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Conserved domains on  [gi|1002303601|ref|XP_015615180|]
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SEC12-like protein 2 [Oryza sativa Japonica Group]

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];
165-362 2.00e-24

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 103.84  E-value: 2.00e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002303601 165 AVSFSGEGSILATGGEDGHLRVFKWPSMDSILEEPDTKTSVKDLTFSSDEHFLAVNRSSGPCRVWDLKSAEVVANLPREA 244
Cdd:COG2319   167 SVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHS 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002303601 245 GEIFGfCRFSNqtdNSQILfVTAmqGDYGKIISWNTTSWTRIGSNKITREAISAFAVSPDCTLLAIGTIEGSIIVLSSKN 324
Cdd:COG2319   247 GSVRS-VAFSP---DGRLL-ASG--SADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLAT 319

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1002303601 325 MRSLVTVkKAHLGIITTLAFSQDSRTLLSTSFDSTARV 362
Cdd:COG2319   320 GKLLRTL-TGHTGAVRSVAFSPDGKTLASGSDDGTVRL 356
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
165-362 2.00e-24

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 103.84  E-value: 2.00e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002303601 165 AVSFSGEGSILATGGEDGHLRVFKWPSMDSILEEPDTKTSVKDLTFSSDEHFLAVNRSSGPCRVWDLKSAEVVANLPREA 244
Cdd:COG2319   167 SVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHS 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002303601 245 GEIFGfCRFSNqtdNSQILfVTAmqGDYGKIISWNTTSWTRIGSNKITREAISAFAVSPDCTLLAIGTIEGSIIVLSSKN 324
Cdd:COG2319   247 GSVRS-VAFSP---DGRLL-ASG--SADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLAT 319

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1002303601 325 MRSLVTVkKAHLGIITTLAFSQDSRTLLSTSFDSTARV 362
Cdd:COG2319   320 GKLLRTL-TGHTGAVRSVAFSPDGKTLASGSDDGTVRL 356
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 164-362 2.60e-19

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: 87.39  E-value: 2.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002303601 164 LAVSFSGEGSILATGGEDGHLRVFKWPSMDSILEEPDTKTSVKDLTFSSDEHFLAVNRSSGPCRVWDLKSAEVVANLPRE 243
Cdd:cd00200    97 SSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGH 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002303601 244 AGEIFGfCRFSnqtDNSQILFVTAmqGDyGKIISWNTTSWTRIGSNKITREAISAFAVSPDCTLLAIGTIEGSIIVLSSK 323
Cdd:cd00200   177 TGEVNS-VAFS---PDGEKLLSSS--SD-GTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLR 249

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1002303601 324 NmRSLVTVKKAHLGIITTLAFSQDSRTLLSTSFDSTARV 362
Cdd:cd00200   250 T-GECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRI 287
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 174-247 1.54e-04

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: 40.34  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002303601 174 ILATGGEDGHLRVFK------WPsmdsiLEEPDTKTSVKDLTFSSDEHFLAVNRSSGPCRVWDLKSAEVVANLPREAGEI 247
Cdd:pfam12894   9 LIALATEDGELLLHRlnwqrvWT-----LSPDKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSAGSDLI 83
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 326-362 1.62e-03

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: 36.14  E-value: 1.62e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1002303601  326 RSLVTVKKAHLGIITTLAFSQDSRTLLSTSFDSTARV 362
Cdd:smart00320   2 GELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKL 38
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
165-362 2.00e-24

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 103.84  E-value: 2.00e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002303601 165 AVSFSGEGSILATGGEDGHLRVFKWPSMDSILEEPDTKTSVKDLTFSSDEHFLAVNRSSGPCRVWDLKSAEVVANLPREA 244
Cdd:COG2319   167 SVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHS 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002303601 245 GEIFGfCRFSNqtdNSQILfVTAmqGDYGKIISWNTTSWTRIGSNKITREAISAFAVSPDCTLLAIGTIEGSIIVLSSKN 324
Cdd:COG2319   247 GSVRS-VAFSP---DGRLL-ASG--SADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLAT 319

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1002303601 325 MRSLVTVkKAHLGIITTLAFSQDSRTLLSTSFDSTARV 362
Cdd:COG2319   320 GKLLRTL-TGHTGAVRSVAFSPDGKTLASGSDDGTVRL 356
WD40 COG2319
WD40 repeat [General function prediction only];
165-362 2.91e-24

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 103.45  E-value: 2.91e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002303601 165 AVSFSGEGSILATGGEDGHLRVFKWPSMDSILEEPDTKTSVKDLTFSSDEHFLAVNRSSGPCRVWDLKSAEVVANLPREA 244
Cdd:COG2319   209 SVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHS 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002303601 245 GEIFGFCrFSnqtDNSQILFVTamqGDYGKIISWNTTSWTRIGSNKITREAISAFAVSPDCTLLAIGTIEGSIIVLSSKN 324
Cdd:COG2319   289 GGVNSVA-FS---PDGKLLASG---SDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLAT 361

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1002303601 325 MRSLVTVKkAHLGIITTLAFSQDSRTLLSTSFDSTARV 362
Cdd:COG2319   362 GELLRTLT-GHTGAVTSVAFSPDGRTLASGSADGTVRL 398
WD40 COG2319
WD40 repeat [General function prediction only];
165-369 3.12e-23

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 100.37  E-value: 3.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002303601 165 AVSFSGEGSILATGGEDGHLRVFKWPSMDSILEEPDTKTSVKDLTFSSDEHFLAVNRSSGPCRVWDLKSAEVVANLPREA 244
Cdd:COG2319   125 SVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHT 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002303601 245 GEIFGfCRFSnqtDNSQILfVTAmqGDYGKIISWNTTSWTRIGSNKITREAISAFAVSPDCTLLAIGTIEGSIIVLSSKN 324
Cdd:COG2319   205 GAVRS-VAFS---PDGKLL-ASG--SADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLAT 277

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1002303601 325 mRSLVTVKKAHLGIITTLAFSQDSRTLLSTSFDSTARVTSIGSPK 369
Cdd:COG2319   278 -GELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGK 321
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 164-362 2.60e-19

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: 87.39  E-value: 2.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002303601 164 LAVSFSGEGSILATGGEDGHLRVFKWPSMDSILEEPDTKTSVKDLTFSSDEHFLAVNRSSGPCRVWDLKSAEVVANLPRE 243
Cdd:cd00200    97 SSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGH 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002303601 244 AGEIFGfCRFSnqtDNSQILFVTAmqGDyGKIISWNTTSWTRIGSNKITREAISAFAVSPDCTLLAIGTIEGSIIVLSSK 323
Cdd:cd00200   177 TGEVNS-VAFS---PDGEKLLSSS--SD-GTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLR 249

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1002303601 324 NmRSLVTVKKAHLGIITTLAFSQDSRTLLSTSFDSTARV 362
Cdd:cd00200   250 T-GECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRI 287
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 165-362 8.21e-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: 83.15  E-value: 8.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002303601 165 AVSFSGEGSILATGGEDGHLRVFKWPSMDSILEEPDTKTSVKDLTFSSDEHFLAvnrSSGP---CRVWDLKSAEVVANLP 241
Cdd:cd00200    14 CVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLA---SGSSdktIRLWDLETGECVRTLT 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002303601 242 REAGEIFGfCRFSnqtDNSQILFVTamqGDYGKIISWNTTSwtriGSNKIT----REAISAFAVSPDCTLLAIGTIEGSI 317
Cdd:cd00200    91 GHTSYVSS-VAFS---PDGRILSSS---SRDKTIKVWDVET----GKCLTTlrghTDWVNSVAFSPDGTFVASSSQDGTI 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1002303601 318 IVLSSKNMRsLVTVKKAHLGIITTLAFSQDSRTLLSTSFDSTARV 362
Cdd:cd00200   160 KLWDLRTGK-CVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKL 203
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 204-362 3.65e-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: 51.18  E-value: 3.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002303601 204 SVKDLTFSSDEHFLAVNRSSGPCRVWDLKSAEVVANLPREAGEIfGFCRFSNQTDnsqiLFVTAmqGDYGKIISWNttsw 283
Cdd:cd00200    11 GVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPV-RDVAASADGT----YLASG--SSDKTIRLWD---- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002303601 284 trIGSNKITRE------AISAFAVSPDCTLLAIGTIEGSIIVLSSKNmRSLVTVKKAHLGIITTLAFSQDSRTLLSTSFD 357
Cdd:cd00200    80 --LETGECVRTltghtsYVSSVAFSPDGRILSSSSRDKTIKVWDVET-GKCLTTLRGHTDWVNSVAFSPDGTFVASSSQD 156


                  ....*
gi 1002303601 358 STARV 362
Cdd:cd00200   157 GTIKL 161
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 296-369 1.37e-05

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: 46.56  E-value: 1.37e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002303601 296 ISAFAVSPDCTLLAIGTIEGSIIVLSSKNMRsLVTVKKAHLGIITTLAFSQDSRTLLSTSFDSTARVTSIGSPK 369
Cdd:cd00200    12 VTCVAFSPDGKLLATGSGDGTIKVWDLETGE-LLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGE 84
WD40 COG2319
WD40 repeat [General function prediction only];
164-233 6.80e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 44.90  E-value: 6.80e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002303601 164 LAVSFSGEGSILATGGEDGHLRVFKWPSMDSILEEPDTKTSVKDLTFSSDEHFLAVNRSSGPCRVWDLKS 233
Cdd:COG2319   334 RSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 174-247 1.54e-04

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: 40.34  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002303601 174 ILATGGEDGHLRVFK------WPsmdsiLEEPDTKTSVKDLTFSSDEHFLAVNRSSGPCRVWDLKSAEVVANLPREAGEI 247
Cdd:pfam12894   9 LIALATEDGELLLHRlnwqrvWT-----LSPDKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSAGSDLI 83
WD40 pfam00400
WD domain, G-beta repeat;
326-362 1.31e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.17  E-value: 1.31e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1002303601 326 RSLVTVKKAHLGIITTLAFSQDSRTLLSTSFDSTARV 362
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKV 37
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 326-362 1.62e-03

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: 36.14  E-value: 1.62e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1002303601  326 RSLVTVKKAHLGIITTLAFSQDSRTLLSTSFDSTARV 362
Cdd:smart00320   2 GELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKL 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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