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Conserved domains on  [gi|28558979|ref|NP_004260|]
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mediator of RNA polymerase II transcription subunit 27 isoform 1 [Homo sapiens]

Protein Classification

mediator of RNA polymerase II transcription subunit 27( domain architecture ID 10569016)

mediator of RNA polymerase II transcription subunit 27 (Med27) 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
Med27 pfam11571
Mediator complex subunit 27; Mediator is a large complex of up to 33 proteins that is ...
228-309 2.42e-34

Mediator complex subunit 27; Mediator is a large complex of up to 33 proteins that is conserved from plants to fungi to humans - the number and representation of individual subunits varying with species {1-2]. It is arranged into four different sections, a core, a head, a tail and a kinase-activity part, and the number of subunits within each of these is what varies with species. Overall, Mediator regulates the transcriptional activity of RNA polymerase II but it would appear that each of the four different sections has a slightly different function. Mediator exists in two major forms in human cells: a smaller form that interacts strongly with pol II and activates transcription, and a large form that does not interact strongly with pol II and does not directly activate transcription. The ubiquitous expression of Med27 mRNA suggests a universal requirement for Med27 in transcriptional initiation. Loss of Crsp34/Med27 decreases amacrine cell number, but increases the number of rod photoreceptor cells.


:

Pssm-ID: 463298  Cd Length: 85  Bit Score: 120.09  E-value: 2.42e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558979   228 LDIWSKSNYQVFQKVTDHATTALLHYQLPQMPDVVVRSFMTWLRSYIKLFQAPCQRCGKFLQ--DGLPPTWRDFR-TLEA 304
Cdd:pfam11571   1 VDLWSPSRYKVFRKLTEHANTAILHFLNSRPPQLDLKSFLDWISSYSNLFSTPCKKCGKLLDsdSFLPPVRRDFRsTWEA 80

                  ....*
gi 28558979   305 FHDTC 309
Cdd:pfam11571  81 YHEEC 85
 
Name Accession Description Interval E-value
Med27 pfam11571
Mediator complex subunit 27; Mediator is a large complex of up to 33 proteins that is ...
228-309 2.42e-34

Mediator complex subunit 27; Mediator is a large complex of up to 33 proteins that is conserved from plants to fungi to humans - the number and representation of individual subunits varying with species {1-2]. It is arranged into four different sections, a core, a head, a tail and a kinase-activity part, and the number of subunits within each of these is what varies with species. Overall, Mediator regulates the transcriptional activity of RNA polymerase II but it would appear that each of the four different sections has a slightly different function. Mediator exists in two major forms in human cells: a smaller form that interacts strongly with pol II and activates transcription, and a large form that does not interact strongly with pol II and does not directly activate transcription. The ubiquitous expression of Med27 mRNA suggests a universal requirement for Med27 in transcriptional initiation. Loss of Crsp34/Med27 decreases amacrine cell number, but increases the number of rod photoreceptor cells.


Pssm-ID: 463298  Cd Length: 85  Bit Score: 120.09  E-value: 2.42e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558979   228 LDIWSKSNYQVFQKVTDHATTALLHYQLPQMPDVVVRSFMTWLRSYIKLFQAPCQRCGKFLQ--DGLPPTWRDFR-TLEA 304
Cdd:pfam11571   1 VDLWSPSRYKVFRKLTEHANTAILHFLNSRPPQLDLKSFLDWISSYSNLFSTPCKKCGKLLDsdSFLPPVRRDFRsTWEA 80

                  ....*
gi 28558979   305 FHDTC 309
Cdd:pfam11571  81 YHEEC 85
 
Name Accession Description Interval E-value
Med27 pfam11571
Mediator complex subunit 27; Mediator is a large complex of up to 33 proteins that is ...
228-309 2.42e-34

Mediator complex subunit 27; Mediator is a large complex of up to 33 proteins that is conserved from plants to fungi to humans - the number and representation of individual subunits varying with species {1-2]. It is arranged into four different sections, a core, a head, a tail and a kinase-activity part, and the number of subunits within each of these is what varies with species. Overall, Mediator regulates the transcriptional activity of RNA polymerase II but it would appear that each of the four different sections has a slightly different function. Mediator exists in two major forms in human cells: a smaller form that interacts strongly with pol II and activates transcription, and a large form that does not interact strongly with pol II and does not directly activate transcription. The ubiquitous expression of Med27 mRNA suggests a universal requirement for Med27 in transcriptional initiation. Loss of Crsp34/Med27 decreases amacrine cell number, but increases the number of rod photoreceptor cells.


Pssm-ID: 463298  Cd Length: 85  Bit Score: 120.09  E-value: 2.42e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558979   228 LDIWSKSNYQVFQKVTDHATTALLHYQLPQMPDVVVRSFMTWLRSYIKLFQAPCQRCGKFLQ--DGLPPTWRDFR-TLEA 304
Cdd:pfam11571   1 VDLWSPSRYKVFRKLTEHANTAILHFLNSRPPQLDLKSFLDWISSYSNLFSTPCKKCGKLLDsdSFLPPVRRDFRsTWEA 80

                  ....*
gi 28558979   305 FHDTC 309
Cdd:pfam11571  81 YHEEC 85
 
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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