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Conserved domains on  [gi|253683431|ref|NP_001156621|]
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ETS translocation variant 1 isoform c [Homo sapiens]

Protein Classification

ETS translocation variant( domain architecture ID 12054215)

ETS translocation variant (ETV) is a transcriptional activator that binds to consensus DNA sequences, such as human ETV1 that binds to the pentanucleotide 5'-CGGA[AT]-3'

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ETS_PEA3_N pfam04621
PEA3 subfamily ETS-domain transcription factor N terminal domain; The N terminus of the PEA3 ...
1-315 2.37e-167

PEA3 subfamily ETS-domain transcription factor N terminal domain; The N terminus of the PEA3 transcription factors is implicated in transactivation and in inhibition of DNA binding. Transactivation is potentiated by activation of the Ras/MAP kinase and protein kinase A signalling cascades. The N terminal region contains conserved MAP kinase phosphorylation sites.


:

Pssm-ID: 461371  Cd Length: 344  Bit Score: 474.60  E-value: 2.37e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253683431    1 MDGFYDQQVPYMVTNSQRGRNCNEKPTNVRKRKFINRDLAHDSEELFQDLSQLQETWLAE-----------------VAF 63
Cdd:pfam04621   1 MDGFYDQQVPFMVPGSSCGEGPLGRPLMDRKRKFMDTELAQDSEELFQDLSQLQETWLAEaqvpddeqfvpdfqsenLAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253683431   64 HGLP-LKIKKEPHSPCSEISSaCSQEQPFKFSYGEKCLYNVSAYDQKPQVGMRPsnpPTPSSTPVSPLHHASP------- 135
Cdd:pfam04621  81 HGPPpAKIKREPQSPSSDLSS-CSHEQSFKYPYGEQCLYNYSAYDRKPPSGFKP---PTPPSTPVSPLQQHSSlktpplq 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253683431  136 ------------NSTHTPKPDRAFPaHLPPSQsiPDSSYPMDHRFRRQLSEPCNSFPPLPTMPREGRPMYQRQMSEPNIP 203
Cdd:pfam04621 157 rqpsplplmrqsPPFAVPRPPRGYM-PMPPSQ--PSNSYPIEHRFQRQLSEPCLPFPPPEGGPRDGRPPYQRQMSEPLVP 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253683431  204 FPPQGFKQEYHDPVYEHNTMVGSAASQSFPPPLMIKQEPRDFAYDSEVPSCHSIYMRQEGFLAHPSRtEGCMFEKGPRQF 283
Cdd:pfam04621 234 YPPQGFKQEYHDPLYEHGPPPGGPPPHRFPPPMMIKQEPRDYGYDSEVPNCQSSYGRSEGFLYPNSH-DGFSYDKDPRLF 312
                         330       340       350
                  ....*....|....*....|....*....|..
gi 253683431  284 YDDTCVVPEKFDGDIKQEPGMYREGPTYQRRG 315
Cdd:pfam04621 313 YDDTCVVPEKLEGKVKQEPGVYREGPPYQRRG 344
ETS smart00413
erythroblast transformation specific domain; variation of the helix-turn-helix motif
316-400 1.90e-49

erythroblast transformation specific domain; variation of the helix-turn-helix motif


:

Pssm-ID: 197710  Cd Length: 87  Bit Score: 163.21  E-value: 1.90e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253683431   316 SLQLWQFLVALLDDPSNSHFIAWTGR-GMEFKLIEPEEVARRWGIQKNRPAMNYDKLSRSLRYYYEKGIMQKVAGERYVY 394
Cdd:smart00413   1 GIQLWQFLLDLLLDPENSDIIKWTDRdEGEFKLVDPEEVARLWGQRKNKPNMNYEKLSRALRYYYKKNILEKVPGKRLVY 80

                   ....*.
gi 253683431   395 KFVCDP 400
Cdd:smart00413  81 KFVKNP 86
 
Name Accession Description Interval E-value
ETS_PEA3_N pfam04621
PEA3 subfamily ETS-domain transcription factor N terminal domain; The N terminus of the PEA3 ...
1-315 2.37e-167

PEA3 subfamily ETS-domain transcription factor N terminal domain; The N terminus of the PEA3 transcription factors is implicated in transactivation and in inhibition of DNA binding. Transactivation is potentiated by activation of the Ras/MAP kinase and protein kinase A signalling cascades. The N terminal region contains conserved MAP kinase phosphorylation sites.


Pssm-ID: 461371  Cd Length: 344  Bit Score: 474.60  E-value: 2.37e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253683431    1 MDGFYDQQVPYMVTNSQRGRNCNEKPTNVRKRKFINRDLAHDSEELFQDLSQLQETWLAE-----------------VAF 63
Cdd:pfam04621   1 MDGFYDQQVPFMVPGSSCGEGPLGRPLMDRKRKFMDTELAQDSEELFQDLSQLQETWLAEaqvpddeqfvpdfqsenLAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253683431   64 HGLP-LKIKKEPHSPCSEISSaCSQEQPFKFSYGEKCLYNVSAYDQKPQVGMRPsnpPTPSSTPVSPLHHASP------- 135
Cdd:pfam04621  81 HGPPpAKIKREPQSPSSDLSS-CSHEQSFKYPYGEQCLYNYSAYDRKPPSGFKP---PTPPSTPVSPLQQHSSlktpplq 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253683431  136 ------------NSTHTPKPDRAFPaHLPPSQsiPDSSYPMDHRFRRQLSEPCNSFPPLPTMPREGRPMYQRQMSEPNIP 203
Cdd:pfam04621 157 rqpsplplmrqsPPFAVPRPPRGYM-PMPPSQ--PSNSYPIEHRFQRQLSEPCLPFPPPEGGPRDGRPPYQRQMSEPLVP 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253683431  204 FPPQGFKQEYHDPVYEHNTMVGSAASQSFPPPLMIKQEPRDFAYDSEVPSCHSIYMRQEGFLAHPSRtEGCMFEKGPRQF 283
Cdd:pfam04621 234 YPPQGFKQEYHDPLYEHGPPPGGPPPHRFPPPMMIKQEPRDYGYDSEVPNCQSSYGRSEGFLYPNSH-DGFSYDKDPRLF 312
                         330       340       350
                  ....*....|....*....|....*....|..
gi 253683431  284 YDDTCVVPEKFDGDIKQEPGMYREGPTYQRRG 315
Cdd:pfam04621 313 YDDTCVVPEKLEGKVKQEPGVYREGPPYQRRG 344
ETS smart00413
erythroblast transformation specific domain; variation of the helix-turn-helix motif
316-400 1.90e-49

erythroblast transformation specific domain; variation of the helix-turn-helix motif


Pssm-ID: 197710  Cd Length: 87  Bit Score: 163.21  E-value: 1.90e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253683431   316 SLQLWQFLVALLDDPSNSHFIAWTGR-GMEFKLIEPEEVARRWGIQKNRPAMNYDKLSRSLRYYYEKGIMQKVAGERYVY 394
Cdd:smart00413   1 GIQLWQFLLDLLLDPENSDIIKWTDRdEGEFKLVDPEEVARLWGQRKNKPNMNYEKLSRALRYYYKKNILEKVPGKRLVY 80

                   ....*.
gi 253683431   395 KFVCDP 400
Cdd:smart00413  81 KFVKNP 86
Ets pfam00178
Ets-domain;
318-396 2.66e-44

Ets-domain;


Pssm-ID: 459700  Cd Length: 80  Bit Score: 149.57  E-value: 2.66e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253683431  318 QLWQFLVALLDDPSNSHFIAWTGR-GMEFKLIEPEEVARRWGIQKNRPAMNYDKLSRSLRYYYEKGIMQKVAGERYVYKF 396
Cdd:pfam00178   1 QLWQFLLDLLTDPEYSDIIKWTDKeEGEFRLVDPEAVARLWGKRKGNPKMTYEKLSRALRYYYKKGILEKVPGKRLTYRF 80
PHA03247 PHA03247
large tegument protein UL36; Provisional
103-252 1.41e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253683431  103 VSAYDQKPQVGMRPSNPPTPSSTPVSPLHHASPNSthtPKPDRAFPAHLPPSQSIPDSSYPMDHRFRrqlSEPCNSFPPL 182
Cdd:PHA03247 2582 VTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSP---LPPDTHAPDPPPPSPSPAANEPDPHPPPT---VPPPERPRDD 2655
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 253683431  183 PTMPREGRPMYQRQMSEPNIPF-PPQGFKQEYHDPVyehntmVGSAASQSFPPPLMIKQEPRDFAYDSEVP 252
Cdd:PHA03247 2656 PAPGRVSRPRRARRLGRAAQASsPPQRPRRRAARPT------VGSLTSLADPPPPPPTPEPAPHALVSATP 2720
 
Name Accession Description Interval E-value
ETS_PEA3_N pfam04621
PEA3 subfamily ETS-domain transcription factor N terminal domain; The N terminus of the PEA3 ...
1-315 2.37e-167

PEA3 subfamily ETS-domain transcription factor N terminal domain; The N terminus of the PEA3 transcription factors is implicated in transactivation and in inhibition of DNA binding. Transactivation is potentiated by activation of the Ras/MAP kinase and protein kinase A signalling cascades. The N terminal region contains conserved MAP kinase phosphorylation sites.


Pssm-ID: 461371  Cd Length: 344  Bit Score: 474.60  E-value: 2.37e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253683431    1 MDGFYDQQVPYMVTNSQRGRNCNEKPTNVRKRKFINRDLAHDSEELFQDLSQLQETWLAE-----------------VAF 63
Cdd:pfam04621   1 MDGFYDQQVPFMVPGSSCGEGPLGRPLMDRKRKFMDTELAQDSEELFQDLSQLQETWLAEaqvpddeqfvpdfqsenLAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253683431   64 HGLP-LKIKKEPHSPCSEISSaCSQEQPFKFSYGEKCLYNVSAYDQKPQVGMRPsnpPTPSSTPVSPLHHASP------- 135
Cdd:pfam04621  81 HGPPpAKIKREPQSPSSDLSS-CSHEQSFKYPYGEQCLYNYSAYDRKPPSGFKP---PTPPSTPVSPLQQHSSlktpplq 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253683431  136 ------------NSTHTPKPDRAFPaHLPPSQsiPDSSYPMDHRFRRQLSEPCNSFPPLPTMPREGRPMYQRQMSEPNIP 203
Cdd:pfam04621 157 rqpsplplmrqsPPFAVPRPPRGYM-PMPPSQ--PSNSYPIEHRFQRQLSEPCLPFPPPEGGPRDGRPPYQRQMSEPLVP 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253683431  204 FPPQGFKQEYHDPVYEHNTMVGSAASQSFPPPLMIKQEPRDFAYDSEVPSCHSIYMRQEGFLAHPSRtEGCMFEKGPRQF 283
Cdd:pfam04621 234 YPPQGFKQEYHDPLYEHGPPPGGPPPHRFPPPMMIKQEPRDYGYDSEVPNCQSSYGRSEGFLYPNSH-DGFSYDKDPRLF 312
                         330       340       350
                  ....*....|....*....|....*....|..
gi 253683431  284 YDDTCVVPEKFDGDIKQEPGMYREGPTYQRRG 315
Cdd:pfam04621 313 YDDTCVVPEKLEGKVKQEPGVYREGPPYQRRG 344
ETS smart00413
erythroblast transformation specific domain; variation of the helix-turn-helix motif
316-400 1.90e-49

erythroblast transformation specific domain; variation of the helix-turn-helix motif


Pssm-ID: 197710  Cd Length: 87  Bit Score: 163.21  E-value: 1.90e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253683431   316 SLQLWQFLVALLDDPSNSHFIAWTGR-GMEFKLIEPEEVARRWGIQKNRPAMNYDKLSRSLRYYYEKGIMQKVAGERYVY 394
Cdd:smart00413   1 GIQLWQFLLDLLLDPENSDIIKWTDRdEGEFKLVDPEEVARLWGQRKNKPNMNYEKLSRALRYYYKKNILEKVPGKRLVY 80

                   ....*.
gi 253683431   395 KFVCDP 400
Cdd:smart00413  81 KFVKNP 86
Ets pfam00178
Ets-domain;
318-396 2.66e-44

Ets-domain;


Pssm-ID: 459700  Cd Length: 80  Bit Score: 149.57  E-value: 2.66e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253683431  318 QLWQFLVALLDDPSNSHFIAWTGR-GMEFKLIEPEEVARRWGIQKNRPAMNYDKLSRSLRYYYEKGIMQKVAGERYVYKF 396
Cdd:pfam00178   1 QLWQFLLDLLTDPEYSDIIKWTDKeEGEFRLVDPEAVARLWGKRKGNPKMTYEKLSRALRYYYKKGILEKVPGKRLTYRF 80
PHA03247 PHA03247
large tegument protein UL36; Provisional
103-252 1.41e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253683431  103 VSAYDQKPQVGMRPSNPPTPSSTPVSPLHHASPNSthtPKPDRAFPAHLPPSQSIPDSSYPMDHRFRrqlSEPCNSFPPL 182
Cdd:PHA03247 2582 VTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSP---LPPDTHAPDPPPPSPSPAANEPDPHPPPT---VPPPERPRDD 2655
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 253683431  183 PTMPREGRPMYQRQMSEPNIPF-PPQGFKQEYHDPVyehntmVGSAASQSFPPPLMIKQEPRDFAYDSEVP 252
Cdd:PHA03247 2656 PAPGRVSRPRRARRLGRAAQASsPPQRPRRRAARPT------VGSLTSLADPPPPPPTPEPAPHALVSATP 2720
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
70-252 4.14e-04

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.83  E-value: 4.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253683431   70 IKKEPHSPCSEISSACSQEQPfkfsygekclynvsAYDQKPQVGMRPSN-PPTPSSTPVSPLHHASPNSTHTP------- 141
Cdd:pfam03154 355 IKPPPTTPIPQLPNPQSHKHP--------------PHLSGPSPFQMNSNlPPPPALKPLSSLSTHHPPSAHPPplqlmpq 420
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253683431  142 ----KPDRAFPAHLPPSQSIP--DSSYPMDHRFRRQLSEPcnSFPPLPTMPREGRPMYQRQMSEPNIPFPPQGFKQEYHD 215
Cdd:pfam03154 421 sqqlPPPPAQPPVLTQSQSLPppAASHPPTSGLHQVPSQS--PFPQHPFVPGGPPPITPPSGPPTSTSSAMPGIQPPSSA 498
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 253683431  216 PVYEHNTMVGSAASQSfpPPLMIKQEPRDFAYDSEVP 252
Cdd:pfam03154 499 SVSSSGPVPAAVSCPL--PPVQIKEEALDEAEEPESP 533
PHA03247 PHA03247
large tegument protein UL36; Provisional
116-206 3.40e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.31  E-value: 3.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253683431  116 PSNPPTPSSTPVSPLHHASPNSTHTP-----KPDRAFPAHLPPSQSIPDSSYPMDHRFRR----QLSEPCNSFP------ 180
Cdd:PHA03247 2826 GPLPPPTSAQPTAPPPPPGPPPPSLPlggsvAPGGDVRRRPPSRSPAAKPAAPARPPVRRlarpAVSRSTESFAlppdqp 2905
                          90       100
                  ....*....|....*....|....*..
gi 253683431  181 -PLPTMPREGRPMYQRQMSEPNIPFPP 206
Cdd:PHA03247 2906 eRPPQPQAPPPPQPQPQPPPPPQPQPP 2932
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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