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Conserved domains on  [gi|70778824|ref|NP_001020547|]
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superkiller complex protein 8 isoform b [Mus musculus]

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];
12-204 1.44e-56

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 183.96  E-value: 1.44e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824  12 WTLAFSPDSQYLATGTHMGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGH 91
Cdd:COG2319 208 RSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGH 287
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824  92 AMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDVGTRTCIHT 171
Cdd:COG2319 288 SGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRT 367
                       170       180       190
                ....*....|....*....|....*....|...
gi 70778824 172 FFDHQDQVWGVKYNGNGSKIVSVGDDQEIHVYD 204
Cdd:COG2319 368 LTGHTGAVTSVAFSPDGRTLASGSADGTVRLWD 400
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
12-204 1.44e-56

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 183.96  E-value: 1.44e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824  12 WTLAFSPDSQYLATGTHMGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGH 91
Cdd:COG2319 208 RSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGH 287
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824  92 AMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDVGTRTCIHT 171
Cdd:COG2319 288 SGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRT 367
                       170       180       190
                ....*....|....*....|....*....|...
gi 70778824 172 FFDHQDQVWGVKYNGNGSKIVSVGDDQEIHVYD 204
Cdd:COG2319 368 LTGHTGAVTSVAFSPDGRTLASGSADGTVRLWD 400
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
12-204 8.80e-46

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: 152.87  E-value: 8.80e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824  12 WTLAFSPDSQYLATGTHMGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGH 91
Cdd:cd00200  97 SSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGH 176
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824  92 AMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDVGTRTCIHT 171
Cdd:cd00200 177 TGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQT 256
                       170       180       190
                ....*....|....*....|....*....|...
gi 70778824 172 FFDHQDQVWGVKYNGNGSKIVSVGDDQEIHVYD 204
Cdd:cd00200 257 LSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
14-101 2.21e-10

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: 55.36  E-value: 2.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824    14 LAFSPDSQYLATGTHMGKVNIFGVeSGKKEY--SLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGH 91
Cdd:pfam12894   1 MSWCPTMDLIALATEDGELLLHRL-NWQRVWtlSPDKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSAG 79
                          90
                  ....*....|
gi 70778824    92 AMPIRSLTFS 101
Cdd:pfam12894  80 SDLITCLGWG 89
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
81-120 2.44e-10

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: 53.86  E-value: 2.44e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 70778824     81 TGKLLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYD 120
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
14-147 2.03e-07

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 50.47  E-value: 2.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824   14 LAFSPDSQYLATGTHMGKVNIFGVESGKKE--------YSLDTRGKfILSIAYSPDGK-YLASGAIDGIINIFDIATGKL 84
Cdd:PLN00181 489 IGFDRDGEFFATAGVNKKIKIFECESIIKDgrdihypvVELASRSK-LSGICWNSYIKsQVASSNFEGVVQVWDVARSQL 567
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 70778824   85 LHTLEGHAMPIRSLTF-SPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASwVLNVAFcPDDT 147
Cdd:PLN00181 568 VTEMKEHEKRVWSIDYsSADPTLLASGSDDGSVKLWSINQGVSIGTIKTKAN-ICCVQF-PSES 629
PQQ_ABC_repeats TIGR03866
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family ...
71-132 5.50e-03

PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family consist of seven repeats each of the YVTN family beta-propeller repeat (see TIGR02276). Members occur invariably as part of a transport operon that is associated with PQQ-dependent catabolism of alcohols such as phenylethanol.


Pssm-ID: 274824 [Multi-domain]  Cd Length: 310  Bit Score: 36.94  E-value: 5.50e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 70778824    71 DGIINIFDIATGKLLHTLEGHAMPiRSLTFSPDSQLL-VTASDDGYIKIYDVQHANLAGTL-SG 132
Cdd:TIGR03866  20 DNTISVIDTATLKVTRTFPVGQRP-RGITFSKDGKLLyVCASDSDTIQVIDPATGEVLHTLpSG 82
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
12-204 1.44e-56

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 183.96  E-value: 1.44e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824  12 WTLAFSPDSQYLATGTHMGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGH 91
Cdd:COG2319 208 RSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGH 287
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824  92 AMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDVGTRTCIHT 171
Cdd:COG2319 288 SGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRT 367
                       170       180       190
                ....*....|....*....|....*....|...
gi 70778824 172 FFDHQDQVWGVKYNGNGSKIVSVGDDQEIHVYD 204
Cdd:COG2319 368 LTGHTGAVTSVAFSPDGRTLASGSADGTVRLWD 400
WD40 COG2319
WD40 repeat [General function prediction only];
12-204 7.04e-56

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 182.03  E-value: 7.04e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824  12 WTLAFSPDSQYLATGTHMGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGH 91
Cdd:COG2319 124 RSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGH 203
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824  92 AMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDVGTRTCIHT 171
Cdd:COG2319 204 TGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRT 283
                       170       180       190
                ....*....|....*....|....*....|...
gi 70778824 172 FFDHQDQVWGVKYNGNGSKIVSVGDDQEIHVYD 204
Cdd:COG2319 284 LTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWD 316
WD40 COG2319
WD40 repeat [General function prediction only];
12-204 9.30e-56

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 182.03  E-value: 9.30e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824  12 WTLAFSPDSQYLATGTHMGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGH 91
Cdd:COG2319 166 TSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGH 245
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824  92 AMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDVGTRTCIHT 171
Cdd:COG2319 246 SGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRT 325
                       170       180       190
                ....*....|....*....|....*....|...
gi 70778824 172 FFDHQDQVWGVKYNGNGSKIVSVGDDQEIHVYD 204
Cdd:COG2319 326 LTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWD 358
WD40 COG2319
WD40 repeat [General function prediction only];
11-204 4.47e-52

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 172.40  E-value: 4.47e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824  11 AWTLAFSPDSQYLATGTHMGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEG 90
Cdd:COG2319  81 VLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTG 160
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824  91 HAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDVGTRTCIH 170
Cdd:COG2319 161 HSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLR 240
                       170       180       190
                ....*....|....*....|....*....|....
gi 70778824 171 TFFDHQDQVWGVKYNGNGSKIVSVGDDQEIHVYD 204
Cdd:COG2319 241 TLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWD 274
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
12-204 8.80e-46

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: 152.87  E-value: 8.80e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824  12 WTLAFSPDSQYLATGTHMGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGH 91
Cdd:cd00200  97 SSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGH 176
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824  92 AMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDVGTRTCIHT 171
Cdd:cd00200 177 TGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQT 256
                       170       180       190
                ....*....|....*....|....*....|...
gi 70778824 172 FFDHQDQVWGVKYNGNGSKIVSVGDDQEIHVYD 204
Cdd:cd00200 257 LSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
14-204 1.75e-45

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: 152.10  E-value: 1.75e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824  14 LAFSPDSQYLATGTHMGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGHAM 93
Cdd:cd00200  15 VAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLTGHTS 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824  94 PIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDVGTRTCIHTFF 173
Cdd:cd00200  95 YVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLT 174
                       170       180       190
                ....*....|....*....|....*....|.
gi 70778824 174 DHQDQVWGVKYNGNGSKIVSVGDDQEIHVYD 204
Cdd:cd00200 175 GHTGEVNSVAFSPDGEKLLSSSSDGTIKLWD 205
WD40 COG2319
WD40 repeat [General function prediction only];
6-204 8.98e-42

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 145.44  E-value: 8.98e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824   6 AGPVDAWTLAFSPDSQYLATGTHMGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLL 85
Cdd:COG2319  34 GLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLL 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824  86 HTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDVGT 165
Cdd:COG2319 114 RTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLAT 193
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 70778824 166 RTCIHTFFDHQDQVWGVKYNGNGSKIVSVGDDQEIHVYD 204
Cdd:COG2319 194 GKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWD 232
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
12-204 1.33e-40

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: 139.39  E-value: 1.33e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824  12 WTLAFSPDSQYLATGTHMGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGH 91
Cdd:cd00200  55 RDVAASADGTYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGH 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824  92 AMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDVGTRTCIHT 171
Cdd:cd00200 135 TDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGT 214
                       170       180       190
                ....*....|....*....|....*....|...
gi 70778824 172 FFDHQDQVWGVKYNGNGSKIVSVGDDQEIHVYD 204
Cdd:cd00200 215 LRGHENGVNSVAFSPDGYLLASGSEDGTIRVWD 247
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
51-204 9.06e-35

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: 124.37  E-value: 9.06e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824  51 KFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTL 130
Cdd:cd00200  10 GGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTL 89
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 70778824 131 SGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDVGTRTCIHTFFDHQDQVWGVKYNGNGSKIVSVGDDQEIHVYD 204
Cdd:cd00200  90 TGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWD 163
WD40 COG2319
WD40 repeat [General function prediction only];
2-122 1.54e-33

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 123.48  E-value: 1.54e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824   2 KSIDAGPVDAWTLAFSPDSQYLATGTHMGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIAT 81
Cdd:COG2319 282 RTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLAT 361
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 70778824  82 GKLLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQ 122
Cdd:COG2319 362 GELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
10-162 1.34e-29

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: 110.89  E-value: 1.34e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824  10 DAWTLAFSPDSQYLATGTHMGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLE 89
Cdd:cd00200 137 WVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLR 216
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 70778824  90 GHAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWD 162
Cdd:cd00200 217 GHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
15-204 2.23e-26

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 104.22  E-value: 2.23e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824  15 AFSPDSQYLATGTHMGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGHAMP 94
Cdd:COG2319   1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824  95 IRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDVGTRTCIHTFFD 174
Cdd:COG2319  81 VLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTG 160
                       170       180       190
                ....*....|....*....|....*....|
gi 70778824 175 HQDQVWGVKYNGNGSKIVSVGDDQEIHVYD 204
Cdd:COG2319 161 HSGAVTSVAFSPDGKLLASGSDDGTVRLWD 190
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
84-204 1.72e-23

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: 94.71  E-value: 1.72e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824  84 LLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDV 163
Cdd:cd00200   1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 70778824 164 GTRTCIHTFFDHQDQVWGVKYNGNGSKIVSVGDDQEIHVYD 204
Cdd:cd00200  81 ETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWD 121
WD40 COG2319
WD40 repeat [General function prediction only];
1-81 1.02e-13

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 68.78  E-value: 1.02e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824   1 MKSIDAGPVDAWTLAFSPDSQYLATGTHMGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIA 80
Cdd:COG2319 323 LRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402

                .
gi 70778824  81 T 81
Cdd:COG2319 403 T 403
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
14-101 2.21e-10

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: 55.36  E-value: 2.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824    14 LAFSPDSQYLATGTHMGKVNIFGVeSGKKEY--SLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGH 91
Cdd:pfam12894   1 MSWCPTMDLIALATEDGELLLHRL-NWQRVWtlSPDKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSAG 79
                          90
                  ....*....|
gi 70778824    92 AMPIRSLTFS 101
Cdd:pfam12894  80 SDLITCLGWG 89
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
81-120 2.44e-10

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: 53.86  E-value: 2.44e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 70778824     81 TGKLLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYD 120
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
15-122 5.64e-10

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


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 58.13  E-value: 5.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824   15 AFSPDSQYLATgthmgkvniFGVESGKKE---YSLDTRGK----------FILSIAYSPDGKYLASGAIDGIINIFDIAT 81
Cdd:COG4946  349 AWSPDGKSIAY---------FSDASGEYElyiAPADGSGEpkqltlgdlgRVFNPVWSPDGKKIAFTDNRGRLWVVDLAS 419
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 70778824   82 GK---LLHtlEGHAMPIRSLTFSPDSQLLVTASDDGY----IKIYDVQ 122
Cdd:COG4946  420 GKvrkVDT--DGYGDGISDLAWSPDSKWLAYSKPGPNqlsqIFLYDVE 465
WD40 pfam00400
WD domain, G-beta repeat;
82-120 2.35e-09

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 51.19  E-value: 2.35e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 70778824    82 GKLLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYD 120
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
3-121 4.40e-08

Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440585 [Multi-domain]  Cd Length: 158  Bit Score: 50.44  E-value: 4.40e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824   3 SIDAGPvdawtlAFSPDSQYLA-TGTHMGKVNIFGVE-SGKKEYSLDTRGKFILSIAYSPDGKYLA-SGAIDGIINIF-- 77
Cdd:COG0823  31 GIDTSP------AWSPDGRRIAfTSDRGGGPQIYVVDaDGGEPRRLTFGGGYNASPSWSPDGKRLAfVSRSDGRFDIYvl 104
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 70778824  78 DIATGKLLHTLEGHAMPirslTFSPDSQLLVTASD-DGYIKIYDV 121
Cdd:COG0823 105 DLDGGAPRRLTDGPGSP----SWSPDGRRIVFSSDrGGRPDLYVV 145
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
14-147 2.03e-07

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 50.47  E-value: 2.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824   14 LAFSPDSQYLATGTHMGKVNIFGVESGKKE--------YSLDTRGKfILSIAYSPDGK-YLASGAIDGIINIFDIATGKL 84
Cdd:PLN00181 489 IGFDRDGEFFATAGVNKKIKIFECESIIKDgrdihypvVELASRSK-LSGICWNSYIKsQVASSNFEGVVQVWDVARSQL 567
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 70778824   85 LHTLEGHAMPIRSLTF-SPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASwVLNVAFcPDDT 147
Cdd:PLN00181 568 VTEMKEHEKRVWSIDYsSADPTLLASGSDDGSVKLWSINQGVSIGTIKTKAN-ICCVQF-PSES 629
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
7-83 2.15e-07

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


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 50.42  E-value: 2.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824    7 GPVDAWTLAFSPDSQYLATGTHMGKVNIFGVESGK-KEYSLDTRGKFILSIAYSPDGKYLASGAIDG----IINIFDIAT 81
Cdd:COG4946  387 DLGRVFNPVWSPDGKKIAFTDNRGRLWVVDLASGKvRKVDTDGYGDGISDLAWSPDSKWLAYSKPGPnqlsQIFLYDVET 466

                 ..
gi 70778824   82 GK 83
Cdd:COG4946  467 GK 468
PTZ00421 PTZ00421
coronin; Provisional
14-135 2.86e-07

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 49.89  E-value: 2.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824   14 LAFSP-DSQYLATGTHMGKVNIFGV-ESGKKEYSLD--------TRGKFILSIAYSPDGkYLASGAIDGIINIFDIATGK 83
Cdd:PTZ00421  81 VAFNPfDPQKLFTASEDGTIMGWGIpEEGLTQNISDpivhlqghTKKVGIVSFHPSAMN-VLASAGADMVVNVWDVERGK 159
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 70778824   84 LLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHAS 135
Cdd:PTZ00421 160 AVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRDGTIVSSVEAHAS 211
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
3-148 3.78e-07

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 48.92  E-value: 3.78e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824   3 SIDAGPVDAWTLAFSPDSQYL-ATGTHMGKVNIFGVESGKKEYSLDTrGKFILSIAYSPDGKYL-ASGAIDGIINIFDIA 80
Cdd:COG3391  62 LGAAAVADADGADAGADGRRLyVANSGSGRVSVIDLATGKVVATIPV-GGGPRGLAVDPDGGRLyVADSGNGRVSVIDTA 140
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 70778824  81 TGKLLHTLEGHAMPiRSLTFSPDSQLLVTASDDG-----YIKIYDVQHANLAGTLSGHASWVlNVAFCPDDTH 148
Cdd:COG3391 141 TGKVVATIPVGAGP-HGIAVDPDGKRLYVANSGSntvsvIVSVIDTATGKVVATIPVGGGPV-GVAVSPDGRR 211
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
165-204 7.69e-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: 41.53  E-value: 7.69e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 70778824    165 TRTCIHTFFDHQDQVWGVKYNGNGSKIVSVGDDQEIHVYD 204
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
10-66 2.67e-05

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: 2.67e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 70778824   10 DAWTLAFSPDSQYLA----TGTHMGKVNIFGVESGKKeYSLdTRGKFI-LSIAYSPDGKYLA 66
Cdd:COG4946  433 GISDLAWSPDSKWLAyskpGPNQLSQIFLYDVETGKT-VQL-TDGRYDdGSPAFSPDGKYLY 492
PTZ00421 PTZ00421
coronin; Provisional
90-204 3.65e-05

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 43.73  E-value: 3.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824   90 GHAMPIRSLTFSP-DSQLLVTASDDGYIKIYDVQHANLAGTLS-------GHASWVLNVAFCPDDTH-FVSSSSDKSVKV 160
Cdd:PTZ00421  73 GQEGPIIDVAFNPfDPQKLFTASEDGTIMGWGIPEEGLTQNISdpivhlqGHTKKVGIVSFHPSAMNvLASAGADMVVNV 152
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 70778824  161 WDVGTRTCIHTFFDHQDQVWGVKYNGNGSKIVSVGDDQEIHVYD 204
Cdd:PTZ00421 153 WDVERGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIID 196
WDR74 cd22857
WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and ...
18-122 4.81e-05

WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and plants is an essential factor for ribosome assembly. In cooperation with the assembly factor NVL2, WDR74 participates in an early cleavage of the pre-rRNA processing pathway. NVL2 is a type II double ring, AAA-ATPase, that may mediate the release of WDR74 from nucleolar pre-60S particles. WDR74 has been implicated in tumorigenesis. In lung cancer, it regulates cell proliferation, cell cycle progression, chemoresistance and cell aggressiveness, by inducing nuclear beta-catenin accumulation and driving downstream Wnt-responsive genes expression. In melanoma, it promotes apoptosis resistance and aggressive behavior by regulating the RPL5-MDM2-p53 pathway. WDR74 contains an N-terminal seven-bladed beta-propeller WD40 domain that associates with the D1-AAA domain of the AAA-ATPase NVL2, and a flexible lysine-rich C-terminus that extends outward from the WD40 domain, and is required for nucleolar localization.


Pssm-ID: 439303 [Multi-domain]  Cd Length: 325  Bit Score: 42.98  E-value: 4.81e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824  18 PDSQYLATGTHMGKVNIFGVESGKKE-YSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGHA-MPI 95
Cdd:cd22857 190 DDHRKIVTGTGYHQVRLYDTRAQRRPvVSVDFGETPIKAVAEDPDGHTVYVGDTSGDLASIDLRTGKLLGCFKGKCgGSI 269
                        90       100
                ....*....|....*....|....*..
gi 70778824  96 RSLTFSPDSQLLVTASDDGYIKIYDVQ 122
Cdd:cd22857 270 RSIARHPELPLIASCGLDRYLRIWDTE 296
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
39-78 1.34e-04

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 38.06  E-value: 1.34e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 70778824     39 SGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFD 78
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
8prop_hemeD1_NirF cd20778
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ...
11-120 1.35e-04

eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; Denitrification is a process that enables biofilm formation of the opportunistic human pathogen Pseudomonas aeruginosa, making it more resilient to antibiotics and highly adaptable to different habitats. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO3- -> NO2- -> 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 cytochrome cd1 (nitrite reductase) NirS via its maturation factor NirF. The nirFDLGHJE genes encode proteins required for heme d1 biosynthesis. NirS, NirF, and NirN, the monomeric dihydro-heme d1 dehydrogenase form a stable complex during nitrite reductase maturation. The nitrite reductase NirS is bound to the denitrification supercomplex via NorB, while the electron donor system NirM and the enzyme maturation machinery NirN-NirF-NirQ, interacting with NirS, are bound via NorC.


Pssm-ID: 467722 [Multi-domain]  Cd Length: 381  Bit Score: 41.89  E-value: 1.35e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824  11 AWtlAFSPDSQYL-ATGTHmgKVNIFGVESGKKEYSLDTRGKFILSIAySPDGKYLA---SGAIDGIINIFDIATGKLLH 86
Cdd:cd20778 245 GW--AVAGDKAFVpAVGEH--RVLVYDTNDWKFIKSIPLAGQPVFAVA-RPDGRYVWvnfSGPDNDTVQVIDTKTLKVVK 319
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 70778824  87 TLE--GHAMPIRsltFSPD-SQLLVTASDDGYIKIYD 120
Cdd:cd20778 320 TLEpgKRVLHME---FTPRgEAVYISVNDDNKVVVYD 353
Nsa1_WDR74-like cd22850
Ribosome biogenesis protein Nsa1 and similar proteins; Ribosome biogenesis protein Nsa1 ...
26-86 1.41e-04

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: 41.85  E-value: 1.41e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 70778824  26 GTHMGKVNIFGVESGKKEYSLdtRGKF---ILSIAYSPD--GKYLASGAIDGIINIFDIATGKLLH 86
Cdd:cd22850 250 GDTSGDLALIDIRTGKLLGRL--LGKYggsITGAVRHPElfDPYLASGGLDRYLRVFDIETRELLA 313
eIF2A pfam08662
Eukaryotic translation initiation factor eIF2A; This is a family of eukaryotic translation ...
45-149 1.71e-04

Eukaryotic translation initiation factor eIF2A; This is a family of eukaryotic translation initiation factors.


Pssm-ID: 462552 [Multi-domain]  Cd Length: 194  Bit Score: 40.72  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824    45 SLDTRGKfILSIAYSPDGK--YLASGAIDGIINIFDiATGKLLHTLEGHamPIRSLTFSPDSQLLVTA---SDDGYIKIY 119
Cdd:pfam08662  55 ELDKEGP-IHDVAWSPNGKefAVIYGYMPAKVSFFD-LKGNVIHSFGEQ--PRNTIFWSPFGRLVLLAgfgNLAGDIEFW 130
                          90       100       110
                  ....*....|....*....|....*....|
gi 70778824   120 DVQHANLAGTLsgHASWVLNVAFCPDDTHF 149
Cdd:pfam08662 131 DVVNKKKIATA--EASNATLCEWSPDGRYF 158
WD40 pfam00400
WD domain, G-beta repeat;
166-204 4.30e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.55  E-value: 4.30e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 70778824   166 RTCIHTFFDHQDQVWGVKYNGNGSKIVSVGDDQEIHVYD 204
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
40-78 4.94e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.55  E-value: 4.94e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 70778824    40 GKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFD 78
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WDR74 cd22857
WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and ...
3-86 8.38e-04

WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and plants is an essential factor for ribosome assembly. In cooperation with the assembly factor NVL2, WDR74 participates in an early cleavage of the pre-rRNA processing pathway. NVL2 is a type II double ring, AAA-ATPase, that may mediate the release of WDR74 from nucleolar pre-60S particles. WDR74 has been implicated in tumorigenesis. In lung cancer, it regulates cell proliferation, cell cycle progression, chemoresistance and cell aggressiveness, by inducing nuclear beta-catenin accumulation and driving downstream Wnt-responsive genes expression. In melanoma, it promotes apoptosis resistance and aggressive behavior by regulating the RPL5-MDM2-p53 pathway. WDR74 contains an N-terminal seven-bladed beta-propeller WD40 domain that associates with the D1-AAA domain of the AAA-ATPase NVL2, and a flexible lysine-rich C-terminus that extends outward from the WD40 domain, and is required for nucleolar localization.


Pssm-ID: 439303 [Multi-domain]  Cd Length: 325  Bit Score: 39.52  E-value: 8.38e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824   3 SIDAGPVDAWTLAFSPDSQYLATGTHMGKVNIFGVESGKKEYSLdtRGK---FILSIAYSPDGKYLASGAIDGIINIFDI 79
Cdd:cd22857 218 SVDFGETPIKAVAEDPDGHTVYVGDTSGDLASIDLRTGKLLGCF--KGKcggSIRSIARHPELPLIASCGLDRYLRIWDT 295

                ....*..
gi 70778824  80 ATGKLLH 86
Cdd:cd22857 296 ETRQLLS 302
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
88-143 1.11e-03

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: 36.87  E-value: 1.11e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 70778824    88 LEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFC 143
Cdd:pfam12894  34 PDKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSAGSDLITCLGWG 89
Pgl COG2706
6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism];
56-131 2.29e-03

6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism];


Pssm-ID: 442025 [Multi-domain]  Cd Length: 352  Bit Score: 37.96  E-value: 2.29e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70778824  56 IAYSPDGKYL-ASGAIDGIINIFDI--ATGKLlhTLEGH-----AMPiRSLTFSPDSQLLVTAS-DDGYIKIYDVQHANl 126
Cdd:COG2706 256 IHISPDGRFLyVSNRGHNSIAVFAIdaDGGKL--TLVGHvptggKWP-RDFAIDPDGRFLLVANqKSDNITVFRIDADT- 331

                ....*
gi 70778824 127 aGTLS 131
Cdd:COG2706 332 -GKLT 335
PQQ_ABC_repeats TIGR03866
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family ...
71-132 5.50e-03

PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family consist of seven repeats each of the YVTN family beta-propeller repeat (see TIGR02276). Members occur invariably as part of a transport operon that is associated with PQQ-dependent catabolism of alcohols such as phenylethanol.


Pssm-ID: 274824 [Multi-domain]  Cd Length: 310  Bit Score: 36.94  E-value: 5.50e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 70778824    71 DGIINIFDIATGKLLHTLEGHAMPiRSLTFSPDSQLL-VTASDDGYIKIYDVQHANLAGTL-SG 132
Cdd:TIGR03866  20 DNTISVIDTATLKVTRTFPVGQRP-RGITFSKDGKLLyVCASDSDTIQVIDPATGEVLHTLpSG 82
 
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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