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Conserved domains on  [gi|13129110|ref|NP_077007|]
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methylosome protein WDR77 isoform 2 [Homo sapiens]

Protein Classification

WD40 repeat domain-containing protein( domain architecture ID 11455410)

WD40 repeat domain-containing protein similar to proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly

CATH:  2.130.10.10
PubMed:  10322433|8090199
SCOP:  4002744

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
94-322 1.91e-26

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 108.46  E-value: 1.91e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129110  94 ILVASDSGAVELWELDENETLIVSKfckyEHDDIVSTVSVLSSGTQAVSGSKDICIKVWDLAQQVVLSSYRAHAAQVTCV 173
Cdd:COG2319 177 LASGSDDGTVRLWDLATGKLLRTLT----GHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSV 252

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129110 174 AASPhKDSVFLSCSEDNRILLWDTRCPKPASQIGcsAPGYLPTSLAWHPqQSEVFVFGDENGTVSLVDTKSTSCVLSSAV 253
Cdd:COG2319 253 AFSP-DGRLLASGSADGTVRLWDLATGELLRTLT--GHSGGVNSVAFSP-DGKLLASGSDDGTVRLWDLATGKLLRTLTG 328

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129110 254 HSQCVTGLVFSPHSvPFLASLSEDCSLAVLD-SSLSELFRSQAHRDFVRDATWSPlNHSLLTTVGWDHQV 322
Cdd:COG2319 329 HTGAVRSVAFSPDG-KTLASGSDDGTVRLWDlATGELLRTLTGHTGAVTSVAFSP-DGRTLASGSADGTV 396
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
94-322 1.91e-26

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 108.46  E-value: 1.91e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129110  94 ILVASDSGAVELWELDENETLIVSKfckyEHDDIVSTVSVLSSGTQAVSGSKDICIKVWDLAQQVVLSSYRAHAAQVTCV 173
Cdd:COG2319 177 LASGSDDGTVRLWDLATGKLLRTLT----GHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSV 252

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129110 174 AASPhKDSVFLSCSEDNRILLWDTRCPKPASQIGcsAPGYLPTSLAWHPqQSEVFVFGDENGTVSLVDTKSTSCVLSSAV 253
Cdd:COG2319 253 AFSP-DGRLLASGSADGTVRLWDLATGELLRTLT--GHSGGVNSVAFSP-DGKLLASGSDDGTVRLWDLATGKLLRTLTG 328

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129110 254 HSQCVTGLVFSPHSvPFLASLSEDCSLAVLD-SSLSELFRSQAHRDFVRDATWSPlNHSLLTTVGWDHQV 322
Cdd:COG2319 329 HTGAVRSVAFSPDG-KTLASGSDDGTVRLWDlATGELLRTLTGHTGAVTSVAFSP-DGRTLASGSADGTV 396
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 80-319 8.50e-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: 104.34  E-value: 8.50e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129110  80 EAGVADLTWVGERGILV-ASDSGAVELWELDENETLIVSKfckyEHDDIVSTVSVLSSGTQAVSGSKDICIKVWDLAQQV 158
Cdd:cd00200   9 TGGVTCVAFSPDGKLLAtGSGDGTIKVWDLETGELLRTLK----GHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGE 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129110 159 VLSSYRAHAAQVTCVAASPHkDSVFLSCSEDNRILLWDTRCPKPASQI-GCSAPGylpTSLAWHPQQSEVFVfGDENGTV 237
Cdd:cd00200  85 CVRTLTGHTSYVSSVAFSPD-GRILSSSSRDKTIKVWDVETGKCLTTLrGHTDWV---NSVAFSPDGTFVAS-SSQDGTI 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129110 238 SLVDTKSTSCVLSSAVHSQCVTGLVFSPHSVPFLASlSEDCSLAVLDSSLSELFRS-QAHRDFVRDATWSPlNHSLLTTV 316
Cdd:cd00200 160 KLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSS-SSDGTIKLWDLSTGKCLGTlRGHENGVNSVAFSP-DGYLLASG 237


                ...
gi 13129110 317 GWD 319
Cdd:cd00200 238 SED 240
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 159-196 7.47e-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: 39.60  E-value: 7.47e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 13129110    159 VLSSYRAHAAQVTCVAASPHkDSVFLSCSEDNRILLWD 196
Cdd:smart00320   4 LLKTLKGHTGPVTSVAFSPD-GKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
160-196 3.00e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 37.71  E-value: 3.00e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 13129110   160 LSSYRAHAAQVTCVAASPHkDSVFLSCSEDNRILLWD 196
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSPD-GKLLASGSDDGTVKVWD 39
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
94-322 1.91e-26

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 108.46  E-value: 1.91e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129110  94 ILVASDSGAVELWELDENETLIVSKfckyEHDDIVSTVSVLSSGTQAVSGSKDICIKVWDLAQQVVLSSYRAHAAQVTCV 173
Cdd:COG2319 177 LASGSDDGTVRLWDLATGKLLRTLT----GHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSV 252

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129110 174 AASPhKDSVFLSCSEDNRILLWDTRCPKPASQIGcsAPGYLPTSLAWHPqQSEVFVFGDENGTVSLVDTKSTSCVLSSAV 253
Cdd:COG2319 253 AFSP-DGRLLASGSADGTVRLWDLATGELLRTLT--GHSGGVNSVAFSP-DGKLLASGSDDGTVRLWDLATGKLLRTLTG 328

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129110 254 HSQCVTGLVFSPHSvPFLASLSEDCSLAVLD-SSLSELFRSQAHRDFVRDATWSPlNHSLLTTVGWDHQV 322
Cdd:COG2319 329 HTGAVRSVAFSPDG-KTLASGSDDGTVRLWDlATGELLRTLTGHTGAVTSVAFSP-DGRTLASGSADGTV 396
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 80-319 8.50e-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: 104.34  E-value: 8.50e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129110  80 EAGVADLTWVGERGILV-ASDSGAVELWELDENETLIVSKfckyEHDDIVSTVSVLSSGTQAVSGSKDICIKVWDLAQQV 158
Cdd:cd00200   9 TGGVTCVAFSPDGKLLAtGSGDGTIKVWDLETGELLRTLK----GHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGE 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129110 159 VLSSYRAHAAQVTCVAASPHkDSVFLSCSEDNRILLWDTRCPKPASQI-GCSAPGylpTSLAWHPQQSEVFVfGDENGTV 237
Cdd:cd00200  85 CVRTLTGHTSYVSSVAFSPD-GRILSSSSRDKTIKVWDVETGKCLTTLrGHTDWV---NSVAFSPDGTFVAS-SSQDGTI 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129110 238 SLVDTKSTSCVLSSAVHSQCVTGLVFSPHSVPFLASlSEDCSLAVLDSSLSELFRS-QAHRDFVRDATWSPlNHSLLTTV 316
Cdd:cd00200 160 KLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSS-SSDGTIKLWDLSTGKCLGTlRGHENGVNSVAFSP-DGYLLASG 237


                ...
gi 13129110 317 GWD 319
Cdd:cd00200 238 SED 240
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 80-282 1.27e-22

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: 95.86  E-value: 1.27e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129110  80 EAGVADLTWVGERGILVAS-DSGAVELWELDENETLIVSKFckyeHDDIVSTVSVLSSGTQAVSGSKDICIKVWDLAQQV 158
Cdd:cd00200  93 TSYVSSVAFSPDGRILSSSsRDKTIKVWDVETGKCLTTLRG----HTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGK 168

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129110 159 VLSSYRAHAAQVTCVAASPhKDSVFLSCSEDNRILLWDTRCPKP-ASQIGCSAPgylPTSLAWHPQqSEVFVFGDENGTV 237
Cdd:cd00200 169 CVATLTGHTGEVNSVAFSP-DGEKLLSSSSDGTIKLWDLSTGKClGTLRGHENG---VNSVAFSPD-GYLLASGSEDGTI 243

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 13129110 238 SLVDTKSTSCVLSSAVHSQCVTGLVFSPHSvPFLASLSEDCSLAV 282
Cdd:cd00200 244 RVWDLRTGECVQTLSGHTNSVTSLAWSPDG-KRLASGSADGTIRI 287
WD40 COG2319
WD40 repeat [General function prediction only];
46-322 1.33e-21

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 94.59  E-value: 1.33e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129110  46 ASSLSGRCWAGSLWLFKDPCAAPNEGFCSAGVQTEAGVADLTWVGERGILVASDSGAVELWELDENETLIVSKFCkyEHD 125
Cdd:COG2319   1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLL--GHT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129110 126 DIVSTVSVLSSGTQAVSGSKDICIKVWDLAQQVVLSSYRAHAAQVTCVAASPhkDSVFL-SCSEDNRILLWDTRCPKPAS 204
Cdd:COG2319  79 AAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSP--DGKTLaSGSADGTVRLWDLATGKLLR 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129110 205 QIgcSAPGYLPTSLAWHPqQSEVFVFGDENGTVSLVDTKSTSCVLSSAVHSQCVTGLVFSPHSvPFLASLSEDCSLAVLD 284
Cdd:COG2319 157 TL--TGHSGAVTSVAFSP-DGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDG-KLLASGSADGTVRLWD 232

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 13129110 285 -SSLSELFRSQAHRDFVRDATWSPlNHSLLTTVGWDHQV 322
Cdd:COG2319 233 lATGKLLRTLTGHSGSVRSVAFSP-DGRLLASGSADGTV 270
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 122-326 1.83e-18

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 83.92  E-value: 1.83e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129110 122 YEHDDIVSTVSVLSSGTQAVSGSKDICIKVWDLAQQVVLSSYRAHAAQVTCVAASPHKDSVFlSCSEDNRILLWDTRCPK 201
Cdd:cd00200   6 KGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLA-SGSSDKTIRLWDLETGE 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129110 202 PASQIGCSAPGylPTSLAWHPqQSEVFVFGDENGTVSLVDTKSTSCVLSSAVHSQCVTGLVFSPHSvPFLASLSEDCSLA 281
Cdd:cd00200  85 CVRTLTGHTSY--VSSVAFSP-DGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDG-TFVASSSQDGTIK 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 13129110 282 VLDSSLSELFRS-QAHRDFVRDATWSPLNHSLLTTVG------WDHQVVHHV 326
Cdd:cd00200 161 LWDLRTGKCVATlTGHTGEVNSVAFSPDGEKLLSSSSdgtiklWDLSTGKCL 212
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 91-196 1.57e-13

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: 70.06  E-value: 1.57e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129110  91 ERGILVASDSGAVELWELDenetlivSKFCKYE---HDDIVSTVSVLSSGTQAVSGSKDICIKVWDLAQQVVLSSYRAHA 167
Cdd:cd00200 189 GEKLLSSSSDGTIKLWDLS-------TGKCLGTlrgHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHT 261

                        90       100
                ....*....|....*....|....*....
gi 13129110 168 AQVTCVAASPHKdSVFLSCSEDNRILLWD 196
Cdd:cd00200 262 NSVTSLAWSPDG-KRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
94-198 5.04e-13

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 69.55  E-value: 5.04e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129110  94 ILVASDSGAVELWELDENETLIVSKfckyEHDDIVSTVSVLSSGTQAVSGSKDICIKVWDLAQQVVLSSYRAHAAQVTCV 173
Cdd:COG2319 303 LASGSDDGTVRLWDLATGKLLRTLT----GHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSV 378

                        90       100
                ....*....|....*....|....*
gi 13129110 174 AASPHkDSVFLSCSEDNRILLWDTR 198
Cdd:COG2319 379 AFSPD-GRTLASGSADGTVRLWDLA 402
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 163-322 5.92e-13

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: 68.13  E-value: 5.92e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129110 163 YRAHAAQVTCVAASPHKDsVFLSCSEDNRILLWDT-RCPKPASQIGCSAPGylpTSLAWHPqQSEVFVFGDENGTVSLVD 241
Cdd:cd00200   5 LKGHTGGVTCVAFSPDGK-LLATGSGDGTIKVWDLeTGELLRTLKGHTGPV---RDVAASA-DGTYLASGSSDKTIRLWD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129110 242 TKSTSCVLSSAVHSQCVTGLVFSPHSvPFLASLSEDCSLAVLDSSLSELFRS-QAHRDFVRDATWSPlNHSLLTTVGWDH 320
Cdd:cd00200  80 LETGECVRTLTGHTSYVSSVAFSPDG-RILSSSSRDKTIKVWDVETGKCLTTlRGHTDWVNSVAFSP-DGTFVASSSQDG 157


                ..
gi 13129110 321 QV 322
Cdd:cd00200 158 TI 159
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 159-196 7.47e-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: 39.60  E-value: 7.47e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 13129110    159 VLSSYRAHAAQVTCVAASPHkDSVFLSCSEDNRILLWD 196
Cdd:smart00320   4 LLKTLKGHTGPVTSVAFSPD-GKYLASGSDDGTIKLWD 40
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
158-265 2.09e-04

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 41.99  E-value: 2.09e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129110 158 VVLSSYRAHAAQVTCVAASPHKDSVFLSCSEDNRILLWDTRCPKPASQIgcsAPGYLPTSLAWHPQQSEVFVFGDENGTV 237
Cdd:COG3391  58 AGLGLGAAAVADADGADAGADGRRLYVANSGSGRVSVIDLATGKVVATI---PVGGGPRGLAVDPDGGRLYVADSGNGRV 134

                        90       100
                ....*....|....*....|....*...
gi 13129110 238 SLVDTKSTSCVLSSAVHSQcVTGLVFSP 265
Cdd:COG3391 135 SVIDTATGKVVATIPVGAG-PHGIAVDP 161
WD40 pfam00400
WD domain, G-beta repeat;
160-196 3.00e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 37.71  E-value: 3.00e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 13129110   160 LSSYRAHAAQVTCVAASPHkDSVFLSCSEDNRILLWD 196
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSPD-GKLLASGSDDGTVKVWD 39
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
75-265 6.13e-04

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 40.83  E-value: 6.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129110  75 AGVQTEAGVADLTWVGERGILVASDSGAVELWELDENETLIVSKFCKYEHDDIVSTVSVLSSGTQAVSGSKDICIKVWDL 154
Cdd:COG3391  18 LAALAVAVAALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGRRLYVANSGSGRVSVIDL 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13129110 155 AQQVVLSSYRAhAAQVTCVAASPHKDSVFLSCSEDNRILLWDTRCPKPASQIgcsAPGYLPTSLAWHPQQSEVFVFGDEN 234
Cdd:COG3391  98 ATGKVVATIPV-GGGPRGLAVDPDGGRLYVADSGNGRVSVIDTATGKVVATI---PVGAGPHGIAVDPDGKRLYVANSGS 173

                       170       180       190
                ....*....|....*....|....*....|....*
gi 13129110 235 GTVSLV----DTKSTScVLSSAVHSQCVTGLVFSP 265
Cdd:COG3391 174 NTVSVIvsviDTATGK-VVATIPVGGGPVGVAVSP 207
WDR74 cd22857
WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and ...
 88-154 4.92e-03

WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and plants is an essential factor for ribosome assembly. In cooperation with the assembly factor NVL2, WDR74 participates in an early cleavage of the pre-rRNA processing pathway. NVL2 is a type II double ring, AAA-ATPase, that may mediate the release of WDR74 from nucleolar pre-60S particles. WDR74 has been implicated in tumorigenesis. In lung cancer, it regulates cell proliferation, cell cycle progression, chemoresistance and cell aggressiveness, by inducing nuclear beta-catenin accumulation and driving downstream Wnt-responsive genes expression. In melanoma, it promotes apoptosis resistance and aggressive behavior by regulating the RPL5-MDM2-p53 pathway. WDR74 contains an N-terminal seven-bladed beta-propeller WD40 domain that associates with the D1-AAA domain of the AAA-ATPase NVL2, and a flexible lysine-rich C-terminus that extends outward from the WD40 domain, and is required for nucleolar localization.


Pssm-ID: 439303 [Multi-domain]  Cd Length: 325  Bit Score: 38.36  E-value: 4.92e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13129110  88 WVG----ERGILVASDSGAVELWELDENETLIVSKFCKYEHDDIVSTVSVLSSGTQAVSGSKDICIKVWDL 154
Cdd:cd22857  85 FVGlhlfSGTLLTCTSKGSLRSTKLPDDSTASSSPTAWVCLGGNLLCMRVDPNENYFAFGGKEVELNVWDL 155
 
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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