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Conserved domains on  [gi|442626657|ref|NP_001260217|]
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receptor of activated protein kinase C 1, isoform B [Drosophila melanogaster]

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 ...
 7-107 7.50e-28

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: 102.41  E-value: 7.50e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626657   7 LRGTLIGHNGWVTQIATNPkDPDTIISASRDKTLIVWKLTRDEdtnygyPQKRLYGHSHFISDVVLSSDGNYALSGSWDQ 86
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSP-DGKLLATGSGDGTIKVWDLETGE------LLRTLKGHTGPVRDVAASADGTYLASGSSDK 73

                         90       100
                 ....*....|....*....|.
gi 442626657  87 TLRLWDLAAGKTTRRFEGHTK 107
Cdd:cd00200   74 TIRLWDLETGECVRTLTGHTS 94
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 7-107 7.50e-28

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: 102.41  E-value: 7.50e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626657   7 LRGTLIGHNGWVTQIATNPkDPDTIISASRDKTLIVWKLTRDEdtnygyPQKRLYGHSHFISDVVLSSDGNYALSGSWDQ 86
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSP-DGKLLATGSGDGTIKVWDLETGE------LLRTLKGHTGPVRDVAASADGTYLASGSSDK 73

                         90       100
                 ....*....|....*....|.
gi 442626657  87 TLRLWDLAAGKTTRRFEGHTK 107
Cdd:cd00200   74 TIRLWDLETGECVRTLTGHTS 94
WD40 COG2319
WD40 repeat [General function prediction only];
3-106 3.16e-21

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 86.50  E-value: 3.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626657   3 ETLQLRGTLIGHNGWVTQIATNPkDPDTIISASRDKTLIVWKLTRdedtnyGYPQKRLYGHSHFISDVVLSSDGNYALSG 82
Cdd:COG2319  150 ATGKLLRTLTGHSGAVTSVAFSP-DGKLLASGSDDGTVRLWDLAT------GKLLRTLTGHTGAVRSVAFSPDGKLLASG 222

                         90       100
                 ....*....|....*....|....
gi 442626657  83 SWDQTLRLWDLAAGKTTRRFEGHT 106
Cdd:COG2319  223 SADGTVRLWDLATGKLLRTLTGHS 246
WD40 pfam00400
WD domain, G-beta repeat;
54-92 1.58e-08

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 46.57  E-value: 1.58e-08
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 442626657   54 GYPQKRLYGHSHFISDVVLSSDGNYALSGSWDQTLRLWD 92
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 54-92 1.97e-07

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: 43.84  E-value: 1.97e-07
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 442626657    54 GYPQKRLYGHSHFISDVVLSSDGNYALSGSWDQTLRLWD 92
Cdd:smart00320   2 GELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 10-83 1.02e-03

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 36.99  E-value: 1.02e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442626657  10 TLIGHNGWVTQIATnpKDPDTIISASRDKTLIVWKLTRDEDTNYGYPQKRLYGHSHFISDVVLSSDGNYALSGS 83
Cdd:PLN00181 656 TMIGHSKTVSYVRF--VDSSTLVSSSTDNTLKLWDLSMSISGINETPLHSFMGHTNVKNFVGLSVSDGYIATGS 727
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 7-107 7.50e-28

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: 102.41  E-value: 7.50e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626657   7 LRGTLIGHNGWVTQIATNPkDPDTIISASRDKTLIVWKLTRDEdtnygyPQKRLYGHSHFISDVVLSSDGNYALSGSWDQ 86
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSP-DGKLLATGSGDGTIKVWDLETGE------LLRTLKGHTGPVRDVAASADGTYLASGSSDK 73

                         90       100
                 ....*....|....*....|.
gi 442626657  87 TLRLWDLAAGKTTRRFEGHTK 107
Cdd:cd00200   74 TIRLWDLETGECVRTLTGHTS 94
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3-107 1.47e-21

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: 85.85  E-value: 1.47e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626657   3 ETLQLRGTLIGHNGWVTQIATNPkDPDTIISASRDKTLIVWkltrdeDTNYGYPQKRLYGHSHFISDVVLSSDGNYALSG 82
Cdd:cd00200   81 ETGECVRTLTGHTSYVSSVAFSP-DGRILSSSSRDKTIKVW------DVETGKCLTTLRGHTDWVNSVAFSPDGTFVASS 153

                         90       100
                 ....*....|....*....|....*
gi 442626657  83 SWDQTLRLWDLAAGKTTRRFEGHTK 107
Cdd:cd00200  154 SQDGTIKLWDLRTGKCVATLTGHTG 178
WD40 COG2319
WD40 repeat [General function prediction only];
3-106 3.16e-21

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 86.50  E-value: 3.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626657   3 ETLQLRGTLIGHNGWVTQIATNPkDPDTIISASRDKTLIVWKLTRdedtnyGYPQKRLYGHSHFISDVVLSSDGNYALSG 82
Cdd:COG2319  150 ATGKLLRTLTGHSGAVTSVAFSP-DGKLLASGSDDGTVRLWDLAT------GKLLRTLTGHTGAVRSVAFSPDGKLLASG 222

                         90       100
                 ....*....|....*....|....
gi 442626657  83 SWDQTLRLWDLAAGKTTRRFEGHT 106
Cdd:COG2319  223 SADGTVRLWDLATGKLLRTLTGHS 246
WD40 COG2319
WD40 repeat [General function prediction only];
3-106 5.55e-21

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 85.73  E-value: 5.55e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626657   3 ETLQLRGTLIGHNGWVTQIATNPkDPDTIISASRDKTLIVWkltrdeDTNYGYPQKRLYGHSHFISDVVLSSDGNYALSG 82
Cdd:COG2319  276 ATGELLRTLTGHSGGVNSVAFSP-DGKLLASGSDDGTVRLW------DLATGKLLRTLTGHTGAVRSVAFSPDGKTLASG 348

                         90       100
                 ....*....|....*....|....
gi 442626657  83 SWDQTLRLWDLAAGKTTRRFEGHT 106
Cdd:COG2319  349 SDDGTVRLWDLATGELLRTLTGHT 372
WD40 COG2319
WD40 repeat [General function prediction only];
3-106 1.20e-20

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 84.58  E-value: 1.20e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626657   3 ETLQLRGTLIGHNGWVTQIATNPkDPDTIISASRDKTLIVWKLTRdedtnyGYPQKRLYGHSHFISDVVLSSDGNYALSG 82
Cdd:COG2319  192 ATGKLLRTLTGHTGAVRSVAFSP-DGKLLASGSADGTVRLWDLAT------GKLLRTLTGHSGSVRSVAFSPDGRLLASG 264

                         90       100
                 ....*....|....*....|....
gi 442626657  83 SWDQTLRLWDLAAGKTTRRFEGHT 106
Cdd:COG2319  265 SADGTVRLWDLATGELLRTLTGHS 288
WD40 COG2319
WD40 repeat [General function prediction only];
3-106 3.24e-20

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 83.42  E-value: 3.24e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626657   3 ETLQLRGTLIGHNGWVTQIATNPkDPDTIISASRDKTLIVWkltrdeDTNYGYPQKRLYGHSHFISDVVLSSDGNYALSG 82
Cdd:COG2319  234 ATGKLLRTLTGHSGSVRSVAFSP-DGRLLASGSADGTVRLW------DLATGELLRTLTGHSGGVNSVAFSPDGKLLASG 306

                         90       100
                 ....*....|....*....|....
gi 442626657  83 SWDQTLRLWDLAAGKTTRRFEGHT 106
Cdd:COG2319  307 SDDGTVRLWDLATGKLLRTLTGHT 330
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3-107 1.03e-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: 78.53  E-value: 1.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626657   3 ETLQLRGTLIGHNGWVTQIATNPkDPDTIISASRDKTLIVWkltrdeDTNYGYPQKRLYGHSHFISDVVLSSDGNYALSG 82
Cdd:cd00200  123 ETGKCLTTLRGHTDWVNSVAFSP-DGTFVASSSQDGTIKLW------DLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSS 195

                         90       100
                 ....*....|....*....|....*
gi 442626657  83 SWDQTLRLWDLAAGKTTRRFEGHTK 107
Cdd:cd00200  196 SSDGTIKLWDLSTGKCLGTLRGHEN 220
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3-107 7.82e-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: 75.83  E-value: 7.82e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626657   3 ETLQLRGTLIGHNGWVTQIATNPkDPDTIISASRDKTLIVWkltrdeDTNYGYPQKRLYGHSHFISDVVLSSDGNYALSG 82
Cdd:cd00200  165 RTGKCVATLTGHTGEVNSVAFSP-DGEKLLSSSSDGTIKLW------DLSTGKCLGTLRGHENGVNSVAFSPDGYLLASG 237

                         90       100
                 ....*....|....*....|....*
gi 442626657  83 SWDQTLRLWDLAAGKTTRRFEGHTK 107
Cdd:cd00200  238 SEDGTIRVWDLRTGECVQTLSGHTN 262
WD40 COG2319
WD40 repeat [General function prediction only];
2-106 3.94e-17

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 74.95  E-value: 3.94e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626657   2 SETLQLRGTLIGHNGWVTQIATNPkDPDTIISASRDKTLIVWkltrdeDTNYGYPQKRLYGHSHFISDVVLSSDGNYALS 81
Cdd:COG2319   65 AAAGALLATLLGHTAAVLSVAFSP-DGRLLASASADGTVRLW------DLATGLLLRTLTGHTGAVRSVAFSPDGKTLAS 137

                         90       100
                 ....*....|....*....|....*
gi 442626657  82 GSWDQTLRLWDLAAGKTTRRFEGHT 106
Cdd:COG2319  138 GSADGTVRLWDLATGKLLRTLTGHS 162
WD40 COG2319
WD40 repeat [General function prediction only];
3-94 4.57e-17

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 74.95  E-value: 4.57e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626657   3 ETLQLRGTLIGHNGWVTQIATNPkDPDTIISASRDKTLIVWkltrdeDTNYGYPQKRLYGHSHFISDVVLSSDGNYALSG 82
Cdd:COG2319  318 ATGKLLRTLTGHTGAVRSVAFSP-DGKTLASGSDDGTVRLW------DLATGELLRTLTGHTGAVTSVAFSPDGRTLASG 390

                         90
                 ....*....|..
gi 442626657  83 SWDQTLRLWDLA 94
Cdd:COG2319  391 SADGTVRLWDLA 402
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 4-92 7.37e-17

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: 7.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626657   4 TLQLRGTLIGHNGWVTQIATNPkDPDTIISASRDKTLIVWkltrdeDTNYGYPQKRLYGHSHFISDVVLSSDGNYALSGS 83
Cdd:cd00200  208 TGKCLGTLRGHENGVNSVAFSP-DGYLLASGSEDGTIRVW------DLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGS 280


                 ....*....
gi 442626657  84 WDQTLRLWD 92
Cdd:cd00200  281 ADGTIRIWD 289
WD40 pfam00400
WD domain, G-beta repeat;
54-92 1.58e-08

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 46.57  E-value: 1.58e-08
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 442626657   54 GYPQKRLYGHSHFISDVVLSSDGNYALSGSWDQTLRLWD 92
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 COG2319
WD40 repeat [General function prediction only];
4-106 6.34e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 48.75  E-value: 6.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626657   4 TLQLRGTLIGHNGWVTQIATNPkDPDTIISASRDKTLIVWkltrdeDTNYGYPQKRLYGHSHFISDVVLSSDGNYALSGS 83
Cdd:COG2319   25 LGALLLLLLGLAAAVASLAASP-DGARLAAGAGDLTLLLL------DAAAGALLATLLGHTAAVLSVAFSPDGRLLASAS 97

                         90       100
                 ....*....|....*....|...
gi 442626657  84 WDQTLRLWDLAAGKTTRRFEGHT 106
Cdd:COG2319   98 ADGTVRLWDLATGLLLRTLTGHT 120
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 54-92 1.97e-07

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: 43.84  E-value: 1.97e-07
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 442626657    54 GYPQKRLYGHSHFISDVVLSSDGNYALSGSWDQTLRLWD 92
Cdd:smart00320   2 GELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 4-44 2.31e-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: 38.45  E-value: 2.31e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 442626657     4 TLQLRGTLIGHNGWVTQIATNPkDPDTIISASRDKTLIVWK 44
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSP-DGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
6-43 5.93e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 37.32  E-value: 5.93e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 442626657    6 QLRGTLIGHNGWVTQIATNPkDPDTIISASRDKTLIVW 43
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSP-DGKLLASGSDDGTVKVW 38
Nup160 pfam11715
Nucleoporin Nup120/160; Nup120 is conserved from fungi to plants to humans, and is homologous ...
 27-103 1.26e-04

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: 39.37  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626657   27 DPDTIISASRDKTLIV---------WKLTRDEDTNYGYPQKRLYGHS----------------HFISDVVLSSDGNYALS 81
Cdd:pfam11715 160 SPLELLVSLADGGLLKltrssdggaWKESTFEPASWLQSLSGLLGWLadptirysgssvalslSAAPAVTTVGGQNFLFT 239

                          90       100
                  ....*....|....*....|..
gi 442626657   82 GSWDQTLRLWDLAAGKTTRRFE 103
Cdd:pfam11715 240 LSLDHTLRVWDLLTGKCLATID 261
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 2-44 9.03e-04

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: 36.93  E-value: 9.03e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 442626657   2 SETLQLRGTLIGHNGWVTQIATNPkDPDTIISASRDKTLIVWK 44
Cdd:cd00200  248 LRTGECVQTLSGHTNSVTSLAWSP-DGKRLASGSADGTIRIWD 289
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 10-83 1.02e-03

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 36.99  E-value: 1.02e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442626657  10 TLIGHNGWVTQIATnpKDPDTIISASRDKTLIVWKLTRDEDTNYGYPQKRLYGHSHFISDVVLSSDGNYALSGS 83
Cdd:PLN00181 656 TMIGHSKTVSYVRF--VDSSTLVSSSTDNTLKLWDLSMSISGINETPLHSFMGHTNVKNFVGLSVSDGYIATGS 727
PTZ00421 PTZ00421
coronin; Provisional
 11-106 2.16e-03

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 36.02  E-value: 2.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626657  11 LIGHNGWVTQIATNPKDPDTIISASRDKTLIVWKLTRDEDT-NYGYPQKRLYGHSHFISDVVLSSDGNYAL-SGSWDQTL 88
Cdd:PTZ00421  71 LLGQEGPIIDVAFNPFDPQKLFTASEDGTIMGWGIPEEGLTqNISDPIVHLQGHTKKVGIVSFHPSAMNVLaSAGADMVV 150

                         90
                 ....*....|....*...
gi 442626657  89 RLWDLAAGKTTRRFEGHT 106
Cdd:PTZ00421 151 NVWDVERGKAVEVIKCHS 168
 
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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