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Conserved domains on  [gi|1072314136|ref|NP_001333156|]
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WD repeat-containing protein 48 isoform 6 [Homo sapiens]

Protein Classification

WD40 and Ubl_WDR48 domain-containing protein( domain architecture ID 13236993)

WD40 and Ubl_WDR48 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF3337 pfam11816
Domain of unknown function (DUF3337); This family of proteins are functionally uncharacterized. ...
 334-498 1.14e-60

Domain of unknown function (DUF3337); This family of proteins are functionally uncharacterized. This family is only found in eukaryotes. This presumed domain is typically between 285 to 342 amino acids in length.


:

Pssm-ID: 463358  Cd Length: 171  Bit Score: 196.75  E-value: 1.14e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072314136 334 VPPHTPVIFGE-----AGGRTLFRLLCRDSGGETEsmLLNETVPQWVIDITVDKNMP--KFNKIPFYLQPHASSGAKTL- 405
Cdd:pfam11816   1 LPPDTTIIISEespdsGGGRDLYRGTVGDIGEDVD--LLEEVAPMWLGDVLLYNKIPpkEPVKISFVLQPWPGSDLPPDk 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072314136 406 ------KKDRLSASDMLQVRKVMEHVYEKIINLDNESQTTSSSNNEKPGEQEKeediavlAEEKIELLCQDQVLDPNMDL 479
Cdd:pfam11816  79 lpelpnKNSRLNANRMLRVRKILAYVAEKLESLTPEMKPPSPDEDENADKKLK-------PEEYLELLCNDQVLPPNMTL 151

                         170
                  ....*....|....*....
gi 1072314136 480 RTVKHFIWKSGGDLTLHYR 498
Cdd:pfam11816 152 ATVKTFIWKSGGDIVLHYR 170
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 5-111 9.14e-23

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 98.18  E-value: 9.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072314136   5 GTIIVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWSLGQQRCIATYRVHDEGVWALQ 84
Cdd:cd00200   147 GTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVA 226

                          90       100
                  ....*....|....*....|....*..
gi 1072314136  85 VNDAFTHVYSGGRDRKIYCTDLRNPDI 111
Cdd:cd00200   227 FSPDGYLLASGSEDGTIRVWDLRTGEC 253
 
Name Accession Description Interval E-value
DUF3337 pfam11816
Domain of unknown function (DUF3337); This family of proteins are functionally uncharacterized. ...
 334-498 1.14e-60

Domain of unknown function (DUF3337); This family of proteins are functionally uncharacterized. This family is only found in eukaryotes. This presumed domain is typically between 285 to 342 amino acids in length.


Pssm-ID: 463358  Cd Length: 171  Bit Score: 196.75  E-value: 1.14e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072314136 334 VPPHTPVIFGE-----AGGRTLFRLLCRDSGGETEsmLLNETVPQWVIDITVDKNMP--KFNKIPFYLQPHASSGAKTL- 405
Cdd:pfam11816   1 LPPDTTIIISEespdsGGGRDLYRGTVGDIGEDVD--LLEEVAPMWLGDVLLYNKIPpkEPVKISFVLQPWPGSDLPPDk 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072314136 406 ------KKDRLSASDMLQVRKVMEHVYEKIINLDNESQTTSSSNNEKPGEQEKeediavlAEEKIELLCQDQVLDPNMDL 479
Cdd:pfam11816  79 lpelpnKNSRLNANRMLRVRKILAYVAEKLESLTPEMKPPSPDEDENADKKLK-------PEEYLELLCNDQVLPPNMTL 151

                         170
                  ....*....|....*....
gi 1072314136 480 RTVKHFIWKSGGDLTLHYR 498
Cdd:pfam11816 152 ATVKTFIWKSGGDIVLHYR 170
Ubl_WDR48 cd17041
Ubiquitin-like (Ubl) domain found in WD repeat-containing protein 48 (WDR48) and similar ...
 386-498 5.58e-49

Ubiquitin-like (Ubl) domain found in WD repeat-containing protein 48 (WDR48) and similar proteins; WDR48, also termed USP1-associated factor 1 (UAF1), or WD repeat endosomal protein, or p80, is required for the histone deubiquitination activity. It stimulates activity of ubiquitin-specific proteases USP1, USP12, and USP46.As potential tumor suppressor, WDR48 in complex with deubiquitinase USP12 suppresses Akt-dependent cell survival signaling by stabilizing PH domain leucine-rich repeat protein phosphatase 1 (PHLPP1). WDR48 also functions as a novel interaction partner of E1 helicase from anogenital human papillomavirus (HPV) types, and plays an essential role in anogenital HPV DNA replication. WDR48 contains a WD40 domain and a ubiquitin-like domain that shows high sequence and structural similarity with RING finger- and WD40-associated ubiquitin-like (RAWUL) domain.


Pssm-ID: 340561  Cd Length: 97  Bit Score: 163.61  E-value: 5.58e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072314136 386 KFNKIPFYLQPHASSGA--KTLKKDRLSASDMLQVRKVMEHVYEKIINLDNESQTtsssnnekpgeqekeediAVLAEEK 463
Cdd:cd17041     1 EFPKISFFLQPHPSSGLppKTLKNDKLSASRMLRVRKVMEYVAEKLLGQEPESQD------------------ASNPEEK 62

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1072314136 464 IELLCQDQVLDPNMDLRTVKHFIWKSGGDLTLHYR 498
Cdd:cd17041    63 LELLCNDQVLDPNMTLATVKHFIWKSGGDLVLHYR 97
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 5-111 9.14e-23

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 98.18  E-value: 9.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072314136   5 GTIIVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWSLGQQRCIATYRVHDEGVWALQ 84
Cdd:cd00200   147 GTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVA 226

                          90       100
                  ....*....|....*....|....*..
gi 1072314136  85 VNDAFTHVYSGGRDRKIYCTDLRNPDI 111
Cdd:cd00200   227 FSPDGYLLASGSEDGTIRVWDLRTGEC 253
WD40 COG2319
WD40 repeat [General function prediction only];
5-115 1.25e-20

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 93.82  E-value: 1.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072314136   5 GTIIVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWSLGQQRCIATYRVHDEGVWALq 84
Cdd:COG2319   174 GKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSV- 252

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1072314136  85 vndAF----THVYSGGRDRKIYCTDLRNPDIRVLI 115
Cdd:COG2319   253 ---AFspdgRLLASGSADGTVRLWDLATGELLRTL 284
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 24-63 2.28e-07

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 46.92  E-value: 2.28e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1072314136   24 TCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWS 63
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 8-111 5.89e-07

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 52.40  E-value: 5.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072314136   8 IVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKAL-LLNRDGTQCLSGSSDGTIRLWSLGQQRCIATYRVhDEGVWALQV- 85
Cdd:PLN00181  548 VASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIdYSSADPTLLASGSDDGSVKLWSINQGVSIGTIKT-KANICCVQFp 626

                          90       100
                  ....*....|....*....|....*.
gi 1072314136  86 NDAFTHVYSGGRDRKIYCTDLRNPDI 111
Cdd:PLN00181  627 SESGRSLAFGSADHKVYYYDLRNPKL 652
WD40 pfam00400
WD domain, G-beta repeat;
28-63 6.81e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.80  E-value: 6.81e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1072314136  28 LMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWS 63
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
 
Name Accession Description Interval E-value
DUF3337 pfam11816
Domain of unknown function (DUF3337); This family of proteins are functionally uncharacterized. ...
 334-498 1.14e-60

Domain of unknown function (DUF3337); This family of proteins are functionally uncharacterized. This family is only found in eukaryotes. This presumed domain is typically between 285 to 342 amino acids in length.


Pssm-ID: 463358  Cd Length: 171  Bit Score: 196.75  E-value: 1.14e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072314136 334 VPPHTPVIFGE-----AGGRTLFRLLCRDSGGETEsmLLNETVPQWVIDITVDKNMP--KFNKIPFYLQPHASSGAKTL- 405
Cdd:pfam11816   1 LPPDTTIIISEespdsGGGRDLYRGTVGDIGEDVD--LLEEVAPMWLGDVLLYNKIPpkEPVKISFVLQPWPGSDLPPDk 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072314136 406 ------KKDRLSASDMLQVRKVMEHVYEKIINLDNESQTTSSSNNEKPGEQEKeediavlAEEKIELLCQDQVLDPNMDL 479
Cdd:pfam11816  79 lpelpnKNSRLNANRMLRVRKILAYVAEKLESLTPEMKPPSPDEDENADKKLK-------PEEYLELLCNDQVLPPNMTL 151

                         170
                  ....*....|....*....
gi 1072314136 480 RTVKHFIWKSGGDLTLHYR 498
Cdd:pfam11816 152 ATVKTFIWKSGGDIVLHYR 170
Ubl_WDR48 cd17041
Ubiquitin-like (Ubl) domain found in WD repeat-containing protein 48 (WDR48) and similar ...
 386-498 5.58e-49

Ubiquitin-like (Ubl) domain found in WD repeat-containing protein 48 (WDR48) and similar proteins; WDR48, also termed USP1-associated factor 1 (UAF1), or WD repeat endosomal protein, or p80, is required for the histone deubiquitination activity. It stimulates activity of ubiquitin-specific proteases USP1, USP12, and USP46.As potential tumor suppressor, WDR48 in complex with deubiquitinase USP12 suppresses Akt-dependent cell survival signaling by stabilizing PH domain leucine-rich repeat protein phosphatase 1 (PHLPP1). WDR48 also functions as a novel interaction partner of E1 helicase from anogenital human papillomavirus (HPV) types, and plays an essential role in anogenital HPV DNA replication. WDR48 contains a WD40 domain and a ubiquitin-like domain that shows high sequence and structural similarity with RING finger- and WD40-associated ubiquitin-like (RAWUL) domain.


Pssm-ID: 340561  Cd Length: 97  Bit Score: 163.61  E-value: 5.58e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072314136 386 KFNKIPFYLQPHASSGA--KTLKKDRLSASDMLQVRKVMEHVYEKIINLDNESQTtsssnnekpgeqekeediAVLAEEK 463
Cdd:cd17041     1 EFPKISFFLQPHPSSGLppKTLKNDKLSASRMLRVRKVMEYVAEKLLGQEPESQD------------------ASNPEEK 62

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1072314136 464 IELLCQDQVLDPNMDLRTVKHFIWKSGGDLTLHYR 498
Cdd:cd17041    63 LELLCNDQVLDPNMTLATVKHFIWKSGGDLVLHYR 97
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 5-111 9.14e-23

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 98.18  E-value: 9.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072314136   5 GTIIVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWSLGQQRCIATYRVHDEGVWALQ 84
Cdd:cd00200   147 GTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVA 226

                          90       100
                  ....*....|....*....|....*..
gi 1072314136  85 VNDAFTHVYSGGRDRKIYCTDLRNPDI 111
Cdd:cd00200   227 FSPDGYLLASGSEDGTIRVWDLRTGEC 253
WD40 COG2319
WD40 repeat [General function prediction only];
5-115 1.25e-20

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 93.82  E-value: 1.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072314136   5 GTIIVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWSLGQQRCIATYRVHDEGVWALq 84
Cdd:COG2319   174 GKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSV- 252

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1072314136  85 vndAF----THVYSGGRDRKIYCTDLRNPDIRVLI 115
Cdd:COG2319   253 ---AFspdgRLLASGSADGTVRLWDLATGELLRTL 284
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 5-101 3.26e-20

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 90.86  E-value: 3.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072314136   5 GTIIVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWSLGQQRCIATYRVHDEGVWALQ 84
Cdd:cd00200    21 GKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVA 100

                          90
                  ....*....|....*..
gi 1072314136  85 VNDAFTHVYSGGRDRKI 101
Cdd:cd00200   101 FSPDGRILSSSSRDKTI 117
WD40 COG2319
WD40 repeat [General function prediction only];
5-101 6.02e-20

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 91.90  E-value: 6.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072314136   5 GTIIVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWSLGQQRCIATYRVHDEGVWALq 84
Cdd:COG2319   300 GKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSV- 378

                          90       100
                  ....*....|....*....|.
gi 1072314136  85 vndAFT----HVYSGGRDRKI 101
Cdd:COG2319   379 ---AFSpdgrTLASGSADGTV 396
WD40 COG2319
WD40 repeat [General function prediction only];
5-101 6.02e-20

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 91.90  E-value: 6.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072314136   5 GTIIVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWSLGQQRCIATYRVHDEGVWALq 84
Cdd:COG2319   216 GKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSV- 294

                          90       100
                  ....*....|....*....|.
gi 1072314136  85 vndAFT----HVYSGGRDRKI 101
Cdd:COG2319   295 ---AFSpdgkLLASGSDDGTV 312
WD40 COG2319
WD40 repeat [General function prediction only];
5-101 9.16e-19

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 88.43  E-value: 9.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072314136   5 GTIIVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWSLGQQRCIATYRVHDEGVWALq 84
Cdd:COG2319   132 GKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSV- 210

                          90       100
                  ....*....|....*....|.
gi 1072314136  85 vndAF----THVYSGGRDRKI 101
Cdd:COG2319   211 ---AFspdgKLLASGSADGTV 228
WD40 COG2319
WD40 repeat [General function prediction only];
5-108 1.69e-18

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 87.27  E-value: 1.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072314136   5 GTIIVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWSLGQQRCIATYRVHDEGVWALQ 84
Cdd:COG2319   258 GRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVA 337

                          90       100
                  ....*....|....*....|....
gi 1072314136  85 VNDAFTHVYSGGRDRKIYCTDLRN 108
Cdd:COG2319   338 FSPDGKTLASGSDDGTVRLWDLAT 361
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 2-107 2.32e-18

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 85.46  E-value: 2.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072314136   2 NQLGTIIVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWSLGQQRCIATYRVHDEGVW 81
Cdd:cd00200   102 SPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVN 181

                          90       100
                  ....*....|....*....|....*.
gi 1072314136  82 ALQVNDAFTHVYSGGRDRKIYCTDLR 107
Cdd:cd00200   182 SVAFSPDGEKLLSSSSDGTIKLWDLS 207
WD40 COG2319
WD40 repeat [General function prediction only];
5-101 4.85e-18

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 86.12  E-value: 4.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072314136   5 GTIIVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWSLGQQRCIATYRVHDEGVWALq 84
Cdd:COG2319    90 GRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSV- 168

                          90       100
                  ....*....|....*....|.
gi 1072314136  85 vndAF----THVYSGGRDRKI 101
Cdd:COG2319   169 ---AFspdgKLLASGSDDGTV 186
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 8-108 4.72e-16

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 78.53  E-value: 4.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072314136   8 IVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWSLGQQRCIATYRVHDEGVWALQVND 87
Cdd:cd00200    66 LASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSP 145

                          90       100
                  ....*....|....*....|.
gi 1072314136  88 AFTHVYSGGRDRKIYCTDLRN 108
Cdd:cd00200   146 DGTFVASSSQDGTIKLWDLRT 166
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 5-101 5.86e-15

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 75.45  E-value: 5.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072314136   5 GTIIVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWSLGQQRCIATYRVHDEGVWALQ 84
Cdd:cd00200   189 GEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLA 268

                          90
                  ....*....|....*..
gi 1072314136  85 VNDAFTHVYSGGRDRKI 101
Cdd:cd00200   269 WSPDGKRLASGSADGTI 285
WD40 COG2319
WD40 repeat [General function prediction only];
5-64 3.00e-13

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 71.48  E-value: 3.00e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072314136   5 GTIIVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWSL 64
Cdd:COG2319   342 GKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401
WD40 COG2319
WD40 repeat [General function prediction only];
4-101 1.83e-10

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 62.62  E-value: 1.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072314136   4 LGTIIVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWSLGQQRCIATYRVHDEGVWAL 83
Cdd:COG2319    47 DGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSV 126

                          90
                  ....*....|....*...
gi 1072314136  84 QVNDAFTHVYSGGRDRKI 101
Cdd:COG2319   127 AFSPDGKTLASGSADGTV 144
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 31-120 2.40e-10

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 61.58  E-value: 2.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072314136  31 LKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWSLGQQRCIATYRVHDEGVWALQVNDAFTHVYSGGRDRKIYCTDLRNPD 110
Cdd:cd00200     5 LKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGE 84

                          90
                  ....*....|.
gi 1072314136 111 -IRVLICEEKA 120
Cdd:cd00200    85 cVRTLTGHTSY 95
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 5-63 3.44e-10

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 60.81  E-value: 3.44e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1072314136   5 GTIIVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWS 63
Cdd:cd00200   231 GYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 24-63 2.28e-07

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 46.92  E-value: 2.28e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1072314136   24 TCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWS 63
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 8-111 5.89e-07

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 52.40  E-value: 5.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072314136   8 IVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKAL-LLNRDGTQCLSGSSDGTIRLWSLGQQRCIATYRVhDEGVWALQV- 85
Cdd:PLN00181  548 VASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIdYSSADPTLLASGSDDGSVKLWSINQGVSIGTIKT-KANICCVQFp 626

                          90       100
                  ....*....|....*....|....*.
gi 1072314136  86 NDAFTHVYSGGRDRKIYCTDLRNPDI 111
Cdd:PLN00181  627 SESGRSLAFGSADHKVYYYDLRNPKL 652
WD40 pfam00400
WD domain, G-beta repeat;
28-63 6.81e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.80  E-value: 6.81e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1072314136  28 LMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWS 63
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
Ubiquitin_like_fold cd00196
Beta-grasp ubiquitin-like fold; Ubiquitin is a protein modifier that is involved in various ...
 403-498 9.56e-07

Beta-grasp ubiquitin-like fold; Ubiquitin is a protein modifier that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. The ubiquitination process comprises a cascade of E1, E2 and E3 enzymes that results in a covalent bond between the C-terminus of ubiquitin and the epsilon-amino group of a substrate lysine. Ubiquitin-like proteins have similar ubiquitin beta-grasp fold and attach to other proteins in a ubiquitin-like manner but with biochemically distinct roles. Ubiquitin and ubiquitin-like proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some other ubiquitin-like domains have adaptor roles in ubiquitin-signaling by mediating protein-protein interaction. In addition to Ubiquitin-like (Ubl) domain, Ras-associating (RA) domain, F0/F1 sub-domain of FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, TGS (ThrRS, GTPase and SpoT) domain, Ras-binding domain (RBD), Ubiquitin regulatory domain X (UBX), Dublecortin-like domain, and RING finger- and WD40-associated ubiquitin-like (RAWUL) domain have beta-grasp ubiquitin-like folds, and are included in this superfamily.


Pssm-ID: 340450  Cd Length: 68  Bit Score: 46.16  E-value: 9.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072314136 403 KTLKKDRLSASDMLQVRKVMEHVYEKIInldnesqttsssnnekpgeqekeediavLAEEKIELLCQDQVLDPNMDLRTv 482
Cdd:cd00196     6 PSLKKIVVAVPPSTTLRQVLEKVAKRIG----------------------------LPPDVIRLLFNGQVLDDLMTAKQ- 56

                          90
                  ....*....|....*.
gi 1072314136 483 khfiWKSGGDLTLHYR 498
Cdd:cd00196    57 ----VGLEPGEELHFV 68
RAWUL pfam16207
RAWUL domain RING finger- and WD40-associated ubiquitin-like; The RAWUL domain is found at the ...
 463-498 3.93e-03

RAWUL domain RING finger- and WD40-associated ubiquitin-like; The RAWUL domain is found at the C-terminus of poly-comb group RING finger proteins. It is a ubiquitin-like domain. RAWUL binds directly to PUFD, a domain on BCOR proteins (BCL6 corepressor). BCOR has emerged as an important player in development and health.


Pssm-ID: 465067  Cd Length: 66  Bit Score: 36.00  E-value: 3.93e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1072314136 463 KIELLCQDQVLDPNMDLRTVKHFIWKSGGDLTLHYR 498
Cdd:pfam16207  31 IVEILYNGEPLPDSYTLDVAYIKYWKRNAPLELYYR 66
RAWUL_PCGF_like cd16102
RRING finger- and WD40-associated ubiquitin-like (RAWUL) domain found in PCGF1-6, RING1 and -2, ...
 460-498 6.03e-03

RRING finger- and WD40-associated ubiquitin-like (RAWUL) domain found in PCGF1-6, RING1 and -2, DRIP and similar proteins; structurally similar to a beta-grasp ubiquitin-like fold; The family includes six Polycomb Group (PcG) RING finger homologs (PCGF1/NSPc1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6/MBLR) that use epigenetic mechanisms to maintain or repress expression of their target genes. They were first discovered in fruit flies that can remodel chromatin such that epigenetic silencing of genes takes place, and are well known for silencing Hox genes through modulation of chromatin structure during embryonic development in fruit flies. PCGF homologs play important roles in cell proliferation, differentiation, and tumorigenesis. They all have been found to associate with ring finger protein 2 (RNF2). The RNF2-PCGF heterodimer is catalytically competent as an E3 ubiquitin transferase and is the scaffold for the assembly of additional components. Moreover, PCGF homologs are critical components in the assembly of distinct Polycomb Repression Complex 1 (PRC1) related complexes which are involved in the maintenance of gene repression and target different genes through distinct mechanisms. The Drosophila PRC1 core complex is formed by the Polycomb (Pc), Polyhomeotic (Ph), Posterior sex combs (Psc), and Sex combs extra (Sce, also known as Ring) subunits. In mammals, the composition of PRC1 is much more diverse and varies depending on the cellular context. All PRC1 complexes contain homologs of the Drosophila Ring protein. Ring1A/RNF1 and Ring1B/RNF2 are E3 ubiquitin ligases that mark lysine 119 of histone H2A with a single ubiquitin group (H2AK119ub). Mammalian homologs of the Drosophila Psc protein, such as PCGF2/Mel-18 or PCGF4/BMI1, regulate PRC1 enzymatic activity. PRC1 complexes can be divided into at least two classes according to the presence or absence of CBX proteins, which are homologs of Drosophila Pc. Canonical PRC1 complexes contain CBX proteins that recognize and bind H3K27me3, the mark deposited by PRC2. Therefore, canonical PRC1 complexes and PRC2 can act together to repress gene transcription and maintain this repression through cell division. Non-canonical PRC1 complexes, containing RYBP (together with additional proteins, such as L3mbtl2 or Kdm2b) rather than the CBX proteins, have recently been described in mammals. PCGF homologs contain a C3HC4-type RING-HC finger, and a RAWUL domain that might be responsible for interaction with Cbx members of the Polycomb repression complexes.


Pssm-ID: 340519  Cd Length: 87  Bit Score: 36.10  E-value: 6.03e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1072314136 460 AEEKIELLCQDQVLDPNMDLRTVKHFIW-KSGGDLTLHYR 498
Cdd:cd16102    48 SEQDLDILCRGELLGKEHTLKFIWRTRWrKQDGPLVLQYR 87
 
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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