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Conserved domains on  [gi|334185156|ref|NP_001189833|]
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Transducin/WD40 repeat-like superfamily protein [Arabidopsis thaliana]

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 ...
 918-1054 9.06e-14

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: 73.52  E-value: 9.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185156  918 IYNFSSGKGIHKLVNFSEGVReslrrlsHVTWMADELHkatyYLFSKSDQRISCVHTQTVEMHQSGSG---AVTALIYH- 993
Cdd:cd00200   161 LWDLRTGKCVATLTGHTGEVN-------SVAFSPDGEK----LLSSSSDGTIKLWDLSTGKCLGTLRGhenGVNSVAFSp 229

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334185156  994 -KGLLFSGFSDGSIRVWNVNKKiaTLLWDIKEHKSTVTCFSLSETGECVLSGSADKTIRVWQ 1054
Cdd:cd00200   230 dGYLLASGSEDGTIRVWDLRTG--ECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
cytochrome_P450 super family cl41757
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
 444-535 2.94e-03

cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs with > 40% sequence identity are members of the same family. There are approximately 2250 CYP families: mammals, insects, plants, fungi, bacteria, and archaea have around 18, 208, 277, 805, 591, and 14 families, respectively. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop. Their monooxygenase activity relies on the reductive scission of molecular oxygen bound to the P450 heme iron, and the delivery of two electrons to the heme iron during the catalytic cycle. CYPs use a variety of redox partners, such as the eukaryotic diflavin enzyme NADPH-cytochrome P450 oxidoreductase and the bacterial/mitochondrial NAD(P)H-ferredoxin reductase and ferredoxin partners. Some CYPs are naturally linked to their redox partners and others have evolved to bypass requirements for redox partners, and instead react directly with hydrogen peroxide or NAD(P)H to facilitate oxidative or reductive catalysis.


The actual alignment was detected with superfamily member PLN02774:

Pssm-ID: 477761 [Multi-domain]  Cd Length: 463  Bit Score: 41.68  E-value: 2.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185156  444 NLQSLIKEVLGNADEKYVSEVTMIYQMLnRKEGFKYSMLKDVILDQLFTAISSSEEkTVIKASMTALtKIISVNRTALEE 523
Cdd:PLN02774  224 NIVRMLRQLIQERRASGETHTDMLGYLM-RKEGNRYKLTDEEIIDQIITILYSGYE-TVSTTSMMAV-KYLHDHPKALQE 300

                          90
                  ....*....|..
gi 334185156  524 VKRKglnlsHLA 535
Cdd:PLN02774  301 LRKE-----HLA 307
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 918-1054 9.06e-14

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: 73.52  E-value: 9.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185156  918 IYNFSSGKGIHKLVNFSEGVReslrrlsHVTWMADELHkatyYLFSKSDQRISCVHTQTVEMHQSGSG---AVTALIYH- 993
Cdd:cd00200   161 LWDLRTGKCVATLTGHTGEVN-------SVAFSPDGEK----LLSSSSDGTIKLWDLSTGKCLGTLRGhenGVNSVAFSp 229

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334185156  994 -KGLLFSGFSDGSIRVWNVNKKiaTLLWDIKEHKSTVTCFSLSETGECVLSGSADKTIRVWQ 1054
Cdd:cd00200   230 dGYLLASGSEDGTIRVWDLRTG--ECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
975-1060 1.18e-09

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 61.85  E-value: 1.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185156  975 QTVEMHqsgSGAVTALIYHKG--LLFSGFSDGSIRVWNVNKkiATLLWDIKEHKSTVTCFSLSETGECVLSGSADKTIRV 1052
Cdd:COG2319   156 RTLTGH---SGAVTSVAFSPDgkLLASGSDDGTVRLWDLAT--GKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRL 230


                  ....*...
gi 334185156 1053 WQIVKGKL 1060
Cdd:COG2319   231 WDLATGKL 238
WD40 pfam00400
WD domain, G-beta repeat;
1017-1053 4.88e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 44.26  E-value: 4.88e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 334185156  1017 TLLWDIKEHKSTVTCFSLSETGECVLSGSADKTIRVW 1053
Cdd:pfam00400    2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 1017-1053 6.40e-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: 44.23  E-value: 6.40e-06
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 334185156   1017 TLLWDIKEHKSTVTCFSLSETGECVLSGSADKTIRVW 1053
Cdd:smart00320    3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
PLN02774 PLN02774
brassinosteroid-6-oxidase
 444-535 2.94e-03

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 41.68  E-value: 2.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185156  444 NLQSLIKEVLGNADEKYVSEVTMIYQMLnRKEGFKYSMLKDVILDQLFTAISSSEEkTVIKASMTALtKIISVNRTALEE 523
Cdd:PLN02774  224 NIVRMLRQLIQERRASGETHTDMLGYLM-RKEGNRYKLTDEEIIDQIITILYSGYE-TVSTTSMMAV-KYLHDHPKALQE 300

                          90
                  ....*....|..
gi 334185156  524 VKRKglnlsHLA 535
Cdd:PLN02774  301 LRKE-----HLA 307
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 918-1054 9.06e-14

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: 73.52  E-value: 9.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185156  918 IYNFSSGKGIHKLVNFSEGVReslrrlsHVTWMADELHkatyYLFSKSDQRISCVHTQTVEMHQSGSG---AVTALIYH- 993
Cdd:cd00200   161 LWDLRTGKCVATLTGHTGEVN-------SVAFSPDGEK----LLSSSSDGTIKLWDLSTGKCLGTLRGhenGVNSVAFSp 229

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334185156  994 -KGLLFSGFSDGSIRVWNVNKKiaTLLWDIKEHKSTVTCFSLSETGECVLSGSADKTIRVWQ 1054
Cdd:cd00200   230 dGYLLASGSEDGTIRVWDLRTG--ECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 973-1261 1.21e-12

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 70.06  E-value: 1.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185156  973 HTQTVEMHQSGsgaVTALIYH--KGLLFSGFSDGSIRVWNV--NKKIATLlwdiKEHKSTVTCFSLSETGECVLSGSADK 1048
Cdd:cd00200     1 LRRTLKGHTGG---VTCVAFSpdGKLLATGSGDGTIKVWDLetGELLRTL----KGHTGPVRDVAASADGTYLASGSSDK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185156 1049 TIRVWQIVKGKLecaeviktkdsIRKLEAFGNMIFVITKGHKMKLLDSSRISQSIfkgkgvksmvsaqgKIYigciDTsi 1128
Cdd:cd00200    74 TIRLWDLETGEC-----------VRTLTGHTSYVSSVAFSPDGRILSSSSRDKTI--------------KVW----DV-- 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185156 1129 qelivankrekEIKAPTRSWRLQNKPINSVVV--YKDMLYSSS--TYV---EMSNIKDLRRNYEPQMSITA----EKGSN 1197
Cdd:cd00200   123 -----------ETGKCLTTLRGHTDWVNSVAFspDGTFVASSSqdGTIklwDLRTGKCVATLTGHTGEVNSvafsPDGEK 191

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334185156 1198 IVAmgvvedfiylnrSSSANTLQIWLRRTQQKVGRLSA-GSKITSLLTAND--IVFCGTEAGVIKGW 1261
Cdd:cd00200   192 LLS------------SSSDGTIKLWDLSTGKCLGTLRGhENGVNSVAFSPDgyLLASGSEDGTIRVW 246
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 915-1062 1.72e-12

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: 69.67  E-value: 1.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185156  915 CICIYNFSSGKGIHKLVNFSEGVreslrrlSHVTWMADelhkaTYYLFSKSDQR-------ISCVHTQTVEMHqsgSGAV 987
Cdd:cd00200    74 TIRLWDLETGECVRTLTGHTSYV-------SSVAFSPD-----GRILSSSSRDKtikvwdvETGKCLTTLRGH---TDWV 138

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185156  988 TALIYH--KGLLFSGFSDGSIRVWNVN--KKIATLlwdiKEHKSTVTCFSLSETGECVLSGSADKTIRVWQIVKGKLEC 1062
Cdd:cd00200   139 NSVAFSpdGTFVASSSQDGTIKLWDLRtgKCVATL----TGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLG 213
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 970-1060 2.62e-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: 65.82  E-value: 2.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185156  970 SCVHTQTVemHQSGSGAVTALIYHKgLLFSGFSDGSIRVWNVNKKiaTLLWDIKEHKSTVTCFSLSETGECVLSGSADKT 1049
Cdd:cd00200    42 ELLRTLKG--HTGPVRDVAASADGT-YLASGSSDKTIRLWDLETG--ECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKT 116

                          90
                  ....*....|.
gi 334185156 1050 IRVWQIVKGKL 1060
Cdd:cd00200   117 IKVWDVETGKC 127
WD40 COG2319
WD40 repeat [General function prediction only];
975-1060 1.18e-09

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 61.85  E-value: 1.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185156  975 QTVEMHqsgSGAVTALIYHKG--LLFSGFSDGSIRVWNVNKkiATLLWDIKEHKSTVTCFSLSETGECVLSGSADKTIRV 1052
Cdd:COG2319   156 RTLTGH---SGAVTSVAFSPDgkLLASGSDDGTVRLWDLAT--GKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRL 230


                  ....*...
gi 334185156 1053 WQIVKGKL 1060
Cdd:COG2319   231 WDLATGKL 238
WD40 COG2319
WD40 repeat [General function prediction only];
984-1060 1.42e-09

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 61.85  E-value: 1.42e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185156  984 SGAVTALIYHKG--LLFSGFSDGSIRVWNVNKKiaTLLWDIKEHKSTVTCFSLSETGECVLSGSADKTIRVWQIVKGKL 1060
Cdd:COG2319   288 SGGVNSVAFSPDgkLLASGSDDGTVRLWDLATG--KLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGEL 364
WD40 COG2319
WD40 repeat [General function prediction only];
980-1055 1.49e-09

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 61.47  E-value: 1.49e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334185156  980 HQSGSGAVTALIYH--KGLLFSGFSDGSIRVWNVNKKiaTLLWDIKEHKSTVTCFSLSETGECVLSGSADKTIRVWQI 1055
Cdd:COG2319   326 LTGHTGAVRSVAFSpdGKTLASGSDDGTVRLWDLATG--ELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401
WD40 COG2319
WD40 repeat [General function prediction only];
984-1095 2.36e-09

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 61.08  E-value: 2.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185156  984 SGAVTALIYHK--GLLFSGFSDGSIRVWNVNKkiATLLWDIKEHKSTVTCFSLSETGECVLSGSADKTIRVWQIVKGKLE 1061
Cdd:COG2319   120 TGAVRSVAFSPdgKTLASGSADGTVRLWDLAT--GKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLL 197

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 334185156 1062 cAEVIKTKDSIRKLeAF---GNMIFVITKGHKMKLLD 1095
Cdd:COG2319   198 -RTLTGHTGAVRSV-AFspdGKLLASGSADGTVRLWD 232
WD40 COG2319
WD40 repeat [General function prediction only];
984-1060 5.51e-09

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 59.92  E-value: 5.51e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185156  984 SGAVTALIYHKG--LLFSGFSDGSIRVWNVNKKiaTLLWDIKEHKSTVTCFSLSETGECVLSGSADKTIRVWQIVKGKL 1060
Cdd:COG2319   246 SGSVRSVAFSPDgrLLASGSADGTVRLWDLATG--ELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKL 322
WD40 COG2319
WD40 repeat [General function prediction only];
984-1060 1.14e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 58.77  E-value: 1.14e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185156  984 SGAVTALIYHKG--LLFSGFSDGSIRVWNVNKKiaTLLWDIKEHKSTVTCFSLSETGECVLSGSADKTIRVWQIVKGKL 1060
Cdd:COG2319   204 TGAVRSVAFSPDgkLLASGSADGTVRLWDLATG--KLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGEL 280
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 969-1060 4.36e-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: 56.19  E-value: 4.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185156  969 ISCVHTqtVEMHQsgsGAVTALIYH--KGLLFSGFSDGSIRVWNVN--KKIATLlwdiKEHKSTVTCFSLSETGECVLSG 1044
Cdd:cd00200   167 GKCVAT--LTGHT---GEVNSVAFSpdGEKLLSSSSDGTIKLWDLStgKCLGTL----RGHENGVNSVAFSPDGYLLASG 237

                          90
                  ....*....|....*.
gi 334185156 1045 SADKTIRVWQIVKGKL 1060
Cdd:cd00200   238 SEDGTIRVWDLRTGEC 253
WD40 COG2319
WD40 repeat [General function prediction only];
995-1060 1.96e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 54.92  E-value: 1.96e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334185156  995 GLLFSGFSDGSIRVWNVNKkiATLLWDIKEHKSTVTCFSLSETGECVLSGSADKTIRVWQIVKGKL 1060
Cdd:COG2319    91 RLLASASADGTVRLWDLAT--GLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKL 154
WD40 pfam00400
WD domain, G-beta repeat;
1017-1053 4.88e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 44.26  E-value: 4.88e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 334185156  1017 TLLWDIKEHKSTVTCFSLSETGECVLSGSADKTIRVW 1053
Cdd:pfam00400    2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 1017-1053 6.40e-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: 44.23  E-value: 6.40e-06
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 334185156   1017 TLLWDIKEHKSTVTCFSLSETGECVLSGSADKTIRVW 1053
Cdd:smart00320    3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
PLN02774 PLN02774
brassinosteroid-6-oxidase
 444-535 2.94e-03

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 41.68  E-value: 2.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185156  444 NLQSLIKEVLGNADEKYVSEVTMIYQMLnRKEGFKYSMLKDVILDQLFTAISSSEEkTVIKASMTALtKIISVNRTALEE 523
Cdd:PLN02774  224 NIVRMLRQLIQERRASGETHTDMLGYLM-RKEGNRYKLTDEEIIDQIITILYSGYE-TVSTTSMMAV-KYLHDHPKALQE 300

                          90
                  ....*....|..
gi 334185156  524 VKRKglnlsHLA 535
Cdd:PLN02774  301 LRKE-----HLA 307
NBCH_WD40 pfam20426
Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at ...
 1022-1059 5.56e-03

Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at the C-terminus of neurobeachin-like proteins.


Pssm-ID: 466575 [Multi-domain]  Cd Length: 350  Bit Score: 40.44  E-value: 5.56e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 334185156  1022 IKEHKSTVTCFSLSETGECVLSGSADKTIRVWQIVKGK 1059
Cdd:pfam20426  120 IRQHKDVVSCVAVTSDGSILATGSYDTTVMVWEVLRGR 157
 
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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