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Conserved domains on  [gi|1958807444|ref|XP_038955685|]
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mediator of RNA polymerase II transcription subunit 14 isoform X1 [Rattus norvegicus]

Protein Classification

mediator of RNA polymerase II transcription subunit 14( domain architecture ID 10554477)

mediator of RNA polymerase II transcription subunit 14 is a component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes

PubMed:  29209056

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Med14 pfam08638
Mediator complex subunit MED14; Saccharomyces cerevisiae RGR1 mediator complex subunit affects ...
57-244 1.45e-72

Mediator complex subunit MED14; Saccharomyces cerevisiae RGR1 mediator complex subunit affects chromatin structure, transcriptional regulation of diverse genes and sporulation, required for glucose repression, HO repression, RME1 repression and sporulation. This subunit is also found in higher eukaryotes and Med14 is the agreed unified nomenclature for this subunit. Med14 is found in the tail region of Mediator.


:

Pssm-ID: 462543  Cd Length: 192  Bit Score: 240.09  E-value: 1.45e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807444   57 LSTLIEFLLHRAYSELMVLTDLLP--RKSDVERKIEIVQFASRTRQLFVRLLALVKWANDAGKVEKCAMISSFLDQQAIL 134
Cdd:pfam08638    4 LSLLVDRLVQRSYNELSELIETLPntSESDVEKKRRLLDFAQRTRQQFIKLLVLVKWSRKAEDVSKLIDLLAFLRQQNMA 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807444  135 FVDTADRLASLARDaLVHARLPSFAIPYAIDVLTTGSYPRLPTCIRDkIIPPDPITKIEKQATLHQLNQILRHRLVTTD- 213
Cdd:pfam08638   84 FEDAADALKNMKRS-LVNARLPNPDLPTALEVLSTGRYPRLPTLIYD-IIPPPPLTPKEILKTLRDLNTLLSIRLNLHEk 161
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1958807444  214 LPPQLANLTVANGRVKFRVEGEFEATLTVMG 244
Cdd:pfam08638  162 IPPQFRNYTIADGRVTFTVPGEFEVDLTIAG 192
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1019-1158 2.61e-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.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 45.53  E-value: 2.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807444 1019 GTSGAYPLTSPPASYHSTVNQSPSMMHT--QSPGALDPS---SPYTMVSPsgragnwpgspqVSGPSPATRLPGMSPANP 1093
Cdd:pfam03154  202 SAPSVPPQGSPATSQPPNQTQSTAAPHTliQQTPTLHPQrlpSPHPPLQP------------MTQPPPPSQVSPQPLPQP 269
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807444 1094 SLHSPVPDVSHSPRAGTSSqtMPTNMPP-PRKLPQRSWAASIP----TILTHSALNILLLPSPTPGLVPG 1158
Cdd:pfam03154  270 SLHGQMPPMPHSLQTGPSH--MQHPVPPqPFPLTPQSSQSQVPpgpsPAAPGQSQQRIHTPPSQSQLQSQ 337
 
Name Accession Description Interval E-value
Med14 pfam08638
Mediator complex subunit MED14; Saccharomyces cerevisiae RGR1 mediator complex subunit affects ...
57-244 1.45e-72

Mediator complex subunit MED14; Saccharomyces cerevisiae RGR1 mediator complex subunit affects chromatin structure, transcriptional regulation of diverse genes and sporulation, required for glucose repression, HO repression, RME1 repression and sporulation. This subunit is also found in higher eukaryotes and Med14 is the agreed unified nomenclature for this subunit. Med14 is found in the tail region of Mediator.


Pssm-ID: 462543  Cd Length: 192  Bit Score: 240.09  E-value: 1.45e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807444   57 LSTLIEFLLHRAYSELMVLTDLLP--RKSDVERKIEIVQFASRTRQLFVRLLALVKWANDAGKVEKCAMISSFLDQQAIL 134
Cdd:pfam08638    4 LSLLVDRLVQRSYNELSELIETLPntSESDVEKKRRLLDFAQRTRQQFIKLLVLVKWSRKAEDVSKLIDLLAFLRQQNMA 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807444  135 FVDTADRLASLARDaLVHARLPSFAIPYAIDVLTTGSYPRLPTCIRDkIIPPDPITKIEKQATLHQLNQILRHRLVTTD- 213
Cdd:pfam08638   84 FEDAADALKNMKRS-LVNARLPNPDLPTALEVLSTGRYPRLPTLIYD-IIPPPPLTPKEILKTLRDLNTLLSIRLNLHEk 161
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1958807444  214 LPPQLANLTVANGRVKFRVEGEFEATLTVMG 244
Cdd:pfam08638  162 IPPQFRNYTIADGRVTFTVPGEFEVDLTIAG 192
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1019-1158 2.61e-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: 45.53  E-value: 2.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807444 1019 GTSGAYPLTSPPASYHSTVNQSPSMMHT--QSPGALDPS---SPYTMVSPsgragnwpgspqVSGPSPATRLPGMSPANP 1093
Cdd:pfam03154  202 SAPSVPPQGSPATSQPPNQTQSTAAPHTliQQTPTLHPQrlpSPHPPLQP------------MTQPPPPSQVSPQPLPQP 269
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807444 1094 SLHSPVPDVSHSPRAGTSSqtMPTNMPP-PRKLPQRSWAASIP----TILTHSALNILLLPSPTPGLVPG 1158
Cdd:pfam03154  270 SLHGQMPPMPHSLQTGPSH--MQHPVPPqPFPLTPQSSQSQVPpgpsPAAPGQSQQRIHTPPSQSQLQSQ 337
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
961-1160 8.33e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.01  E-value: 8.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807444  961 PAPGLKTFLNMFVDSNQDARRRSVNEDDNPPSPIGGDMMDSLISQLQPPQQQPFPKQPGTSGAYPLTSPPasyhstvnqs 1040
Cdd:PHA03307     3 NAPDLYDLIEAAAEGGEFFPRPPATPGDAADDLLSGSQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPP---------- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807444 1041 PSMMHTQSPGALDPSSPYTMVSPSGRAGNWPGSP-QVSGPSPATRLPGMSPANPsLHSPVPDVSHSPRAGTSSQTMPTNM 1119
Cdd:PHA03307    73 PGPGTEAPANESRSTPTWSLSTLAPASPAREGSPtPPGPSSPDPPPPTPPPASP-PPSPAPDLSEMLRPVGSPGPPPAAS 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1958807444 1120 PPPRKLPQRSWAASIPTILtHSALNILLLPSPTPGLVPGLA 1160
Cdd:PHA03307   152 PPAAGASPAAVASDAASSR-QAALPLSSPEETARAPSSPPA 191
 
Name Accession Description Interval E-value
Med14 pfam08638
Mediator complex subunit MED14; Saccharomyces cerevisiae RGR1 mediator complex subunit affects ...
57-244 1.45e-72

Mediator complex subunit MED14; Saccharomyces cerevisiae RGR1 mediator complex subunit affects chromatin structure, transcriptional regulation of diverse genes and sporulation, required for glucose repression, HO repression, RME1 repression and sporulation. This subunit is also found in higher eukaryotes and Med14 is the agreed unified nomenclature for this subunit. Med14 is found in the tail region of Mediator.


Pssm-ID: 462543  Cd Length: 192  Bit Score: 240.09  E-value: 1.45e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807444   57 LSTLIEFLLHRAYSELMVLTDLLP--RKSDVERKIEIVQFASRTRQLFVRLLALVKWANDAGKVEKCAMISSFLDQQAIL 134
Cdd:pfam08638    4 LSLLVDRLVQRSYNELSELIETLPntSESDVEKKRRLLDFAQRTRQQFIKLLVLVKWSRKAEDVSKLIDLLAFLRQQNMA 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807444  135 FVDTADRLASLARDaLVHARLPSFAIPYAIDVLTTGSYPRLPTCIRDkIIPPDPITKIEKQATLHQLNQILRHRLVTTD- 213
Cdd:pfam08638   84 FEDAADALKNMKRS-LVNARLPNPDLPTALEVLSTGRYPRLPTLIYD-IIPPPPLTPKEILKTLRDLNTLLSIRLNLHEk 161
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1958807444  214 LPPQLANLTVANGRVKFRVEGEFEATLTVMG 244
Cdd:pfam08638  162 IPPQFRNYTIADGRVTFTVPGEFEVDLTIAG 192
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1019-1158 2.61e-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: 45.53  E-value: 2.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807444 1019 GTSGAYPLTSPPASYHSTVNQSPSMMHT--QSPGALDPS---SPYTMVSPsgragnwpgspqVSGPSPATRLPGMSPANP 1093
Cdd:pfam03154  202 SAPSVPPQGSPATSQPPNQTQSTAAPHTliQQTPTLHPQrlpSPHPPLQP------------MTQPPPPSQVSPQPLPQP 269
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807444 1094 SLHSPVPDVSHSPRAGTSSqtMPTNMPP-PRKLPQRSWAASIP----TILTHSALNILLLPSPTPGLVPG 1158
Cdd:pfam03154  270 SLHGQMPPMPHSLQTGPSH--MQHPVPPqPFPLTPQSSQSQVPpgpsPAAPGQSQQRIHTPPSQSQLQSQ 337
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1028-1127 2.79e-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: 45.53  E-value: 2.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807444 1028 SPPASYHSTVNQSPSMMHTQSPGALDPSSPYTMVSPSGRAGNWPGSPQVSG-PSPATRLPGMSP-----------ANPSL 1095
Cdd:pfam03154  158 SDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPqGSPATSQPPNQTqstaaphtliqQTPTL 237
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1958807444 1096 HSPVPDVSHSPragtsSQTMPTNMPPPRKLPQ 1127
Cdd:pfam03154  238 HPQRLPSPHPP-----LQPMTQPPPPSQVSPQ 264
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
961-1160 8.33e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.01  E-value: 8.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807444  961 PAPGLKTFLNMFVDSNQDARRRSVNEDDNPPSPIGGDMMDSLISQLQPPQQQPFPKQPGTSGAYPLTSPPasyhstvnqs 1040
Cdd:PHA03307     3 NAPDLYDLIEAAAEGGEFFPRPPATPGDAADDLLSGSQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPP---------- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807444 1041 PSMMHTQSPGALDPSSPYTMVSPSGRAGNWPGSP-QVSGPSPATRLPGMSPANPsLHSPVPDVSHSPRAGTSSQTMPTNM 1119
Cdd:PHA03307    73 PGPGTEAPANESRSTPTWSLSTLAPASPAREGSPtPPGPSSPDPPPPTPPPASP-PPSPAPDLSEMLRPVGSPGPPPAAS 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1958807444 1120 PPPRKLPQRSWAASIPTILtHSALNILLLPSPTPGLVPGLA 1160
Cdd:PHA03307   152 PPAAGASPAAVASDAASSR-QAALPLSSPEETARAPSSPPA 191
PHA03247 PHA03247
large tegument protein UL36; Provisional
1020-1157 5.20e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 5.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807444 1020 TSGAYPLTSPPASYHSTVNQSPSMMHTQSPGALDPSSPYTMVSPSGRAGNWPGSPQVSGPSPATRLPgMSPANPSLHSPV 1099
Cdd:PHA03247  2770 APPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQP-TAPPPPPGPPPP 2848
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958807444 1100 P-----------DVShspRAGTSSQTMPTNMPPPRkLPQRSWAASIPTILTHSalnillLPSPTPGLVP 1157
Cdd:PHA03247  2849 SlplggsvapggDVR---RRPPSRSPAAKPAAPAR-PPVRRLARPAVSRSTES------FALPPDQPER 2907
 
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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