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Conserved domains on  [gi|1907085924|ref|XP_036013079|]
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ETS translocation variant 1 isoform X7 [Mus musculus]

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 ...
21-275 6.44e-127

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: 370.21  E-value: 6.44e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085924  21 VAFHGLP-LKIKKEPHSPCSELgSACSQEQPFKFSYGEKCLYNVSAYDQKPQVGMRPsnpPTPSSTPVSPLHHASP---- 95
Cdd:pfam04621  78 LAFHGPPpAKIKREPQSPSSDL-SSCSHEQSFKYPYGEQCLYNYSAYDRKPPSGFKP---PTPPSTPVSPLQQHSSlktp 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085924  96 ---------------NTAHTPKPDRAFPaHLPPSQsiPDSTYPMDHRFRRQLSEPCNSFPPLPTMPREGRPMYQRQMSEP 160
Cdd:pfam04621 154 plqrqpsplplmrqsPPFAVPRPPRGYM-PMPPSQ--PSNSYPIEHRFQRQLSEPCLPFPPPEGGPRDGRPPYQRQMSEP 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085924 161 NIPFPPQGFKQEYHDPVYEHTTMVGGAASQSFPPPLMIKQEPRDFAYDSEVPSCHSIYMRQEGFLAHPSRtEGCMFEKGP 240
Cdd:pfam04621 231 LVPYPPQGFKQEYHDPLYEHGPPPGGPPPHRFPPPMMIKQEPRDYGYDSEVPNCQSSYGRSEGFLYPNSH-DGFSYDKDP 309
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1907085924 241 RQFYDDTCVVPEKFDGDIKQEPGMYREGPTYQRRG 275
Cdd:pfam04621 310 RLFYDDTCVVPEKLEGKVKQEPGVYREGPPYQRRG 344
ETS smart00413
erythroblast transformation specific domain; variation of the helix-turn-helix motif
276-360 1.22e-50

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


:

Pssm-ID: 197710  Cd Length: 87  Bit Score: 165.52  E-value: 1.22e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085924  276 SLQLWQFLVALLDDPSNSHFIAWTGR-GMEFKLIEPEEVARRWGIQKNRPAMNYDKLSRSLRYYYEKGIMQKVAGERYVY 354
Cdd:smart00413   1 GIQLWQFLLDLLLDPENSDIIKWTDRdEGEFKLVDPEEVARLWGQRKNKPNMNYEKLSRALRYYYKKNILEKVPGKRLVY 80

                   ....*.
gi 1907085924  355 KFVCDP 360
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 ...
21-275 6.44e-127

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: 370.21  E-value: 6.44e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085924  21 VAFHGLP-LKIKKEPHSPCSELgSACSQEQPFKFSYGEKCLYNVSAYDQKPQVGMRPsnpPTPSSTPVSPLHHASP---- 95
Cdd:pfam04621  78 LAFHGPPpAKIKREPQSPSSDL-SSCSHEQSFKYPYGEQCLYNYSAYDRKPPSGFKP---PTPPSTPVSPLQQHSSlktp 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085924  96 ---------------NTAHTPKPDRAFPaHLPPSQsiPDSTYPMDHRFRRQLSEPCNSFPPLPTMPREGRPMYQRQMSEP 160
Cdd:pfam04621 154 plqrqpsplplmrqsPPFAVPRPPRGYM-PMPPSQ--PSNSYPIEHRFQRQLSEPCLPFPPPEGGPRDGRPPYQRQMSEP 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085924 161 NIPFPPQGFKQEYHDPVYEHTTMVGGAASQSFPPPLMIKQEPRDFAYDSEVPSCHSIYMRQEGFLAHPSRtEGCMFEKGP 240
Cdd:pfam04621 231 LVPYPPQGFKQEYHDPLYEHGPPPGGPPPHRFPPPMMIKQEPRDYGYDSEVPNCQSSYGRSEGFLYPNSH-DGFSYDKDP 309
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1907085924 241 RQFYDDTCVVPEKFDGDIKQEPGMYREGPTYQRRG 275
Cdd:pfam04621 310 RLFYDDTCVVPEKLEGKVKQEPGVYREGPPYQRRG 344
ETS smart00413
erythroblast transformation specific domain; variation of the helix-turn-helix motif
276-360 1.22e-50

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


Pssm-ID: 197710  Cd Length: 87  Bit Score: 165.52  E-value: 1.22e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085924  276 SLQLWQFLVALLDDPSNSHFIAWTGR-GMEFKLIEPEEVARRWGIQKNRPAMNYDKLSRSLRYYYEKGIMQKVAGERYVY 354
Cdd:smart00413   1 GIQLWQFLLDLLLDPENSDIIKWTDRdEGEFKLVDPEEVARLWGQRKNKPNMNYEKLSRALRYYYKKNILEKVPGKRLVY 80

                   ....*.
gi 1907085924  355 KFVCDP 360
Cdd:smart00413  81 KFVKNP 86
Ets pfam00178
Ets-domain;
278-356 2.30e-45

Ets-domain;


Pssm-ID: 459700  Cd Length: 80  Bit Score: 151.49  E-value: 2.30e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085924 278 QLWQFLVALLDDPSNSHFIAWTGR-GMEFKLIEPEEVARRWGIQKNRPAMNYDKLSRSLRYYYEKGIMQKVAGERYVYKF 356
Cdd:pfam00178   1 QLWQFLLDLLTDPEYSDIIKWTDKeEGEFRLVDPEAVARLWGKRKGNPKMTYEKLSRALRYYYKKGILEKVPGKRLTYRF 80
PHA03247 PHA03247
large tegument protein UL36; Provisional
70-212 7.62e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 7.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085924   70 PQVGMRPSNPPTPS--STPVSPlhhASPNTAHTPKPDRAFPAHLPPSQSIPDSTYPMD--------HRFRRQLSEPCNSF 139
Cdd:PHA03247  2571 PRPAPRPSEPAVTSraRRPDAP---PQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDppppspspAANEPDPHPPPTVP 2647
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907085924  140 PP-----LPTMPREGRPMYQRQMSEPNIPF-PPQGFKQEYHDPVyehttmVGGAASQSFPPPLMIKQEPRDFAYDSEVP 212
Cdd:PHA03247  2648 PPerprdDPAPGRVSRPRRARRLGRAAQASsPPQRPRRRAARPT------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 ...
21-275 6.44e-127

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: 370.21  E-value: 6.44e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085924  21 VAFHGLP-LKIKKEPHSPCSELgSACSQEQPFKFSYGEKCLYNVSAYDQKPQVGMRPsnpPTPSSTPVSPLHHASP---- 95
Cdd:pfam04621  78 LAFHGPPpAKIKREPQSPSSDL-SSCSHEQSFKYPYGEQCLYNYSAYDRKPPSGFKP---PTPPSTPVSPLQQHSSlktp 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085924  96 ---------------NTAHTPKPDRAFPaHLPPSQsiPDSTYPMDHRFRRQLSEPCNSFPPLPTMPREGRPMYQRQMSEP 160
Cdd:pfam04621 154 plqrqpsplplmrqsPPFAVPRPPRGYM-PMPPSQ--PSNSYPIEHRFQRQLSEPCLPFPPPEGGPRDGRPPYQRQMSEP 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085924 161 NIPFPPQGFKQEYHDPVYEHTTMVGGAASQSFPPPLMIKQEPRDFAYDSEVPSCHSIYMRQEGFLAHPSRtEGCMFEKGP 240
Cdd:pfam04621 231 LVPYPPQGFKQEYHDPLYEHGPPPGGPPPHRFPPPMMIKQEPRDYGYDSEVPNCQSSYGRSEGFLYPNSH-DGFSYDKDP 309
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1907085924 241 RQFYDDTCVVPEKFDGDIKQEPGMYREGPTYQRRG 275
Cdd:pfam04621 310 RLFYDDTCVVPEKLEGKVKQEPGVYREGPPYQRRG 344
ETS smart00413
erythroblast transformation specific domain; variation of the helix-turn-helix motif
276-360 1.22e-50

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


Pssm-ID: 197710  Cd Length: 87  Bit Score: 165.52  E-value: 1.22e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085924  276 SLQLWQFLVALLDDPSNSHFIAWTGR-GMEFKLIEPEEVARRWGIQKNRPAMNYDKLSRSLRYYYEKGIMQKVAGERYVY 354
Cdd:smart00413   1 GIQLWQFLLDLLLDPENSDIIKWTDRdEGEFKLVDPEEVARLWGQRKNKPNMNYEKLSRALRYYYKKNILEKVPGKRLVY 80

                   ....*.
gi 1907085924  355 KFVCDP 360
Cdd:smart00413  81 KFVKNP 86
Ets pfam00178
Ets-domain;
278-356 2.30e-45

Ets-domain;


Pssm-ID: 459700  Cd Length: 80  Bit Score: 151.49  E-value: 2.30e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085924 278 QLWQFLVALLDDPSNSHFIAWTGR-GMEFKLIEPEEVARRWGIQKNRPAMNYDKLSRSLRYYYEKGIMQKVAGERYVYKF 356
Cdd:pfam00178   1 QLWQFLLDLLTDPEYSDIIKWTDKeEGEFRLVDPEAVARLWGKRKGNPKMTYEKLSRALRYYYKKGILEKVPGKRLTYRF 80
PHA03247 PHA03247
large tegument protein UL36; Provisional
70-212 7.62e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 7.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085924   70 PQVGMRPSNPPTPS--STPVSPlhhASPNTAHTPKPDRAFPAHLPPSQSIPDSTYPMD--------HRFRRQLSEPCNSF 139
Cdd:PHA03247  2571 PRPAPRPSEPAVTSraRRPDAP---PQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDppppspspAANEPDPHPPPTVP 2647
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907085924  140 PP-----LPTMPREGRPMYQRQMSEPNIPF-PPQGFKQEYHDPVyehttmVGGAASQSFPPPLMIKQEPRDFAYDSEVP 212
Cdd:PHA03247  2648 PPerprdDPAPGRVSRPRRARRLGRAAQASsPPQRPRRRAARPT------VGSLTSLADPPPPPPTPEPAPHALVSATP 2720
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
30-212 2.25e-03

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 40.52  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085924  30 IKKEPHSPCSELGSACSQEQPfkfsygekclynvsAYDQKPQVGMRPSN-PPTPSSTPVSPLHHASPNTAHTP------- 101
Cdd:pfam03154 355 IKPPPTTPIPQLPNPQSHKHP--------------PHLSGPSPFQMNSNlPPPPALKPLSSLSTHHPPSAHPPplqlmpq 420
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085924 102 ----KPDRAFPAHLPPSQSIPDSTYPMDHRFRRQLSEPCNSFPPLPTMPREGRPMYQRQMSEPNIPFPPQGFKQEYHDPV 177
Cdd:pfam03154 421 sqqlPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPTSTSSAMPGIQPPSSASV 500
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1907085924 178 yeHTTMVGGAASQSFPPPLMIKQEPRDFAYDSEVP 212
Cdd:pfam03154 501 --SSSGPVPAAVSCPLPPVQIKEEALDEAEEPESP 533
PRK10263 PRK10263
DNA translocase FtsK; Provisional
70-202 5.78e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 39.30  E-value: 5.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085924   70 PQVGmRPSNPPTPSSTPVSPlHHASPNTAHTPKPDRAFPAHlPPSQSIPDSTYPMDHRFRRQLSEPC--NSFPPLPTMPR 147
Cdd:PRK10263   366 PQTG-EPVIAPAPEGYPQQS-QYAQPAVQYNEPLQQPVQPQ-QPYYAPAAEQPAQQPYYAPAPEQPAqqPYYAPAPEQPV 442
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907085924  148 EGRPMYQRQMSEPNIPFPPQGFKQEYHDPVYEHTTMVggaASQSFPPPLMIKQEP 202
Cdd:PRK10263   443 AGNAWQAEEQQSTFAPQSTYQTEQTYQQPAAQEPLYQ---QPQPVEQQPVVEPEP 494
PHA03247 PHA03247
large tegument protein UL36; Provisional
70-171 9.91e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 38.38  E-value: 9.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085924   70 PQVGMRPSNPPTPSSTPVSPLhhaSPNTAHTPKPDRAFPAHLPPSQSIPDSTYPMDHRFRRQLSEPCNSFPPLPTMPReg 149
Cdd:PHA03247  2808 PAAVLAPAAALPPAASPAGPL---PPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPP-- 2882
                           90       100
                   ....*....|....*....|..
gi 1907085924  150 rpmyQRQMSEPNIPFPPQGFKQ 171
Cdd:PHA03247  2883 ----VRRLARPAVSRSTESFAL 2900
 
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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