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Conserved domains on  [gi|1063759688|ref|NP_001318136|]
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mediator of RNA polymerase II transcription subunit 25 isoform 3 [Mus musculus]

Protein Classification

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 ...
 12-226 1.27e-119

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: 359.30  E-value: 1.27e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688  12 GGLVADVVFVIEGTANLGPYFEELRKHYLLPAIEYFNGGPPAETDFGGDYGGTQYSLVVFNTVDCAPESYVQCHAPTSSA 91
Cdd:pfam11265   1 SSVVADVVFVVEGTANLGAYFNELKTNYILPTLEYFNGGPIEERDYGSENGSTLYGLVVYHAADCLPEPSVQCYGPTSSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688  92 YEFVTWLDGIKFMGGGGESCSLIAEGLSTALQLFDDFKKMREQIG-QTHRVCLLICNSPPYLLPAVESTTYSGCTTESLV 170
Cdd:pfam11265  81 HKFLQWLDKIDFSGGGGESCALIAEGLATALQCFDDLQKIRENPGlACQRHCILICNSPPYQLPVMESPTYTGKTAEQLA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063759688 171 QKIGERGIHFSIVSPRKLPALRLLFEKAAPPallEPLQQPADVSQDPRHMVLVRGL 226
Cdd:pfam11265 161 ALMAERNIHLSIISPRKIPALFKLFEKAGPD---LPSSPSKNYAKDPRHLVLLRGF 213
Med25 pfam11232
Mediator complex subunit 25 PTOV activation and synapsin 2; Mediator is a large complex of up ...
 396-545 1.54e-79

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: 252.27  E-value: 1.54e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688 396 SNKLLAWSGVLEWQEKPKpasvDANTKLTRSLPCQV--YVNHGE-NLKTEQWPQKLIMQLIPQQLLTTLG-PLFRNSRMV 471
Cdd:pfam11232   1 SQRELIWSGVLEWQEKMS----DQNPKITRTLPCQVsnSVKNGEpELKAEKWPQKLIMQLMPKTLLGNIGgALLRNSRVV 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063759688 472 QFHFTNKDLESLKGLYRIMGNGFAGCVHF---PHTAPCEVRVLMLLYSSKKKIFMGLIPYDQSGFVNGIRQVITNHK 545
Cdd:pfam11232  77 VFHFTPTDLEALKSLYRVMSNGFAGCVHFpgiPANPQCDIKVLMLLYSPKKNAFMGLIPNDQAAFVNRLRQVIKKQK 153
Med25_SD1 super family cl25802
Mediator complex subunit 25 synapsin 1; The overall function of the full-length Med25 is ...
 228-383 4.20e-32

Mediator complex subunit 25 synapsin 1; 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, this 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 The function of the SD domains is unclear.


The actual alignment was detected with superfamily member pfam11235:

Pssm-ID: 463244 [Multi-domain]  Cd Length: 157  Bit Score: 122.20  E-value: 4.20e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688 228 LPVGGSSTSGSLQTKQAVPLPPAPASAATLSAAPPQALPPVPPQYQVPGNLSAAQVAAQNAVEAAKSQKAGLGPRFSPIN 307
Cdd:pfam11235   1 LPVGGGSAPGPLQSKQPVPLPPAAPSGATLSAAPQQPLPPVPPQYQVPGNLSAAQVAAQNAVEAAKNQKAGLGPRFSPIT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063759688 308 PLQQAAPGVGPPFSQAPAPPLAP-VPPGAPKPPPASQPSLVSTVAPGPVLAAPAQPGAPSLAGTVTPGGVNGPSAAQ 383
Cdd:pfam11235  81 PLQQAAPGVGPPFSQAPAPQLPPgPPGAPKPVPPASQPSLVSTVAPGSGLAPTAQPGAPSMAGTVAPGGVSGPSPAQ 157
Med25_NR-box pfam11244
Mediator complex subunit 25 C-terminal NR box-containing; The overall function of the ...
 657-713 5.18e-21

Mediator complex subunit 25 C-terminal NR box-containing; 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 this C-terminal NR box-containing domain (646-650) from C69-747. The NR box of MED25 is critical for its recruitment to the promoter, probably through an interaction with pre bound RAR.


:

Pssm-ID: 463246 [Multi-domain]  Cd Length: 89  Bit Score: 88.17  E-value: 5.18e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063759688 657 TGVPPPQASLHHLQPPGAPTLLPPHQSMGQPQLGPQLLHPPPAQSWPTQLPQRAPLP 713
Cdd:pfam11244   1 TSVPQTQQPLHHMQQAAQGMLPHQHQAPGQQQLGQTLMHQAPAQSWGAQLPPRAPLP 57
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 561-720 2.73e-05

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: 47.84  E-value: 2.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688 561 QQAPPVL---GPILEEQARPPQNLLQLRAPQPQPqgavgaSAATGQPQPQGATQAPTGAPQGPPGAAPGPPPSGPILRPQ 637
Cdd:pfam03154 168 QTQPPVLqaqSGAASPPSPPPPGTTQAATAGPTP------SAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQR 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688 638 NPGANPQLRSLLLNPAPPQTGVPP-PQASLHHLQPPGA----------PTLLPPH-------QSMGQPQLGPQLLHPPPA 699
Cdd:pfam03154 242 LPSPHPPLQPMTQPPPPSQVSPQPlPQPSLHGQMPPMPhslqtgpshmQHPVPPQpfpltpqSSQSQVPPGPSPAAPGQS 321

                         170       180
                  ....*....|....*....|.
gi 1063759688 700 QSWPTQLPQRAPLPVAKRKRE 720
Cdd:pfam03154 322 QQRIHTPPSQSQLQSQQPPRE 342
DUF4371 super family cl46273
Domain of unknown function (DUF4371);
728-786 1.32e-04

Domain of unknown function (DUF4371);


The actual alignment was detected with superfamily member pfam18658:

Pssm-ID: 480613  Cd Length: 64  Bit Score: 40.72  E-value: 1.32e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063759688 728 EKWERDYFFV--EVKSMPTCLICKKNVSVLKEYNLKRHYESQHsKSYDQYTAQSRDTLLQE 786
Cdd:pfam18658   2 ERWRLEYLMDydPGRNGLVCMVCGESLASLKLSTIKRHILQKH-PDTLSLSPEEKEAILEA 61
 
Name Accession Description Interval E-value
Med25_VWA pfam11265
Mediator complex subunit 25 von Willebrand factor type A; The overall function of the ...
 12-226 1.27e-119

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: 359.30  E-value: 1.27e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688  12 GGLVADVVFVIEGTANLGPYFEELRKHYLLPAIEYFNGGPPAETDFGGDYGGTQYSLVVFNTVDCAPESYVQCHAPTSSA 91
Cdd:pfam11265   1 SSVVADVVFVVEGTANLGAYFNELKTNYILPTLEYFNGGPIEERDYGSENGSTLYGLVVYHAADCLPEPSVQCYGPTSSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688  92 YEFVTWLDGIKFMGGGGESCSLIAEGLSTALQLFDDFKKMREQIG-QTHRVCLLICNSPPYLLPAVESTTYSGCTTESLV 170
Cdd:pfam11265  81 HKFLQWLDKIDFSGGGGESCALIAEGLATALQCFDDLQKIRENPGlACQRHCILICNSPPYQLPVMESPTYTGKTAEQLA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063759688 171 QKIGERGIHFSIVSPRKLPALRLLFEKAAPPallEPLQQPADVSQDPRHMVLVRGL 226
Cdd:pfam11265 161 ALMAERNIHLSIISPRKIPALFKLFEKAGPD---LPSSPSKNYAKDPRHLVLLRGF 213
Med25 pfam11232
Mediator complex subunit 25 PTOV activation and synapsin 2; Mediator is a large complex of up ...
 396-545 1.54e-79

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: 252.27  E-value: 1.54e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688 396 SNKLLAWSGVLEWQEKPKpasvDANTKLTRSLPCQV--YVNHGE-NLKTEQWPQKLIMQLIPQQLLTTLG-PLFRNSRMV 471
Cdd:pfam11232   1 SQRELIWSGVLEWQEKMS----DQNPKITRTLPCQVsnSVKNGEpELKAEKWPQKLIMQLMPKTLLGNIGgALLRNSRVV 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063759688 472 QFHFTNKDLESLKGLYRIMGNGFAGCVHF---PHTAPCEVRVLMLLYSSKKKIFMGLIPYDQSGFVNGIRQVITNHK 545
Cdd:pfam11232  77 VFHFTPTDLEALKSLYRVMSNGFAGCVHFpgiPANPQCDIKVLMLLYSPKKNAFMGLIPNDQAAFVNRLRQVIKKQK 153
Med25_SD1 pfam11235
Mediator complex subunit 25 synapsin 1; The overall function of the full-length Med25 is ...
 228-383 4.20e-32

Mediator complex subunit 25 synapsin 1; 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, this 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 The function of the SD domains is unclear.


Pssm-ID: 463244 [Multi-domain]  Cd Length: 157  Bit Score: 122.20  E-value: 4.20e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688 228 LPVGGSSTSGSLQTKQAVPLPPAPASAATLSAAPPQALPPVPPQYQVPGNLSAAQVAAQNAVEAAKSQKAGLGPRFSPIN 307
Cdd:pfam11235   1 LPVGGGSAPGPLQSKQPVPLPPAAPSGATLSAAPQQPLPPVPPQYQVPGNLSAAQVAAQNAVEAAKNQKAGLGPRFSPIT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063759688 308 PLQQAAPGVGPPFSQAPAPPLAP-VPPGAPKPPPASQPSLVSTVAPGPVLAAPAQPGAPSLAGTVTPGGVNGPSAAQ 383
Cdd:pfam11235  81 PLQQAAPGVGPPFSQAPAPQLPPgPPGAPKPVPPASQPSLVSTVAPGSGLAPTAQPGAPSMAGTVAPGGVSGPSPAQ 157
Med25_NR-box pfam11244
Mediator complex subunit 25 C-terminal NR box-containing; The overall function of the ...
 657-713 5.18e-21

Mediator complex subunit 25 C-terminal NR box-containing; 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 this C-terminal NR box-containing domain (646-650) from C69-747. The NR box of MED25 is critical for its recruitment to the promoter, probably through an interaction with pre bound RAR.


Pssm-ID: 463246 [Multi-domain]  Cd Length: 89  Bit Score: 88.17  E-value: 5.18e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063759688 657 TGVPPPQASLHHLQPPGAPTLLPPHQSMGQPQLGPQLLHPPPAQSWPTQLPQRAPLP 713
Cdd:pfam11244   1 TSVPQTQQPLHHMQQAAQGMLPHQHQAPGQQQLGQTLMHQAPAQSWGAQLPPRAPLP 57
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 561-720 2.73e-05

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: 47.84  E-value: 2.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688 561 QQAPPVL---GPILEEQARPPQNLLQLRAPQPQPqgavgaSAATGQPQPQGATQAPTGAPQGPPGAAPGPPPSGPILRPQ 637
Cdd:pfam03154 168 QTQPPVLqaqSGAASPPSPPPPGTTQAATAGPTP------SAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQR 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688 638 NPGANPQLRSLLLNPAPPQTGVPP-PQASLHHLQPPGA----------PTLLPPH-------QSMGQPQLGPQLLHPPPA 699
Cdd:pfam03154 242 LPSPHPPLQPMTQPPPPSQVSPQPlPQPSLHGQMPPMPhslqtgpshmQHPVPPQpfpltpqSSQSQVPPGPSPAAPGQS 321

                         170       180
                  ....*....|....*....|.
gi 1063759688 700 QSWPTQLPQRAPLPVAKRKRE 720
Cdd:pfam03154 322 QQRIHTPPSQSQLQSQQPPRE 342
zf-C2H2_12 pfam18658
Spin-doc zinc-finger; This is a zinc finger domain C2H2 type which can be found in SPIN1 ...
 728-786 1.32e-04

Spin-doc zinc-finger; This is a zinc finger domain C2H2 type which can be found in SPIN1 docking protein (SPIN-DOC) and Epm2a-interacting protein 1 (Epm2aip1). SPIN-DOC is a Spindlin1 (SPIN1) regulator that directly binds and strongly disrupts its histone methylation reading ability, causing it to disassociate from chromatin. Epm2aip1 is a glycogen synthase (GS)-associated protein. In the absence of Epm2aip1, the sensitivity of the liver to insulin, in which GS is a principal actor, is impaired.


Pssm-ID: 465831  Cd Length: 64  Bit Score: 40.72  E-value: 1.32e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063759688 728 EKWERDYFFV--EVKSMPTCLICKKNVSVLKEYNLKRHYESQHsKSYDQYTAQSRDTLLQE 786
Cdd:pfam18658   2 ERWRLEYLMDydPGRNGLVCMVCGESLASLKLSTIKRHILQKH-PDTLSLSPEEKEAILEA 61
PHA03247 PHA03247
large tegument protein UL36; Provisional
 560-721 6.06e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 6.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688  560 AQQAPPVLGPILEEQARPPqnllqLRAPQPQPQGAVGASAATGQP-QPQGATQAPtgapqgppGAAPGPPPSGPILRPQN 638
Cdd:PHA03247  2822 ASPAGPLPPPTSAQPTAPP-----PPPGPPPPSLPLGGSVAPGGDvRRRPPSRSP--------AAKPAAPARPPVRRLAR 2888

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688  639 PGANPQLRSLLLNPAPPQtgvPPPQASlhhLQPPGAPTLLPPHQSMGQPQLGPQLLHPPPAQSWPTQLPQRAPLPVAKRK 718
Cdd:PHA03247  2889 PAVSRSTESFALPPDQPE---RPPQPQ---APPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQP 2962


                   ...
gi 1063759688  719 REG 721
Cdd:PHA03247  2963 WLG 2965
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 559-715 8.02e-03

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 39.66  E-value: 8.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688 559 GAQQAPPVLGPIleeqaRPPQNLLQLRAPQP-QPQGAVGAS--AATGQPQPQGATQAPTGapqgppgaapgpppsgpiLR 635
Cdd:COG5180   306 GVASAPPATRPV-----RPPGGARDPGTPRPgQPTERPAGVpeAASDAGQPPSAYPPAEE------------------AV 362

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688 636 PQNPGAN--PQLRSLLLNPAPPQTGVPPPQASLHHLQPPGAPTLLPPHQSMGQPQLGPQLLHPPPAQSWPTQLPQRAPLP 713
Cdd:COG5180   363 PGKPLEQgaPRPGSSGGDGAPFQPPNGAPQPGLGRRGAPGPPMGAGDLVQAALDGGGRETASLGGAAGGAGQGPKADFVP 442


                  ..
gi 1063759688 714 VA 715
Cdd:COG5180   443 GD 444
 
Name Accession Description Interval E-value
Med25_VWA pfam11265
Mediator complex subunit 25 von Willebrand factor type A; The overall function of the ...
 12-226 1.27e-119

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: 359.30  E-value: 1.27e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688  12 GGLVADVVFVIEGTANLGPYFEELRKHYLLPAIEYFNGGPPAETDFGGDYGGTQYSLVVFNTVDCAPESYVQCHAPTSSA 91
Cdd:pfam11265   1 SSVVADVVFVVEGTANLGAYFNELKTNYILPTLEYFNGGPIEERDYGSENGSTLYGLVVYHAADCLPEPSVQCYGPTSSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688  92 YEFVTWLDGIKFMGGGGESCSLIAEGLSTALQLFDDFKKMREQIG-QTHRVCLLICNSPPYLLPAVESTTYSGCTTESLV 170
Cdd:pfam11265  81 HKFLQWLDKIDFSGGGGESCALIAEGLATALQCFDDLQKIRENPGlACQRHCILICNSPPYQLPVMESPTYTGKTAEQLA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063759688 171 QKIGERGIHFSIVSPRKLPALRLLFEKAAPPallEPLQQPADVSQDPRHMVLVRGL 226
Cdd:pfam11265 161 ALMAERNIHLSIISPRKIPALFKLFEKAGPD---LPSSPSKNYAKDPRHLVLLRGF 213
Med25 pfam11232
Mediator complex subunit 25 PTOV activation and synapsin 2; Mediator is a large complex of up ...
 396-545 1.54e-79

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: 252.27  E-value: 1.54e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688 396 SNKLLAWSGVLEWQEKPKpasvDANTKLTRSLPCQV--YVNHGE-NLKTEQWPQKLIMQLIPQQLLTTLG-PLFRNSRMV 471
Cdd:pfam11232   1 SQRELIWSGVLEWQEKMS----DQNPKITRTLPCQVsnSVKNGEpELKAEKWPQKLIMQLMPKTLLGNIGgALLRNSRVV 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063759688 472 QFHFTNKDLESLKGLYRIMGNGFAGCVHF---PHTAPCEVRVLMLLYSSKKKIFMGLIPYDQSGFVNGIRQVITNHK 545
Cdd:pfam11232  77 VFHFTPTDLEALKSLYRVMSNGFAGCVHFpgiPANPQCDIKVLMLLYSPKKNAFMGLIPNDQAAFVNRLRQVIKKQK 153
Med25_SD1 pfam11235
Mediator complex subunit 25 synapsin 1; The overall function of the full-length Med25 is ...
 228-383 4.20e-32

Mediator complex subunit 25 synapsin 1; 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, this 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 The function of the SD domains is unclear.


Pssm-ID: 463244 [Multi-domain]  Cd Length: 157  Bit Score: 122.20  E-value: 4.20e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688 228 LPVGGSSTSGSLQTKQAVPLPPAPASAATLSAAPPQALPPVPPQYQVPGNLSAAQVAAQNAVEAAKSQKAGLGPRFSPIN 307
Cdd:pfam11235   1 LPVGGGSAPGPLQSKQPVPLPPAAPSGATLSAAPQQPLPPVPPQYQVPGNLSAAQVAAQNAVEAAKNQKAGLGPRFSPIT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063759688 308 PLQQAAPGVGPPFSQAPAPPLAP-VPPGAPKPPPASQPSLVSTVAPGPVLAAPAQPGAPSLAGTVTPGGVNGPSAAQ 383
Cdd:pfam11235  81 PLQQAAPGVGPPFSQAPAPQLPPgPPGAPKPVPPASQPSLVSTVAPGSGLAPTAQPGAPSMAGTVAPGGVSGPSPAQ 157
Med25_NR-box pfam11244
Mediator complex subunit 25 C-terminal NR box-containing; The overall function of the ...
 657-713 5.18e-21

Mediator complex subunit 25 C-terminal NR box-containing; 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 this C-terminal NR box-containing domain (646-650) from C69-747. The NR box of MED25 is critical for its recruitment to the promoter, probably through an interaction with pre bound RAR.


Pssm-ID: 463246 [Multi-domain]  Cd Length: 89  Bit Score: 88.17  E-value: 5.18e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063759688 657 TGVPPPQASLHHLQPPGAPTLLPPHQSMGQPQLGPQLLHPPPAQSWPTQLPQRAPLP 713
Cdd:pfam11244   1 TSVPQTQQPLHHMQQAAQGMLPHQHQAPGQQQLGQTLMHQAPAQSWGAQLPPRAPLP 57
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 561-720 2.73e-05

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: 47.84  E-value: 2.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688 561 QQAPPVL---GPILEEQARPPQNLLQLRAPQPQPqgavgaSAATGQPQPQGATQAPTGAPQGPPGAAPGPPPSGPILRPQ 637
Cdd:pfam03154 168 QTQPPVLqaqSGAASPPSPPPPGTTQAATAGPTP------SAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQR 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688 638 NPGANPQLRSLLLNPAPPQTGVPP-PQASLHHLQPPGA----------PTLLPPH-------QSMGQPQLGPQLLHPPPA 699
Cdd:pfam03154 242 LPSPHPPLQPMTQPPPPSQVSPQPlPQPSLHGQMPPMPhslqtgpshmQHPVPPQpfpltpqSSQSQVPPGPSPAAPGQS 321

                         170       180
                  ....*....|....*....|.
gi 1063759688 700 QSWPTQLPQRAPLPVAKRKRE 720
Cdd:pfam03154 322 QQRIHTPPSQSQLQSQQPPRE 342
zf-C2H2_12 pfam18658
Spin-doc zinc-finger; This is a zinc finger domain C2H2 type which can be found in SPIN1 ...
 728-786 1.32e-04

Spin-doc zinc-finger; This is a zinc finger domain C2H2 type which can be found in SPIN1 docking protein (SPIN-DOC) and Epm2a-interacting protein 1 (Epm2aip1). SPIN-DOC is a Spindlin1 (SPIN1) regulator that directly binds and strongly disrupts its histone methylation reading ability, causing it to disassociate from chromatin. Epm2aip1 is a glycogen synthase (GS)-associated protein. In the absence of Epm2aip1, the sensitivity of the liver to insulin, in which GS is a principal actor, is impaired.


Pssm-ID: 465831  Cd Length: 64  Bit Score: 40.72  E-value: 1.32e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063759688 728 EKWERDYFFV--EVKSMPTCLICKKNVSVLKEYNLKRHYESQHsKSYDQYTAQSRDTLLQE 786
Cdd:pfam18658   2 ERWRLEYLMDydPGRNGLVCMVCGESLASLKLSTIKRHILQKH-PDTLSLSPEEKEAILEA 61
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 586-717 1.67e-04

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 45.41  E-value: 1.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688 586 APQPQPQGAVGASAATG---------------QPQPQGATQAPTGapqgppgaapgpppsgpilrPQNPGANPQLRSLLL 650
Cdd:pfam09770 174 APAPQPAAQPASLPAPSrkmmsleeveaamraQAKKPAQQPAPAP--------------------AQPPAAPPAQQAQQQ 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688 651 NPAPPQTGVPPPQASLHHLQPPGAPTLLPPH-------------QSMGQPQLGPQLLHPPPAQSWPTQLPQRAPLPVAKR 717
Cdd:pfam09770 234 QQFPPQIQQQQQPQQQPQQPQQHPGQGHPVTilqrpqspqpdpaQPSIQPQAQQFHQQPPPVPVQPTQILQNPNRLSAAR 313
VWA pfam00092
von Willebrand factor type A domain;
17-135 2.27e-04

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 42.65  E-value: 2.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688  17 DVVFVIEGTANLGPY-FEELRKhYLLPAIEYFNGGPPaetdfggdygGTQYSLVVFNtvdcapeSYVQCHAPTSSAY--- 92
Cdd:pfam00092   1 DIVFLLDGSGSIGGDnFEKVKE-FLKKLVESLDIGPD----------GTRVGLVQYS-------SDVRTEFPLNDYSske 62

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1063759688  93 EFVTWLDGIKFMGGGGescSLIAEGLSTALQ-LFDDFKKMREQI 135
Cdd:pfam00092  63 ELLSAVDNLRYLGGGT---TNTGKALKYALEnLFSSAAGARPGA 103
PHA03247 PHA03247
large tegument protein UL36; Provisional
 560-721 6.06e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 6.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688  560 AQQAPPVLGPILEEQARPPqnllqLRAPQPQPQGAVGASAATGQP-QPQGATQAPtgapqgppGAAPGPPPSGPILRPQN 638
Cdd:PHA03247  2822 ASPAGPLPPPTSAQPTAPP-----PPPGPPPPSLPLGGSVAPGGDvRRRPPSRSP--------AAKPAAPARPPVRRLAR 2888

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688  639 PGANPQLRSLLLNPAPPQtgvPPPQASlhhLQPPGAPTLLPPHQSMGQPQLGPQLLHPPPAQSWPTQLPQRAPLPVAKRK 718
Cdd:PHA03247  2889 PAVSRSTESFALPPDQPE---RPPQPQ---APPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQP 2962


                   ...
gi 1063759688  719 REG 721
Cdd:PHA03247  2963 WLG 2965
PHA03378 PHA03378
EBNA-3B; Provisional
 575-711 2.04e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 41.59  E-value: 2.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688 575 ARPPQnllqlRAPQPQPQGAvgasAATGQPQPQGATQAPTGAPQGPPGAAPGPPPSGPILRPqnPGANPqlrSLLLNPAP 654
Cdd:PHA03378  694 MQPPP-----RAPTPMRPPA----APPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARP--PAAAP---GRARPPAA 759

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063759688 655 PQTGVPPPQASlhhlqpPGAPTLLPPHQS----MGQPQLGPQLLHPPPAQSWPTQLPQRAP 711
Cdd:PHA03378  760 APGRARPPAAA------PGAPTPQPPPQAppapQQRPRGAPTPQPPPQAGPTSMQLMPRAA 814
PHA03247 PHA03247
large tegument protein UL36; Provisional
 563-715 2.53e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 2.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688  563 APPVLGPiLEEQARPPQnllQLRAPQPQPQGAVGASAATGQPQPQGATQAPTGAPQGPPGAAPGPPPSGPILRPqnpgAN 642
Cdd:PHA03247  2688 ARPTVGS-LTSLADPPP---PPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARP----AR 2759

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688  643 PQLRSLLLNPAPPQTGVPPPQASlhhLQPPGAPTLLPPHQSMGQPQ---------LGPQLLHPPPAQSWPTQLPQRAPLP 713
Cdd:PHA03247  2760 PPTTAGPPAPAPPAAPAAGPPRR---LTRPAVASLSESRESLPSPWdpadppaavLAPAAALPPAASPAGPLPPPTSAQP 2836


                   ..
gi 1063759688  714 VA 715
Cdd:PHA03247  2837 TA 2838
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 560-715 4.54e-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: 4.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688 560 AQQAPPVLGPILEEQARPPQNLLQLRAPQPQPQGAVGASAATGQPQ----PQGATQaPTGAPQGPPGAAPGPPPSGPILR 635
Cdd:pfam03154 195 ATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQrlpsPHPPLQ-PMTQPPPPSQVSPQPLPQPSLHG 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688 636 PQNPGANPQLR--SLLLNPAPPQTGVPPPQASlhHLQPPGAPTLLPPHQSMGQPQLGpqllhPPPAQSWPTQLPQRAPLP 713
Cdd:pfam03154 274 QMPPMPHSLQTgpSHMQHPVPPQPFPLTPQSS--QSQVPPGPSPAAPGQSQQRIHTP-----PSQSQLQSQQPPREQPLP 346


                  ..
gi 1063759688 714 VA 715
Cdd:pfam03154 347 PA 348
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 560-701 5.23e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.35  E-value: 5.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688 560 AQQAPPVLGPILEEQARPPQNLLQLRAPQPQpqgAVGASAATGQPQPQGATQAPTGAPQGPPGAAPGPPPSGPILRPQNP 639
Cdd:PRK07764  586 AVVGPAPGAAGGEGPPAPASSGPPEEAARPA---APAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDA 662

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063759688 640 GANPQLRSLLLNPAPPQTGVPPPQASLHHL---QPPGAPTLLPPHQSMGQPQLGPQLLHPPPAQS 701
Cdd:PRK07764  663 SDGGDGWPAKAGGAAPAAPPPAPAPAAPAApagAAPAQPAPAPAATPPAGQADDPAAQPPQAAQG 727
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 560-689 6.23e-03

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 40.02  E-value: 6.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688 560 AQQAPPVLGPILEEQARPPQNLLQLRAPQPQP-QGAVGASAATGQPQPQGATQAPTGapqgppgaapgpppsgpILrpQN 638
Cdd:pfam09770 245 QPQQQPQQPQQHPGQGHPVTILQRPQSPQPDPaQPSIQPQAQQFHQQPPPVPVQPTQ-----------------IL--QN 305

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1063759688 639 PgaNPQLRSLLLNPAPPQTGVPPPQASLHHLQPPGAPTllPPHQSMGQPQL 689
Cdd:pfam09770 306 P--NRLSAARVGYPQNPQPGVQPAPAHQAHRQQGSFGR--QAPIITHPQQL 352
PHA03247 PHA03247
large tegument protein UL36; Provisional
 586-724 7.10e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.31  E-value: 7.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688  586 APQPQPQGAVGASAATGQPQPQGATQAPTGAPQGPPgaapGPPPSGPILRPQNPGANPQLRslllnpAPPQTGVPPPQAS 665
Cdd:PHA03247  2809 AAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPG----PPPPSLPLGGSVAPGGDVRRR------PPSRSPAAKPAAP 2878

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063759688  666 LHhlqPP----GAPTLLPPHQSMGQPQLGPQLLHPPPAQSWPTQLPQRAPLPVAKRKREGEGR 724
Cdd:PHA03247  2879 AR---PPvrrlARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR 2938
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 565-713 7.23e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.07  E-value: 7.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688  565 PVLGPILEEQARPPQNLLQLRAPQpQPQGAVGASAATGQPQpqgatqAPTGAPQGPPGAAPGPPPSGPILRPQNPGAnPQ 644
Cdd:PRK10263   743 PLFTPIVEPVQQPQQPVAPQQQYQ-QPQQPVAPQPQYQQPQ------QPVAPQPQYQQPQQPVAPQPQYQQPQQPVA-PQ 814

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063759688  645 LRSlllnPAPPQTGVPPPQASLHhlQPPGAPtllpphqsmgQPQlgPQLLHP---PPAQSWPTQLPQrAPLP 713
Cdd:PRK10263   815 PQY----QQPQQPVAPQPQYQQP--QQPVAP----------QPQ--DTLLHPllmRNGDSRPLHKPT-TPLP 867
PHA03378 PHA03378
EBNA-3B; Provisional
 588-714 7.88e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 40.05  E-value: 7.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688 588 QPQPQGA-----VGASAATGQPQPQGATQAPTgapqgppgaapgpppsgpilrPQNPGANPQLRSLLLNPAPPQTGVP-- 660
Cdd:PHA03378  675 QPSPTGAntmlpIQWAPGTMQPPPRAPTPMRP---------------------PAAPPGRAQRPAAATGRARPPAAAPgr 733

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063759688 661 ------------PPQASLHHLQPP-GAPTLLPPHQS-------MGQPQLGPQLLHPPPAQSWPTQLPQRAPLPV 714
Cdd:PHA03378  734 arppaaapgrarPPAAAPGRARPPaAAPGRARPPAAapgaptpQPPPQAPPAPQQRPRGAPTPQPPPQAGPTSM 807
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 559-715 8.02e-03

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 39.66  E-value: 8.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688 559 GAQQAPPVLGPIleeqaRPPQNLLQLRAPQP-QPQGAVGAS--AATGQPQPQGATQAPTGapqgppgaapgpppsgpiLR 635
Cdd:COG5180   306 GVASAPPATRPV-----RPPGGARDPGTPRPgQPTERPAGVpeAASDAGQPPSAYPPAEE------------------AV 362

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063759688 636 PQNPGAN--PQLRSLLLNPAPPQTGVPPPQASLHHLQPPGAPTLLPPHQSMGQPQLGPQLLHPPPAQSWPTQLPQRAPLP 713
Cdd:COG5180   363 PGKPLEQgaPRPGSSGGDGAPFQPPNGAPQPGLGRRGAPGPPMGAGDLVQAALDGGGRETASLGGAAGGAGQGPKADFVP 442


                  ..
gi 1063759688 714 VA 715
Cdd:COG5180   443 GD 444
 
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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