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Conserved domains on  [gi|21356325|ref|NP_650854|]
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mediator complex subunit 25 [Drosophila melanogaster]

Protein Classification

Med25_VWA and Med25 domain-containing protein( domain architecture ID 10567997)

Med25_VWA and Med25 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Med25_VWA pfam11265
Mediator complex subunit 25 von Willebrand factor type A; The overall function of the ...
 5-218 1.05e-115

Mediator complex subunit 25 von Willebrand factor type A; The overall function of the full-length Med25 is efficiently to coordinate the transcriptional activation of RAR/RXR (retinoic acid receptor/retinoic X receptor) in higher eukaryotic cells. Human Med25 consists of several domains with different binding properties, the N-terminal, VWA domain which is this one, an SD2 domain from residues 229-381, a PTOV(B) or ACID domain from 395-545, an SD2 domain from residues 564-645 and a C-terminal NR box-containing domain (646-650) from 646-747. This VWA or von Willebrand factor type A domain when bound to RAR and the histone acetyltransferase CBP is responsible for recruiting Med1 to the rest of the Mediator complex.


:

Pssm-ID: 463253  Cd Length: 213  Bit Score: 350.83  E-value: 1.05e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356325     5 QIPLADVVFVIEGSAINGAYINELKTNYILPTLEHFTTGSIDEREYLiAERFATLYGIVVYRTAANLLEPVCSTYGPFLQ 84
Cdd:pfam11265   1 SSVVADVVFVVEGTANLGAYFNELKTNYILPTLEYFNGGPIEERDYG-SENGSTLYGLVVYHAADCLPEPSVQCYGPTSS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356325    85 PQKVMETIERLPLVGGGMESCAHMAEGFAAAHGCFDDISERRQLLDQtSVQRHCILICNSPPYQMPTTESWKYPGKSCEQ 164
Cdd:pfam11265  80 PHKFLQWLDKIDFSGGGGESCALIAEGLATALQCFDDLQKIRENPGL-ACQRHCILICNSPPYQLPVMESPTYTGKTAEQ 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 21356325   165 LAALFNERKINLSIIAPRKMPVLFKLFMKADGDQPI-TSKNYAKNIRHLVLLKGY 218
Cdd:pfam11265 159 LAALMAERNIHLSIISPRKIPALFKLFEKAGPDLPSsPSKNYAKDPRHLVLLRGF 213
Med25 pfam11232
Mediator complex subunit 25 PTOV activation and synapsin 2; Mediator is a large complex of up ...
 520-671 1.02e-80

Mediator complex subunit 25 PTOV activation and synapsin 2; 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. It is arranged into four different sections, a core, a head, a tail and a kinase-active 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. The overall function of the full-length Med25 is efficiently to coordinate the transcriptional activation of RAR/RXR (retinoic acid receptor/retinoic X receptor) in higher eukaryotic cells. Human Med25 consists of several domains with different binding properties, the N-terminal, VWA domain, an SD1 - synapsin 1 - domain from residues 229-381, a PTOV(B) or ACID domain from 395-545, an SD2 domain from residues 564-645 and a C-terminal NR box-containing domain (646-650) from 646-747. This family is the combined PTOV and SD2 domains. the PTOV domain being the domain through which Med25 co-operates with the histone acetyltransferase CBP, but the function of the SD2 domain is unclear.


:

Pssm-ID: 463243  Cd Length: 154  Bit Score: 256.50  E-value: 1.02e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356325   520 SLREKIWTGVLEWSEKPKSDQQKIPHTLQCTVCTNIKDGEPEIKAENWPPKLLMQLMPKHLVGNIGGQFLKDSKMVVFRP 599
Cdd:pfam11232   1 SQRELIWSGVLEWQEKMSDQNPKITRTLPCQVSNSVKNGEPELKAEKWPQKLIMQLMPKTLLGNIGGALLRNSRVVVFHF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21356325   600 TP--GEALDSLAKMMTSGYAGCVHFSSIPNSPACDLKVLILLYTPDRNAFLGFIPNNQAMFVERLRKVIQQKQH 671
Cdd:pfam11232  81 TPtdLEALKSLYRVMSNGFAGCVHFPGIPANPQCDIKVLMLLYSPKKNAFMGLIPNDQAAFVNRLRQVIKKQKQ 154
 
Name Accession Description Interval E-value
Med25_VWA pfam11265
Mediator complex subunit 25 von Willebrand factor type A; The overall function of the ...
 5-218 1.05e-115

Mediator complex subunit 25 von Willebrand factor type A; The overall function of the full-length Med25 is efficiently to coordinate the transcriptional activation of RAR/RXR (retinoic acid receptor/retinoic X receptor) in higher eukaryotic cells. Human Med25 consists of several domains with different binding properties, the N-terminal, VWA domain which is this one, an SD2 domain from residues 229-381, a PTOV(B) or ACID domain from 395-545, an SD2 domain from residues 564-645 and a C-terminal NR box-containing domain (646-650) from 646-747. This VWA or von Willebrand factor type A domain when bound to RAR and the histone acetyltransferase CBP is responsible for recruiting Med1 to the rest of the Mediator complex.


Pssm-ID: 463253  Cd Length: 213  Bit Score: 350.83  E-value: 1.05e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356325     5 QIPLADVVFVIEGSAINGAYINELKTNYILPTLEHFTTGSIDEREYLiAERFATLYGIVVYRTAANLLEPVCSTYGPFLQ 84
Cdd:pfam11265   1 SSVVADVVFVVEGTANLGAYFNELKTNYILPTLEYFNGGPIEERDYG-SENGSTLYGLVVYHAADCLPEPSVQCYGPTSS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356325    85 PQKVMETIERLPLVGGGMESCAHMAEGFAAAHGCFDDISERRQLLDQtSVQRHCILICNSPPYQMPTTESWKYPGKSCEQ 164
Cdd:pfam11265  80 PHKFLQWLDKIDFSGGGGESCALIAEGLATALQCFDDLQKIRENPGL-ACQRHCILICNSPPYQLPVMESPTYTGKTAEQ 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 21356325   165 LAALFNERKINLSIIAPRKMPVLFKLFMKADGDQPI-TSKNYAKNIRHLVLLKGY 218
Cdd:pfam11265 159 LAALMAERNIHLSIISPRKIPALFKLFEKAGPDLPSsPSKNYAKDPRHLVLLRGF 213
Med25 pfam11232
Mediator complex subunit 25 PTOV activation and synapsin 2; Mediator is a large complex of up ...
 520-671 1.02e-80

Mediator complex subunit 25 PTOV activation and synapsin 2; 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. It is arranged into four different sections, a core, a head, a tail and a kinase-active 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. The overall function of the full-length Med25 is efficiently to coordinate the transcriptional activation of RAR/RXR (retinoic acid receptor/retinoic X receptor) in higher eukaryotic cells. Human Med25 consists of several domains with different binding properties, the N-terminal, VWA domain, an SD1 - synapsin 1 - domain from residues 229-381, a PTOV(B) or ACID domain from 395-545, an SD2 domain from residues 564-645 and a C-terminal NR box-containing domain (646-650) from 646-747. This family is the combined PTOV and SD2 domains. the PTOV domain being the domain through which Med25 co-operates with the histone acetyltransferase CBP, but the function of the SD2 domain is unclear.


Pssm-ID: 463243  Cd Length: 154  Bit Score: 256.50  E-value: 1.02e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356325   520 SLREKIWTGVLEWSEKPKSDQQKIPHTLQCTVCTNIKDGEPEIKAENWPPKLLMQLMPKHLVGNIGGQFLKDSKMVVFRP 599
Cdd:pfam11232   1 SQRELIWSGVLEWQEKMSDQNPKITRTLPCQVSNSVKNGEPELKAEKWPQKLIMQLMPKTLLGNIGGALLRNSRVVVFHF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21356325   600 TP--GEALDSLAKMMTSGYAGCVHFSSIPNSPACDLKVLILLYTPDRNAFLGFIPNNQAMFVERLRKVIQQKQH 671
Cdd:pfam11232  81 TPtdLEALKSLYRVMSNGFAGCVHFPGIPANPQCDIKVLMLLYSPKKNAFMGLIPNDQAAFVNRLRQVIKKQKQ 154
 
Name Accession Description Interval E-value
Med25_VWA pfam11265
Mediator complex subunit 25 von Willebrand factor type A; The overall function of the ...
 5-218 1.05e-115

Mediator complex subunit 25 von Willebrand factor type A; The overall function of the full-length Med25 is efficiently to coordinate the transcriptional activation of RAR/RXR (retinoic acid receptor/retinoic X receptor) in higher eukaryotic cells. Human Med25 consists of several domains with different binding properties, the N-terminal, VWA domain which is this one, an SD2 domain from residues 229-381, a PTOV(B) or ACID domain from 395-545, an SD2 domain from residues 564-645 and a C-terminal NR box-containing domain (646-650) from 646-747. This VWA or von Willebrand factor type A domain when bound to RAR and the histone acetyltransferase CBP is responsible for recruiting Med1 to the rest of the Mediator complex.


Pssm-ID: 463253  Cd Length: 213  Bit Score: 350.83  E-value: 1.05e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356325     5 QIPLADVVFVIEGSAINGAYINELKTNYILPTLEHFTTGSIDEREYLiAERFATLYGIVVYRTAANLLEPVCSTYGPFLQ 84
Cdd:pfam11265   1 SSVVADVVFVVEGTANLGAYFNELKTNYILPTLEYFNGGPIEERDYG-SENGSTLYGLVVYHAADCLPEPSVQCYGPTSS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356325    85 PQKVMETIERLPLVGGGMESCAHMAEGFAAAHGCFDDISERRQLLDQtSVQRHCILICNSPPYQMPTTESWKYPGKSCEQ 164
Cdd:pfam11265  80 PHKFLQWLDKIDFSGGGGESCALIAEGLATALQCFDDLQKIRENPGL-ACQRHCILICNSPPYQLPVMESPTYTGKTAEQ 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 21356325   165 LAALFNERKINLSIIAPRKMPVLFKLFMKADGDQPI-TSKNYAKNIRHLVLLKGY 218
Cdd:pfam11265 159 LAALMAERNIHLSIISPRKIPALFKLFEKAGPDLPSsPSKNYAKDPRHLVLLRGF 213
Med25 pfam11232
Mediator complex subunit 25 PTOV activation and synapsin 2; Mediator is a large complex of up ...
 520-671 1.02e-80

Mediator complex subunit 25 PTOV activation and synapsin 2; 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. It is arranged into four different sections, a core, a head, a tail and a kinase-active 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. The overall function of the full-length Med25 is efficiently to coordinate the transcriptional activation of RAR/RXR (retinoic acid receptor/retinoic X receptor) in higher eukaryotic cells. Human Med25 consists of several domains with different binding properties, the N-terminal, VWA domain, an SD1 - synapsin 1 - domain from residues 229-381, a PTOV(B) or ACID domain from 395-545, an SD2 domain from residues 564-645 and a C-terminal NR box-containing domain (646-650) from 646-747. This family is the combined PTOV and SD2 domains. the PTOV domain being the domain through which Med25 co-operates with the histone acetyltransferase CBP, but the function of the SD2 domain is unclear.


Pssm-ID: 463243  Cd Length: 154  Bit Score: 256.50  E-value: 1.02e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356325   520 SLREKIWTGVLEWSEKPKSDQQKIPHTLQCTVCTNIKDGEPEIKAENWPPKLLMQLMPKHLVGNIGGQFLKDSKMVVFRP 599
Cdd:pfam11232   1 SQRELIWSGVLEWQEKMSDQNPKITRTLPCQVSNSVKNGEPELKAEKWPQKLIMQLMPKTLLGNIGGALLRNSRVVVFHF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21356325   600 TP--GEALDSLAKMMTSGYAGCVHFSSIPNSPACDLKVLILLYTPDRNAFLGFIPNNQAMFVERLRKVIQQKQH 671
Cdd:pfam11232  81 TPtdLEALKSLYRVMSNGFAGCVHFPGIPANPQCDIKVLMLLYSPKKNAFMGLIPNDQAAFVNRLRQVIKKQKQ 154
 
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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