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Conserved domains on  [gi|194386864|dbj|BAG59798|]
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unnamed protein product [Homo sapiens]

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

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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. ...
 427-591 3.00e-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: 197.90  E-value: 3.00e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864  427 VPPHTPVIFGE-----AGGRTLFRLLCRDSGGETEsmLLNETVPQWVIDITVDKNMP--KFNKIPFYLQPHASSGAKTL- 498
Cdd:pfam11816   1 LPPDTTIIISEespdsGGGRDLYRGTVGDIGEDVD--LLEEVAPMWLGDVLLYNKIPpkEPVKISFVLQPWPGSDLPPDk 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864  499 ------KKDRLSASDMLQVRKVMEHVYEKIINLDNESQTTSSSNNEKPGEQEKeediavlAEEKIELLCQDQVLDPNMDL 572
Cdd:pfam11816  79 lpelpnKNSRLNANRMLRVRKILAYVAEKLESLTPEMKPPSPDEDENADKKLK-------PEEYLELLCNDQVLPPNMTL 151

                         170
                  ....*....|....*....
gi 194386864  573 RTVKHFIWKSGGDLTLHYR 591
Cdd:pfam11816 152 ATVKTFIWKSGGDIVLHYR 170
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3-204 5.53e-46

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: 164.05  E-value: 5.53e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864   3 CQSAQVISASSDTTVKVWNAHKGFCMSTLRTHKDYVKALAYAKDKELVASAGLDRQIFLWDVNTLTALTasnntvttsSL 82
Cdd:cd00200   61 ADGTYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLT---------TL 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864  83 SGNKDSIYSLAMNQLGTIIVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWSLGQQRC 162
Cdd:cd00200  132 RGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKC 211

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 194386864 163 IATYRVHDEGVWALQVNDAFTHVYSGGRDRKIYCTDLRNPDI 204
Cdd:cd00200  212 LGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGEC 253
 
Name Accession Description Interval E-value
DUF3337 pfam11816
Domain of unknown function (DUF3337); This family of proteins are functionally uncharacterized. ...
 427-591 3.00e-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: 197.90  E-value: 3.00e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864  427 VPPHTPVIFGE-----AGGRTLFRLLCRDSGGETEsmLLNETVPQWVIDITVDKNMP--KFNKIPFYLQPHASSGAKTL- 498
Cdd:pfam11816   1 LPPDTTIIISEespdsGGGRDLYRGTVGDIGEDVD--LLEEVAPMWLGDVLLYNKIPpkEPVKISFVLQPWPGSDLPPDk 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864  499 ------KKDRLSASDMLQVRKVMEHVYEKIINLDNESQTTSSSNNEKPGEQEKeediavlAEEKIELLCQDQVLDPNMDL 572
Cdd:pfam11816  79 lpelpnKNSRLNANRMLRVRKILAYVAEKLESLTPEMKPPSPDEDENADKKLK-------PEEYLELLCNDQVLPPNMTL 151

                         170
                  ....*....|....*....
gi 194386864  573 RTVKHFIWKSGGDLTLHYR 591
Cdd:pfam11816 152 ATVKTFIWKSGGDIVLHYR 170
Ubl_WDR48 cd17041
Ubiquitin-like (Ubl) domain found in WD repeat-containing protein 48 (WDR48) and similar ...
 479-591 1.43e-48

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: 163.99  E-value: 1.43e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864 479 KFNKIPFYLQPHASSGA--KTLKKDRLSASDMLQVRKVMEHVYEKIINLDNESQTtsssnnekpgeqekeediAVLAEEK 556
Cdd:cd17041    1 EFPKISFFLQPHPSSGLppKTLKNDKLSASRMLRVRKVMEYVAEKLLGQEPESQD------------------ASNPEEK 62

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 194386864 557 IELLCQDQVLDPNMDLRTVKHFIWKSGGDLTLHYR 591
Cdd:cd17041   63 LELLCNDQVLDPNMTLATVKHFIWKSGGDLVLHYR 97
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3-204 5.53e-46

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: 164.05  E-value: 5.53e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864   3 CQSAQVISASSDTTVKVWNAHKGFCMSTLRTHKDYVKALAYAKDKELVASAGLDRQIFLWDVNTLTALTasnntvttsSL 82
Cdd:cd00200   61 ADGTYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLT---------TL 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864  83 SGNKDSIYSLAMNQLGTIIVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWSLGQQRC 162
Cdd:cd00200  132 RGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKC 211

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 194386864 163 IATYRVHDEGVWALQVNDAFTHVYSGGRDRKIYCTDLRNPDI 204
Cdd:cd00200  212 LGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGEC 253
WD40 COG2319
WD40 repeat [General function prediction only];
7-194 2.60e-42

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 157.00  E-value: 2.60e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864   7 QVISASSDTTVKVWNAHKGFCMSTLRTHKDYVKALAYAKDKELVASAGLDRQIFLWDVNTLTALTasnntvttsSLSGNK 86
Cdd:COG2319  218 LLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLR---------TLTGHS 288

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864  87 DSIYSLAMNQLGTIIVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWSLGQQRCIATY 166
Cdd:COG2319  289 GGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL 368

                        170       180       190
                 ....*....|....*....|....*....|..
gi 194386864 167 RVHDEGVWALqvndAFT----HVYSGGRDRKI 194
Cdd:COG2319  369 TGHTGAVTSV----AFSpdgrTLASGSADGTV 396
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 31-204 1.43e-10

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 64.34  E-value: 1.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864  31 LRTHKDYVKALAYAKDKELVASAGLDRQIFLWDVNTLTAlTASNNTVTTSSLSGnKDSIYSLAMNQ-LGTIIVSGSTEKV 109
Cdd:PLN00181 479 LLNSSNLVCAIGFDRDGEFFATAGVNKKIKIFECESIIK-DGRDIHYPVVELAS-RSKLSGICWNSyIKSQVASSNFEGV 556

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864 110 LRVWDPRTCAKLMKLKGHTDNVKAL-LLNRDGTQCLSGSSDGTIRLWSLGQQRCIATYRVhDEGVWALQV-NDAFTHVYS 187
Cdd:PLN00181 557 VQVWDVARSQLVTEMKEHEKRVWSIdYSSADPTLLASGSDDGSVKLWSINQGVSIGTIKT-KANICCVQFpSESGRSLAF 635

                        170
                 ....*....|....*..
gi 194386864 188 GGRDRKIYCTDLRNPDI 204
Cdd:PLN00181 636 GSADHKVYYYDLRNPKL 652
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 117-156 4.04e-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: 46.54  E-value: 4.04e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 194386864   117 TCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWS 156
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
121-156 1.19e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.41  E-value: 1.19e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 194386864  121 LMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWS 156
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. ...
 427-591 3.00e-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: 197.90  E-value: 3.00e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864  427 VPPHTPVIFGE-----AGGRTLFRLLCRDSGGETEsmLLNETVPQWVIDITVDKNMP--KFNKIPFYLQPHASSGAKTL- 498
Cdd:pfam11816   1 LPPDTTIIISEespdsGGGRDLYRGTVGDIGEDVD--LLEEVAPMWLGDVLLYNKIPpkEPVKISFVLQPWPGSDLPPDk 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864  499 ------KKDRLSASDMLQVRKVMEHVYEKIINLDNESQTTSSSNNEKPGEQEKeediavlAEEKIELLCQDQVLDPNMDL 572
Cdd:pfam11816  79 lpelpnKNSRLNANRMLRVRKILAYVAEKLESLTPEMKPPSPDEDENADKKLK-------PEEYLELLCNDQVLPPNMTL 151

                         170
                  ....*....|....*....
gi 194386864  573 RTVKHFIWKSGGDLTLHYR 591
Cdd:pfam11816 152 ATVKTFIWKSGGDIVLHYR 170
Ubl_WDR48 cd17041
Ubiquitin-like (Ubl) domain found in WD repeat-containing protein 48 (WDR48) and similar ...
 479-591 1.43e-48

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: 163.99  E-value: 1.43e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864 479 KFNKIPFYLQPHASSGA--KTLKKDRLSASDMLQVRKVMEHVYEKIINLDNESQTtsssnnekpgeqekeediAVLAEEK 556
Cdd:cd17041    1 EFPKISFFLQPHPSSGLppKTLKNDKLSASRMLRVRKVMEYVAEKLLGQEPESQD------------------ASNPEEK 62

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 194386864 557 IELLCQDQVLDPNMDLRTVKHFIWKSGGDLTLHYR 591
Cdd:cd17041   63 LELLCNDQVLDPNMTLATVKHFIWKSGGDLVLHYR 97
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3-204 5.53e-46

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: 164.05  E-value: 5.53e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864   3 CQSAQVISASSDTTVKVWNAHKGFCMSTLRTHKDYVKALAYAKDKELVASAGLDRQIFLWDVNTLTALTasnntvttsSL 82
Cdd:cd00200   61 ADGTYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLT---------TL 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864  83 SGNKDSIYSLAMNQLGTIIVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWSLGQQRC 162
Cdd:cd00200  132 RGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKC 211

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 194386864 163 IATYRVHDEGVWALQVNDAFTHVYSGGRDRKIYCTDLRNPDI 204
Cdd:cd00200  212 LGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGEC 253
WD40 COG2319
WD40 repeat [General function prediction only];
7-194 2.60e-42

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 157.00  E-value: 2.60e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864   7 QVISASSDTTVKVWNAHKGFCMSTLRTHKDYVKALAYAKDKELVASAGLDRQIFLWDVNTLTALTasnntvttsSLSGNK 86
Cdd:COG2319  218 LLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLR---------TLTGHS 288

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864  87 DSIYSLAMNQLGTIIVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWSLGQQRCIATY 166
Cdd:COG2319  289 GGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL 368

                        170       180       190
                 ....*....|....*....|....*....|..
gi 194386864 167 RVHDEGVWALqvndAFT----HVYSGGRDRKI 194
Cdd:COG2319  369 TGHTGAVTSV----AFSpdgrTLASGSADGTV 396
WD40 COG2319
WD40 repeat [General function prediction only];
7-201 4.86e-41

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 153.53  E-value: 4.86e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864   7 QVISASSDTTVKVWNAHKGFCMSTLRTHKDYVKALAYAKDKELVASAGLDRQIFLWDVNTLTALTasnntvttsSLSGNK 86
Cdd:COG2319  176 LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLR---------TLTGHS 246

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864  87 DSIYSLAMNQLGTIIVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWSLGQQRCIATY 166
Cdd:COG2319  247 GSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTL 326

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 194386864 167 RVHDEGVWALQVNDAFTHVYSGGRDRKIYCTDLRN 201
Cdd:COG2319  327 TGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLAT 361
WD40 COG2319
WD40 repeat [General function prediction only];
6-208 5.76e-41

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 153.53  E-value: 5.76e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864   6 AQVISASSDTTVKVWNAHKGFCMSTLRTHKDYVKALAYAKDKELVASAGLDRQIFLWDVNTLTALTasnntvttsSLSGN 85
Cdd:COG2319   91 RLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLR---------TLTGH 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864  86 KDSIYSLAMNQLGTIIVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWSLGQQRCIAT 165
Cdd:COG2319  162 SGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRT 241

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 194386864 166 YRVHDEGVWALqvndAF----THVYSGGRDRKIYCTDLRNPDIRVLI 208
Cdd:COG2319  242 LTGHSGSVRSV----AFspdgRLLASGSADGTVRLWDLATGELLRTL 284
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 8-194 2.67e-36

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: 137.47  E-value: 2.67e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864   8 VISASSDTTVKVWNAHKGFCMSTLRTHKDYVKALAYAKDKELVASAGLDRQIFLWDVNTLTALTasnntvttsSLSGNKD 87
Cdd:cd00200  108 LSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVA---------TLTGHTG 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864  88 SIYSLAMNQLGTIIVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWSLGQQRCIATYR 167
Cdd:cd00200  179 EVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLS 258

                        170       180
                 ....*....|....*....|....*..
gi 194386864 168 VHDEGVWALQVNDAFTHVYSGGRDRKI 194
Cdd:cd00200  259 GHTNSVTSLAWSPDGKRLASGSADGTI 285
WD40 COG2319
WD40 repeat [General function prediction only];
8-157 6.53e-35

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 136.19  E-value: 6.53e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864   8 VISASSDTTVKVWNAHKGFCMSTLRTHKDYVKALAYAKDKELVASAGLDRQIFLWDVNTLTALTasnntvttsSLSGNKD 87
Cdd:COG2319  261 LASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLR---------TLTGHTG 331

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864  88 SIYSLAMNQLGTIIVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWSL 157
Cdd:COG2319  332 AVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 8-156 3.40e-31

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: 122.83  E-value: 3.40e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864   8 VISASSDTTVKVWNAHKGFCMSTLRTHKDYVKALAYAKDKELVASAGLDRQIFLWDVNTLTALTasnntvttsSLSGNKD 87
Cdd:cd00200  150 VASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLG---------TLRGHEN 220

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194386864  88 SIYSLAMNQLGTIIVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWS 156
Cdd:cd00200  221 GVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 27-200 4.27e-29

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: 117.05  E-value: 4.27e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864  27 CMSTLRTHKDYVKALAYAKDKELVASAGLDRQIFLWDVNTLTALT------------------------ASNNTV----- 77
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRtlkghtgpvrdvaasadgtylasgSSDKTIrlwdl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864  78 ----TTSSLSGNKDSIYSLAMNQLGTIIVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIR 153
Cdd:cd00200   81 etgeCVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIK 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 194386864 154 LWSLGQQRCIATYRVHDEGVWALQVNDAFTHVYSGGRDRKIYCTDLR 200
Cdd:cd00200  161 LWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLS 207
WD40 COG2319
WD40 repeat [General function prediction only];
4-194 1.35e-24

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 106.15  E-value: 1.35e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864   4 QSAQVISASSDTTVKVWNAHKGFCMSTLRTHKDYVKALAYAKDKELVASAGLDRQIFLWDVNTLTALTasnntvttsSLS 83
Cdd:COG2319    5 DGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLA---------TLL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864  84 GNKDSIYSLAMNQLGTIIVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWSLGQQRCI 163
Cdd:COG2319   76 GHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLL 155

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 194386864 164 ATYRVHDEGVWALqvndAF----THVYSGGRDRKI 194
Cdd:COG2319  156 RTLTGHSGAVTSV----AFspdgKLLASGSDDGTV 186
WD40 COG2319
WD40 repeat [General function prediction only];
7-117 1.75e-20

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 93.82  E-value: 1.75e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864   7 QVISASSDTTVKVWNAHKGFCMSTLRTHKDYVKALAYAKDKELVASAGLDRQIFLWDVNTLTALTasnntvttsSLSGNK 86
Cdd:COG2319  302 LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLR---------TLTGHT 372

                         90       100       110
                 ....*....|....*....|....*....|.
gi 194386864  87 DSIYSLAMNQLGTIIVSGSTEKVLRVWDPRT 117
Cdd:COG2319  373 GAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
42-194 7.42e-12

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 67.63  E-value: 7.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864  42 AYAKDKELVASAGLDRQIFLWDVNTLTALTAsnntvttssLSGNKDSIYSLAMNQLGTIIVSGSTEKVLRVWDPRTCAKL 121
Cdd:COG2319    1 ALSADGAALAAASADLALALLAAALGALLLL---------LLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALL 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194386864 122 MKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWSLGQQRCIATYRVHDEGVWALQVNDAFTHVYSGGRDRKI 194
Cdd:COG2319   72 ATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTV 144
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 31-204 1.43e-10

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 64.34  E-value: 1.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864  31 LRTHKDYVKALAYAKDKELVASAGLDRQIFLWDVNTLTAlTASNNTVTTSSLSGnKDSIYSLAMNQ-LGTIIVSGSTEKV 109
Cdd:PLN00181 479 LLNSSNLVCAIGFDRDGEFFATAGVNKKIKIFECESIIK-DGRDIHYPVVELAS-RSKLSGICWNSyIKSQVASSNFEGV 556

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864 110 LRVWDPRTCAKLMKLKGHTDNVKAL-LLNRDGTQCLSGSSDGTIRLWSLGQQRCIATYRVhDEGVWALQV-NDAFTHVYS 187
Cdd:PLN00181 557 VQVWDVARSQLVTEMKEHEKRVWSIdYSSADPTLLASGSDDGSVKLWSINQGVSIGTIKT-KANICCVQFpSESGRSLAF 635

                        170
                 ....*....|....*..
gi 194386864 188 GGRDRKIYCTDLRNPDI 204
Cdd:PLN00181 636 GSADHKVYYYDLRNPKL 652
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 124-213 5.66e-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: 5.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864 124 LKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWSLGQQRCIATYRVHDEGVWALQVNDAFTHVYSGGRDRKIYCTDLRNPD 203
Cdd:cd00200    5 LKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGE 84

                         90
                 ....*....|.
gi 194386864 204 -IRVLICEEKA 213
Cdd:cd00200   85 cVRTLTGHTSY 95
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 117-156 4.04e-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: 46.54  E-value: 4.04e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 194386864   117 TCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWS 156
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PTZ00421 PTZ00421
coronin; Provisional
 5-118 5.97e-07

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 52.20  E-value: 5.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864   5 SAQVISASSDTTVKVWN-AHKGFCMST------LRTHKDYVKALAY-AKDKELVASAGLDRQIFLWDVNTLTALTasnnt 76
Cdd:PTZ00421  88 PQKLFTASEDGTIMGWGiPEEGLTQNIsdpivhLQGHTKKVGIVSFhPSAMNVLASAGADMVVNVWDVERGKAVE----- 162

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 194386864  77 vTTSSLSgnkDSIYSLAMNQLGTIIVSGSTEKVLRVWDPRTC 118
Cdd:PTZ00421 163 -VIKCHS---DQITSLEWNLDGSLLCTTSKDKKLNIIDPRDG 200
Ubiquitin_like_fold cd00196
Beta-grasp ubiquitin-like fold; Ubiquitin is a protein modifier that is involved in various ...
 496-591 6.92e-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: 46.93  E-value: 6.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864 496 KTLKKDRLSASDMLQVRKVMEHVYEKIInldnesqttsssnnekpgeqekeediavLAEEKIELLCQDQVLDPNMDLRTv 575
Cdd:cd00196    6 PSLKKIVVAVPPSTTLRQVLEKVAKRIG----------------------------LPPDVIRLLFNGQVLDDLMTAKQ- 56

                         90
                 ....*....|....*.
gi 194386864 576 khfiWKSGGDLTLHYR 591
Cdd:cd00196   57 ----VGLEPGEELHFV 68
WD40 pfam00400
WD domain, G-beta repeat;
121-156 1.19e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.41  E-value: 1.19e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 194386864  121 LMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWS 156
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 24-63 1.26e-05

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: 42.30  E-value: 1.26e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 194386864    24 KGFCMSTLRTHKDYVKALAYAKDKELVASAGLDRQIFLWD 63
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 6-157 1.61e-05

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 48.16  E-value: 1.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864   6 AQVISASSDTTVKVWNAHKGFCMSTLRTHKDYVKALAYAK-DKELVASAGLDRQIFLWDVNTLTALTASNNTVTTSSLSG 84
Cdd:PLN00181 546 SQVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSaDPTLLASGSDDGSVKLWSINQGVSIGTIKTKANICCVQF 625

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194386864  85 NKDSIYSLAMnqlgtiivsGSTEKVLRVWDPRTCA-KLMKLKGHTDNVKALLLnRDGTQCLSGSSDGTIRLWSL 157
Cdd:PLN00181 626 PSESGRSLAF---------GSADHKVYYYDLRNPKlPLCTMIGHSKTVSYVRF-VDSSTLVSSSTDNTLKLWDL 689
WD40 pfam00400
WD domain, G-beta repeat;
25-63 3.67e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 41.18  E-value: 3.67e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 194386864   25 GFCMSTLRTHKDYVKALAYAKDKELVASAGLDRQIFLWD 63
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PTZ00421 PTZ00421
coronin; Provisional
 10-120 1.70e-04

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 44.50  E-value: 1.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386864  10 SASSDTTVKVWNAHKGFCMSTLRTHKDYVKALAYAKDKELVASAGLDRQIFLWDVNTLTALTASNNTVTTSSlsgnKDSI 89
Cdd:PTZ00421 143 SAGADMVVNVWDVERGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRDGTIVSSVEAHASAKS----QRCL 218

                         90       100       110
                 ....*....|....*....|....*....|.
gi 194386864  90 YSLAMNQLGTIIVSGSTEKVLRVWDPRTCAK 120
Cdd:PTZ00421 219 WAKRKDLIITLGCSKSQQRQIMLWDTRKMAS 249
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 80-114 5.25e-04

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: 37.68  E-value: 5.25e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 194386864    80 SSLSGNKDSIYSLAMNQLGTIIVSGSTEKVLRVWD 114
Cdd:smart00320   6 KTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
79-114 1.22e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.94  E-value: 1.22e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 194386864   79 TSSLSGNKDSIYSLAMNQLGTIIVSGSTEKVLRVWD 114
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
RAWUL pfam16207
RAWUL domain RING finger- and WD40-associated ubiquitin-like; The RAWUL domain is found at the ...
 556-591 4.74e-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: 4.74e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 194386864  556 KIELLCQDQVLDPNMDLRTVKHFIWKSGGDLTLHYR 591
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, ...
 553-591 7.24e-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: 7.24e-03
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                 ....*....|....*....|....*....|....*....|
gi 194386864 553 AEEKIELLCQDQVLDPNMDLRTVKHFIW-KSGGDLTLHYR 591
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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