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Conserved domains on  [gi|25148359|ref|NP_497931|]
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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

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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. ...
 530-678 2.84e-50

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: 172.48  E-value: 2.84e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359   530 LPEHTPLIICE-----GNGRPLYRLLVGDAGKEfeANELAQIAPMWVIDAIERNQLP--KFNKMPFYLLPHPSTNPKQP- 601
Cdd:pfam11816   1 LPPDTTIIISEespdsGGGRDLYRGTVGDIGED--VDLLEEVAPMWLGDVLLYNKIPpkEPVKISFVLQPWPGSDLPPDk 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359   602 ------KKDRLSATEMLQVKKVMEHVYEKILSTNDVGSIPLNQIHT----------KMEMYCNDQRLEPDMDLRTVKHLY 665
Cdd:pfam11816  79 lpelpnKNSRLNANRMLRVRKILAYVAEKLESLTPEMKPPSPDEDEnadkklkpeeYLELLCNDQVLPPNMTLATVKTFI 158

                         170
                  ....*....|...
gi 25148359   666 WKQSGELLLHYKP 678
Cdd:pfam11816 159 WKSGGDIVLHYRR 171
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 29-322 4.61e-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: 170.59  E-value: 4.61e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359  29 RSAVSALQYDAQNGRLFTGGSDTIIRTWSVphhkdafsarggvrspgknSPVQYQGSLEQHTDWVNDMILCGHGKILISA 108
Cdd:cd00200   9 TGGVTCVAFSPDGKLLATGSGDGTIKVWDL-------------------ETGELLRTLKGHTGPVRDVAASADGTYLASG 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359 109 SNDTTVKVWNIERDNkhgfidCIRT---HKDYVSCLAYAPIVEKAVSASFDHNIFVYDINaNFKTVNNLIGCKDSIYSLA 185
Cdd:cd00200  70 SSDKTIRLWDLETGE------CVRTltgHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVE-TGKCLTTLRGHTDWVNSVA 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359 186 TTPNLSLVLGAGTEKCIRLFDPRTNEKIMKLRGHTDNVRALVVNDDGTRALSAGSDATIRLWDIGQQRCIATCIAHEEGV 265
Cdd:cd00200 143 FSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGV 222

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25148359 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. ...
 530-678 2.84e-50

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: 172.48  E-value: 2.84e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359   530 LPEHTPLIICE-----GNGRPLYRLLVGDAGKEfeANELAQIAPMWVIDAIERNQLP--KFNKMPFYLLPHPSTNPKQP- 601
Cdd:pfam11816   1 LPPDTTIIISEespdsGGGRDLYRGTVGDIGED--VDLLEEVAPMWLGDVLLYNKIPpkEPVKISFVLQPWPGSDLPPDk 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359   602 ------KKDRLSATEMLQVKKVMEHVYEKILSTNDVGSIPLNQIHT----------KMEMYCNDQRLEPDMDLRTVKHLY 665
Cdd:pfam11816  79 lpelpnKNSRLNANRMLRVRKILAYVAEKLESLTPEMKPPSPDEDEnadkklkpeeYLELLCNDQVLPPNMTLATVKTFI 158

                         170
                  ....*....|...
gi 25148359   666 WKQSGELLLHYKP 678
Cdd:pfam11816 159 WKSGGDIVLHYRR 171
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 29-322 4.61e-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: 170.59  E-value: 4.61e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359  29 RSAVSALQYDAQNGRLFTGGSDTIIRTWSVphhkdafsarggvrspgknSPVQYQGSLEQHTDWVNDMILCGHGKILISA 108
Cdd:cd00200   9 TGGVTCVAFSPDGKLLATGSGDGTIKVWDL-------------------ETGELLRTLKGHTGPVRDVAASADGTYLASG 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359 109 SNDTTVKVWNIERDNkhgfidCIRT---HKDYVSCLAYAPIVEKAVSASFDHNIFVYDINaNFKTVNNLIGCKDSIYSLA 185
Cdd:cd00200  70 SSDKTIRLWDLETGE------CVRTltgHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVE-TGKCLTTLRGHTDWVNSVA 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359 186 TTPNLSLVLGAGTEKCIRLFDPRTNEKIMKLRGHTDNVRALVVNDDGTRALSAGSDATIRLWDIGQQRCIATCIAHEEGV 265
Cdd:cd00200 143 FSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGV 222

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25148359 266 WTLQVDSSFTTVYSAGKDKMVVKTPLYDFTKSQLLFKEEAPVKKLLLSEK---------DNPVSLW 322
Cdd:cd00200 223 NSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDgkrlasgsaDGTIRIW 288
WD40 COG2319
WD40 repeat [General function prediction only];
29-286 4.96e-39

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 148.91  E-value: 4.96e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359  29 RSAVSALQYDAQNGRLFTGGSDTIIRTWSV---------PHHKD-----AFSA----------RGGVR--SPGKNSPVQy 82
Cdd:COG2319 120 TGAVRSVAFSPDGKTLASGSADGTVRLWDLatgkllrtlTGHSGavtsvAFSPdgkllasgsdDGTVRlwDLATGKLLR- 198

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359  83 qgSLEQHTDWVNDMILCGHGKILISASNDTTVKVWNIERDNkhgFIDCIRTHKDYVSCLAYAPIVEKAVSASFDHNIFVY 162
Cdd:COG2319 199 --TLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGK---LLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLW 273

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359 163 DINANfKTVNNLIGCKDSIYSLATTPNLSLVLGAGTEKCIRLFDPRTNEKIMKLRGHTDNVRALVVNDDGTRALSAGSDA 242
Cdd:COG2319 274 DLATG-ELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDG 352

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 25148359 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 ...
 582-677 5.37e-38

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: 136.26  E-value: 5.37e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359 582 KFNKMPFYLLPHPSTN--PKQPKKDRLSATEMLQVKKVMEHVYEKILstndvGSIPLNQIHT----KMEMYCNDQRLEPD 655
Cdd:cd17041   1 EFPKISFFLQPHPSSGlpPKTLKNDKLSASRMLRVRKVMEYVAEKLL-----GQEPESQDASnpeeKLELLCNDQVLDPN 75

                        90       100
                ....*....|....*....|..
gi 25148359 656 MDLRTVKHLYWKQSGELLLHYK 677
Cdd:cd17041  76 MTLATVKHFIWKSGGDLVLHYR 97
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 209-248 2.77e-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: 2.77e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 25148359    209 TNEKIMKLRGHTDNVRALVVNDDGTRALSAGSDATIRLWD 248
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
210-248 2.27e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 44.64  E-value: 2.27e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 25148359   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. ...
 530-678 2.84e-50

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: 172.48  E-value: 2.84e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359   530 LPEHTPLIICE-----GNGRPLYRLLVGDAGKEfeANELAQIAPMWVIDAIERNQLP--KFNKMPFYLLPHPSTNPKQP- 601
Cdd:pfam11816   1 LPPDTTIIISEespdsGGGRDLYRGTVGDIGED--VDLLEEVAPMWLGDVLLYNKIPpkEPVKISFVLQPWPGSDLPPDk 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359   602 ------KKDRLSATEMLQVKKVMEHVYEKILSTNDVGSIPLNQIHT----------KMEMYCNDQRLEPDMDLRTVKHLY 665
Cdd:pfam11816  79 lpelpnKNSRLNANRMLRVRKILAYVAEKLESLTPEMKPPSPDEDEnadkklkpeeYLELLCNDQVLPPNMTLATVKTFI 158

                         170
                  ....*....|...
gi 25148359   666 WKQSGELLLHYKP 678
Cdd:pfam11816 159 WKSGGDIVLHYRR 171
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 29-322 4.61e-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: 170.59  E-value: 4.61e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359  29 RSAVSALQYDAQNGRLFTGGSDTIIRTWSVphhkdafsarggvrspgknSPVQYQGSLEQHTDWVNDMILCGHGKILISA 108
Cdd:cd00200   9 TGGVTCVAFSPDGKLLATGSGDGTIKVWDL-------------------ETGELLRTLKGHTGPVRDVAASADGTYLASG 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359 109 SNDTTVKVWNIERDNkhgfidCIRT---HKDYVSCLAYAPIVEKAVSASFDHNIFVYDINaNFKTVNNLIGCKDSIYSLA 185
Cdd:cd00200  70 SSDKTIRLWDLETGE------CVRTltgHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVE-TGKCLTTLRGHTDWVNSVA 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359 186 TTPNLSLVLGAGTEKCIRLFDPRTNEKIMKLRGHTDNVRALVVNDDGTRALSAGSDATIRLWDIGQQRCIATCIAHEEGV 265
Cdd:cd00200 143 FSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGV 222

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25148359 266 WTLQVDSSFTTVYSAGKDKMVVKTPLYDFTKSQLLFKEEAPVKKLLLSEK---------DNPVSLW 322
Cdd:cd00200 223 NSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDgkrlasgsaDGTIRIW 288
WD40 COG2319
WD40 repeat [General function prediction only];
29-286 4.96e-39

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 148.91  E-value: 4.96e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359  29 RSAVSALQYDAQNGRLFTGGSDTIIRTWSV---------PHHKD-----AFSA----------RGGVR--SPGKNSPVQy 82
Cdd:COG2319 120 TGAVRSVAFSPDGKTLASGSADGTVRLWDLatgkllrtlTGHSGavtsvAFSPdgkllasgsdDGTVRlwDLATGKLLR- 198

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359  83 qgSLEQHTDWVNDMILCGHGKILISASNDTTVKVWNIERDNkhgFIDCIRTHKDYVSCLAYAPIVEKAVSASFDHNIFVY 162
Cdd:COG2319 199 --TLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGK---LLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLW 273

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359 163 DINANfKTVNNLIGCKDSIYSLATTPNLSLVLGAGTEKCIRLFDPRTNEKIMKLRGHTDNVRALVVNDDGTRALSAGSDA 242
Cdd:COG2319 274 DLATG-ELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDG 352

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 25148359 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 1.79e-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: 144.01  E-value: 1.79e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359  89 HTDWVNDMILCGHGKILISASNDTTVKVWNIERDnkhgfiDCIRT---HKDYVSCLAYAPIVEKAVSASFDHNIFVYDIN 165
Cdd:cd00200   8 HTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETG------ELLRTlkgHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359 166 ANfKTVNNLIGCKDSIYSLATTPNLSLVLGAGTEKCIRLFDPRTNEKIMKLRGHTDNVRALVVNDDGTRALSAGSDATIR 245
Cdd:cd00200  82 TG-ECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIK 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359 246 LWDIGQQRCIATCIAHEEGVWTLQVDSSFTTVYSAGKDKMVvktPLYDFTKSQLLfkeeapvkKLLLSEKDNPVSLWVGt 325
Cdd:cd00200 161 LWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTI---KLWDLSTGKCL--------GTLRGHENGVNSVAFS- 228

                       250       260
                ....*....|....*....|....
gi 25148359 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 ...
 582-677 5.37e-38

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: 136.26  E-value: 5.37e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359 582 KFNKMPFYLLPHPSTN--PKQPKKDRLSATEMLQVKKVMEHVYEKILstndvGSIPLNQIHT----KMEMYCNDQRLEPD 655
Cdd:cd17041   1 EFPKISFFLQPHPSSGlpPKTLKNDKLSASRMLRVRKVMEYVAEKLL-----GQEPESQDASnpeeKLELLCNDQVLDPN 75

                        90       100
                ....*....|....*....|..
gi 25148359 656 MDLRTVKHLYWKQSGELLLHYK 677
Cdd:cd17041  76 MTLATVKHFIWKSGGDLVLHYR 97
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 30-248 5.48e-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: 5.48e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359  30 SAVSALQYDAQNGRLFTGGSDTIIRTWSVP---------HHKD-----AFSARGGVRSPG---------KNSPVQYQGSL 86
Cdd:cd00200  52 GPVRDVAASADGTYLASGSSDKTIRLWDLEtgecvrtltGHTSyvssvAFSPDGRILSSSsrdktikvwDVETGKCLTTL 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359  87 EQHTDWVNDMILCGHGKILISASNDTTVKVWNIeRDNKhgfidCIRT---HKDYVSCLAYAPIVEKAVSASFDHNIFVYD 163
Cdd:cd00200 132 RGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL-RTGK-----CVATltgHTGEVNSVAFSPDGEKLLSSSSDGTIKLWD 205

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359 164 INAnFKTVNNLIGCKDSIYSLATTPNLSLVLGAGTEKCIRLFDPRTNEKIMKLRGHTDNVRALVVNDDGTRALSAGSDAT 243
Cdd:cd00200 206 LST-GKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGT 284


                ....*
gi 25148359 244 IRLWD 248
Cdd:cd00200 285 IRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
29-249 2.19e-32

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 129.65  E-value: 2.19e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359  29 RSAVSALQYDAQNGRLFTGGSDTIIRTWSV---------PHHKD-----AFSARG----------GVR--SPGKNSPVQy 82
Cdd:COG2319 162 SGAVTSVAFSPDGKLLASGSDDGTVRLWDLatgkllrtlTGHTGavrsvAFSPDGkllasgsadgTVRlwDLATGKLLR- 240

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359  83 qgSLEQHTDWVNDMILCGHGKILISASNDTTVKVWNIERDnkhgfiDCIRT---HKDYVSCLAYAPIVEKAVSASFDHNI 159
Cdd:COG2319 241 --TLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATG------ELLRTltgHSGGVNSVAFSPDGKLLASGSDDGTV 312

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359 160 FVYDInANFKTVNNLIGCKDSIYSLATTPNLSLVLGAGTEKCIRLFDPRTNEKIMKLRGHTDNVRALVVNDDGTRALSAG 239
Cdd:COG2319 313 RLWDL-ATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGS 391

                       250
                ....*....|
gi 25148359 240 SDATIRLWDI 249
Cdd:COG2319 392 ADGTVRLWDL 401
WD40 COG2319
WD40 repeat [General function prediction only];
31-300 5.24e-32

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 128.49  E-value: 5.24e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359  31 AVSALQYDAQNGRLFTGGSDTIIRTWSVPHHKDAFSARGGVRSPGKNSPVQYQGSLEQHTDWVNDMILCGHGKILISASN 110
Cdd:COG2319  19 ALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASA 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359 111 DTTVKVWNIERdnkHGFIDCIRTHKDYVSCLAYAPIVEKAVSASFDHNIFVYDInANFKTVNNLIGCKDSIYSLATTPNL 190
Cdd:COG2319  99 DGTVRLWDLAT---GLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDL-ATGKLLRTLTGHSGAVTSVAFSPDG 174

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359 191 SLVLGAGTEKCIRLFDPRTNEKIMKLRGHTDNVRALVVNDDGTRALSAGSDATIRLWDIGQQRCIATCIAHEEGVWTLQV 270
Cdd:COG2319 175 KLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAF 254

                       250       260       270
                ....*....|....*....|....*....|
gi 25148359 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 8.56e-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: 107.81  E-value: 8.56e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359 128 IDCIRTHKDYVSCLAYAPIVEKAVSASFDHNIFVYDINANFKtVNNLIGCKDSIYSLATTPNLSLVLGAGTEKCIRLFDP 207
Cdd:cd00200   2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGEL-LRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25148359 208 RTNEKIMKLRGHTDNVRALVVNDDGTRALSAGSDATIRLWDIGQQRCIATCIAHEEGVWTLQVDSSFTTVYSAGKDKMV 286
Cdd:cd00200  81 ETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTI 159
WD40 COG2319
WD40 repeat [General function prediction only];
83-353 5.95e-25

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 107.69  E-value: 5.95e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359  83 QGSLEQHTDWVNDMILCGHGKILISASNDTTVKVWNIERdnkHGFIDCIRTHKDYVSCLAYAPIVEKAVSASFDHNIFVY 162
Cdd:COG2319  29 LLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAA---GALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLW 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359 163 DINANfKTVNNLIGCKDSIYSLATTPNLSLVLGAGTEKCIRLFDPRTNEKIMKLRGHTDNVRALVVNDDGTRALSAGSDA 242
Cdd:COG2319 106 DLATG-LLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDG 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359 243 TIRLWDIGQQRCIATCIAHEEGVWTLQVDSSFTTVYSAGKDKMVVktpLYDFTKSQLLFkeeapvkklLLSEKDNPVS-- 320
Cdd:COG2319 185 TVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVR---LWDLATGKLLR---------TLTGHSGSVRsv 252

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 25148359 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 4.67e-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: 4.67e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359 216 LRGHTDNVRALVVNDDGTRALSAGSDATIRLWDIGQQRCIATCIAHEEGVWTLQVDSSFTTVYSAGKDKMVVktpLYDFT 295
Cdd:cd00200   5 LKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIR---LWDLE 81


                ....*
gi 25148359 296 KSQLL 300
Cdd:cd00200  82 TGECV 86
WD40 COG2319
WD40 repeat [General function prediction only];
30-120 5.30e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 55.69  E-value: 5.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359  30 SAVSALQYDAQNGRLFTGGSDTIIRTWSV---------PHHKD-----AFSARGG------------VRSPGKNSPVQyq 83
Cdd:COG2319 289 GGVNSVAFSPDGKLLASGSDDGTVRLWDLatgkllrtlTGHTGavrsvAFSPDGKtlasgsddgtvrLWDLATGELLR-- 366

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 25148359  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 2.77e-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: 2.77e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 25148359    209 TNEKIMKLRGHTDNVRALVVNDDGTRALSAGSDATIRLWD 248
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
210-248 2.27e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 44.64  E-value: 2.27e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 25148359   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 5.57e-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: 5.57e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 25148359     85 SLEQHTDWVNDMILCGHGKILISASNDTTVKVWN 118
Cdd:smart00320   7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
81-118 1.97e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 41.95  E-value: 1.97e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 25148359    81 QYQGSLEQHTDWVNDMILCGHGKILISASNDTTVKVWN 118
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
Ubiquitin_like_fold cd00196
Beta-grasp ubiquitin-like fold; Ubiquitin is a protein modifier that is involved in various ...
 602-673 3.95e-03

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: 36.53  E-value: 3.95e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25148359 602 KKDRLSATEMLQVKKVMEHVYEKILSTNDVgsiplnqihtkMEMYCNDQRLEPDMDLRTVKhlywKQSGELL 673
Cdd:cd00196   9 KKIVVAVPPSTTLRQVLEKVAKRIGLPPDV-----------IRLLFNGQVLDDLMTAKQVG----LEPGEEL 65
RAWUL_PCGF_like cd16102
RRING finger- and WD40-associated ubiquitin-like (RAWUL) domain found in PCGF1-6, RING1 and -2, ...
 590-676 4.87e-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: 36.49  E-value: 4.87e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148359 590 LLPHPST----NPKQPKKD-RLSA-TEMLQVKKVMEHVYeKILSTNDVgsiplnqihtkmEMYCNDQRLEPDMDLRTVKH 663
Cdd:cd16102   6 LEPSESNlggkLPQLEKPYlRCSArATVGHLKKFLRRKL-KLDSEQDL------------DILCRGELLGKEHTLKFIWR 72

                        90
                ....*....|....
gi 25148359 664 LYW-KQSGELLLHY 676
Cdd:cd16102  73 TRWrKQDGPLVLQY 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.
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