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Conserved domains on  [gi|1907199447|ref|XP_036011067|]
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superkiller complex protein 8 isoform X1 [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];
13-302 1.21e-74

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 234.42  E-value: 1.21e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447  13 QAHDDAIWSVAWETNKKenieTVVTGSLDDLVKVWKWRDERLelQWSLEGHQLGVVSVDISHTLPIAASSSLDAHIRLWD 92
Cdd:COG2319   117 TGHTGAVRSVAFSPDGK----TLASGSADGTVRLWDLATGKL--LRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWD 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447  93 LENGKQMKSIDAGPVDAWTLAFSPDSQYLATGTHMGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGII 172
Cdd:COG2319   191 LATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTV 270

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447 173 NIFDIATGKLLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSS 252
Cdd:COG2319   271 RLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSD 350

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907199447 253 DKSVKVWDVGTRTCIHTFFDHQDQVWGVKYNGNGSKIVSVGDDQEIHVYD 302
Cdd:COG2319   351 DGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWD 400
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
13-302 1.21e-74

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 234.42  E-value: 1.21e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447  13 QAHDDAIWSVAWETNKKenieTVVTGSLDDLVKVWKWRDERLelQWSLEGHQLGVVSVDISHTLPIAASSSLDAHIRLWD 92
Cdd:COG2319   117 TGHTGAVRSVAFSPDGK----TLASGSADGTVRLWDLATGKL--LRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWD 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447  93 LENGKQMKSIDAGPVDAWTLAFSPDSQYLATGTHMGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGII 172
Cdd:COG2319   191 LATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTV 270

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447 173 NIFDIATGKLLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSS 252
Cdd:COG2319   271 RLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSD 350

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907199447 253 DKSVKVWDVGTRTCIHTFFDHQDQVWGVKYNGNGSKIVSVGDDQEIHVYD 302
Cdd:COG2319   351 DGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWD 400
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 13-302 2.34e-61

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: 196.40  E-value: 2.34e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447  13 QAHDDAIWSVAWETNKKenieTVVTGSLDDLVKVWKWRDERLELQwsLEGHQLGVVSVDISHTLPIAASSSLDAHIRLWD 92
Cdd:cd00200     6 KGHTGGVTCVAFSPDGK----LLATGSGDGTIKVWDLETGELLRT--LKGHTGPVRDVAASADGTYLASGSSDKTIRLWD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447  93 LENGKQMKSI--DAGPVdaWTLAFSPDSQYLATGTHMGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDG 170
Cdd:cd00200    80 LETGECVRTLtgHTSYV--SSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447 171 IINIFDIATGKLLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSS 250
Cdd:cd00200   158 TIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASG 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907199447 251 SSDKSVKVWDVGTRTCIHTFFDHQDQVWGVKYNGNGSKIVSVGDDQEIHVYD 302
Cdd:cd00200   238 SEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 179-218 6.61e-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: 53.47  E-value: 6.61e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1907199447  179 TGKLLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYD 218
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 112-199 2.77e-09

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: 53.44  E-value: 2.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447 112 LAFSPDSQYLATGTHMGKVNIFGVeSGKKEY--SLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGH 189
Cdd:pfam12894   1 MSWCPTMDLIALATEDGELLLHRL-NWQRVWtlSPDKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSAG 79

                          90
                  ....*....|
gi 1907199447 190 AMPIRSLTFS 199
Cdd:pfam12894  80 SDLITCLGWG 89
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 80-219 9.89e-09

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 56.25  E-value: 9.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447  80 ASSSLDAHIRLWDLENGKQMKSIDAGPVDAWTLAF-SPDSQYLATGTHMGKVNIFGVESGKKEYSLDTRGKFILSIAYSP 158
Cdd:PLN00181  549 ASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYsSADPTLLASGSDDGSVKLWSINQGVSIGTIKTKANICCVQFPSE 628

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907199447 159 DGKYLASGAIDGIINIFDIATGKL-LHTLEGHAMPIRSLTFSpDSQLLVTASDDGYIKIYDV 219
Cdd:PLN00181  629 SGRSLAFGSADHKVYYYDLRNPKLpLCTMIGHSKTVSYVRFV-DSSTLVSSSTDNTLKLWDL 689
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
13-302 1.21e-74

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 234.42  E-value: 1.21e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447  13 QAHDDAIWSVAWETNKKenieTVVTGSLDDLVKVWKWRDERLelQWSLEGHQLGVVSVDISHTLPIAASSSLDAHIRLWD 92
Cdd:COG2319   117 TGHTGAVRSVAFSPDGK----TLASGSADGTVRLWDLATGKL--LRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWD 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447  93 LENGKQMKSIDAGPVDAWTLAFSPDSQYLATGTHMGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGII 172
Cdd:COG2319   191 LATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTV 270

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447 173 NIFDIATGKLLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSS 252
Cdd:COG2319   271 RLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSD 350

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907199447 253 DKSVKVWDVGTRTCIHTFFDHQDQVWGVKYNGNGSKIVSVGDDQEIHVYD 302
Cdd:COG2319   351 DGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWD 400
WD40 COG2319
WD40 repeat [General function prediction only];
36-302 5.88e-65

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 209.38  E-value: 5.88e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447  36 VTGSLDDLVKVWKWRDERLELQWSLEGHQLGVVSVDISHTLPIAASSSLDAHIRLWDLENGKQMKSIDAGPVDAWTLAFS 115
Cdd:COG2319    50 RLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFS 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447 116 PDSQYLATGTHMGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGHAMPIRS 195
Cdd:COG2319   130 PDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRS 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447 196 LTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDVGTRTCIHTFFDHQD 275
Cdd:COG2319   210 VAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSG 289

                         250       260
                  ....*....|....*....|....*..
gi 1907199447 276 QVWGVKYNGNGSKIVSVGDDQEIHVYD 302
Cdd:COG2319   290 GVNSVAFSPDGKLLASGSDDGTVRLWD 316
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 13-302 2.34e-61

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: 196.40  E-value: 2.34e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447  13 QAHDDAIWSVAWETNKKenieTVVTGSLDDLVKVWKWRDERLELQwsLEGHQLGVVSVDISHTLPIAASSSLDAHIRLWD 92
Cdd:cd00200     6 KGHTGGVTCVAFSPDGK----LLATGSGDGTIKVWDLETGELLRT--LKGHTGPVRDVAASADGTYLASGSSDKTIRLWD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447  93 LENGKQMKSI--DAGPVdaWTLAFSPDSQYLATGTHMGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDG 170
Cdd:cd00200    80 LETGECVRTLtgHTSYV--SSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447 171 IINIFDIATGKLLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSS 250
Cdd:cd00200   158 TIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASG 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907199447 251 SSDKSVKVWDVGTRTCIHTFFDHQDQVWGVKYNGNGSKIVSVGDDQEIHVYD 302
Cdd:cd00200   238 SEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
36-302 7.59e-57

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 188.20  E-value: 7.59e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447  36 VTGSLDDLVKVWKWRDERLELQWSLEGHQLGVVSVDISHTLPIAASSSLDAHIRLWDLENGKQMKSIDAGPVDAWTLAFS 115
Cdd:COG2319     8 ALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447 116 PDSQYLATGTHMGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGHAMPIRS 195
Cdd:COG2319    88 PDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTS 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447 196 LTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDVGTRTCIHTFFDHQD 275
Cdd:COG2319   168 VAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSG 247

                         250       260
                  ....*....|....*....|....*..
gi 1907199447 276 QVWGVKYNGNGSKIVSVGDDQEIHVYD 302
Cdd:COG2319   248 SVRSVAFSPDGRLLASGSADGTVRLWD 274
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 60-302 2.98e-49

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: 165.20  E-value: 2.98e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447  60 LEGHQLGVVSVDISHTLPIAASSSLDAHIRLWDLENGKQMKSIDAGPVDAWTLAFSPDSQYLATGTHMGKVNIFGVESGK 139
Cdd:cd00200     5 LKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447 140 KEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYDV 219
Cdd:cd00200    85 CVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447 220 QHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDVGTRTCIHTFFDHQDQVWGVKYNGNGSKIVSVGDDQEIH 299
Cdd:cd00200   165 RTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIR 244


                  ...
gi 1907199447 300 VYD 302
Cdd:cd00200   245 VWD 247
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 8-260 3.24e-49

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: 165.20  E-value: 3.24e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447   8 LFKQEQAHDDAIWSVAWETNKKenieTVVTGSLDDLVKVWKWRDErlELQWSLEGHQLGVVSVDISHTLPIAASSSLDAH 87
Cdd:cd00200    43 LLRTLKGHTGPVRDVAASADGT----YLASGSSDKTIRLWDLETG--ECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKT 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447  88 IRLWDLENGKQMKSIDAGPVDAWTLAFSPDSQYLATGTHMGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGA 167
Cdd:cd00200   117 IKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSS 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447 168 IDGIINIFDIATGKLLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHF 247
Cdd:cd00200   197 SDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRL 276

                         250
                  ....*....|...
gi 1907199447 248 VSSSSDKSVKVWD 260
Cdd:cd00200   277 ASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 182-302 3.26e-22

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: 93.94  E-value: 3.26e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447 182 LLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDV 261
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907199447 262 GTRTCIHTFFDHQDQVWGVKYNGNGSKIVSVGDDQEIHVYD 302
Cdd:cd00200    81 ETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWD 121
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
78-212 1.43e-12

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 65.87  E-value: 1.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447  78 IAASSSLDAHIRLWDLENGKQMKSIDAGPvDAWTLAFSPDSQYL-ATGTHMGKVNIFGVESGKKEYSLDTrGKFILSIAY 156
Cdd:COG3391    82 LYVANSGSGRVSVIDLATGKVVATIPVGG-GPRGLAVDPDGGRLyVADSGNGRVSVIDTATGKVVATIPV-GAGPHGIAV 159

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907199447 157 SPDGKYL-----ASGAIDGIINIFDIATGKLLHTLEGHAMPIrSLTFSPD-SQLLVTASDDG 212
Cdd:COG3391   160 DPDGKRLyvansGSNTVSVIVSVIDTATGKVVATIPVGGGPV-GVAVSPDgRRLYVANRGSN 220
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 179-218 6.61e-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: 53.47  E-value: 6.61e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1907199447  179 TGKLLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYD 218
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
 78-219 6.95e-10

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: 56.60  E-value: 6.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447  78 IAASSSLD--AHIRLWDLENGKQMK-----SIDAGPvdawtlAFSPDSQYLA-TGTHMGKVNIFGVE-SGKKEYSLDTRG 148
Cdd:COG0823     1 LAFTLSRDgnSDIYVVDLDGGEPRRltnspGIDTSP------AWSPDGRRIAfTSDRGGGPQIYVVDaDGGEPRRLTFGG 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907199447 149 KFILSIAYSPDGKYLA-SGAIDGIINIF--DIATGKLLHTLEGHAMPirslTFSPDSQLLVTASD-DGYIKIYDV 219
Cdd:COG0823    75 GYNASPSWSPDGKRLAfVSRSDGRFDIYvlDLDGGAPRRLTDGPGSP----SWSPDGRRIVFSSDrGGRPDLYVV 145
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 112-199 2.77e-09

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: 53.44  E-value: 2.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447 112 LAFSPDSQYLATGTHMGKVNIFGVeSGKKEY--SLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGH 189
Cdd:pfam12894   1 MSWCPTMDLIALATEDGELLLHRL-NWQRVWtlSPDKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSAG 79

                          90
                  ....*....|
gi 1907199447 190 AMPIRSLTFS 199
Cdd:pfam12894  80 SDLITCLGWG 89
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 113-220 3.17e-09

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


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 57.74  E-value: 3.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447  113 AFSPDSQYLATgthmgkvniFGVESGKKE---YSLDTRGK----------FILSIAYSPDGKYLASGAIDGIINIFDIAT 179
Cdd:COG4946    349 AWSPDGKSIAY---------FSDASGEYElyiAPADGSGEpkqltlgdlgRVFNPVWSPDGKKIAFTDNRGRLWVVDLAS 419

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1907199447  180 GK---LLHtlEGHAMPIRSLTFSPDSQLLVTASDDGY----IKIYDVQ 220
Cdd:COG4946    420 GKvrkVDT--DGYGDGISDLAWSPDSKWLAYSKPGPNqlsqIFLYDVE 465
WD40 pfam00400
WD domain, G-beta repeat;
180-218 5.87e-09

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 50.81  E-value: 5.87e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907199447 180 GKLLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYD 218
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 80-219 9.89e-09

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 56.25  E-value: 9.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447  80 ASSSLDAHIRLWDLENGKQMKSIDAGPVDAWTLAF-SPDSQYLATGTHMGKVNIFGVESGKKEYSLDTRGKFILSIAYSP 158
Cdd:PLN00181  549 ASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYsSADPTLLASGSDDGSVKLWSINQGVSIGTIKTKANICCVQFPSE 628

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907199447 159 DGKYLASGAIDGIINIFDIATGKL-LHTLEGHAMPIRSLTFSpDSQLLVTASDDGYIKIYDV 219
Cdd:PLN00181  629 SGRSLAFGSADHKVYYYDLRNPKLpLCTMIGHSKTVSYVRFV-DSSTLVSSSTDNTLKLWDL 689
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
101-246 1.21e-07

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 51.62  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447 101 SIDAGPVDAWTLAFSPDSQYL-ATGTHMGKVNIFGVESGKKEYSLDTrGKFILSIAYSPDGKYL-ASGAIDGIINIFDIA 178
Cdd:COG3391    62 LGAAAVADADGADAGADGRRLyVANSGSGRVSVIDLATGKVVATIPV-GGGPRGLAVDPDGGRLyVADSGNGRVSVIDTA 140

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907199447 179 TGKLLHTLEGHAMPiRSLTFSPDSQLLVTASDDG-----YIKIYDVQHANLAGTLSGHASWVlNVAFCPDDTH 246
Cdd:COG3391   141 TGKVVATIPVGAGP-HGIAVDPDGKRLYVANSGSntvsvIVSVIDTATGKVVATIPVGGGPV-GVAVSPDGRR 211
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 92-181 3.60e-07

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


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 51.58  E-value: 3.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447   92 DLENGKQMKSIDAG-PVDAWTLAFSPDSQYLATGTHMGKVNIFGVESGK-KEYSLDTRGKFILSIAYSPDGKYLASGAID 169
Cdd:COG4946    373 PADGSGEPKQLTLGdLGRVFNPVWSPDGKKIAFTDNRGRLWVVDLASGKvRKVDTDGYGDGISDLAWSPDSKWLAYSKPG 452

                           90
                   ....*....|....*.
gi 1907199447  170 G----IINIFDIATGK 181
Cdd:COG4946    453 PnqlsQIFLYDVETGK 468
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 52-164 6.67e-07

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


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 50.81  E-value: 6.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447   52 ERLELQWSLEGHQLGVVsvdishtlpiaassslDAHIRLW--DLENGKQMKsIDAGP--VDAWTLAFSPDSQYLA----T 123
Cdd:COG4946    390 RVFNPVWSPDGKKIAFT----------------DNRGRLWvvDLASGKVRK-VDTDGygDGISDLAWSPDSKWLAyskpG 452

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1907199447  124 GTHMGKVNIFGVESGKKeYSLdTRGKFI-LSIAYSPDGKYLA 164
Cdd:COG4946    453 PNQLSQIFLYDVETGKT-VQL-TDGRYDdGSPAFSPDGKYLY 492
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 112-245 6.97e-07

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 50.47  E-value: 6.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447 112 LAFSPDSQYLATGTHMGKVNIFGVESGKKE--------YSLDTRGKfILSIAYSPDGK-YLASGAIDGIINIFDIATGKL 182
Cdd:PLN00181  489 IGFDRDGEFFATAGVNKKIKIFECESIIKDgrdihypvVELASRSK-LSGICWNSYIKsQVASSNFEGVVQVWDVARSQL 567

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907199447 183 LHTLEGHAMPIRSLTF-SPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASwVLNVAFcPDDT 245
Cdd:PLN00181  568 VTEMKEHEKRVWSIDYsSADPTLLASGSDDGSVKLWSINQGVSIGTIKTKAN-ICCVQF-PSES 629
PTZ00421 PTZ00421
coronin; Provisional
 112-233 1.41e-06

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 49.51  E-value: 1.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447 112 LAFSP-DSQYLATGTHMGKVNIFGV-ESGKKEYSLD--------TRGKFILSIAYSPDGkYLASGAIDGIINIFDIATGK 181
Cdd:PTZ00421   81 VAFNPfDPQKLFTASEDGTIMGWGIpEEGLTQNISDpivhlqghTKKVGIVSFHPSAMN-VLASAGADMVVNVWDVERGK 159

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907199447 182 LLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHAS 233
Cdd:PTZ00421  160 AVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRDGTIVSSVEAHAS 211
8prop_hemeD1_NirF cd20778
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ...
 86-218 4.69e-06

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: 47.66  E-value: 4.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447  86 AHIRLWDLENGKQMKSIDAG------PVD------AWtlAFSPDSQYL-ATGTHmgKVNIFGVESGKKEYSLDTRGKFIL 152
Cdd:cd20778   210 GLLDLWKPERGVRRILLDYGkgeeklPVYkmphleGW--AVAGDKAFVpAVGEH--RVLVYDTNDWKFIKSIPLAGQPVF 285

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907199447 153 SIAySPDGKYLA---SGAIDGIINIFDIATGKLLHTLE--GHAMPIRsltFSPD-SQLLVTASDDGYIKIYD 218
Cdd:cd20778   286 AVA-RPDGRYVWvnfSGPDNDTVQVIDTKTLKVVKTLEpgKRVLHME---FTPRgEAVYISVNDDNKVVVYD 353
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 263-302 1.39e-05

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 41.53  E-value: 1.39e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1907199447  263 TRTCIHTFFDHQDQVWGVKYNGNGSKIVSVGDDQEIHVYD 302
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
Nsa1_WDR74-like cd22850
Ribosome biogenesis protein Nsa1 and similar proteins; Ribosome biogenesis protein Nsa1 ...
 87-184 3.87e-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: 44.54  E-value: 3.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447  87 HIRLWDLENG-KQMKSIDAGPvdawTLAFSPDSQYLATGTHMGKVNIFGVESGKKEYSLdtRGKF---ILSIAYSPD--G 160
Cdd:cd22850   216 QVRLYDTSAGrRPVFSEKPIK----KPEEDLDGHTVYVGDTSGDLALIDIRTGKLLGRL--LGKYggsITGAVRHPElfD 289

                          90       100
                  ....*....|....*....|....
gi 1907199447 161 KYLASGAIDGIINIFDIATGKLLH 184
Cdd:cd22850   290 PYLASGGLDRYLRVFDIETRELLA 313
WDR74 cd22857
WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and ...
 116-220 1.25e-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: 42.98  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447 116 PDSQYLATGTHMGKVNIFGVESGKKE-YSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGHA-MPI 193
Cdd:cd22857   190 DDHRKIVTGTGYHQVRLYDTRAQRRPvVSVDFGETPIKAVAEDPDGHTVYVGDTSGDLASIDLRTGKLLGCFKGKCgGSI 269

                          90       100
                  ....*....|....*....|....*..
gi 1907199447 194 RSLTFSPDSQLLVTASDDGYIKIYDVQ 220
Cdd:cd22857   270 RSIARHPELPLIASCGLDRYLRIWDTE 296
PTZ00421 PTZ00421
coronin; Provisional
 188-302 1.41e-04

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 43.34  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447 188 GHAMPIRSLTFSP-DSQLLVTASDDGYIKIYDVQHANLAGTLS-------GHASWVLNVAFCPDDTH-FVSSSSDKSVKV 258
Cdd:PTZ00421   73 GQEGPIIDVAFNPfDPQKLFTASEDGTIMGWGIPEEGLTQNISdpivhlqGHTKKVGIVSFHPSAMNvLASAGADMVVNV 152

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1907199447 259 WDVGTRTCIHTFFDHQDQVWGVKYNGNGSKIVSVGDDQEIHVYD 302
Cdd:PTZ00421  153 WDVERGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIID 196
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 137-176 2.23e-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: 2.23e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1907199447  137 SGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFD 176
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
eIF2A pfam08662
Eukaryotic translation initiation factor eIF2A; This is a family of eukaryotic translation ...
 143-247 3.57e-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: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447 143 SLDTRGKfILSIAYSPDGK--YLASGAIDGIINIFDiATGKLLHTLEGHamPIRSLTFSPDSQLLVTA---SDDGYIKIY 217
Cdd:pfam08662  55 ELDKEGP-IHDVAWSPNGKefAVIYGYMPAKVSFFD-LKGNVIHSFGEQ--PRNTIFWSPFGRLVLLAgfgNLAGDIEFW 130

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907199447 218 DVQHANLAGTLsgHASWVLNVAFCPDDTHF 247
Cdd:pfam08662 131 DVVNKKKIATA--EASNATLCEWSPDGRYF 158
WD40 pfam00400
WD domain, G-beta repeat;
264-302 7.03e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.55  E-value: 7.03e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907199447 264 RTCIHTFFDHQDQVWGVKYNGNGSKIVSVGDDQEIHVYD 302
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
138-176 8.15e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.55  E-value: 8.15e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907199447 138 GKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFD 176
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
55-92 8.56e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.55  E-value: 8.56e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1907199447  55 ELQWSLEGHQLGVVSVDISHTLPIAASSSLDAHIRLWD 92
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WDR74 cd22857
WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and ...
 87-184 1.26e-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: 39.90  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447  87 HIRLWDLENGKQ-MKSIDAGPVDAWTLAFSPDSQYLATGTHMGKVNIFGVESGKKEYSLdtRGK---FILSIAYSPDGKY 162
Cdd:cd22857   203 QVRLYDTRAQRRpVVSVDFGETPIKAVAEDPDGHTVYVGDTSGDLASIDLRTGKLLGCF--KGKcggSIRSIARHPELPL 280

                          90       100
                  ....*....|....*....|..
gi 1907199447 163 LASGAIDGIINIFDIATGKLLH 184
Cdd:cd22857   281 IASCGLDRYLRIWDTETRQLLS 302
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 55-92 1.46e-03

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 35.75  E-value: 1.46e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1907199447   55 ELQWSLEGHQLGVVSVDISHTLPIAASSSLDAHIRLWD 92
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 186-241 4.38e-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: 35.72  E-value: 4.38e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907199447 186 LEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFC 241
Cdd:pfam12894  34 PDKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSAGSDLITCLGWG 89
Pgl COG2706
6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism];
112-247 5.99e-03

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


Pssm-ID: 442025 [Multi-domain]  Cd Length: 352  Bit Score: 37.96  E-value: 5.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447 112 LAFSPDSQYL--ATGTHMGKVNIFGVESGKKEYSL----DTRGKFILSIAYSPDGKYLASGA-IDGIINIFDI-ATGKLL 183
Cdd:COG2706    50 LALSPDGRFLyaVNEVDDGGVSAFRIDPADGTLTLlntvSSGGASPCHLSVDPDGRFLFVANyGGGSVSVFPIdADGSLG 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199447 184 -------HTLEGHAMP------IRSLTFSPDSQLLVtASDDG--YIKIYDVQHANlaGTLSGHASWVLN-------VAFC 241
Cdd:COG2706   130 epvqviqHEGSGPNPErqegphAHSVVFDPDGRFLY-VPDLGtdRIYVYRLDPAT--GKLPEPPEVSLPpgsgprhLAFH 206


                  ....*.
gi 1907199447 242 PDDTHF 247
Cdd:COG2706   207 PNGRFA 212
PRK03817 PRK03817
galactokinase; Provisional
 30-83 9.59e-03

galactokinase; Provisional


Pssm-ID: 235163 [Multi-domain]  Cd Length: 351  Bit Score: 37.28  E-value: 9.59e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907199447  30 ENIETVVTGSLDDLVKVWKWRDERLELQWSLE--GHQLGVVSVDISHTLPIAA--SSS 83
Cdd:PRK03817   47 ENFNEEKTFELDKLEKLNSWADYIKGVIWVLEkrGYEVGGVKGKVSSNLPIGAglSSS 104
 
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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