NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|212645782|ref|NP_001129837|]
View 

WD repeat-containing protein 48 homolog [Caenorhabditis elegans]

Protein Classification

WD repeat WDR48 family protein( domain architecture ID 10078073)

WD repeat WDR48 family protein similar to WD repeat-containing protein 48, a regulator of deubiquitinating complexes, which acts as a strong activator of USP1, USP12 and USP46

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
DUF3337 pfam11816
Domain of unknown function (DUF3337); This family of proteins are functionally uncharacterized. ...
 530-695 2.14e-49

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: 170.55  E-value: 2.14e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782  530 LPEHTPLIICE-----GNGRPLYRLLVGDAGKEfeANELAQIAPMWVIDAIERNQLP--KFNKMPFYLLPHPSTNPKQP- 601
Cdd:pfam11816   1 LPPDTTIIISEespdsGGGRDLYRGTVGDIGED--VDLLEEVAPMWLGDVLLYNKIPpkEPVKISFVLQPWPGSDLPPDk 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782  602 ------KKDRLSATEMLQVKKVMEHVYEKIL------STNDGKVFRNKKILMVFEDitvgsiplnqihtKMEMYCNDQRL 669
Cdd:pfam11816  79 lpelpnKNSRLNANRMLRVRKILAYVAEKLEsltpemKPPSPDEDENADKKLKPEE-------------YLELLCNDQVL 145

                         170       180
                  ....*....|....*....|....*.
gi 212645782  670 EPDMDLRTVKHLYWKQSGELLLHYKP 695
Cdd:pfam11816 146 PPNMTLATVKTFIWKSGGDIVLHYRR 171
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 29-322 4.09e-48

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: 170.98  E-value: 4.09e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782  29 RSAVSALQYDAQNGRLFTGGSDTIIRTWSVphhkdafsarggvrspgknSPVQYQGSLEQHTDWVNDMILCGHGKILISA 108
Cdd:cd00200    9 TGGVTCVAFSPDGKLLATGSGDGTIKVWDL-------------------ETGELLRTLKGHTGPVRDVAASADGTYLASG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782 109 SNDTTVKVWNIERDNkhgfidCIRT---HKDYVSCLAYAPIVEKAVSASFDHNIFVYDINaNFKTVNNLIGCKDSIYSLA 185
Cdd:cd00200   70 SSDKTIRLWDLETGE------CVRTltgHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVE-TGKCLTTLRGHTDWVNSVA 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782 186 TTPNLSLVLGAGTEKCIRLFDPRTNEKIMKLRGHTDNVRALVVNDDGTRALSAGSDATIRLWDIGQQRCIATCIAHEEGV 265
Cdd:cd00200  143 FSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGV 222

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212645782 266 WTLQVDSSFTTVYSAGKDKMVVKTPLYDFTKSQLLFKEEAPVKKLLLSEK---------DNPVSLW 322
Cdd:cd00200  223 NSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDgkrlasgsaDGTIRIW 288
 
Name Accession Description Interval E-value
DUF3337 pfam11816
Domain of unknown function (DUF3337); This family of proteins are functionally uncharacterized. ...
 530-695 2.14e-49

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: 170.55  E-value: 2.14e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782  530 LPEHTPLIICE-----GNGRPLYRLLVGDAGKEfeANELAQIAPMWVIDAIERNQLP--KFNKMPFYLLPHPSTNPKQP- 601
Cdd:pfam11816   1 LPPDTTIIISEespdsGGGRDLYRGTVGDIGED--VDLLEEVAPMWLGDVLLYNKIPpkEPVKISFVLQPWPGSDLPPDk 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782  602 ------KKDRLSATEMLQVKKVMEHVYEKIL------STNDGKVFRNKKILMVFEDitvgsiplnqihtKMEMYCNDQRL 669
Cdd:pfam11816  79 lpelpnKNSRLNANRMLRVRKILAYVAEKLEsltpemKPPSPDEDENADKKLKPEE-------------YLELLCNDQVL 145

                         170       180
                  ....*....|....*....|....*.
gi 212645782  670 EPDMDLRTVKHLYWKQSGELLLHYKP 695
Cdd:pfam11816 146 PPNMTLATVKTFIWKSGGDIVLHYRR 171
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 29-322 4.09e-48

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: 170.98  E-value: 4.09e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782  29 RSAVSALQYDAQNGRLFTGGSDTIIRTWSVphhkdafsarggvrspgknSPVQYQGSLEQHTDWVNDMILCGHGKILISA 108
Cdd:cd00200    9 TGGVTCVAFSPDGKLLATGSGDGTIKVWDL-------------------ETGELLRTLKGHTGPVRDVAASADGTYLASG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782 109 SNDTTVKVWNIERDNkhgfidCIRT---HKDYVSCLAYAPIVEKAVSASFDHNIFVYDINaNFKTVNNLIGCKDSIYSLA 185
Cdd:cd00200   70 SSDKTIRLWDLETGE------CVRTltgHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVE-TGKCLTTLRGHTDWVNSVA 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782 186 TTPNLSLVLGAGTEKCIRLFDPRTNEKIMKLRGHTDNVRALVVNDDGTRALSAGSDATIRLWDIGQQRCIATCIAHEEGV 265
Cdd:cd00200  143 FSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGV 222

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212645782 266 WTLQVDSSFTTVYSAGKDKMVVKTPLYDFTKSQLLFKEEAPVKKLLLSEK---------DNPVSLW 322
Cdd:cd00200  223 NSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDgkrlasgsaDGTIRIW 288
WD40 COG2319
WD40 repeat [General function prediction only];
29-286 5.61e-39

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 148.91  E-value: 5.61e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782  29 RSAVSALQYDAQNGRLFTGGSDTIIRTWSV---------PHHKD-----AFSA----------RGGVR--SPGKNSPVQy 82
Cdd:COG2319  120 TGAVRSVAFSPDGKTLASGSADGTVRLWDLatgkllrtlTGHSGavtsvAFSPdgkllasgsdDGTVRlwDLATGKLLR- 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782  83 qgSLEQHTDWVNDMILCGHGKILISASNDTTVKVWNIERDNkhgFIDCIRTHKDYVSCLAYAPIVEKAVSASFDHNIFVY 162
Cdd:COG2319  199 --TLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGK---LLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLW 273

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782 163 DINANfKTVNNLIGCKDSIYSLATTPNLSLVLGAGTEKCIRLFDPRTNEKIMKLRGHTDNVRALVVNDDGTRALSAGSDA 242
Cdd:COG2319  274 DLATG-ELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDG 352

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 212645782 243 TIRLWDIGQQRCIATCIAHEEGVWTLQVDSSFTTVYSAGKDKMV 286
Cdd:COG2319  353 TVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTV 396
Ubl_WDR48 cd17041
Ubiquitin-like (Ubl) domain found in WD repeat-containing protein 48 (WDR48) and similar ...
 582-694 1.47e-35

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: 129.33  E-value: 1.47e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782 582 KFNKMPFYLLPHPSTN--PKQPKKDRLSATEMLQVKKVMEHVYEKILstndgkvfrnkkilmvfeditvGSIPLNQIHT- 658
Cdd:cd17041    1 EFPKISFFLQPHPSSGlpPKTLKNDKLSASRMLRVRKVMEYVAEKLL----------------------GQEPESQDASn 58

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 212645782 659 ---KMEMYCNDQRLEPDMDLRTVKHLYWKQSGELLLHYK 694
Cdd:cd17041   59 peeKLELLCNDQVLDPNMTLATVKHFIWKSGGDLVLHYR 97
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 209-248 2.71e-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: 47.31  E-value: 2.71e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 212645782   209 TNEKIMKLRGHTDNVRALVVNDDGTRALSAGSDATIRLWD 248
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
210-248 2.17e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 44.64  E-value: 2.17e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 212645782  210 NEKIMKLRGHTDNVRALVVNDDGTRALSAGSDATIRLWD 248
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
 
Name Accession Description Interval E-value
DUF3337 pfam11816
Domain of unknown function (DUF3337); This family of proteins are functionally uncharacterized. ...
 530-695 2.14e-49

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: 170.55  E-value: 2.14e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782  530 LPEHTPLIICE-----GNGRPLYRLLVGDAGKEfeANELAQIAPMWVIDAIERNQLP--KFNKMPFYLLPHPSTNPKQP- 601
Cdd:pfam11816   1 LPPDTTIIISEespdsGGGRDLYRGTVGDIGED--VDLLEEVAPMWLGDVLLYNKIPpkEPVKISFVLQPWPGSDLPPDk 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782  602 ------KKDRLSATEMLQVKKVMEHVYEKIL------STNDGKVFRNKKILMVFEDitvgsiplnqihtKMEMYCNDQRL 669
Cdd:pfam11816  79 lpelpnKNSRLNANRMLRVRKILAYVAEKLEsltpemKPPSPDEDENADKKLKPEE-------------YLELLCNDQVL 145

                         170       180
                  ....*....|....*....|....*.
gi 212645782  670 EPDMDLRTVKHLYWKQSGELLLHYKP 695
Cdd:pfam11816 146 PPNMTLATVKTFIWKSGGDIVLHYRR 171
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 29-322 4.09e-48

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: 170.98  E-value: 4.09e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782  29 RSAVSALQYDAQNGRLFTGGSDTIIRTWSVphhkdafsarggvrspgknSPVQYQGSLEQHTDWVNDMILCGHGKILISA 108
Cdd:cd00200    9 TGGVTCVAFSPDGKLLATGSGDGTIKVWDL-------------------ETGELLRTLKGHTGPVRDVAASADGTYLASG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782 109 SNDTTVKVWNIERDNkhgfidCIRT---HKDYVSCLAYAPIVEKAVSASFDHNIFVYDINaNFKTVNNLIGCKDSIYSLA 185
Cdd:cd00200   70 SSDKTIRLWDLETGE------CVRTltgHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVE-TGKCLTTLRGHTDWVNSVA 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782 186 TTPNLSLVLGAGTEKCIRLFDPRTNEKIMKLRGHTDNVRALVVNDDGTRALSAGSDATIRLWDIGQQRCIATCIAHEEGV 265
Cdd:cd00200  143 FSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGV 222

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212645782 266 WTLQVDSSFTTVYSAGKDKMVVKTPLYDFTKSQLLFKEEAPVKKLLLSEK---------DNPVSLW 322
Cdd:cd00200  223 NSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDgkrlasgsaDGTIRIW 288
WD40 COG2319
WD40 repeat [General function prediction only];
29-286 5.61e-39

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 148.91  E-value: 5.61e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782  29 RSAVSALQYDAQNGRLFTGGSDTIIRTWSV---------PHHKD-----AFSA----------RGGVR--SPGKNSPVQy 82
Cdd:COG2319  120 TGAVRSVAFSPDGKTLASGSADGTVRLWDLatgkllrtlTGHSGavtsvAFSPdgkllasgsdDGTVRlwDLATGKLLR- 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782  83 qgSLEQHTDWVNDMILCGHGKILISASNDTTVKVWNIERDNkhgFIDCIRTHKDYVSCLAYAPIVEKAVSASFDHNIFVY 162
Cdd:COG2319  199 --TLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGK---LLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLW 273

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782 163 DINANfKTVNNLIGCKDSIYSLATTPNLSLVLGAGTEKCIRLFDPRTNEKIMKLRGHTDNVRALVVNDDGTRALSAGSDA 242
Cdd:COG2319  274 DLATG-ELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDG 352

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 212645782 243 TIRLWDIGQQRCIATCIAHEEGVWTLQVDSSFTTVYSAGKDKMV 286
Cdd:COG2319  353 TVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTV 396
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 89-349 1.48e-38

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: 144.40  E-value: 1.48e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782  89 HTDWVNDMILCGHGKILISASNDTTVKVWNIERDnkhgfiDCIRT---HKDYVSCLAYAPIVEKAVSASFDHNIFVYDIN 165
Cdd:cd00200    8 HTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETG------ELLRTlkgHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782 166 ANfKTVNNLIGCKDSIYSLATTPNLSLVLGAGTEKCIRLFDPRTNEKIMKLRGHTDNVRALVVNDDGTRALSAGSDATIR 245
Cdd:cd00200   82 TG-ECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782 246 LWDIGQQRCIATCIAHEEGVWTLQVDSSFTTVYSAGKDKMVvktPLYDFTKSQLLfkeeapvkKLLLSEKDNPVSLWVGt 325
Cdd:cd00200  161 LWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTI---KLWDLSTGKCL--------GTLRGHENGVNSVAFS- 228

                        250       260
                 ....*....|....*....|....
gi 212645782 326 wksdikrwsirPSAQLSIGGDEDG 349
Cdd:cd00200  229 -----------PDGYLLASGSEDG 241
Ubl_WDR48 cd17041
Ubiquitin-like (Ubl) domain found in WD repeat-containing protein 48 (WDR48) and similar ...
 582-694 1.47e-35

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: 129.33  E-value: 1.47e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782 582 KFNKMPFYLLPHPSTN--PKQPKKDRLSATEMLQVKKVMEHVYEKILstndgkvfrnkkilmvfeditvGSIPLNQIHT- 658
Cdd:cd17041    1 EFPKISFFLQPHPSSGlpPKTLKNDKLSASRMLRVRKVMEYVAEKLL----------------------GQEPESQDASn 58

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 212645782 659 ---KMEMYCNDQRLEPDMDLRTVKHLYWKQSGELLLHYK 694
Cdd:cd17041   59 peeKLELLCNDQVLDPNMTLATVKHFIWKSGGDLVLHYR 97
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 30-248 5.09e-33

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: 128.61  E-value: 5.09e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782  30 SAVSALQYDAQNGRLFTGGSDTIIRTWSVP---------HHKD-----AFSARGGVRSPG---------KNSPVQYQGSL 86
Cdd:cd00200   52 GPVRDVAASADGTYLASGSSDKTIRLWDLEtgecvrtltGHTSyvssvAFSPDGRILSSSsrdktikvwDVETGKCLTTL 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782  87 EQHTDWVNDMILCGHGKILISASNDTTVKVWNIeRDNKhgfidCIRT---HKDYVSCLAYAPIVEKAVSASFDHNIFVYD 163
Cdd:cd00200  132 RGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL-RTGK-----CVATltgHTGEVNSVAFSPDGEKLLSSSSDGTIKLWD 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782 164 INAnFKTVNNLIGCKDSIYSLATTPNLSLVLGAGTEKCIRLFDPRTNEKIMKLRGHTDNVRALVVNDDGTRALSAGSDAT 243
Cdd:cd00200  206 LST-GKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGT 284


                 ....*
gi 212645782 244 IRLWD 248
Cdd:cd00200  285 IRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
29-249 2.36e-32

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 129.65  E-value: 2.36e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782  29 RSAVSALQYDAQNGRLFTGGSDTIIRTWSV---------PHHKD-----AFSARG----------GVR--SPGKNSPVQy 82
Cdd:COG2319  162 SGAVTSVAFSPDGKLLASGSDDGTVRLWDLatgkllrtlTGHTGavrsvAFSPDGkllasgsadgTVRlwDLATGKLLR- 240

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782  83 qgSLEQHTDWVNDMILCGHGKILISASNDTTVKVWNIERDnkhgfiDCIRT---HKDYVSCLAYAPIVEKAVSASFDHNI 159
Cdd:COG2319  241 --TLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATG------ELLRTltgHSGGVNSVAFSPDGKLLASGSDDGTV 312

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782 160 FVYDInANFKTVNNLIGCKDSIYSLATTPNLSLVLGAGTEKCIRLFDPRTNEKIMKLRGHTDNVRALVVNDDGTRALSAG 239
Cdd:COG2319  313 RLWDL-ATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGS 391

                        250
                 ....*....|
gi 212645782 240 SDATIRLWDI 249
Cdd:COG2319  392 ADGTVRLWDL 401
WD40 COG2319
WD40 repeat [General function prediction only];
31-300 5.65e-32

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 128.49  E-value: 5.65e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782  31 AVSALQYDAQNGRLFTGGSDTIIRTWSVPHHKDAFSARGGVRSPGKNSPVQYQGSLEQHTDWVNDMILCGHGKILISASN 110
Cdd:COG2319   19 ALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASA 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782 111 DTTVKVWNIERdnkHGFIDCIRTHKDYVSCLAYAPIVEKAVSASFDHNIFVYDInANFKTVNNLIGCKDSIYSLATTPNL 190
Cdd:COG2319   99 DGTVRLWDLAT---GLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDL-ATGKLLRTLTGHSGAVTSVAFSPDG 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782 191 SLVLGAGTEKCIRLFDPRTNEKIMKLRGHTDNVRALVVNDDGTRALSAGSDATIRLWDIGQQRCIATCIAHEEGVWTLQV 270
Cdd:COG2319  175 KLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAF 254

                        250       260       270
                 ....*....|....*....|....*....|
gi 212645782 271 DSSFTTVYSAGKDKMVVktpLYDFTKSQLL 300
Cdd:COG2319  255 SPDGRLLASGSADGTVR---LWDLATGELL 281
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 128-286 7.59e-26

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: 108.19  E-value: 7.59e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782 128 IDCIRTHKDYVSCLAYAPIVEKAVSASFDHNIFVYDINANFKtVNNLIGCKDSIYSLATTPNLSLVLGAGTEKCIRLFDP 207
Cdd:cd00200    2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGEL-LRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 212645782 208 RTNEKIMKLRGHTDNVRALVVNDDGTRALSAGSDATIRLWDIGQQRCIATCIAHEEGVWTLQVDSSFTTVYSAGKDKMV 286
Cdd:cd00200   81 ETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTI 159
WD40 COG2319
WD40 repeat [General function prediction only];
83-353 6.24e-25

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 107.69  E-value: 6.24e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782  83 QGSLEQHTDWVNDMILCGHGKILISASNDTTVKVWNIERdnkHGFIDCIRTHKDYVSCLAYAPIVEKAVSASFDHNIFVY 162
Cdd:COG2319   29 LLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAA---GALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLW 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782 163 DINANfKTVNNLIGCKDSIYSLATTPNLSLVLGAGTEKCIRLFDPRTNEKIMKLRGHTDNVRALVVNDDGTRALSAGSDA 242
Cdd:COG2319  106 DLATG-LLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDG 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782 243 TIRLWDIGQQRCIATCIAHEEGVWTLQVDSSFTTVYSAGKDKMVVktpLYDFTKSQLLFkeeapvkklLLSEKDNPVS-- 320
Cdd:COG2319  185 TVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVR---LWDLATGKLLR---------TLTGHSGSVRsv 252

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 212645782 321 --------LWVGTWKSDIKRWSIRPSAQLSIGGDEDGPSTS 353
Cdd:COG2319  253 afspdgrlLASGSADGTVRLWDLATGELLRTLTGHSGGVNS 293
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 216-300 4.41e-11

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: 64.28  E-value: 4.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782 216 LRGHTDNVRALVVNDDGTRALSAGSDATIRLWDIGQQRCIATCIAHEEGVWTLQVDSSFTTVYSAGKDKMVVktpLYDFT 295
Cdd:cd00200    5 LKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIR---LWDLE 81


                 ....*
gi 212645782 296 KSQLL 300
Cdd:cd00200   82 TGECV 86
WD40 COG2319
WD40 repeat [General function prediction only];
30-120 5.48e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 55.69  E-value: 5.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645782  30 SAVSALQYDAQNGRLFTGGSDTIIRTWSV---------PHHKD-----AFSARGG------------VRSPGKNSPVQyq 83
Cdd:COG2319  289 GGVNSVAFSPDGKLLASGSDDGTVRLWDLatgkllrtlTGHTGavrsvAFSPDGKtlasgsddgtvrLWDLATGELLR-- 366

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 212645782  84 gSLEQHTDWVNDMILCGHGKILISASNDTTVKVWNIE 120
Cdd:COG2319  367 -TLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 209-248 2.71e-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: 47.31  E-value: 2.71e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 212645782   209 TNEKIMKLRGHTDNVRALVVNDDGTRALSAGSDATIRLWD 248
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
210-248 2.17e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 44.64  E-value: 2.17e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 212645782  210 NEKIMKLRGHTDNVRALVVNDDGTRALSAGSDATIRLWD 248
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 85-118 5.39e-06

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: 43.46  E-value: 5.39e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 212645782    85 SLEQHTDWVNDMILCGHGKILISASNDTTVKVWN 118
Cdd:smart00320   7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
81-118 1.86e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 41.95  E-value: 1.86e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 212645782   81 QYQGSLEQHTDWVNDMILCGHGKILISASNDTTVKVWN 118
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
RAWUL_PCGF_like cd16102
RRING finger- and WD40-associated ubiquitin-like (RAWUL) domain found in PCGF1-6, RING1 and -2, ...
 661-693 8.99e-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: 8.99e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 212645782 661 EMYCNDQRLEPDMDLRTVKHLYW-KQSGELLLHY 693
Cdd:cd16102   53 DILCRGELLGKEHTLKFIWRTRWrKQDGPLVLQY 86
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH