int pfam02865
STAT protein, protein interaction domain; STAT proteins (Signal Transducers and Activators of ...
2-122 6.45e-32

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: 308484  Cd Length: 122  Bit Score: 122.71  E-value: 6.45e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572      2 AQWEMLQNLDSLFLDQLHQVYSQSiLPMDVRQHLATWIEDQNWREAALGS-DDAKANMLYFSILDQL-NQWDHYSSDSNh 79
Cdd:pfam02865   1 ALWAKLQQLPGDALEQVQQLYGDH-FPIEVRHYLASWIESQDWEDADPDPqDESQATVLFHNLLQELqSQASRLSQEDN- 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 9910572     80 FLLQHNLRKFSRDIQ-TFPNGPTQLAEMIFNLLLEEQRILNQAQ 122
Cdd:pfam02865  79 FLLKHKLREIARNFQnRYQDNPLELARIIRNCLREEKRIVQQAE 122
STAT2_C pfam12188
Signal transducer and activator of transcription 2 C terminal; This domain family is found in ...
853-907 5.83e-20

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: 314971  Cd Length: 56  Bit Score: 86.74  E-value: 5.83e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 9910572    853 LQQPSESDLPEDLQQISVEDLKKLSNP-STEYITTNENPMLAGESSGDETSIPYHS 907
Cdd:pfam12188   1 SQPVPEPDLPHDLQHLNTEDMEIFRNSiNIEEIMPNGDPLLAGQNTGDEAYISCPS 56
SH2 pfam00017
SH2 domain;
575-646 4.67e-11

SH2 domain;


Pssm-ID: 278446  Cd Length: 77  Bit Score: 61.46  E-value: 4.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572    575 IMGFVSRNQ-ERRLLKKMLSGTFLLRFSETSEGGITCSWVehqDDDKVEIYSVQP--------YTKEVLQSLPltEIIRH 645
Cdd:pfam00017   2 YHGKISREEaERLLLNGKPDGTFLVRESESTPGGYTLSVR---DDGKVKHYKIQStdnggyyiSGGVKFSSLA--ELVEH 76

                  .
gi 9910572    646 Y 646
Cdd:pfam00017  77 Y 77
SH2 smart00252
Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides ...
576-647 3.24e-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: 59.16  E-value: 3.24e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9910572     576 MGFVSRNQERRLLKKMLSGTFLLRFSETSEGGITCSWVehqDDDKVEIYSVQP------YTKEVLQSLPLTEIIRHYQ 647
Cdd:smart00252   5 HGFISREEAEKLLKNEGDGDFLVRDSESSPGDYVLSVR---VKGKVKHYRIRRnedgkfYLEGGRKFPSLVELVEHYQ 79
Trypan_PARP pfam05887
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ...
742-820 9.19e-08

Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei procyclic acidic repetitive protein (PARP) like sequences. The procyclic acidic repetitive protein (parp) genes of Trypanosoma brucei encode a small family of abundant surface proteins whose expression is restricted to the procyclic form of the parasite. They are found at two unlinked loci, parpA and parpB; transcription of both loci is developmentally regulated.


Pssm-ID: 114603  Cd Length: 145  Bit Score: 52.65  E-value: 9.19e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9910572    742 GTELKVDPILSTAPQVLLEPAPQVLLEPAPQVPLEPAPQVLLEPAPQVLLEPAPQVLLEPAPqvllEPAPQVQLEPAPQ 820
Cdd:pfam05887  47 GTKVGADDTNGTDPDDEPEEEEEPEPEEEGEEEPEPEEEGEEEPEPEETGEEEPEPEPEPEP----EPEPEPEPEPEPE 121
PHA03247 PHA03247
large tegument protein UL36; Provisional
749-859 5.29e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021  Cd Length: 3151  Bit Score: 53.79  E-value: 5.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572    749 PILSTAPQV--LLEPAPQVLLEPAPQVPLEPAPQVLLEPAPQVLLEPAPQVLLEPAPQVLLEPAPQVQLEPAPQVLLELA 826
Cdd:PHA03247 2875 PAAPARPPVrrLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGE 2954
                          90       100       110
                  ....*....|....*....|....*....|...
gi 9910572    827 PQVLLePAPQvLLELAPQVQLEPAHLLQQPSES 859
Cdd:PHA03247 2955 PSGAV-PQPW-LGALVPGRVAVPRFRVPQPAPS 2985
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
702-895 2.04e-04

polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.


Pssm-ID: 274311  Cd Length: 2582  Bit Score: 45.38  E-value: 2.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572     702 DELQQPLELKQDSEslevnAELLLAHDQELPLMMQTGLVlgtelKVDPILSTAPQ----VLLEPAPQVLLEPAPQVPLEP 777
Cdd:TIGR02813 1084 ESLQRSMELFHQHQ-----AETLKVHEQYLNLQTDSNIV-----KLSPLATQAPViksvVTQAPVVQVTISVAPAAPVLP 1153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572     778 ApqvlLEPAPQVLLEPAPQVL-LEPAPQVLLEP--APQVQ-LEPAPQVLLELAPQVLLEPAP--QVLLELAPQVQLEPAH 851
Cdd:TIGR02813 1154 A----VVSPPVVSAAPAQSVAtAVAMAPVAEVPiaVPVQQsVDYMPSVAQAAAPQASVNDSAiqQVMMEVVAEKTGYPTE 1229
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 9910572     852 LLQQpsESDLPEDLqqiSVEDLKKLSNPSTEYITTNENPMLAGE 895
Cdd:TIGR02813 1230 MLEL--EMDMEADL---GIDSIKRVEILGSVQEIINDLPELNPE 1268
VI_FHA TIGR03354
type VI secretion system FHA domain protein; Members of this protein family are FHA ...
707-833 2.35e-03

type VI secretion system FHA domain protein; Members of this protein family are FHA (forkhead-associated) domain-containing proteins that are part of type VI secretion loci in a considerable number of bacteria, most of which are known pathogens. Species include Pseudomonas aeruginosa PAO1, Aeromonas hydrophila, Yersinia pestis, Burkholderia mallei, etc. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 274537  Cd Length: 396  Bit Score: 41.20  E-value: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572    707 PLELKQDSE----SLEVNAELLLAHDQELPLM--MQTGLvlgTELKVDPILSTAPQVLLEPAPQVLLEPAPQVPLEPAPQ 780
Cdd:TIGR03354  83 PVRLEQGDRlrlgDYEIRVSLGDPLVSRQASEsrADTSL---PTAGGPPTPDPAPLAQLDPLKALDQEPLSAADLDDLSA 159
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 9910572    781 VLLEPAPQVLLEPAPQVLLEPAPQVLLEPAPQVQLEPAPQVLLELAPQVLLEP 833
Cdd:TIGR03354 160 PLFPPLDARLPAFAAPIDAEPTMVPPFVPLPAPEPAPAPASQAPSSDAVALTP 212
 
Name Accession Description Interval E-value
SH2_STAT2 cd10373
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 2 ...
554-704 6.58e-102

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: 317.22  E-value: 6.58e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572  554 WLDKILELVHDHLKDLWKDGRIMGFVSRNQERRLLKKMLSGTFLLRFSETSEGGITCSWVEHQDDDKVEIYSVQPYTKEV 633
Cdd:cd10373   1 WLDKILELVHDHLKDLWKDGRIMGFVSRNQERRLLKKTISGTFLLRFSETSEGGITCSWVEHQDDDKVLIYSVQPYTKEV 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9910572  634 LQSLPLTEIIRHYQVLAEENIPENPLRFLYPRIPRDEAFGCYYQEKVNFEEQRKYLKHKLIVISNRQVDEL 704
Cdd:cd10373  81 LQSLPLTEIIRHYQLLTEENIPENPLRFLYPRIPRDEAFGCYYQEKVNLEEREKYLKHKLIVVSNRQVDEL 151
STAT_bind pfam02864
STAT protein, DNA binding domain; STAT proteins (Signal Transducers and Activators of ...
316-563 5.24e-83

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: 308483  Cd Length: 246  Bit Score: 270.24  E-value: 5.24e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572    316 FVVETQPcmpqtlhrPLILKTGNKFTVRTRLLV--RLQEGSESLKAEVSVDRNSD----LPGFRKFNILTS-------NQ 382
Cdd:pfam02864   1 FVVEKQP--------PQVLKTQTKFSATVRLLVggKLPEHNNPPKVKVSIDSESQaralLKGFTKVNMEESqnsgeinNT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572    383 KTLTPEEGQRQgLIWDFGFLTLVEQRAvgagKGNKGPLAVTEELHVISFVVEYVYQGLKMKLQTDTLPVVIISNMNQLSI 462
Cdd:pfam02864  73 GALEYHQTSGQ-LSADFRNLQLKEIKR----GGRKGTESVTEEKFALLFQTQFTLGELVFDLQTLSLPVVVIVHGNQEPN 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572    463 AWASILWFNMlSPNPKNQQFFCqAPKAPWSLLGPVLSWQFSSYVGRGLDSEQLGMLRTKLFGKSCKMEDALLSWVDFCKR 542
Cdd:pfam02864 148 AWATILWDNA-FAEPGRVPFFV-PPKVPWPQLAEALSWKFSSGTGRGLSDEQLNYLAEKLFGDPSSYPDSLVSWSQFCKE 225
                         250       260
                  ....*....|....*....|.
gi 9910572    543 ESPPGKIPFWTWLDKILELVH 563
Cdd:pfam02864 226 NLPGRNFTFWEWFDGILDLIK 246
STAT_alpha pfam01017
STAT protein, all-alpha domain; STAT proteins (Signal Transducers and Activators of ...
141-314 5.93e-54

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: 307245  Cd Length: 177  Bit Score: 186.64  E-value: 5.93e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572    141 QLEIENRIQGLHVDIEFLVRSIRQLKDEQDVFSFRYTVFSLKKT---SSSDPHQSQQAQLVQATANKVDRMRKEVLDISK 217
Cdd:pfam01017   1 QQEIEQRLQELRNRVQETEQDIRQLEDLQDEFDFKYKELQKLEAqnnDSEEKELKQEKELLQQMLNELDQKRKEVLDKLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572    218 GLVGRLTTLVDLLL-PKLDEWKVQQQKSCIGAPPPELqLEQLEQWLTAGAKFLFHLRQLLKQLKEMSHMLRYKGDMFGQG 296
Cdd:pfam01017  81 ELLNLLETLQELLLdEELIEWKRRQQLACIGAPPNSC-LDQLQNWFTALAELLWQLRQQLKKLEELRQKLTYEGDPLTDG 159
                         170
                  ....*....|....*...
gi 9910572    297 VDLQNAQVMELLQRLLQR 314
Cdd:pfam01017 160 LPQLNARVTELLSSLVTS 177
SH2_STAT1 cd10372
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 1 ...
554-694 9.18e-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: 165.85  E-value: 9.18e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572  554 WLDKILELVHDHLKDLWKDGRIMGFVSRNQERRLLKKMLSGTFLLRFSETS-EGGITCSWVEH-QDDDKVEIYSVQPYTK 631
Cdd:cd10372   1 WIESILELIKKHLLSLWNDGCIMGFISKERERALLKDQQPGTFLLRFSESSrEGAITFTWVERsQNGGEPDFHAVEPYTK 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9910572  632 EVLQSLPLTEIIRHYQVLAEENIPENPLRFLYPRIPRDEAFGCYY------QEKVNFEEQRK--YLKHKLI 694
Cdd:cd10372  81 KELSAVTFPDIIRNYKVMAAENIPENPLKYLYPNIDKDHAFGKYYsrpkeaPEPMELDGPKGtgYIKTELI 151
SH2_STAT4 cd10375
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) ...
554-681 4.31e-46

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: 163.90  E-value: 4.31e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572  554 WLDKILELVHDHLKDLWKDGRIMGFVSRNQERRLLKKMLSGTFLLRFSETSEGGITCSWVEHQDDDKVEIYSVQPYTKEV 633
Cdd:cd10375   1 WLEAILDLIKKHILPLWIDGYIMGFVSKEKERLLLKDKMPGTFLLRFSESHLGGITFTWVDQSENGEVRFHSVEPYNKGR 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 9910572  634 LQSLPLTEIIRHYQVLAEENIPENPLRFLYPRIPRDEAFGCYYQEKVN 681
Cdd:cd10375  81 LSALPFADILRDYKVIMAENIPENPLKYLYPDIPKDKAFGKHYSSQPC 128
SH2_STAT_family cd09919
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) ...
554-678 1.53e-44

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: 158.52  E-value: 1.53e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572  554 WLDKILELVHDHLKDLWKDGRIMGFVSRNQERRLLKKMLSGTFLLRFSETSEGGITCSWVEHQDDDKVEIYSVQPYTKEV 633
Cdd:cd09919   1 WFFAIMLLTKRHLLKLWQDGLIMGFISKEEAEDLLKKKPPGTFLLRFSDSELGGITIAWVNEDPDGQSQVIHLQPYTKKD 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 9910572  634 LQSLPLTEIIRHYQvlaeenipenPLRFLYPRIPRDEAFGCYYQE 678
Cdd:cd09919  81 LDIRSLADRIRDLP----------QLVYLYPDIPKDEAFGKYYSP 115
SH2_STAT3 cd10374
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 3 ...
551-697 3.19e-41

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: 150.57  E-value: 3.19e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572  551 FWTWLDKILELVHDHLKDLWKDGRIMGFVSRNQERRLLKKMLSGTFLLRFSETS-EGGITCSWVEHQDDDKVEIYSVQPY 629
Cdd:cd10374   8 FWVWLDNIIDLVKKYILALWNEGYIMGFISKERERAILSTKPPGTFLLRFSESSkEGGVTFTWVEKDISGKTQIQSVEPY 87
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9910572  630 TKEVLQSLPLTEIIRHYQVLAEENIPENPLRFLYPRIPRDEAFGCYYQEKVNFEEQ------RKYLKHKLIVIS 697
Cdd:cd10374  88 TKQQLNNMSFAEIIMGYKIMDATNILVSPLVYLYPDIPKEEAFGKYCRPESQEHPEadpgsaAPYLKTKFICVT 161
STAT_int smart00964
STAT protein, protein interaction domain; STAT proteins (Signal Transducers and Activators of ...
2-123 4.08e-40

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: 145.90  E-value: 4.08e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572       2 AQWEMLQNLDSLFLDQLHQVYSQSiLPMDVRQHLATWIEDQNWREAALgsDDAKANMLYFSILDQL-NQWDHYSSDSNhF 80
Cdd:smart00964   1 SQWAQLQQLDSKFLEQVQQLYGDN-FPMELRHYLADWIESQDWELAAN--DEAQATRLFHNLLEQLdQQLSRFSQESN-F 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 9910572      81 LLQHNLRKFSRDIQTFPNG-PTQLAEMIFNLLLEEQRILNQAQR 123
Cdd:smart00964  77 LLKHNLRHIKSNLQSLYQEnPLELARIIRNILQEERRILAEASR 120
STAT_int pfam02865
STAT protein, protein interaction domain; STAT proteins (Signal Transducers and Activators of ...
2-122 6.45e-32

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: 308484  Cd Length: 122  Bit Score: 122.71  E-value: 6.45e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572      2 AQWEMLQNLDSLFLDQLHQVYSQSiLPMDVRQHLATWIEDQNWREAALGS-DDAKANMLYFSILDQL-NQWDHYSSDSNh 79
Cdd:pfam02865   1 ALWAKLQQLPGDALEQVQQLYGDH-FPIEVRHYLASWIESQDWEDADPDPqDESQATVLFHNLLQELqSQASRLSQEDN- 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 9910572     80 FLLQHNLRKFSRDIQ-TFPNGPTQLAEMIFNLLLEEQRILNQAQ 122
Cdd:pfam02865  79 FLLKHKLREIARNFQnRYQDNPLELARIIRNCLREEKRIVQQAE 122
SH2_STAT6 cd10377
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 6 ...
554-679 6.08e-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: 103.33  E-value: 6.08e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572  554 WLDKILELVHDHLKDLWKDGRIMGFVSRNQERRLLKKMLSGTFLLRFSETSEGGITCSWVEHQDDDKVEIYSVQPYTKEV 633
Cdd:cd10377   1 WFDGVLDLTKRCLRSYWSDRLIIGFISKQYVTSLLLNEPDGTFLLRFSDSEIGGITIAHVIRGQDGSPQIENIQPFSAKD 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 9910572  634 LQSLPLTEIIRHyqvLAEenipenpLRFLYPRIPRDEAFGCYYQEK 679
Cdd:cd10377  81 LSIRSLGDRIRD---LAQ-------LKNLYPKKPKDEAFRSHYKPE 116
STAT2_C pfam12188
Signal transducer and activator of transcription 2 C terminal; This domain family is found in ...
853-907 5.83e-20

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: 314971  Cd Length: 56  Bit Score: 86.74  E-value: 5.83e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 9910572    853 LQQPSESDLPEDLQQISVEDLKKLSNP-STEYITTNENPMLAGESSGDETSIPYHS 907
Cdd:pfam12188   1 SQPVPEPDLPHDLQHLNTEDMEIFRNSiNIEEIMPNGDPLLAGQNTGDEAYISCPS 56
SH2_STAT5 cd10376
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) 5 ...
554-676 8.85e-16

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: 76.94  E-value: 8.85e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572  554 WLDKILELVHDHLKDLWKDGRIMGFVSRNQERRLLKKMLSGTFLLRFSETSEGGITCSWveHQDDDKVEIYSVQPYTKev 633
Cdd:cd10376   1 WFDGVMEVLKKHLKPHWNDGAILGFVNKQQAHDLLINKPDGTFLLRFSDSEIGGITIAW--KFDSPDRALWNLMPFTT-- 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 9910572  634 lqslplteiiRHYQV--LAEENIPENPLRFLYPRIPRDEAFGCYY 676
Cdd:cd10376  77 ----------RDFSIrsLADRLGDLNYLIYVFPDRPKDEVFSKYY 111
SH2_STAT5a cd10421
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) ...
554-676 4.67e-15

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: 74.69  E-value: 4.67e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572  554 WLDKILELVHDHLKDLWKDGRIMGFVSRNQERRLLKKMLSGTFLLRFSETSEGGITCSWveHQDDDKVEIYSVQPYTKev 633
Cdd:cd10421   1 WFDGVMEVLKKHHKPHWNDGAILGFVNKQQAHDLLINKPDGTFLLRFSDSEIGGITIAW--KFDSPDRNLWNLKPFTT-- 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 9910572  634 lqslplteiiRHYQV--LAEENIPENPLRFLYPRIPRDEAFGCYY 676
Cdd:cd10421  77 ----------RDFSIrsLADRLGDLNYLIYVFPDRPKDEVFSKYY 111
SH2_STAT5b cd10420
Src homology 2 (SH2) domain found in signal transducer and activator of transcription (STAT) ...
554-676 8.01e-15

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: 74.34  E-value: 8.01e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572  554 WLDKILELVHDHLKDLWKDGRIMGFVSRNQERRLLKKMLSGTFLLRFSETSEGGITCSWveHQDDDKVEIYSVQPYTKEV 633
Cdd:cd10420   1 WFDGVMEVLKKHLKPHWNDGAILGFVNKQQAHDLLINKPDGTFLLRFSDSEIGGITIAW--KFDSQERMFWNLMPFTTRD 78
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 9910572  634 LQSLPLTEIIRHYQVLAeenipenplrFLYPRIPRDEAFGCYY 676
Cdd:cd10420  79 FSIRSLADRLGDLNYLI----------YVFPDRPKDEVYSKYY 111
SH2 pfam00017
SH2 domain;
575-646 4.67e-11

SH2 domain;


Pssm-ID: 278446  Cd Length: 77  Bit Score: 61.46  E-value: 4.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572    575 IMGFVSRNQ-ERRLLKKMLSGTFLLRFSETSEGGITCSWVehqDDDKVEIYSVQP--------YTKEVLQSLPltEIIRH 645
Cdd:pfam00017   2 YHGKISREEaERLLLNGKPDGTFLVRESESTPGGYTLSVR---DDGKVKHYKIQStdnggyyiSGGVKFSSLA--ELVEH 76

                  .
gi 9910572    646 Y 646
Cdd:pfam00017  77 Y 77
SH2 smart00252
Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides ...
576-647 3.24e-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: 59.16  E-value: 3.24e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9910572     576 MGFVSRNQERRLLKKMLSGTFLLRFSETSEGGITCSWVehqDDDKVEIYSVQP------YTKEVLQSLPLTEIIRHYQ 647
Cdd:smart00252   5 HGFISREEAEKLLKNEGDGDFLVRDSESSPGDYVLSVR---VKGKVKHYRIRRnedgkfYLEGGRKFPSLVELVEHYQ 79
Trypan_PARP pfam05887
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ...
742-820 9.19e-08

Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei procyclic acidic repetitive protein (PARP) like sequences. The procyclic acidic repetitive protein (parp) genes of Trypanosoma brucei encode a small family of abundant surface proteins whose expression is restricted to the procyclic form of the parasite. They are found at two unlinked loci, parpA and parpB; transcription of both loci is developmentally regulated.


Pssm-ID: 114603  Cd Length: 145  Bit Score: 52.65  E-value: 9.19e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9910572    742 GTELKVDPILSTAPQVLLEPAPQVLLEPAPQVPLEPAPQVLLEPAPQVLLEPAPQVLLEPAPqvllEPAPQVQLEPAPQ 820
Cdd:pfam05887  47 GTKVGADDTNGTDPDDEPEEEEEPEPEEEGEEEPEPEEEGEEEPEPEETGEEEPEPEPEPEP----EPEPEPEPEPEPE 121
Trypan_PARP pfam05887
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ...
768-842 3.65e-07

Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei procyclic acidic repetitive protein (PARP) like sequences. The procyclic acidic repetitive protein (parp) genes of Trypanosoma brucei encode a small family of abundant surface proteins whose expression is restricted to the procyclic form of the parasite. They are found at two unlinked loci, parpA and parpB; transcription of both loci is developmentally regulated.


Pssm-ID: 114603  Cd Length: 145  Bit Score: 50.73  E-value: 3.65e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9910572    768 EPAPQVPLEPAPqvllEPAPQVLLEPAPQVLLEPAPQVLLEPAPQVQLEPAPQVLLELAPQVLLEPAPQVLLELA 842
Cdd:pfam05887  61 DDEPEEEEEPEP----EEEGEEEPEPEEEGEEEPEPEETGEEEPEPEPEPEPEPEPEPEPEPEPEPGAATLKSVA 131
PHA03247 PHA03247
large tegument protein UL36; Provisional
749-859 5.29e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021  Cd Length: 3151  Bit Score: 53.79  E-value: 5.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572    749 PILSTAPQV--LLEPAPQVLLEPAPQVPLEPAPQVLLEPAPQVLLEPAPQVLLEPAPQVLLEPAPQVQLEPAPQVLLELA 826
Cdd:PHA03247 2875 PAAPARPPVrrLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGE 2954
                          90       100       110
                  ....*....|....*....|....*....|...
gi 9910572    827 PQVLLePAPQvLLELAPQVQLEPAHLLQQPSES 859
Cdd:PHA03247 2955 PSGAV-PQPW-LGALVPGRVAVPRFRVPQPAPS 2985
PRK11633 PRK11633
cell division protein DedD; Provisional
752-820 3.56e-06

cell division protein DedD; Provisional


Pssm-ID: 236940  Cd Length: 226  Bit Score: 48.85  E-value: 3.56e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9910572   752 STAPQVLLEPAPQVLLEPAPQVPLEPAPQvllePAPQVllEPAPQVLLEPAPQVLLEPAPQVQLEPAPQ 820
Cdd:PRK11633  84 SLDPATVAPPNTPVEPEPAPVEPPKPKPV----EKPKP--KPKPQQKVEAPPAPKPEPKPVVEEKAAPT 146
PRK11633 PRK11633
cell division protein DedD; Provisional
747-815 1.27e-05

cell division protein DedD; Provisional


Pssm-ID: 236940  Cd Length: 226  Bit Score: 47.30  E-value: 1.27e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9910572   747 VDPILSTAPQVLLEPAPQVLLEPAPQvplePAPQVLLEPAPQVLLEPAPQVLLEPAPQVLLEPAPQ-----VQL 815
Cdd:PRK11633  85 LDPATVAPPNTPVEPEPAPVEPPKPK----PVEKPKPKPKPQQKVEAPPAPKPEPKPVVEEKAAPTgkayvVQL 154
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
761-856 5.15e-05

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 313063  Cd Length: 837  Bit Score: 46.92  E-value: 5.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572    761 PAPQVLLEPAPQVPLEPAPQVLLEPAPQVLLEPAPQVLLEPA-PQVLLEPAPQVQLEPAPQVLLELAPQVLLEPAPQVLL 839
Cdd:pfam09770 205 PAQQPAPAPPQQPQAPPAQQQQQQQQFPPQQQQQQQPQQQPQqPQQHPGQGHPVTILQRPQSKQPDPPQPSPQPQAQPFH 284
                          90
                  ....*....|....*..
gi 9910572    840 ELAPQVQLEPAHLLQQP 856
Cdd:pfam09770 285 QQPPPVPVQPTQILQNP 301
CBP_CCPA pfam17040
Cellulose-complementing protein A; This is a family of bacterial cellulose-complementing ...
753-907 8.30e-05

Cellulose-complementing protein A; This is a family of bacterial cellulose-complementing protein A proteins necessary for cellulose biosynthesis. Cellulose is necessary for biofilm formation in bacteria. (Roemling U. and Galperin M.Y. "Bacterial cellulose biosynthesis. Diversity of operons and subunits" (manuscript in preparation)).


Pssm-ID: 319101  Cd Length: 342  Bit Score: 45.62  E-value: 8.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572    753 TAPQVLLEPAPQVLLEPAPQVPLEPAPQVLLEPAPqvllePAPQVLlePAPQVLLEPAPQVQLEPAPQVLLELAPQVLLE 832
Cdd:pfam17040  54 TAVEEQVTPAPQIAVAPPPPPVVPDPPAIVTETAP-----PPPVVV--SAPVTYEPPAAAVPAEPPVQEAPVQAAPVPPA 126
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9910572    833 PAPQVlLELAPQVQLEPAHL-LQQPSESDLPEDLQQISVEDLKKLSNPSTEYITTNENPMLAGESSGDETS-IPYHS 907
Cdd:pfam17040 127 PVPPI-AEQAPPAAPDPASVpYANVAAAPVPPDPAPVTPAPQARVTGPNTRMVEPFSRPQVRTVQEGATPSrVPSRS 202
SH2 cd00173
Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they ...
577-646 1.12e-04

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: 42.44  E-value: 1.12e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9910572  577 GFVSRNQERRLLKKMLSGTFLLRFSETSEGGITCSWVEHQDDDK-VEIYSVQPYTKEVLQSLP----LTEIIRHY 646
Cdd:cd00173   5 GSISREEAERLLRGKPDGTFLVRESSSEPGDYVLSVRSGDGKVKhYLIERNEGGYYLLGGSGRtfpsLPELVEHY 79
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
702-895 2.04e-04

polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.


Pssm-ID: 274311  Cd Length: 2582  Bit Score: 45.38  E-value: 2.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572     702 DELQQPLELKQDSEslevnAELLLAHDQELPLMMQTGLVlgtelKVDPILSTAPQ----VLLEPAPQVLLEPAPQVPLEP 777
Cdd:TIGR02813 1084 ESLQRSMELFHQHQ-----AETLKVHEQYLNLQTDSNIV-----KLSPLATQAPViksvVTQAPVVQVTISVAPAAPVLP 1153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572     778 ApqvlLEPAPQVLLEPAPQVL-LEPAPQVLLEP--APQVQ-LEPAPQVLLELAPQVLLEPAP--QVLLELAPQVQLEPAH 851
Cdd:TIGR02813 1154 A----VVSPPVVSAAPAQSVAtAVAMAPVAEVPiaVPVQQsVDYMPSVAQAAAPQASVNDSAiqQVMMEVVAEKTGYPTE 1229
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 9910572     852 LLQQpsESDLPEDLqqiSVEDLKKLSNPSTEYITTNENPMLAGE 895
Cdd:TIGR02813 1230 MLEL--EMDMEADL---GIDSIKRVEILGSVQEIINDLPELNPE 1268
PRK11633 PRK11633
cell division protein DedD; Provisional
769-828 2.28e-04

cell division protein DedD; Provisional


Pssm-ID: 236940  Cd Length: 226  Bit Score: 43.45  E-value: 2.28e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572   769 PAPQVPLEPAPQVLLEPAPQvllePAPQVLLEPAPQVLLEPAPQVQLEPAPQVLLELAPQ 828
Cdd:PRK11633  91 APPNTPVEPEPAPVEPPKPK----PVEKPKPKPKPQQKVEAPPAPKPEPKPVVEEKAAPT 146
PHA03379 PHA03379
EBNA-3A; Provisional
709-862 2.99e-04

EBNA-3A; Provisional


Pssm-ID: 223066  Cd Length: 935  Bit Score: 44.66  E-value: 2.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572   709 ELKQDSESLEVNAElllahDQELPLMMQTGlvlGTELKVDPILSTAPQVLL--------EPAPQVLLEPAPQVPLEPAPQ 780
Cdd:PHA03379 348 ETREESEDTESDGD-----DEELPRIVSRE---GTKRKRPPIFLRRLHRLLlmragkltERAREALEKASEPTYGTPRPP 419
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572   781 VLLePAPQVL--LEPAPqvllEPAPQVLLEPAPQVQLEPAPqvlleLAPQVLLEPAPQVLLELAPQVQLEPAHLLQQPSE 858
Cdd:PHA03379 420 VEK-PRPEVPqsLETAT----SHGSAQVPEPPPVHDLEPGP-----LHDQHSMAPCPVAQLPPGPLQDLEPGDQLPGVVQ 489

                 ....
gi 9910572   859 SDLP 862
Cdd:PHA03379 490 DGRP 493
Rib_recp_KP_reg pfam05104
Ribosome receptor lysine/proline rich region; This highly conserved region is found towards ...
760-850 3.35e-04

Ribosome receptor lysine/proline rich region; This highly conserved region is found towards the C-terminus of the transmembrane domain. The function is unclear.


Pssm-ID: 309995  Cd Length: 162  Bit Score: 41.91  E-value: 3.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572    760 EPAPQVLLEPAPQVPLEPAPQVLLEPAPqvLLEPAPQVLLEPAPQVllePAPQVQLEPAPQVLLELAPQVLLEPAPQVLL 839
Cdd:pfam05104  59 EPAEASEPYVEVVPEAPPAPPPPAKPAP--VPEPVPPPKKSKPPSV---KPAAVAKAPAPVLAQAAPPQAKPAPSPKDKK 133
                          90
                  ....*....|..
gi 9910572    840 ELAPQVQ-LEPA 850
Cdd:pfam05104 134 KPEKKVAkVEPA 145
PHA03247 PHA03247
large tegument protein UL36; Provisional
769-850 4.58e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021  Cd Length: 3151  Bit Score: 44.16  E-value: 4.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572    769 PAPQVPLEPAPQVLLEPAPQVLLEPAPQVLLEPAPQvllePAPQVQLEPAPQVLLELA--PQVLLEPAPQVLLELAPQVQ 846
Cdd:PHA03247 2873 AKPAAPARPPVRRLARPAVSRSTESFALPPDQPERP----PQPQAPPPPQPQPQPPPPpqPQPPPPPPPRPQPPLAPTTD 2948

                  ....
gi 9910572    847 LEPA 850
Cdd:PHA03247 2949 PAGA 2952
TonB_N pfam16031
TonB N-terminal region; TonB_N is a short domain found just downstream of the ...
747-819 5.28e-04

TonB N-terminal region; TonB_N is a short domain found just downstream of the cytoplasmic-membrane anchor at the N-terminus of TonB proteins. The exact function is not known.


Pssm-ID: 318287  Cd Length: 129  Bit Score: 41.02  E-value: 5.28e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9910572    747 VDPILST--APQVLLEPAPQVllePAPQVPLEPAPqvllEPAPqvllEPAPQVLLEP---APQVLLEPAPQVQLEPAP 819
Cdd:pfam16031   6 EQPISVTmvAPADLEPPPPAA---PEPQPAPEPEV----EPEP----EPEPEVLPEPpkeAPIPKPKPVPKPKPKPKP 72
PRK03427 PRK03427
cell division protein ZipA; Provisional
749-858 5.44e-04

cell division protein ZipA; Provisional


Pssm-ID: 235124  Cd Length: 333  Bit Score: 43.10  E-value: 5.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572   749 PILSTAPQVLLEPAPQVLLEPAP-QVPLEPAPQVLLEPAPQVllePAPQVLLEPAPQvLLEPAPQVQlEPAPQvlleLAP 827
Cdd:PRK03427  95 PYASAQPRQPVQQPPEAQVPPQHaPRPAQPAPQPVQQPAYQP---QPEQPLQQPVSP-QVAPAPQPV-HSAPQ----PAQ 165
                         90       100       110
                 ....*....|....*....|....*....|.
gi 9910572   828 QVLLEPAPQVLLELAPQVQLEPAHLLQQPSE 858
Cdd:PRK03427 166 QAFQPAEPVAAPQPEPVAEPAPVMDKPKRKE 196
Rib_recp_KP_reg pfam05104
Ribosome receptor lysine/proline rich region; This highly conserved region is found towards ...
760-850 6.77e-04

Ribosome receptor lysine/proline rich region; This highly conserved region is found towards the C-terminus of the transmembrane domain. The function is unclear.


Pssm-ID: 309995  Cd Length: 162  Bit Score: 41.14  E-value: 6.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572    760 EPAPQVLLEPAPQVPLEPAPQVLLEPAPQVLLE-----PAPQVLLEPAPQVLLEPAPQVQLEPAPQVLLELAPQVL-LEP 833
Cdd:pfam05104  65 EPYVEVVPEAPPAPPPPAKPAPVPEPVPPPKKSkppsvKPAAVAKAPAPVLAQAAPPQAKPAPSPKDKKKPEKKVAkVEP 144
                          90
                  ....*....|....*..
gi 9910572    834 APQVLLELAPQVQLEPA 850
Cdd:pfam05104 145 APTKGKPPISSQKAAPL 161
PRK10263 PRK10263
DNA translocase FtsK; Provisional
747-884 7.55e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669  Cd Length: 1355  Bit Score: 43.15  E-value: 7.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572    747 VDPILSTAPQVLLEPAPQvllepAPQVPLEPAPQVllePAPQVLLEPAPQVlLEPAPQVLLEPAPQVQ--LEPAPQVLLE 824
Cdd:PRK10263  337 VEPVTQTPPVASVDVPPA-----QPTVAWQPVPGP---QTGEPVIAPAPEG-YPQQSQYAQPAVQYNEplQQPVQPQQPY 407
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9910572    825 LAPQVLLEPAPQVLLELA--PQVQLEPAHLLQQPSESDLPEDLQQISVEDLKKLSNPSTEYI 884
Cdd:PRK10263  408 YAPAAEQPAQQPYYAPAPeqPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYQTEQTYQ 469
Rib_recp_KP_reg pfam05104
Ribosome receptor lysine/proline rich region; This highly conserved region is found towards ...
729-835 1.13e-03

Ribosome receptor lysine/proline rich region; This highly conserved region is found towards the C-terminus of the transmembrane domain. The function is unclear.


Pssm-ID: 309995  Cd Length: 162  Bit Score: 40.37  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572    729 QELPLMMQTGLVLGTELKVDPILSTAPQVLLEPAPQVLLEPAPQVPlepAPQVLLEPAPqVLLEPAP-QVLLEPAPQVLL 807
Cdd:pfam05104  58 QEPAEASEPYVEVVPEAPPAPPPPAKPAPVPEPVPPPKKSKPPSVK---PAAVAKAPAP-VLAQAAPpQAKPAPSPKDKK 133
                          90       100
                  ....*....|....*....|....*....
gi 9910572    808 EPAPQVQ-LEPAPQVLLELAPQVLLEPAP 835
Cdd:pfam05104 134 KPEKKVAkVEPAPTKGKPPISSQKAAPLP 162
PRK03427 PRK03427
cell division protein ZipA; Provisional
759-863 1.15e-03

cell division protein ZipA; Provisional


Pssm-ID: 235124  Cd Length: 333  Bit Score: 41.94  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572   759 LEPAPQVLLEPAPQVPLEPAPQVLLePAPQVLLEPAPQVllePAPQVLLEPAPQvQLEPAPQVLlELAPQvllePAPQVL 838
Cdd:PRK03427  99 AQPRQPVQQPPEAQVPPQHAPRPAQ-PAPQPVQQPAYQP---QPEQPLQQPVSP-QVAPAPQPV-HSAPQ----PAQQAF 168
                         90       100
                 ....*....|....*....|....*
gi 9910572   839 LELAPQVQLEPAHLLQQPSESDLPE 863
Cdd:PRK03427 169 QPAEPVAAPQPEPVAEPAPVMDKPK 193
PRK11633 PRK11633
cell division protein DedD; Provisional
770-847 2.06e-03

cell division protein DedD; Provisional


Pssm-ID: 236940  Cd Length: 226  Bit Score: 40.76  E-value: 2.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572   770 APQVPLEPAPQVllepAPQVLLEPAPQVLLEPAPQVLLE--PAPQVQLEPAPQVLLELAPQVLLEPAPQVLLELAPQ--- 844
Cdd:PRK11633  74 AVRAGDAAAPSL----DPATVAPPNTPVEPEPAPVEPPKpkPVEKPKPKPKPQQKVEAPPAPKPEPKPVVEEKAAPTgka 149

                 ....*
gi 9910572   845 --VQL 847
Cdd:PRK11633 150 yvVQL 154
VI_FHA TIGR03354
type VI secretion system FHA domain protein; Members of this protein family are FHA ...
707-833 2.35e-03

type VI secretion system FHA domain protein; Members of this protein family are FHA (forkhead-associated) domain-containing proteins that are part of type VI secretion loci in a considerable number of bacteria, most of which are known pathogens. Species include Pseudomonas aeruginosa PAO1, Aeromonas hydrophila, Yersinia pestis, Burkholderia mallei, etc. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 274537  Cd Length: 396  Bit Score: 41.20  E-value: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572    707 PLELKQDSE----SLEVNAELLLAHDQELPLM--MQTGLvlgTELKVDPILSTAPQVLLEPAPQVLLEPAPQVPLEPAPQ 780
Cdd:TIGR03354  83 PVRLEQGDRlrlgDYEIRVSLGDPLVSRQASEsrADTSL---PTAGGPPTPDPAPLAQLDPLKALDQEPLSAADLDDLSA 159
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 9910572    781 VLLEPAPQVLLEPAPQVLLEPAPQVLLEPAPQVQLEPAPQVLLELAPQVLLEP 833
Cdd:TIGR03354 160 PLFPPLDARLPAFAAPIDAEPTMVPPFVPLPAPEPAPAPASQAPSSDAVALTP 212
PRK10819 PRK10819
transport protein TonB; Provisional
757-819 3.13e-03

transport protein TonB; Provisional


Pssm-ID: 236768  Cd Length: 246  Bit Score: 40.05  E-value: 3.13e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9910572   757 VLLEPAPQvllEPAPQVPLEPAPQVLLEPAPQVLLEPAPqvllePAPQVLLEPAPQVQLEPAP 819
Cdd:PRK10819  51 TMVAPADL---EPPQAVQPPPEPVVEPEPEPEPIPEPPK-----EAPVVIPKPEPKPKPKPKP 105
PRK11633 PRK11633
cell division protein DedD; Provisional
749-836 4.46e-03

cell division protein DedD; Provisional


Pssm-ID: 236940  Cd Length: 226  Bit Score: 39.60  E-value: 4.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572   749 PILSTAPQVLLEpAPQVLLEPAPQV--PLEPAPQVLLEPAPQVLLEPAPQvllePAPQVLLEPAPQVQLEPAPQVLLELA 826
Cdd:PRK11633  62 ALPTQPPEGAAE-AVRAGDAAAPSLdpATVAPPNTPVEPEPAPVEPPKPK----PVEKPKPKPKPQQKVEAPPAPKPEPK 136
                         90
                 ....*....|
gi 9910572   827 PQVLLEPAPQ 836
Cdd:PRK11633 137 PVVEEKAAPT 146
DUF1421 pfam07223
Protein of unknown function (DUF1421); This family represents a conserved region approximately ...
753-866 4.64e-03

Protein of unknown function (DUF1421); This family represents a conserved region approximately 350 residues long within a number of plant proteins of unknown function.


Pssm-ID: 311273  Cd Length: 389  Bit Score: 40.23  E-value: 4.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572    753 TAPQVLlEPAPQVLLEPAPQVPLEPAP--QVLLEPAPQVLLEPAPQVLLEPAPQVLLEP-APQVQLEPAPQVLLELAPQV 829
Cdd:pfam07223  47 SAQSVS-ASKPQDNSQSHQQLPLPLALphQVNAPNAPPPQFQSPPPLILQQLVPVQLPTqLPQQQINQQEPYYMPPQQHP 125
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 9910572    830 llePAPQvllelaPQVQLEPAHLLQQPSESDLPEDLQ 866
Cdd:pfam07223 126 ---ENTH------QQYQVPPAQQPQLPQYPPQAPHQY 153
DUF1421 pfam07223
Protein of unknown function (DUF1421); This family represents a conserved region approximately ...
792-857 6.50e-03

Protein of unknown function (DUF1421); This family represents a conserved region approximately 350 residues long within a number of plant proteins of unknown function.


Pssm-ID: 311273  Cd Length: 389  Bit Score: 39.85  E-value: 6.50e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9910572    792 EPAPQVLLEPAPQVLLEPAPQVQLEPAP--QVLLELAPQVLLEPAPQVLLELAPQVQLePAHLLQQPS 857
Cdd:pfam07223  45 EDSAQSVSASKPQDNSQSHQQLPLPLALphQVNAPNAPPPQFQSPPPLILQQLVPVQL-PTQLPQQQI 111
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
754-860 6.92e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138  Cd Length: 647  Bit Score: 39.85  E-value: 6.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910572   754 APQVLLEPAPQVLLEPAPQVPLEPAPQVLLEPAPQVLLEPAPQVLLEPAPQVLLEPAPQVQLEPAPQVLLELAPQVLLEP 833
Cdd:PRK07994 370 VPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQRAQGATKAKKSEPAAASRA 449
                         90       100
                 ....*....|....*....|....*...
gi 9910572   834 AP-QVLLELAPQVQLEPAHLLQQPSESD 860
Cdd:PRK07994 450 RPvNSALERLASVRPAPSALEKAPAKKE 477
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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