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Conserved domains on  [gi|21312212|ref|NP_082610|]
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nucleoporin Nup37 [Mus musculus]

Protein Classification

WD40 repeat domain-containing protein( domain architecture ID 1000017)

WD40 repeat domain-containing protein folds into a beta-propeller structure and functions as a scaffold, providing a platform for the interaction and assembly of several proteins into a signalosome; similar to 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

CATH:  2.130.10.10
Gene Ontology:  GO:0005515
PubMed:  10322433|8090199|30069656|29026209
SCOP:  4002744

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 64-260 2.10e-17

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


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 80.84  E-value: 2.10e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312212  64 KTLRTFH-HGVRVDGIAWSPETKLdslppvikFCTSAADLKIRLFtsDLQDKNEYKVLEGHSDFINDLVFHPkEGQELAS 142
Cdd:cd00200  84 ECVRTLTgHTSYVSSVAFSPDGRI--------LSSSSRDKTIKVW--DVETGKCLTTLRGHTDWVNSVAFSP-DGTFVAS 152

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312212 143 VSDDHTCRIWNLEGKQTAHFLLH--SPGMSVCWHPEEtFKLMVAEKNGTIRFYDLMAQQAILSLQSEQTPLMSAHWCLKN 220
Cdd:cd00200 153 SSQDGTIKLWDLRTGKCVATLTGhtGEVNSVAFSPDG-EKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDG 231

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 21312212 221 TFKVGAVAGNDWIIWDiTRSSYPQETRPVHMDRAHLFRWS 260
Cdd:cd00200 232 YLLASGSEDGTIRVWD-LRTGECVQTLSGHTNSVTSLAWS 270
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 64-260 2.10e-17

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: 80.84  E-value: 2.10e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312212  64 KTLRTFH-HGVRVDGIAWSPETKLdslppvikFCTSAADLKIRLFtsDLQDKNEYKVLEGHSDFINDLVFHPkEGQELAS 142
Cdd:cd00200  84 ECVRTLTgHTSYVSSVAFSPDGRI--------LSSSSRDKTIKVW--DVETGKCLTTLRGHTDWVNSVAFSP-DGTFVAS 152

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312212 143 VSDDHTCRIWNLEGKQTAHFLLH--SPGMSVCWHPEEtFKLMVAEKNGTIRFYDLMAQQAILSLQSEQTPLMSAHWCLKN 220
Cdd:cd00200 153 SSQDGTIKLWDLRTGKCVATLTGhtGEVNSVAFSPDG-EKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDG 231

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 21312212 221 TFKVGAVAGNDWIIWDiTRSSYPQETRPVHMDRAHLFRWS 260
Cdd:cd00200 232 YLLASGSEDGTIRVWD-LRTGECVQTLSGHTNSVTSLAWS 270
WD40 COG2319
WD40 repeat [General function prediction only];
64-216 6.38e-17

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 80.73  E-value: 6.38e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312212  64 KTLRTF-HHGVRVDGIAWSPETKLdslppvikFCTSAADLKIRLFtsDLQDKNEYKVLEGHSDFINDLVFHPKeGQELAS 142
Cdd:COG2319 195 KLLRTLtGHTGAVRSVAFSPDGKL--------LASGSADGTVRLW--DLATGKLLRTLTGHSGSVRSVAFSPD-GRLLAS 263

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21312212 143 VSDDHTCRIWNLEGKQTAHFLLHSPG--MSVCWHPEETFkLMVAEKNGTIRFYDLMAQQAILSLQSEQTPLMSAHW 216
Cdd:COG2319 264 GSADGTVRLWDLATGELLRTLTGHSGgvNSVAFSPDGKL-LASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAF 338
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 113-153 2.11e-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: 43.84  E-value: 2.11e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 21312212    113 DKNEYKVLEGHSDFINDLVFHPkEGQELASVSDDHTCRIWN 153
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSP-DGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
118-153 6.58e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 42.33  E-value: 6.58e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 21312212   118 KVLEGHSDFINDLVFHPkEGQELASVSDDHTCRIWN 153
Cdd:pfam00400   5 KTLEGHTGSVTSLAFSP-DGKLLASGSDDGTVKVWD 39
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 64-260 2.10e-17

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: 80.84  E-value: 2.10e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312212  64 KTLRTFH-HGVRVDGIAWSPETKLdslppvikFCTSAADLKIRLFtsDLQDKNEYKVLEGHSDFINDLVFHPkEGQELAS 142
Cdd:cd00200  84 ECVRTLTgHTSYVSSVAFSPDGRI--------LSSSSRDKTIKVW--DVETGKCLTTLRGHTDWVNSVAFSP-DGTFVAS 152

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312212 143 VSDDHTCRIWNLEGKQTAHFLLH--SPGMSVCWHPEEtFKLMVAEKNGTIRFYDLMAQQAILSLQSEQTPLMSAHWCLKN 220
Cdd:cd00200 153 SSQDGTIKLWDLRTGKCVATLTGhtGEVNSVAFSPDG-EKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDG 231

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 21312212 221 TFKVGAVAGNDWIIWDiTRSSYPQETRPVHMDRAHLFRWS 260
Cdd:cd00200 232 YLLASGSEDGTIRVWD-LRTGECVQTLSGHTNSVTSLAWS 270
WD40 COG2319
WD40 repeat [General function prediction only];
64-216 6.38e-17

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 80.73  E-value: 6.38e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312212  64 KTLRTF-HHGVRVDGIAWSPETKLdslppvikFCTSAADLKIRLFtsDLQDKNEYKVLEGHSDFINDLVFHPKeGQELAS 142
Cdd:COG2319 195 KLLRTLtGHTGAVRSVAFSPDGKL--------LASGSADGTVRLW--DLATGKLLRTLTGHSGSVRSVAFSPD-GRLLAS 263

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21312212 143 VSDDHTCRIWNLEGKQTAHFLLHSPG--MSVCWHPEETFkLMVAEKNGTIRFYDLMAQQAILSLQSEQTPLMSAHW 216
Cdd:COG2319 264 GSADGTVRLWDLATGELLRTLTGHSGgvNSVAFSPDGKL-LASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAF 338
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 71-322 3.13e-16

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 77.38  E-value: 3.13e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312212  71 HGVRVDGIAWSPETKLdslppvikFCTSAADLKIRLFtsDLQDKNEYKVLEGHSDFINDLVFHPKeGQELASVSDDHTCR 150
Cdd:cd00200   8 HTGGVTCVAFSPDGKL--------LATGSGDGTIKVW--DLETGELLRTLKGHTGPVRDVAASAD-GTYLASGSSDKTIR 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312212 151 IWNLEGKQTAH-FLLH-SPGMSVCWHPEETFkLMVAEKNGTIRFYDLMAQQAILSLQSEQTPLMSAHWCLKNTFKVGAVA 228
Cdd:cd00200  77 LWDLETGECVRtLTGHtSYVSSVAFSPDGRI-LSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQ 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312212 229 GNDWIIWDItRSSYPQETRPVHMDRAHLFRWSAISENLFATTG------YpgKMASQFQIHHL-GHSQPVLigSVAVGSG 301
Cdd:cd00200 156 DGTIKLWDL-RTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSdgtiklW--DLSTGKCLGTLrGHENGVN--SVAFSPD 230

                       250       260
                ....*....|....*....|.
gi 21312212 302 LSWhrtlpLCAVGGDHKLLFW 322
Cdd:cd00200 231 GYL-----LASGSEDGTIRVW 246
WD40 COG2319
WD40 repeat [General function prediction only];
64-297 5.86e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 78.03  E-value: 5.86e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312212  64 KTLRTF-HHGVRVDGIAWSPETKLdslppVIkfcTSAADLKIRLFtsDLQDKNEYKVLEGHSDFINDLVFHPkEGQELAS 142
Cdd:COG2319 153 KLLRTLtGHSGAVTSVAFSPDGKL-----LA---SGSDDGTVRLW--DLATGKLLRTLTGHTGAVRSVAFSP-DGKLLAS 221

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312212 143 VSDDHTCRIWNLEGKQTAHFLLHSPGM--SVCWHPEETFkLMVAEKNGTIRFYDLMAQQAILSLQSEQTPLMSAHWCLKN 220
Cdd:COG2319 222 GSADGTVRLWDLATGKLLRTLTGHSGSvrSVAFSPDGRL-LASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDG 300

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312212 221 TFKVGAVAGNDWIIWDItrssypQETRPVHMDRAHLFRWSAIS----ENLFATTGYPGK-----MASQFQIHHL-GHSQP 290
Cdd:COG2319 301 KLLASGSDDGTVRLWDL------ATGKLLRTLTGHTGAVRSVAfspdGKTLASGSDDGTvrlwdLATGELLRTLtGHTGA 374


                ....*..
gi 21312212 291 VLigSVA 297
Cdd:COG2319 375 VT--SVA 379
WD40 COG2319
WD40 repeat [General function prediction only];
64-195 4.46e-15

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 75.33  E-value: 4.46e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312212  64 KTLRTF-HHGVRVDGIAWSPETKLdslppvikFCTSAADLKIRLFtsDLQDKNEYKVLEGHSDFINDLVFHPKeGQELAS 142
Cdd:COG2319 279 ELLRTLtGHSGGVNSVAFSPDGKL--------LASGSDDGTVRLW--DLATGKLLRTLTGHTGAVRSVAFSPD-GKTLAS 347

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21312212 143 VSDDHTCRIWNLEGKQTAHFLL-HSPG-MSVCWHPEETFkLMVAEKNGTIRFYDL 195
Cdd:COG2319 348 GSDDGTVRLWDLATGELLRTLTgHTGAvTSVAFSPDGRT-LASGSADGTVRLWDL 401
WD40 COG2319
WD40 repeat [General function prediction only];
71-238 2.65e-13

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 69.94  E-value: 2.65e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312212  71 HGVRVDGIAWSPETKLDSlppvikfcTSAADLKIRLFtsDLQDKNEYKVLEGHSDFINDLVFHPkEGQELASVSDDHTCR 150
Cdd:COG2319  77 HTAAVLSVAFSPDGRLLA--------SASADGTVRLW--DLATGLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGTVR 145

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312212 151 IWNLE-GKQTAHFLLHSPGM-SVCWHPEETFkLMVAEKNGTIRFYDLMAQQAILSLQSEQTPLMSAHWCLKNTFKVGAVA 228
Cdd:COG2319 146 LWDLAtGKLLRTLTGHSGAVtSVAFSPDGKL-LASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSA 224

                       170
                ....*....|
gi 21312212 229 GNDWIIWDIT 238
Cdd:COG2319 225 DGTVRLWDLA 234
WD40 COG2319
WD40 repeat [General function prediction only];
64-156 2.96e-11

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 63.78  E-value: 2.96e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312212  64 KTLRTF-HHGVRVDGIAWSPETKLdslppvikFCTSAADLKIRLFtsDLQDKNEYKVLEGHSDFINDLVFHPkEGQELAS 142
Cdd:COG2319 321 KLLRTLtGHTGAVRSVAFSPDGKT--------LASGSDDGTVRLW--DLATGELLRTLTGHTGAVTSVAFSP-DGRTLAS 389

                        90
                ....*....|....
gi 21312212 143 VSDDHTCRIWNLEG 156
Cdd:COG2319 390 GSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 59-153 7.05e-09

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: 55.80  E-value: 7.05e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312212  59 EGIQYKTLRTfhHGVRVDGIAWSPETKLdslppvikFCTSAADLKIRLFtsDLQDKNEYKVLEGHSDFINDLVFHPkEGQ 138
Cdd:cd00200 208 TGKCLGTLRG--HENGVNSVAFSPDGYL--------LASGSEDGTIRVW--DLRTGECVQTLSGHTNSVTSLAWSP-DGK 274

                        90
                ....*....|....*
gi 21312212 139 ELASVSDDHTCRIWN 153
Cdd:cd00200 275 RLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 116-322 2.05e-08

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: 54.65  E-value: 2.05e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312212 116 EYKVLEGHSDFINDLVFHPkEGQELASVSDDHTCRIWNLEGKQTAHFL-LHSPGMSVC-WHPEETFkLMVAEKNGTIRFY 193
Cdd:cd00200   1 LRRTLKGHTGGVTCVAFSP-DGKLLATGSGDGTIKVWDLETGELLRTLkGHTGPVRDVaASADGTY-LASGSSDKTIRLW 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312212 194 DLMAQQAILSLQSEQTPLMSAHWCLKNTFKVGAVAGNDWIIWDItRSSYPQETRPVHMDRAHLFRWSaiSENLFATTGYP 273
Cdd:cd00200  79 DLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDV-ETGKCLTTLRGHTDWVNSVAFS--PDGTFVASSSQ 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21312212 274 GKMASQFQIH-------HLGHSQPVligsvavgSGLSWHRTL-PLCAVGGDHKLLFW 322
Cdd:cd00200 156 DGTIKLWDLRtgkcvatLTGHTGEV--------NSVAFSPDGeKLLSSSSDGTIKLW 204
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 113-153 2.11e-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: 43.84  E-value: 2.11e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 21312212    113 DKNEYKVLEGHSDFINDLVFHPkEGQELASVSDDHTCRIWN 153
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSP-DGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
118-153 6.58e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 42.33  E-value: 6.58e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 21312212   118 KVLEGHSDFINDLVFHPkEGQELASVSDDHTCRIWN 153
Cdd:pfam00400   5 KTLEGHTGSVTSLAFSP-DGKLLASGSDDGTVKVWD 39
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 170-217 6.22e-03

Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC,


Pssm-ID: 403945 [Multi-domain]  Cd Length: 91  Bit Score: 35.33  E-value: 6.22e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 21312212   170 SVCWHPEETFkLMVAEKNGTIRFYDLMAQQAILSLQSEQTPLMSAHWC 217
Cdd:pfam12894  43 SLAWRPDGKL-LAVGYSDGTVRLLDAENGKIVHHFSAGSDLITCLGWG 89
 
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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