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Conserved domains on  [gi|1039012511|gb|ANM62294|]
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Transducin/WD40 repeat-like superfamily protein [Arabidopsis thaliana]

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];
267-424 1.89e-21

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 95.75  E-value: 1.89e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039012511 267 TSIAWVPggDGSFVA-AHADGNLYVYeknkegatdssfsairdptqfSVDKAKysksnPVARWHIGQGAINSIAFSNDGA 345
Cdd:COG2319   250 RSVAFSP--DGRLLAsGSADGTVRLW---------------------DLATGE-----LLRTLTGHSGGVNSVAFSPDGK 301

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039012511 346 YLATVGRDGYLRIFDFSTQKLVCGVKSYYGALLCCAWSMDGKYLLTGGEDDLVQVWSMEDRKVVAWGEGHNSWVSGVAF 424
Cdd:COG2319   302 LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAF 380
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
267-424 1.89e-21

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 95.75  E-value: 1.89e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039012511 267 TSIAWVPggDGSFVA-AHADGNLYVYeknkegatdssfsairdptqfSVDKAKysksnPVARWHIGQGAINSIAFSNDGA 345
Cdd:COG2319   250 RSVAFSP--DGRLLAsGSADGTVRLW---------------------DLATGE-----LLRTLTGHSGGVNSVAFSPDGK 301

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039012511 346 YLATVGRDGYLRIFDFSTQKLVCGVKSYYGALLCCAWSMDGKYLLTGGEDDLVQVWSMEDRKVVAWGEGHNSWVSGVAF 424
Cdd:COG2319   302 LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAF 380
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 333-425 1.93e-15

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: 76.60  E-value: 1.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039012511 333 GAINSIAFSNDGAYLATVGRDGYLRIFDFSTQKLVCGVKSYYGALLCCAWSMDGKYLLTGGEDDLVQVWSMEDRKVVAWG 412
Cdd:cd00200    10 GGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTL 89

                          90
                  ....*....|...
gi 1039012511 413 EGHNSWVSGVAFD 425
Cdd:cd00200    90 TGHTSYVSSVAFS 102
Nup160 pfam11715
Nucleoporin Nup120/160; Nup120 is conserved from fungi to plants to humans, and is homologous ...
 179-406 9.27e-07

Nucleoporin Nup120/160; Nup120 is conserved from fungi to plants to humans, and is homologous with the Nup160 of vertebrates. The nuclear core complex, or NPC, mediates macromolecular transport across the nuclear envelope. Deletion of the NUP120 gene causes clustering of NPCs at one side of the nuclear envelope, moderate nucleolar fragmentation and slower cell growth. The vertebrate NPC is estimated to contain between 30 and 60 different proteins. most of which are not known. Two important ones in creating the nucleoporin basket are Nup98 and Nup153, and Nup120, in conjunction with Nup 133, interacts with these two and itself plays a role in mRNA export. Nup160, Nup133, Nup96, and Nup107 are all targets of phosphorylation. The phosphorylation sites are clustered mainly at the N-terminal regions of these proteins, which are predicted to be natively disordered. The entire Nup107-160 sub-complex is stable throughout the cell cycle, thus it seems unlikely that phosphorylation affects interactions within the Nup107-160 sub-complex, but rather that it regulates the association of the sub-complex with the NPC and other proteins.


Pssm-ID: 432020 [Multi-domain]  Cd Length: 540  Bit Score: 51.31  E-value: 9.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039012511 179 VFNVGDAIFISDLNSQDKDPVKSIHIS-NSNPMCHAFHPDAKDGHDLLIGL---NSGDVYTVSLRQQLQdvgkKLVSAQH 254
Cdd:pfam11715  57 VLTDGRVLELVDLSLKSSLANLTLRLDfPSPILPSCVCFTDSEDGDVLIVIvttASVHLYSLRLRPDFF----RLPDAIF 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039012511 255 YNkDGSVNNSR---CTSIAWVPGG--DGS---FVAAHADGNLYVYEKNKEGAT--------DSSFSAIRDPTQFSVD-KA 317
Cdd:pfam11715 133 GD-LGDWCKSYvpsSFSGFSKPGRlvAVSpleLLVSLADGGLLKLTRSSDGGAwkestfepASWLQSLSGLLGWLADpTI 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039012511 318 KYSKSNPvarwHIGQGAINSIAFSNDGAYLATVGRDGYLRIFDFSTQKLV---------------CGVKS--YYGALLCC 380
Cdd:pfam11715 212 RYSGSSV----ALSLSAAPAVTTVGGQNFLFTLSLDHTLRVWDLLTGKCLatidlldlelpqdssSWLTLdpAPSSLIRV 287

                         250       260
                  ....*....|....*....|....*...
gi 1039012511 381 AWSMDGKYLLT--GGEDDLVQVWSMEDR 406
Cdd:pfam11715 288 SGSFRAYLVLTysPSSNGQFKFWKVKSN 315
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 321-360 3.81e-05

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: 40.76  E-value: 3.81e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1039012511  321 KSNPVARWHIGQGAINSIAFSNDGAYLATVGRDGYLRIFD 360
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
267-424 1.89e-21

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 95.75  E-value: 1.89e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039012511 267 TSIAWVPggDGSFVA-AHADGNLYVYeknkegatdssfsairdptqfSVDKAKysksnPVARWHIGQGAINSIAFSNDGA 345
Cdd:COG2319   250 RSVAFSP--DGRLLAsGSADGTVRLW---------------------DLATGE-----LLRTLTGHSGGVNSVAFSPDGK 301

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039012511 346 YLATVGRDGYLRIFDFSTQKLVCGVKSYYGALLCCAWSMDGKYLLTGGEDDLVQVWSMEDRKVVAWGEGHNSWVSGVAF 424
Cdd:COG2319   302 LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAF 380
WD40 COG2319
WD40 repeat [General function prediction only];
324-424 2.65e-21

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 95.36  E-value: 2.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039012511 324 PVARWHIGQGAINSIAFSNDGAYLATVGRDGYLRIFDFSTQKLVCGVKSYYGALLCCAWSMDGKYLLTGGEDDLVQVWSM 403
Cdd:COG2319   238 LLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL 317

                          90       100
                  ....*....|....*....|.
gi 1039012511 404 EDRKVVAWGEGHNSWVSGVAF 424
Cdd:COG2319   318 ATGKLLRTLTGHTGAVRSVAF 338
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 333-425 1.93e-15

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: 76.60  E-value: 1.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039012511 333 GAINSIAFSNDGAYLATVGRDGYLRIFDFSTQKLVCGVKSYYGALLCCAWSMDGKYLLTGGEDDLVQVWSMEDRKVVAWG 412
Cdd:cd00200    10 GGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTL 89

                          90
                  ....*....|...
gi 1039012511 413 EGHNSWVSGVAFD 425
Cdd:cd00200    90 TGHTSYVSSVAFS 102
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 332-428 4.98e-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: 72.37  E-value: 4.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039012511 332 QGAINSIAFSNDGAYLATVGRDGYLRIFDFSTQKLVCGVKSYYGALLCCAWSMDGKYLLTGGEDDLVQVWSMEDRKVVAW 411
Cdd:cd00200   135 TDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGT 214

                          90
                  ....*....|....*....
gi 1039012511 412 GEGHNSWVSGVAF--DSYW 428
Cdd:cd00200   215 LRGHENGVNSVAFspDGYL 233
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 332-425 2.51e-13

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: 2.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039012511 332 QGAINSIAFSNDGAYLATVGRDGYLRIFDFSTQKLVCGVKSYYGALLCCAWSMDGKYLLTGGEDDLVQVWSMEDRKVVAW 411
Cdd:cd00200   177 TGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQT 256

                          90
                  ....*....|....
gi 1039012511 412 GEGHNSWVSGVAFD 425
Cdd:cd00200   257 LSGHTNSVTSLAWS 270
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 332-425 5.27e-13

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: 69.29  E-value: 5.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039012511 332 QGAINSIAFSNDGAYLATVGRDGYLRIFDFSTQKLVCGVKSYYGALLCCAWSMDGKYLLTGGEDDLVQVWSMEDRKVVAW 411
Cdd:cd00200    51 TGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTT 130

                          90
                  ....*....|....
gi 1039012511 412 GEGHNSWVSGVAFD 425
Cdd:cd00200   131 LRGHTDWVNSVAFS 144
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 332-402 9.08e-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: 56.57  E-value: 9.08e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039012511 332 QGAINSIAFSNDGAYLATVGRDGYLRIFDFSTQKLVCGVKSYYGALLCCAWSMDGKYLLTGGEDDLVQVWS 402
Cdd:cd00200   219 ENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
Nup160 pfam11715
Nucleoporin Nup120/160; Nup120 is conserved from fungi to plants to humans, and is homologous ...
 179-406 9.27e-07

Nucleoporin Nup120/160; Nup120 is conserved from fungi to plants to humans, and is homologous with the Nup160 of vertebrates. The nuclear core complex, or NPC, mediates macromolecular transport across the nuclear envelope. Deletion of the NUP120 gene causes clustering of NPCs at one side of the nuclear envelope, moderate nucleolar fragmentation and slower cell growth. The vertebrate NPC is estimated to contain between 30 and 60 different proteins. most of which are not known. Two important ones in creating the nucleoporin basket are Nup98 and Nup153, and Nup120, in conjunction with Nup 133, interacts with these two and itself plays a role in mRNA export. Nup160, Nup133, Nup96, and Nup107 are all targets of phosphorylation. The phosphorylation sites are clustered mainly at the N-terminal regions of these proteins, which are predicted to be natively disordered. The entire Nup107-160 sub-complex is stable throughout the cell cycle, thus it seems unlikely that phosphorylation affects interactions within the Nup107-160 sub-complex, but rather that it regulates the association of the sub-complex with the NPC and other proteins.


Pssm-ID: 432020 [Multi-domain]  Cd Length: 540  Bit Score: 51.31  E-value: 9.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039012511 179 VFNVGDAIFISDLNSQDKDPVKSIHIS-NSNPMCHAFHPDAKDGHDLLIGL---NSGDVYTVSLRQQLQdvgkKLVSAQH 254
Cdd:pfam11715  57 VLTDGRVLELVDLSLKSSLANLTLRLDfPSPILPSCVCFTDSEDGDVLIVIvttASVHLYSLRLRPDFF----RLPDAIF 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039012511 255 YNkDGSVNNSR---CTSIAWVPGG--DGS---FVAAHADGNLYVYEKNKEGAT--------DSSFSAIRDPTQFSVD-KA 317
Cdd:pfam11715 133 GD-LGDWCKSYvpsSFSGFSKPGRlvAVSpleLLVSLADGGLLKLTRSSDGGAwkestfepASWLQSLSGLLGWLADpTI 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039012511 318 KYSKSNPvarwHIGQGAINSIAFSNDGAYLATVGRDGYLRIFDFSTQKLV---------------CGVKS--YYGALLCC 380
Cdd:pfam11715 212 RYSGSSV----ALSLSAAPAVTTVGGQNFLFTLSLDHTLRVWDLLTGKCLatidlldlelpqdssSWLTLdpAPSSLIRV 287

                         250       260
                  ....*....|....*....|....*...
gi 1039012511 381 AWSMDGKYLLT--GGEDDLVQVWSMEDR 406
Cdd:pfam11715 288 SGSFRAYLVLTysPSSNGQFKFWKVKSN 315
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 375-427 9.34e-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: 50.41  E-value: 9.34e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039012511 375 GALLCCAWSMDGKYLLTGGEDDLVQVWSMEDRKVVAWGEGHNSWVSGVAFDSY 427
Cdd:cd00200    10 GGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASAD 62
Nsa1 cd22858
Ribosome Biogenesis Protein Nsa1; Ribosome biogenesis protein Nsa1 (Nop7-associated 1) from ...
 318-407 1.14e-06

Ribosome Biogenesis Protein Nsa1; Ribosome biogenesis protein Nsa1 (Nop7-associated 1) from fungi is an essential factor for ribosome assembly. In cooperation with the assembly factor Rix7, Nsa1 participates in an early cleavage of the pre-rRNA processing pathway. Rix7 is a type II double ring, AAA-ATPase, that may mediate the release of Nsa1 from nucleolar pre-60S particles. The release of Nsa1 from a discrete preribosomal particle may trigger the progression of 60S ribosome biogenesis. Nsa1 is essential for cell viability in yeast. It contains an N-terminal seven-bladed beta-propeller WD40 domain that associates with the D1-AAA domain of the AAA-ATPase Rix7, and a flexible lysine-rich C-terminus that extends outward from the WD40 domain, and is required for nucleolar localization.


Pssm-ID: 439304  Cd Length: 399  Bit Score: 50.68  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039012511 318 KYSKSNPVarwhigqGAINSIAFSNDGaYLATVGRDGYLRIFDFSTQKLVCgvKSYYGALLCCAWsmdgkyLLTGGEDDL 397
Cdd:cd22858   300 KYGGGDIT-------GAVSAVDVFEDK-YLATGGLDRYLRVFDLETRELLA--KVYVGSKISSVL------LLDDEDIEL 363

                          90
                  ....*....|
gi 1039012511 398 VQVWSMEDRK 407
Cdd:cd22858   364 PESEKKKKKK 373
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 331-385 3.59e-05

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: 42.27  E-value: 3.59e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039012511 331 GQGAINSIAFSNDGAYLATVGRDGYLRIFDFSTQKLVCGVKSYYGALLCCAWSMD 385
Cdd:pfam12894  37 EDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSAGSDLITCLGWGEN 91
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 321-360 3.81e-05

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: 40.76  E-value: 3.81e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1039012511  321 KSNPVARWHIGQGAINSIAFSNDGAYLATVGRDGYLRIFD 360
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 231-389 1.45e-04

Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown];


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 44.26  E-value: 1.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039012511  231 GDVYTVSlrqqlqdvgkklvsaqhyNKDGSVNN------SRCTSIAWVPggDGSFVAA--HADG--NLYVYEKNKEGAtd 300
Cdd:COG4946    322 GEVFTVP------------------AEKGPTRNltntpgVRERLPAWSP--DGKSIAYfsDASGeyELYIAPADGSGE-- 379

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039012511  301 ssfsairdPTQFSVDKAKYsksnpvarwhigqgaINSIAFSNDGAYLATVGRDGYLRIFDFSTQKLVCGVKSYYGAL-LC 379
Cdd:COG4946    380 --------PKQLTLGDLGR---------------VFNPVWSPDGKKIAFTDNRGRLWVVDLASGKVRKVDTDGYGDGiSD 436

                          170
                   ....*....|
gi 1039012511  380 CAWSMDGKYL 389
Cdd:COG4946    437 LAWSPDSKWL 446
8prop_heme_binding_protein cd20718
eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; ...
 323-393 9.60e-04

eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; Members here contain an 8-bladed beta-propeller heme-binding domain in cytochrome cd1 (nitrite reductase) and similar proteins including NirN and NirF. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO(3-)-> NO(2-)-> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic nitrite reductase NirS via its maturation factor NirF. NirN and NirF form a stable complex with the nitrite reductase NirS during enzyme maturation. NirF is involved in heme d1 insertion.


Pssm-ID: 467720 [Multi-domain]  Cd Length: 380  Bit Score: 41.17  E-value: 9.60e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039012511 323 NPVARWHIGQGAINSIAFSNDGAYLATVGRDGYLRIFDFSTQKLVCGVK-SYYGALLccAWSMDGKYLLTGG 393
Cdd:cd20718    49 EVLGRIDDGGAQVHVVVFSPDGRFAYVISRDGWLTKIDLYTLRPVASIRiGVNSRGI--ALSDDGKYVIAGN 118
Nsa1_WDR74-like cd22850
Ribosome biogenesis protein Nsa1 and similar proteins; Ribosome biogenesis protein Nsa1 ...
 316-387 1.32e-03

Ribosome biogenesis protein Nsa1 and similar proteins; Ribosome biogenesis protein Nsa1 (Nop7-associated 1) from fungi and WDR74 (WD repeat-containing protein 74) from mammals and plants, are homologous essential factors for ribosome assembly. In cooperation with the assembly factor Rix7/NVL2, Nsa1/WDR74 participates in an early cleavage of the pre-rRNA processing pathway. Rix7/NVL2 is a type II double ring, AAA-ATPase, that may mediate the release of Nsa1/WDR74 from nucleolar pre-60S particles. Nsa1/WDR74 contains an N-terminal seven-bladed beta-propeller WD40 domain that associates with the D1-AAA domain of the AAA-ATPase Rix7/NVL2, and a flexible lysine-rich C-terminus that extends outward from the WD40 domain, and is required for nucleolar localization.


Pssm-ID: 439302 [Multi-domain]  Cd Length: 333  Bit Score: 40.69  E-value: 1.32e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039012511 316 KAKYSKSNpvarwhigQGAINSIAFSNDgaYLATVGRDGYLRIFDFSTQKLVcgVKSYYGALLCCAWSMDGK 387
Cdd:cd22850   271 LGKYGGSI--------TGAVRHPELFDP--YLASGGLDRYLRVFDIETRELL--AKVYLGKQILTVVVLDDE 330
WD40 pfam00400
WD domain, G-beta repeat;
332-360 1.48e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.17  E-value: 1.48e-03
                          10        20
                  ....*....|....*....|....*....
gi 1039012511 332 QGAINSIAFSNDGAYLATVGRDGYLRIFD 360
Cdd:pfam00400  11 TGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 375-402 3.73e-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: 34.98  E-value: 3.73e-03
                           10        20
                   ....*....|....*....|....*...
gi 1039012511  375 GALLCCAWSMDGKYLLTGGEDDLVQVWS 402
Cdd:smart00320  13 GPVTSVAFSPDGKYLASGSDDGTIKLWD 40
Nsa1_WDR74-like cd22850
Ribosome biogenesis protein Nsa1 and similar proteins; Ribosome biogenesis protein Nsa1 ...
 259-405 6.71e-03

Ribosome biogenesis protein Nsa1 and similar proteins; Ribosome biogenesis protein Nsa1 (Nop7-associated 1) from fungi and WDR74 (WD repeat-containing protein 74) from mammals and plants, are homologous essential factors for ribosome assembly. In cooperation with the assembly factor Rix7/NVL2, Nsa1/WDR74 participates in an early cleavage of the pre-rRNA processing pathway. Rix7/NVL2 is a type II double ring, AAA-ATPase, that may mediate the release of Nsa1/WDR74 from nucleolar pre-60S particles. Nsa1/WDR74 contains an N-terminal seven-bladed beta-propeller WD40 domain that associates with the D1-AAA domain of the AAA-ATPase Rix7/NVL2, and a flexible lysine-rich C-terminus that extends outward from the WD40 domain, and is required for nucleolar localization.


Pssm-ID: 439302 [Multi-domain]  Cd Length: 333  Bit Score: 38.38  E-value: 6.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039012511 259 GSVNNSRCTSIAWVPGGDGSFVAAHADGNLYVYEKNKEgaTDSSFSAIRDptqFSVDKAKYSKSNPVarwhigqgainSI 338
Cdd:cd22850    30 SEGLSNAVQRLSLVDRSDPLLLVARRNGNGEVYVLSPV--DGELFELLSS---IEGLTRSKEEDKFV-----------GL 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039012511 339 AFSNDGAYLATVGRDGYLRIFDFSTQK---LVCGVKSYYGALLCC--AWSMDGKYLLTGGEDDLVQVWSMED 405
Cdd:cd22850    94 HLLRSLGLLTCATKSGLLHIIDLEDSKkdsLEVKAPLTLPGFLSAfrVNPTDEGVFAYGGKENDLKLWDLEK 165
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
323-425 9.82e-03

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 37.75  E-value: 9.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039012511 323 NPVARWHIGQGAINsIAFSNDGAYL-ATVGRDGYLRIFDFSTQKLV----CGVKSYYgallcCAWSMDGKYLLTGGEDD- 396
Cdd:COG3391   101 KVVATIPVGGGPRG-LAVDPDGGRLyVADSGNGRVSVIDTATGKVVatipVGAGPHG-----IAVDPDGKRLYVANSGSn 174

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1039012511 397 ----LVQVWSMEDRKVVA-WGEGHNswVSGVAFD 425
Cdd:COG3391   175 tvsvIVSVIDTATGKVVAtIPVGGG--PVGVAVS 206
 
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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