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Conserved domains on  [gi|7019503|ref|NP_037520|]
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guanine nucleotide-exchange factor SEC12 isoform 1 [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];
160-353 1.68e-14

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 74.56  E-value: 1.68e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019503  160 VCFNHDNTLLATGGTDGYVRVWKVPSLEKVLEFKAHEGEIEDLALGPDGK-LVTVGRDLKASVW--QKDQLVTQLHWQEN 236
Cdd:COG2319 210 VAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRlLASGSADGTVRLWdlATGELLRTLTGHSG 289

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019503  237 GPT---FSstpyryqacrfgqvPDqpaGLRLF------TVQIphkrlrqpppcyltaWDGSNFLPLRTKSCGHEVVSCLD 307
Cdd:COG2319 290 GVNsvaFS--------------PD---GKLLAsgsddgTVRL---------------WDLATGKLLRTLTGHTGAVRSVA 337

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 7019503  308 VSESGTFLGLGTVTGSVAIYIAFSLQCLyYVREAHGIVVTDVAFLP 353
Cdd:COG2319 338 FSPDGKTLASGSDDGTVRLWDLATGELL-RTLTGHTGAVTSVAFSP 382
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
160-353 1.68e-14

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 74.56  E-value: 1.68e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019503  160 VCFNHDNTLLATGGTDGYVRVWKVPSLEKVLEFKAHEGEIEDLALGPDGK-LVTVGRDLKASVW--QKDQLVTQLHWQEN 236
Cdd:COG2319 210 VAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRlLASGSADGTVRLWdlATGELLRTLTGHSG 289

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019503  237 GPT---FSstpyryqacrfgqvPDqpaGLRLF------TVQIphkrlrqpppcyltaWDGSNFLPLRTKSCGHEVVSCLD 307
Cdd:COG2319 290 GVNsvaFS--------------PD---GKLLAsgsddgTVRL---------------WDLATGKLLRTLTGHTGAVRSVA 337

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 7019503  308 VSESGTFLGLGTVTGSVAIYIAFSLQCLyYVREAHGIVVTDVAFLP 353
Cdd:COG2319 338 FSPDGKTLASGSDDGTVRLWDLATGELL-RTLTGHTGAVTSVAFSP 382
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 159-375 2.03e-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: 2.03e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019503  159 VVCFNHDNTLLATGGTDGYVRVWKVPSLEKVLEFKAHEGEIEDLALGPDGK-LVTVGRDLKASVWQKD------------ 225
Cdd:cd00200  14 CVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTyLASGSSDKTIRLWDLEtgecvrtltght 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019503  226 QLVTQLHWQENGPTFSSTpYRYQACRFGQVPDqpaGLRLFTVQiPHKR----LRQPPP----------CYLTAWDGSNFL 291
Cdd:cd00200  94 SYVSSVAFSPDGRILSSS-SRDKTIKVWDVET---GKCLTTLR-GHTDwvnsVAFSPDgtfvasssqdGTIKLWDLRTGK 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019503  292 PLRTKScGHE-VVSCLDVSESGTFLGLGTVTGSVAIYIAFSLQCLyYVREAHGIVVTDVAFLP----------------- 353
Cdd:cd00200 169 CVATLT-GHTgEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCL-GTLRGHENGVNSVAFSPdgyllasgsedgtirvw 246

                       250       260
                ....*....|....*....|....
gi 7019503  354 --EKGRGPELLGSHETALFSVAVD 375
Cdd:cd00200 247 dlRTGECVQTLSGHTNSVTSLAWS 270
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 160-182 2.12e-04

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 38.45  E-value: 2.12e-04
                           10        20
                   ....*....|....*....|...
gi 7019503     160 VCFNHDNTLLATGGTDGYVRVWK 182
Cdd:smart00320  18 VAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
160-181 1.68e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 35.78  E-value: 1.68e-03
                          10        20
                  ....*....|....*....|..
gi 7019503    160 VCFNHDNTLLATGGTDGYVRVW 181
Cdd:pfam00400  17 LAFSPDGKLLASGSDDGTVKVW 38
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
160-353 1.68e-14

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 74.56  E-value: 1.68e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019503  160 VCFNHDNTLLATGGTDGYVRVWKVPSLEKVLEFKAHEGEIEDLALGPDGK-LVTVGRDLKASVW--QKDQLVTQLHWQEN 236
Cdd:COG2319 210 VAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRlLASGSADGTVRLWdlATGELLRTLTGHSG 289

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019503  237 GPT---FSstpyryqacrfgqvPDqpaGLRLF------TVQIphkrlrqpppcyltaWDGSNFLPLRTKSCGHEVVSCLD 307
Cdd:COG2319 290 GVNsvaFS--------------PD---GKLLAsgsddgTVRL---------------WDLATGKLLRTLTGHTGAVRSVA 337

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 7019503  308 VSESGTFLGLGTVTGSVAIYIAFSLQCLyYVREAHGIVVTDVAFLP 353
Cdd:COG2319 338 FSPDGKTLASGSDDGTVRLWDLATGELL-RTLTGHTGAVTSVAFSP 382
WD40 COG2319
WD40 repeat [General function prediction only];
160-353 7.89e-13

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 69.55  E-value: 7.89e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019503  160 VCFNHDNTLLATGGTDGYVRVWKVPSLEKVLEFKAHEGEIEDLALGPDGK-LVTVGRDLKASVW--QKDQLVTQLHWQEN 236
Cdd:COG2319 168 VAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKlLASGSADGTVRLWdlATGKLLRTLTGHSG 247

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019503  237 GPT---FSstpyryqacrfgqvPDqpaGLRLF------TVQIphkrlrqpppcyltaWDGSNFLPLRTKSCGHEVVSCLD 307
Cdd:COG2319 248 SVRsvaFS--------------PD---GRLLAsgsadgTVRL---------------WDLATGELLRTLTGHSGGVNSVA 295

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 7019503  308 VSESGTFLGLGTVTGSVAIYIAFSLQCLyYVREAHGIVVTDVAFLP 353
Cdd:COG2319 296 FSPDGKLLASGSDDGTVRLWDLATGKLL-RTLTGHTGAVRSVAFSP 340
WD40 COG2319
WD40 repeat [General function prediction only];
160-353 6.60e-12

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 66.86  E-value: 6.60e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019503  160 VCFNHDNTLLATGGTDGYVRVWKVPSLEKVLEFKAHEGEIEDLALGPDGK-LVTVGRDLKASVW--QKDQLVTQLHWQEN 236
Cdd:COG2319 126 VAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKlLASGSDDGTVRLWdlATGKLLRTLTGHTG 205

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019503  237 GPT---FSstpyryqacrfgqvPDqpaGLRLF------TVQIphkrlrqpppcyltaWDGSNFLPLRTKSCGHEVVSCLD 307
Cdd:COG2319 206 AVRsvaFS--------------PD---GKLLAsgsadgTVRL---------------WDLATGKLLRTLTGHSGSVRSVA 253

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 7019503  308 VSESGTFLGLGTVTGSVAIYIAFSLQCLyYVREAHGIVVTDVAFLP 353
Cdd:COG2319 254 FSPDGRLLASGSADGTVRLWDLATGELL-RTLTGHSGGVNSVAFSP 298
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 159-375 2.03e-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: 2.03e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019503  159 VVCFNHDNTLLATGGTDGYVRVWKVPSLEKVLEFKAHEGEIEDLALGPDGK-LVTVGRDLKASVWQKD------------ 225
Cdd:cd00200  14 CVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTyLASGSSDKTIRLWDLEtgecvrtltght 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019503  226 QLVTQLHWQENGPTFSSTpYRYQACRFGQVPDqpaGLRLFTVQiPHKR----LRQPPP----------CYLTAWDGSNFL 291
Cdd:cd00200  94 SYVSSVAFSPDGRILSSS-SRDKTIKVWDVET---GKCLTTLR-GHTDwvnsVAFSPDgtfvasssqdGTIKLWDLRTGK 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019503  292 PLRTKScGHE-VVSCLDVSESGTFLGLGTVTGSVAIYIAFSLQCLyYVREAHGIVVTDVAFLP----------------- 353
Cdd:cd00200 169 CVATLT-GHTgEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCL-GTLRGHENGVNSVAFSPdgyllasgsedgtirvw 246

                       250       260
                ....*....|....*....|....
gi 7019503  354 --EKGRGPELLGSHETALFSVAVD 375
Cdd:cd00200 247 dlRTGECVQTLSGHTNSVTSLAWS 270
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 158-323 2.51e-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: 63.89  E-value: 2.51e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019503  158 KVVCFNHDNTLLATGGTDGYVRVWKVPSLEKVLEFKAHEGEIEDLALGPDG-KLVTVGRDLKASVW--QKDQLVTQLHWQ 234
Cdd:cd00200 139 NSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGeKLLSSSSDGTIKLWdlSTGKCLGTLRGH 218

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019503  235 ENGPTfsstpyryqACRFGqvPDQpaglRLFTVQIPHKRLRQpppcyltaWDGSNFLPLRTKScGHEV-VSCLDVSESGT 313
Cdd:cd00200 219 ENGVN---------SVAFS--PDG----YLLASGSEDGTIRV--------WDLRTGECVQTLS-GHTNsVTSLAWSPDGK 274

                       170
                ....*....|
gi 7019503  314 FLglgtVTGS 323
Cdd:cd00200 275 RL----ASGS 280
WD40 COG2319
WD40 repeat [General function prediction only];
160-223 1.25e-10

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 62.62  E-value: 1.25e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7019503  160 VCFNHDNTLLATGGTDGYVRVWKVPSLEKVLEFKAHEGEIEDLALGPDGK-LVTVGRDLKASVWQ 223
Cdd:COG2319 336 VAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRtLASGSADGTVRLWD 400
WD40 COG2319
WD40 repeat [General function prediction only];
139-353 3.18e-09

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 58.38  E-value: 3.18e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019503  139 LRVENLQAVQTDFSSDPLQKVVCFNHDNTLLATGGTDGYVRVWKVPSLEKVLEFKAHEGEIEDLALGPDGK-LVTVGRDL 217
Cdd:COG2319  63 LDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKtLASGSADG 142

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019503  218 KASVW--QKDQLVTQLHWQENGPT---FSstpyryqacrfgqvPDqpaGLRLF------TVQIphkrlrqpppcyltaWD 286
Cdd:COG2319 143 TVRLWdlATGKLLRTLTGHSGAVTsvaFS--------------PD---GKLLAsgsddgTVRL---------------WD 190

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7019503  287 GSNFLPLRTKSCGHEVVSCLDVSESGTFLGLGTVTGSVAIYIAFSLQCLyYVREAHGIVVTDVAFLP 353
Cdd:COG2319 191 LATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLL-RTLTGHSGSVRSVAFSP 256
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 160-357 6.05e-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: 56.96  E-value: 6.05e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019503  160 VCFNHDNTLLATGGTDGYVRVWKVPSLEKVLEFKAHEGEIEDLALGPDGKLVTVG-RDLKASVW--QKDQLVTQLHwQEN 236
Cdd:cd00200  99 VAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSsQDGTIKLWdlRTGKCVATLT-GHT 177

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019503  237 GPTFSSTPYryqacrfgqvpdqPAGLRLFTV----QIphkRLrqpppcyltaWDgsnflpLRTKSC-----GHEV-VSCL 306
Cdd:cd00200 178 GEVNSVAFS-------------PDGEKLLSSssdgTI---KL----------WD------LSTGKClgtlrGHENgVNSV 225

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 7019503  307 DVSESGTFLGLGTVTGSVAIYIAFSLQCLyYVREAHGIVVTDVAFLPEKGR 357
Cdd:cd00200 226 AFSPDGYLLASGSEDGTIRVWDLRTGECV-QTLSGHTNSVTSLAWSPDGKR 275
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 160-223 6.63e-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: 53.49  E-value: 6.63e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7019503  160 VCFNHDNTLLATGGTDGYVRVWKVPSLEKVLEFKAHEGEIEDLALGPDGK-LVTVGRDLKASVWQ 223
Cdd:cd00200 225 VAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKrLASGSADGTIRIWD 289
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 160-182 2.12e-04

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 38.45  E-value: 2.12e-04
                           10        20
                   ....*....|....*....|...
gi 7019503     160 VCFNHDNTLLATGGTDGYVRVWK 182
Cdd:smart00320  18 VAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
160-181 1.68e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 35.78  E-value: 1.68e-03
                          10        20
                  ....*....|....*....|..
gi 7019503    160 VCFNHDNTLLATGGTDGYVRVW 181
Cdd:pfam00400  17 LAFSPDGKLLASGSDDGTVKVW 38
 
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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