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Conserved domains on  [gi|735997339|ref|NP_001290177|]
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superkiller complex protein 8 isoform b [Homo sapiens]

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
17-209 2.09e-57

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 186.27  E-value: 2.09e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339  17 WTLAFSPDSQYLATGTHVGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGH 96
Cdd:COG2319  208 RSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGH 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339  97 AMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDVGTRTCVHT 176
Cdd:COG2319  288 SGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRT 367

                        170       180       190
                 ....*....|....*....|....*....|...
gi 735997339 177 FFDHQDQVWGVKYNGNGSKIVSVGDDQEIHIYD 209
Cdd:COG2319  368 LTGHTGAVTSVAFSPDGRTLASGSADGTVRLWD 400
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
17-209 2.09e-57

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 186.27  E-value: 2.09e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339  17 WTLAFSPDSQYLATGTHVGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGH 96
Cdd:COG2319  208 RSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGH 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339  97 AMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDVGTRTCVHT 176
Cdd:COG2319  288 SGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRT 367

                        170       180       190
                 ....*....|....*....|....*....|...
gi 735997339 177 FFDHQDQVWGVKYNGNGSKIVSVGDDQEIHIYD 209
Cdd:COG2319  368 LTGHTGAVTSVAFSPDGRTLASGSADGTVRLWD 400
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 17-209 2.22e-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: 154.80  E-value: 2.22e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339  17 WTLAFSPDSQYLATGTHVGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGH 96
Cdd:cd00200   97 SSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGH 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339  97 AMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDVGTRTCVHT 176
Cdd:cd00200  177 TGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQT 256

                        170       180       190
                 ....*....|....*....|....*....|...
gi 735997339 177 FFDHQDQVWGVKYNGNGSKIVSVGDDQEIHIYD 209
Cdd:cd00200  257 LSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 86-125 1.64e-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: 54.24  E-value: 1.64e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 735997339    86 TGKLLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYD 125
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 19-106 2.01e-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: 2.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339   19 LAFSPDSQYLATGTHVGKVNIFGVeSGKKEY--SLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGH 96
Cdd:pfam12894   1 MSWCPTMDLIALATEDGELLLHRL-NWQRVWtlSPDKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSAG 79

                          90
                  ....*....|
gi 735997339   97 AMPIRSLTFS 106
Cdd:pfam12894  80 SDLITCLGWG 89
PTZ00421 PTZ00421
coronin; Provisional
 7-140 2.18e-07

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 50.28  E-value: 2.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339   7 ILFKQEQvDAWTLAFSP-DSQYLATGTHVGKVNIFGV-ESGKKEYSLD--------TRGKFILSIAYSPDGkYLASGAID 76
Cdd:PTZ00421  70 ILLGQEG-PIIDVAFNPfDPQKLFTASEDGTIMGWGIpEEGLTQNISDpivhlqghTKKVGIVSFHPSAMN-VLASAGAD 147

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 735997339  77 GIINIFDIATGKLLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHAS 140
Cdd:PTZ00421 148 MVVNVWDVERGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRDGTIVSSVEAHAS 211
PQQ_ABC_repeats TIGR03866
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family ...
 76-137 4.79e-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: 4.79e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 735997339   76 DGIINIFDIATGKLLHTLEGHAMPiRSLTFSPDSQLL-VTASDDGYIKIYDVQHANLAGTL-SG 137
Cdd:TIGR03866  20 DNTISVIDTATLKVTRTFPVGQRP-RGITFSKDGKLLyVCASDSDTIQVIDPATGEVLHTLpSG 82
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
17-209 2.09e-57

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 186.27  E-value: 2.09e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339  17 WTLAFSPDSQYLATGTHVGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGH 96
Cdd:COG2319  208 RSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGH 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339  97 AMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDVGTRTCVHT 176
Cdd:COG2319  288 SGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRT 367

                        170       180       190
                 ....*....|....*....|....*....|...
gi 735997339 177 FFDHQDQVWGVKYNGNGSKIVSVGDDQEIHIYD 209
Cdd:COG2319  368 LTGHTGAVTSVAFSPDGRTLASGSADGTVRLWD 400
WD40 COG2319
WD40 repeat [General function prediction only];
17-209 6.87e-57

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 185.11  E-value: 6.87e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339  17 WTLAFSPDSQYLATGTHVGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGH 96
Cdd:COG2319  124 RSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGH 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339  97 AMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDVGTRTCVHT 176
Cdd:COG2319  204 TGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRT 283

                        170       180       190
                 ....*....|....*....|....*....|...
gi 735997339 177 FFDHQDQVWGVKYNGNGSKIVSVGDDQEIHIYD 209
Cdd:COG2319  284 LTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWD 316
WD40 COG2319
WD40 repeat [General function prediction only];
17-209 2.09e-56

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 183.57  E-value: 2.09e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339  17 WTLAFSPDSQYLATGTHVGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGH 96
Cdd:COG2319  166 TSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGH 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339  97 AMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDVGTRTCVHT 176
Cdd:COG2319  246 SGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRT 325

                        170       180       190
                 ....*....|....*....|....*....|...
gi 735997339 177 FFDHQDQVWGVKYNGNGSKIVSVGDDQEIHIYD 209
Cdd:COG2319  326 LTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWD 358
WD40 COG2319
WD40 repeat [General function prediction only];
16-209 8.87e-53

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 174.33  E-value: 8.87e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339  16 AWTLAFSPDSQYLATGTHVGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEG 95
Cdd:COG2319   81 VLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTG 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339  96 HAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDVGTRTCVH 175
Cdd:COG2319  161 HSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLR 240

                        170       180       190
                 ....*....|....*....|....*....|....
gi 735997339 176 TFFDHQDQVWGVKYNGNGSKIVSVGDDQEIHIYD 209
Cdd:COG2319  241 TLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWD 274
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 17-209 2.22e-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: 154.80  E-value: 2.22e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339  17 WTLAFSPDSQYLATGTHVGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGH 96
Cdd:cd00200   97 SSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGH 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339  97 AMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDVGTRTCVHT 176
Cdd:cd00200  177 TGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQT 256

                        170       180       190
                 ....*....|....*....|....*....|...
gi 735997339 177 FFDHQDQVWGVKYNGNGSKIVSVGDDQEIHIYD 209
Cdd:cd00200  257 LSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 19-209 8.97e-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: 8.97e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339  19 LAFSPDSQYLATGTHVGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGHAM 98
Cdd:cd00200   15 VAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLTGHTS 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339  99 PIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDVGTRTCVHTFF 178
Cdd:cd00200   95 YVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLT 174

                        170       180       190
                 ....*....|....*....|....*....|.
gi 735997339 179 DHQDQVWGVKYNGNGSKIVSVGDDQEIHIYD 209
Cdd:cd00200  175 GHTGEVNSVAFSPDGEKLLSSSSDGTIKLWD 205
WD40 COG2319
WD40 repeat [General function prediction only];
15-209 3.29e-42

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 146.59  E-value: 3.29e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339  15 DAWTLAFSPDSQYLATGTHVGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLE 94
Cdd:COG2319   38 AVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLT 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339  95 GHAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDVGTRTCV 174
Cdd:COG2319  118 GHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLL 197

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 735997339 175 HTFFDHQDQVWGVKYNGNGSKIVSVGDDQEIHIYD 209
Cdd:COG2319  198 RTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWD 232
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 2-209 1.13e-41

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: 142.47  E-value: 1.13e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339   2 TNQYGILFKQEQVDAWTLAFSPDSQYLATGTHVGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINI 81
Cdd:cd00200   40 TGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKV 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339  82 FDIATGKLLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDK 161
Cdd:cd00200  120 WDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDG 199

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 735997339 162 SVKVWDVGTRTCVHTFFDHQDQVWGVKYNGNGSKIVSVGDDQEIHIYD 209
Cdd:cd00200  200 TIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWD 247
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 56-209 4.48e-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: 125.53  E-value: 4.48e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339  56 KFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTL 135
Cdd:cd00200   10 GGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTL 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 735997339 136 SGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDVGTRTCVHTFFDHQDQVWGVKYNGNGSKIVSVGDDQEIHIYD 209
Cdd:cd00200   90 TGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWD 163
WD40 COG2319
WD40 repeat [General function prediction only];
2-127 2.21e-34

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 126.18  E-value: 2.21e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339   2 TNQYGILFKQEQVDAWTLAFSPDSQYLATGTHVGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINI 81
Cdd:COG2319  277 TGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRL 356

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 735997339  82 FDIATGKLLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQ 127
Cdd:COG2319  357 WDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 15-167 7.94e-30

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: 111.66  E-value: 7.94e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339  15 DAWTLAFSPDSQYLATGTHVGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLE 94
Cdd:cd00200  137 WVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLR 216

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 735997339  95 GHAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWD 167
Cdd:cd00200  217 GHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
20-209 6.82e-27

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 105.76  E-value: 6.82e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339  20 AFSPDSQYLATGTHVGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGHAMP 99
Cdd:COG2319    1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339 100 IRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDVGTRTCVHTFFD 179
Cdd:COG2319   81 VLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTG 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 735997339 180 HQDQVWGVKYNGNGSKIVSVGDDQEIHIYD 209
Cdd:COG2319  161 HSGAVTSVAFSPDGKLLASGSDDGTVRLWD 190
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 9-125 4.74e-24

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: 96.25  E-value: 4.74e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339   9 FKQEQVDAWTLAFSPDSQYLATGTHVGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGK 88
Cdd:cd00200  173 LTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGE 252

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 735997339  89 LLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYD 125
Cdd:cd00200  253 CVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 89-209 9.92e-24

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: 95.48  E-value: 9.92e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339  89 LLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDV 168
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 735997339 169 GTRTCVHTFFDHQDQVWGVKYNGNGSKIVSVGDDQEIHIYD 209
Cdd:cd00200   81 ETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWD 121
WD40 COG2319
WD40 repeat [General function prediction only];
9-86 2.84e-14

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 70.33  E-value: 2.84e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 735997339   9 FKQEQVDAWTLAFSPDSQYLATGTHVGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIAT 86
Cdd:COG2319  326 LTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 86-125 1.64e-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: 54.24  E-value: 1.64e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 735997339    86 TGKLLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYD 125
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 19-106 2.01e-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: 2.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339   19 LAFSPDSQYLATGTHVGKVNIFGVeSGKKEY--SLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGH 96
Cdd:pfam12894   1 MSWCPTMDLIALATEDGELLLHRL-NWQRVWtlSPDKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSAG 79

                          90
                  ....*....|
gi 735997339   97 AMPIRSLTFS 106
Cdd:pfam12894  80 SDLITCLGWG 89
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 20-127 3.18e-10

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


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 58.90  E-value: 3.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339   20 AFSPDSQYLATGTHVG---KVNIFGVESGKKEYSL-DTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGK---LLHt 92
Cdd:COG4946   349 AWSPDGKSIAYFSDASgeyELYIAPADGSGEPKQLtLGDLGRVFNPVWSPDGKKIAFTDNRGRLWVVDLASGKvrkVDT- 427

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 735997339   93 lEGHAMPIRSLTFSPDSQLLVTASDDGY----IKIYDVQ 127
Cdd:COG4946   428 -DGYGDGISDLAWSPDSKWLAYSKPGPNqlsqIFLYDVE 465
WD40 pfam00400
WD domain, G-beta repeat;
87-125 1.58e-09

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 51.58  E-value: 1.58e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 735997339   87 GKLLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYD 125
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
 20-126 5.10e-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: 5.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339  20 AFSPDSQYLA-TGTHVGKVNIFGVE-SGKKEYSLDTRGKFILSIAYSPDGKYLA-SGAIDGIINIF--DIATGKLLHTLE 94
Cdd:COG0823   37 AWSPDGRRIAfTSDRGGGPQIYVVDaDGGEPRRLTFGGGYNASPSWSPDGKRLAfVSRSDGRFDIYvlDLDGGAPRRLTD 116

                         90       100       110
                 ....*....|....*....|....*....|...
gi 735997339  95 GHAMPirslTFSPDSQLLVTASD-DGYIKIYDV 126
Cdd:COG0823  117 GPGSP----SWSPDGRRIVFSSDrGGRPDLYVV 145
PTZ00421 PTZ00421
coronin; Provisional
 7-140 2.18e-07

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 50.28  E-value: 2.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339   7 ILFKQEQvDAWTLAFSP-DSQYLATGTHVGKVNIFGV-ESGKKEYSLD--------TRGKFILSIAYSPDGkYLASGAID 76
Cdd:PTZ00421  70 ILLGQEG-PIIDVAFNPfDPQKLFTASEDGTIMGWGIpEEGLTQNISDpivhlqghTKKVGIVSFHPSAMN-VLASAGAD 147

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 735997339  77 GIINIFDIATGKLLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHAS 140
Cdd:PTZ00421 148 MVVNVWDVERGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRDGTIVSSVEAHAS 211
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 19-152 2.82e-07

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 50.09  E-value: 2.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339  19 LAFSPDSQYLATGTHVGKVNIFGVESGKKE--------YSLDTRGKfILSIAYSPDGK-YLASGAIDGIINIFDIATGKL 89
Cdd:PLN00181 489 IGFDRDGEFFATAGVNKKIKIFECESIIKDgrdihypvVELASRSK-LSGICWNSYIKsQVASSNFEGVVQVWDVARSQL 567

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 735997339  90 LHTLEGHAMPIRSLTF-SPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASwVLNVAFcPDDT 152
Cdd:PLN00181 568 VTEMKEHEKRVWSIDYsSADPTLLASGSDDGSVKLWSINQGVSIGTIKTKAN-ICCVQF-PSES 629
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
29-153 3.93e-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: 3.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339  29 ATGTHVGKVNIFGVESGKKEYSLDTrGKFILSIAYSPDGKYL-ASGAIDGIINIFDIATGKLLHTLEGHAMPiRSLTFSP 107
Cdd:COG3391   84 VANSGSGRVSVIDLATGKVVATIPV-GGGPRGLAVDPDGGRLyVADSGNGRVSVIDTATGKVVATIPVGAGP-HGIAVDP 161

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 735997339 108 DSQLLVTASDDG-----YIKIYDVQHANLAGTLSGHASWVlNVAFCPDDTH 153
Cdd:COG3391  162 DGKRLYVANSGSntvsvIVSVIDTATGKVVATIPVGGGPV-GVAVSPDGRR 211
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 17-88 5.62e-07

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


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 49.27  E-value: 5.62e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 735997339   17 WTLAFSPDSQYLATGTHVGKVNIFGVESGK-KEYSLDTRGKFILSIAYSPDGKYLASGAIDG----IINIFDIATGK 88
Cdd:COG4946   392 FNPVWSPDGKKIAFTDNRGRLWVVDLASGKvRKVDTDGYGDGISDLAWSPDSKWLAYSKPGPnqlsQIFLYDVETGK 468
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 170-209 4.70e-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: 42.30  E-value: 4.70e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 735997339   170 TRTCVHTFFDHQDQVWGVKYNGNGSKIVSVGDDQEIHIYD 209
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PTZ00421 PTZ00421
coronin; Provisional
 95-209 1.13e-05

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 45.27  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339  95 GHAMPIRSLTFSP-DSQLLVTASDDGYIKIYDVQHANLAGTLS-------GHASWVLNVAFCPDDTH-FVSSSSDKSVKV 165
Cdd:PTZ00421  73 GQEGPIIDVAFNPfDPQKLFTASEDGTIMGWGIPEEGLTQNISdpivhlqGHTKKVGIVSFHPSAMNvLASAGADMVVNV 152

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 735997339 166 WDVGTRTCVHTFFDHQDQVWGVKYNGNGSKIVSVGDDQEIHIYD 209
Cdd:PTZ00421 153 WDVERGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIID 196
WDR74 cd22857
WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and ...
 19-127 5.09e-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: 5.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339  19 LAF-SPDSQY-LATGTHVGKVNIFGVESGKKE-YSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEG 95
Cdd:cd22857  184 LTFlSKDDHRkIVTGTGYHQVRLYDTRAQRRPvVSVDFGETPIKAVAEDPDGHTVYVGDTSGDLASIDLRTGKLLGCFKG 263

                         90       100       110
                 ....*....|....*....|....*....|...
gi 735997339  96 HA-MPIRSLTFSPDSQLLVTASDDGYIKIYDVQ 127
Cdd:cd22857  264 KCgGSIRSIARHPELPLIASCGLDRYLRIWDTE 296
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 15-71 5.10e-05

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


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 43.49  E-value: 5.10e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 735997339   15 DAWTLAFSPDSQYLA----TGTHVGKVNIFGVESGKKeYSLdTRGKFI-LSIAYSPDGKYLA 71
Cdd:COG4946   433 GISDLAWSPDSKWLAyskpGPNQLSQIFLYDVETGKT-VQL-TDGRYDdGSPAFSPDGKYLY 492
Nsa1_WDR74-like cd22850
Ribosome biogenesis protein Nsa1 and similar proteins; Ribosome biogenesis protein Nsa1 ...
 31-91 9.46e-05

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: 42.23  E-value: 9.46e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 735997339  31 GTHVGKVNIFGVESGKKEYSLdtRGKF---ILSIAYSPD--GKYLASGAIDGIINIFDIATGKLLH 91
Cdd:cd22850  250 GDTSGDLALIDIRTGKLLGRL--LGKYggsITGAVRHPElfDPYLASGGLDRYLRVFDIETRELLA 313
8prop_hemeD1_NirF cd20778
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ...
 16-125 9.82e-05

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: 42.27  E-value: 9.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339  16 AWtlAFSPDSQYL-ATGTHvgKVNIFGVESGKKEYSLDTRGKFILSIAySPDGKYLA---SGAIDGIINIFDIATGKLLH 91
Cdd:cd20778  245 GW--AVAGDKAFVpAVGEH--RVLVYDTNDWKFIKSIPLAGQPVFAVA-RPDGRYVWvnfSGPDNDTVQVIDTKTLKVVK 319

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 735997339  92 TLE--GHAMPIRsltFSPD-SQLLVTASDDGYIKIYD 125
Cdd:cd20778  320 TLEpgKRVLHME---FTPRgEAVYISVNDDNKVVVYD 353
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 44-83 1.06e-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: 38.45  E-value: 1.06e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 735997339    44 SGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFD 83
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
eIF2A pfam08662
Eukaryotic translation initiation factor eIF2A; This is a family of eukaryotic translation ...
 50-154 2.16e-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: 2.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339   50 SLDTRGKfILSIAYSPDGK--YLASGAIDGIINIFDiATGKLLHTLEGHamPIRSLTFSPDSQLLVTA---SDDGYIKIY 124
Cdd:pfam08662  55 ELDKEGP-IHDVAWSPNGKefAVIYGYMPAKVSFFD-LKGNVIHSFGEQ--PRNTIFWSPFGRLVLLAgfgNLAGDIEFW 130

                          90       100       110
                  ....*....|....*....|....*....|
gi 735997339  125 DVQHANLAGTLsgHASWVLNVAFCPDDTHF 154
Cdd:pfam08662 131 DVVNKKKIATA--EASNATLCEWSPDGRYF 158
WD40 pfam00400
WD domain, G-beta repeat;
171-209 2.70e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 37.32  E-value: 2.70e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 735997339  171 RTCVHTFFDHQDQVWGVKYNGNGSKIVSVGDDQEIHIYD 209
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
45-83 3.82e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.94  E-value: 3.82e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 735997339   45 GKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFD 83
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 93-148 9.95e-04

Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC,


Pssm-ID: 403945 [Multi-domain]  Cd Length: 91  Bit Score: 36.87  E-value: 9.95e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 735997339   93 LEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFC 148
Cdd:pfam12894  34 PDKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSAGSDLITCLGWG 89
Pgl COG2706
6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism];
61-136 1.87e-03

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


Pssm-ID: 442025 [Multi-domain]  Cd Length: 352  Bit Score: 38.35  E-value: 1.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997339  61 IAYSPDGKYL-ASGAIDGIINIFDI--ATGKLlhTLEGH-----AMPiRSLTFSPDSQLLVTAS-DDGYIKIYDVQHANl 131
Cdd:COG2706  256 IHISPDGRFLyVSNRGHNSIAVFAIdaDGGKL--TLVGHvptggKWP-RDFAIDPDGRFLLVANqKSDNITVFRIDADT- 331


                 ....*
gi 735997339 132 aGTLS 136
Cdd:COG2706  332 -GKLT 335
PQQ_ABC_repeats TIGR03866
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family ...
 76-137 4.79e-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: 4.79e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 735997339   76 DGIINIFDIATGKLLHTLEGHAMPiRSLTFSPDSQLL-VTASDDGYIKIYDVQHANLAGTL-SG 137
Cdd:TIGR03866  20 DNTISVIDTATLKVTRTFPVGQRP-RGITFSKDGKLLyVCASDSDTIQVIDPATGEVLHTLpSG 82
WDR74 cd22857
WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and ...
 17-91 8.49e-03

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: 36.44  E-value: 8.49e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 735997339  17 WTLAFSPDSQYLATGTHVGKVNIFGVESGKKEYSLdtRGK---FILSIAYSPDGKYLASGAIDGIINIFDIATGKLLH 91
Cdd:cd22857  227 KAVAEDPDGHTVYVGDTSGDLASIDLRTGKLLGCF--KGKcggSIRSIARHPELPLIASCGLDRYLRIWDTETRQLLS 302
 
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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