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Conserved domains on  [gi|1622854296|ref|XP_028687292|]
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prolactin regulatory element-binding protein isoform X1 [Macaca mulatta]

Protein Classification

WD40 repeat domain-containing protein( domain architecture ID 13234759)

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 COG2319
WD40 repeat [General function prediction only];
162-243 4.93e-12

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 66.47  E-value: 4.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854296 162 VCFNHDNTLLATGGTDGYVRVWKVPSLEKVLEFKAHEGEIEDLALGPDGK-LVTVGRDLKASVW--QKNQLVTQLHWQEN 238
Cdd:COG2319   210 VAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRlLASGSADGTVRLWdlATGELLRTLTGHSG 289


                  ....*...
gi 1622854296 239 GPT---FS 243
Cdd:COG2319   290 GVNsvaFS 297
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 161-347 2.13e-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.


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 57.73  E-value: 2.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854296 161 VVCFNHDNTLLATGGTDGYVRVWKVPSLEKVLEFKAHEGEIEDLALGPDGK-LVTVGRDLKASVWQKN------------ 227
Cdd:cd00200    14 CVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTyLASGSSDKTIRLWDLEtgecvrtltght 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854296 228 QLVTQLHWQENGPTFSSTpYRYQACRFGQVPDqpaGLRLFTVQiPHKR----LRQPPP----------CYLTAWDGSNFL 293
Cdd:cd00200    94 SYVSSVAFSPDGRILSSS-SRDKTIKVWDVET---GKCLTTLR-GHTDwvnsVAFSPDgtfvasssqdGTIKLWDLRTGK 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622854296 294 PLRTKScGHE-VISCLNVSESGTFLGLGTVTGSVAIY--------------------IAFSLQGVFLCGS---CSCYV 347
Cdd:cd00200   169 CVATLT-GHTgEVNSVAFSPDGEKLLSSSSDGTIKLWdlstgkclgtlrghengvnsVAFSPDGYLLASGsedGTIRV 245
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
162-243 4.93e-12

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 66.47  E-value: 4.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854296 162 VCFNHDNTLLATGGTDGYVRVWKVPSLEKVLEFKAHEGEIEDLALGPDGK-LVTVGRDLKASVW--QKNQLVTQLHWQEN 238
Cdd:COG2319   210 VAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRlLASGSADGTVRLWdlATGELLRTLTGHSG 289


                  ....*...
gi 1622854296 239 GPT---FS 243
Cdd:COG2319   290 GVNsvaFS 297
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 160-224 6.15e-10

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 59.27  E-value: 6.15e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622854296 160 KVVCFNHDNTLLATGGTDGYVRVWKVPSLEKVLEFKAHEGEIEDLALGPDG-KLVTVGRDLKASVW 224
Cdd:cd00200   139 NSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGeKLLSSSSDGTIKLW 204
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 161-347 2.13e-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: 57.73  E-value: 2.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854296 161 VVCFNHDNTLLATGGTDGYVRVWKVPSLEKVLEFKAHEGEIEDLALGPDGK-LVTVGRDLKASVWQKN------------ 227
Cdd:cd00200    14 CVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTyLASGSSDKTIRLWDLEtgecvrtltght 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854296 228 QLVTQLHWQENGPTFSSTpYRYQACRFGQVPDqpaGLRLFTVQiPHKR----LRQPPP----------CYLTAWDGSNFL 293
Cdd:cd00200    94 SYVSSVAFSPDGRILSSS-SRDKTIKVWDVET---GKCLTTLR-GHTDwvnsVAFSPDgtfvasssqdGTIKLWDLRTGK 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622854296 294 PLRTKScGHE-VISCLNVSESGTFLGLGTVTGSVAIY--------------------IAFSLQGVFLCGS---CSCYV 347
Cdd:cd00200   169 CVATLT-GHTgEVNSVAFSPDGEKLLSSSSDGTIKLWdlstgkclgtlrghengvnsVAFSPDGYLLASGsedGTIRV 245
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 162-184 1.79e-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: 1.79e-04
                           10        20
                   ....*....|....*....|...
gi 1622854296  162 VCFNHDNTLLATGGTDGYVRVWK 184
Cdd:smart00320  18 VAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
162-183 1.25e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.17  E-value: 1.25e-03
                          10        20
                  ....*....|....*....|..
gi 1622854296 162 VCFNHDNTLLATGGTDGYVRVW 183
Cdd:pfam00400  17 LAFSPDGKLLASGSDDGTVKVW 38
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
162-243 4.93e-12

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 66.47  E-value: 4.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854296 162 VCFNHDNTLLATGGTDGYVRVWKVPSLEKVLEFKAHEGEIEDLALGPDGK-LVTVGRDLKASVW--QKNQLVTQLHWQEN 238
Cdd:COG2319   210 VAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRlLASGSADGTVRLWdlATGELLRTLTGHSG 289


                  ....*...
gi 1622854296 239 GPT---FS 243
Cdd:COG2319   290 GVNsvaFS 297
WD40 COG2319
WD40 repeat [General function prediction only];
162-243 8.21e-12

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 65.70  E-value: 8.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854296 162 VCFNHDNTLLATGGTDGYVRVWKVPSLEKVLEFKAHEGEIEDLALGPDGK-LVTVGRDLKASVW--QKNQLVTQLHWQEN 238
Cdd:COG2319   168 VAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKlLASGSADGTVRLWdlATGKLLRTLTGHSG 247


                  ....*...
gi 1622854296 239 GPT---FS 243
Cdd:COG2319   248 SVRsvaFS 255
WD40 COG2319
WD40 repeat [General function prediction only];
162-224 3.32e-11

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 63.78  E-value: 3.32e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622854296 162 VCFNHDNTLLATGGTDGYVRVWKVPSLEKVLEFKAHEGEIEDLALGPDGK-LVTVGRDLKASVW 224
Cdd:COG2319   126 VAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKlLASGSDDGTVRLW 189
WD40 COG2319
WD40 repeat [General function prediction only];
162-225 4.09e-11

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 63.78  E-value: 4.09e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622854296 162 VCFNHDNTLLATGGTDGYVRVWKVPSLEKVLEFKAHEGEIEDLALGPDGK-LVTVGRDLKASVWQ 225
Cdd:COG2319   336 VAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRtLASGSADGTVRLWD 400
WD40 COG2319
WD40 repeat [General function prediction only];
162-224 2.08e-10

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 61.47  E-value: 2.08e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622854296 162 VCFNHDNTLLATGGTDGYVRVWKVPSLEKVLEFKAHEGEIEDLALGPDGK-LVTVGRDLKASVW 224
Cdd:COG2319   252 VAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKlLASGSDDGTVRLW 315
WD40 COG2319
WD40 repeat [General function prediction only];
162-224 3.12e-10

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 61.08  E-value: 3.12e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622854296 162 VCFNHDNTLLATGGTDGYVRVWKVPSLEKVLEFKAHEGEIEDLALGPDGK-LVTVGRDLKASVW 224
Cdd:COG2319   294 VAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKtLASGSDDGTVRLW 357
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 160-224 6.15e-10

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 59.27  E-value: 6.15e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622854296 160 KVVCFNHDNTLLATGGTDGYVRVWKVPSLEKVLEFKAHEGEIEDLALGPDG-KLVTVGRDLKASVW 224
Cdd:cd00200   139 NSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGeKLLSSSSDGTIKLW 204
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 161-347 2.13e-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: 57.73  E-value: 2.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854296 161 VVCFNHDNTLLATGGTDGYVRVWKVPSLEKVLEFKAHEGEIEDLALGPDGK-LVTVGRDLKASVWQKN------------ 227
Cdd:cd00200    14 CVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTyLASGSSDKTIRLWDLEtgecvrtltght 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854296 228 QLVTQLHWQENGPTFSSTpYRYQACRFGQVPDqpaGLRLFTVQiPHKR----LRQPPP----------CYLTAWDGSNFL 293
Cdd:cd00200    94 SYVSSVAFSPDGRILSSS-SRDKTIKVWDVET---GKCLTTLR-GHTDwvnsVAFSPDgtfvasssqdGTIKLWDLRTGK 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622854296 294 PLRTKScGHE-VISCLNVSESGTFLGLGTVTGSVAIY--------------------IAFSLQGVFLCGS---CSCYV 347
Cdd:cd00200   169 CVATLT-GHTgEVNSVAFSPDGEKLLSSSSDGTIKLWdlstgkclgtlrghengvnsVAFSPDGYLLASGsedGTIRV 245
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 162-225 4.43e-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: 53.88  E-value: 4.43e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622854296 162 VCFNHDNTLLATGGTDGYVRVWKVPSLEKVLEFKAHEGEIEDLALGPDGK-LVTVGRDLKASVWQ 225
Cdd:cd00200   225 VAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKrLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 162-245 2.05e-07

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: 51.57  E-value: 2.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854296 162 VCFNHDNTLLATGGTDGYVRVWKVPSLEKVLEFKAHEGEIEDLALGPDGKLVTVG-RDLKASVWQK------------NQ 228
Cdd:cd00200   183 VAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGsEDGTIRVWDLrtgecvqtlsghTN 262

                          90
                  ....*....|....*..
gi 1622854296 229 LVTQLHWQENGPTFSST 245
Cdd:cd00200   263 SVTSLAWSPDGKRLASG 279
WD40 COG2319
WD40 repeat [General function prediction only];
141-329 3.07e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 51.84  E-value: 3.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854296 141 LRVENLQAVQTDFSSDPLQKVVCFNHDNTLLATGGTDGYVRVWKVPSLEKVLEFKAHEGEIEDLALGPDGK-LVTVGRDL 219
Cdd:COG2319    63 LDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKtLASGSADG 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854296 220 KASVW--QKNQLVTQLHWQENGPT---FSstpyryqacrfgqvPDqpaGLRLF------TVQIphkrlrqpppcyltaWD 288
Cdd:COG2319   143 TVRLWdlATGKLLRTLTGHSGAVTsvaFS--------------PD---GKLLAsgsddgTVRL---------------WD 190

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1622854296 289 GSNFLPLRTKSCGHEVISCLNVSESGTFLGLGTVTGSVAIY 329
Cdd:COG2319   191 LATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLW 231
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 162-184 1.79e-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: 1.79e-04
                           10        20
                   ....*....|....*....|...
gi 1622854296  162 VCFNHDNTLLATGGTDGYVRVWK 184
Cdd:smart00320  18 VAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
162-183 1.25e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.17  E-value: 1.25e-03
                          10        20
                  ....*....|....*....|..
gi 1622854296 162 VCFNHDNTLLATGGTDGYVRVW 183
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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