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Conserved domains on  [gi|1622875468|ref|XP_014973797|]
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mediator of RNA polymerase II transcription subunit 31 isoform X1 [Macaca mulatta]

Protein Classification

mediator of RNA polymerase II transcription subunit 31( domain architecture ID 10529302)

mediator of RNA polymerase II transcription subunit 31 is a component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Med31 pfam05669
SOH1; The family consists of Saccharomyces cerevisiae SOH1 homologs. SOH1 is responsible for ...
105-157 4.03e-39

SOH1; The family consists of Saccharomyces cerevisiae SOH1 homologs. SOH1 is responsible for the repression of temperature sensitive growth of the HPR1 mutant and has been found to be a component of the RNA polymerase II transcription complex. SOH1 not only interacts with factors involved in DNA repair, but transcription as well. Thus, the SOH1 protein may serve to couple these two processes.


:

Pssm-ID: 428575  Cd Length: 95  Bit Score: 128.79  E-value: 4.03e-39
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622875468 105 RLRFQLELEFVQCLANPNYLNFLAQRGYFKDKAFVNYLKYLLYWKDPEYAKYL 157
Cdd:pfam05669   1 KTRFELELEFVQSLANPQYLNHLAQNGYLEDPAFINYLKYLQYWKEPEYAKFL 53
 
Name Accession Description Interval E-value
Med31 pfam05669
SOH1; The family consists of Saccharomyces cerevisiae SOH1 homologs. SOH1 is responsible for ...
105-157 4.03e-39

SOH1; The family consists of Saccharomyces cerevisiae SOH1 homologs. SOH1 is responsible for the repression of temperature sensitive growth of the HPR1 mutant and has been found to be a component of the RNA polymerase II transcription complex. SOH1 not only interacts with factors involved in DNA repair, but transcription as well. Thus, the SOH1 protein may serve to couple these two processes.


Pssm-ID: 428575  Cd Length: 95  Bit Score: 128.79  E-value: 4.03e-39
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622875468 105 RLRFQLELEFVQCLANPNYLNFLAQRGYFKDKAFVNYLKYLLYWKDPEYAKYL 157
Cdd:pfam05669   1 KTRFELELEFVQSLANPQYLNHLAQNGYLEDPAFINYLKYLQYWKEPEYAKFL 53
SOH1 COG5088
Rad5p-binding protein [General function prediction only];
107-157 6.05e-22

Rad5p-binding protein [General function prediction only];


Pssm-ID: 227420  Cd Length: 114  Bit Score: 85.70  E-value: 6.05e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622875468 107 RFQLELEFVQCLANPNYLNFLAQRGYFKDKAFVNYLKYLLYWKDPEYAKYL 157
Cdd:COG5088    16 RFEVELEFVQSLANPQYLTLLTQQQIFESENFKNYLKYLEYWRNPEYSQFI 66
 
Name Accession Description Interval E-value
Med31 pfam05669
SOH1; The family consists of Saccharomyces cerevisiae SOH1 homologs. SOH1 is responsible for ...
105-157 4.03e-39

SOH1; The family consists of Saccharomyces cerevisiae SOH1 homologs. SOH1 is responsible for the repression of temperature sensitive growth of the HPR1 mutant and has been found to be a component of the RNA polymerase II transcription complex. SOH1 not only interacts with factors involved in DNA repair, but transcription as well. Thus, the SOH1 protein may serve to couple these two processes.


Pssm-ID: 428575  Cd Length: 95  Bit Score: 128.79  E-value: 4.03e-39
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622875468 105 RLRFQLELEFVQCLANPNYLNFLAQRGYFKDKAFVNYLKYLLYWKDPEYAKYL 157
Cdd:pfam05669   1 KTRFELELEFVQSLANPQYLNHLAQNGYLEDPAFINYLKYLQYWKEPEYAKFL 53
SOH1 COG5088
Rad5p-binding protein [General function prediction only];
107-157 6.05e-22

Rad5p-binding protein [General function prediction only];


Pssm-ID: 227420  Cd Length: 114  Bit Score: 85.70  E-value: 6.05e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622875468 107 RFQLELEFVQCLANPNYLNFLAQRGYFKDKAFVNYLKYLLYWKDPEYAKYL 157
Cdd:COG5088    16 RFEVELEFVQSLANPQYLTLLTQQQIFESENFKNYLKYLEYWRNPEYSQFI 66
 
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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