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Conserved domains on  [gi|13277350|ref|NP_075680|]
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superkiller complex protein 8 isoform a [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 13277350  13 QAHDDAIWSVAWETNKKenieTVVTGSLDDLVKVWKWRDERLelQWSLEGHQLGVVSVDISHTLPIAASSSLDAHIRLWD 92
Cdd:COG2319 117 TGHTGAVRSVAFSPDGK----TLASGSADGTVRLWDLATGKL--LRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWD 190

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277350  93 LENGKQMKSIDAGPVDAWTLAFSPDSQYLATGTHMGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGII 172
Cdd:COG2319 191 LATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTV 270

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277350 173 NIFDIATGKLLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSS 252
Cdd:COG2319 271 RLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSD 350

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 13277350 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 13277350  13 QAHDDAIWSVAWETNKKenieTVVTGSLDDLVKVWKWRDERLelQWSLEGHQLGVVSVDISHTLPIAASSSLDAHIRLWD 92
Cdd:COG2319 117 TGHTGAVRSVAFSPDGK----TLASGSADGTVRLWDLATGKL--LRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWD 190

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277350  93 LENGKQMKSIDAGPVDAWTLAFSPDSQYLATGTHMGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGII 172
Cdd:COG2319 191 LATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTV 270

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277350 173 NIFDIATGKLLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSS 252
Cdd:COG2319 271 RLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSD 350

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 13277350 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 13277350  13 QAHDDAIWSVAWETNKKenieTVVTGSLDDLVKVWKWRDERLELQwsLEGHQLGVVSVDISHTLPIAASSSLDAHIRLWD 92
Cdd:cd00200   6 KGHTGGVTCVAFSPDGK----LLATGSGDGTIKVWDLETGELLRT--LKGHTGPVRDVAASADGTYLASGSSDKTIRLWD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277350  93 LENGKQMKSI--DAGPVdaWTLAFSPDSQYLATGTHMGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDG 170
Cdd:cd00200  80 LETGECVRTLtgHTSYV--SSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDG 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277350 171 IINIFDIATGKLLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSS 250
Cdd:cd00200 158 TIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASG 237

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 13277350 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 13277350    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 13277350   112 LAFSPDSQYLATGTHMGKVNIFGVeSGKKEY--SLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGH 189
Cdd:pfam12894   1 MSWCPTMDLIALATEDGELLLHRL-NWQRVWtlSPDKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSAG 79

                          90
                  ....*....|
gi 13277350   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 13277350   80 ASSSLDAHIRLWDLENGKQMKSIDAGPVDAWTLAF-SPDSQYLATGTHMGKVNIFGVESGKKEYSLDTRGKFILSIAYSP 158
Cdd:PLN00181 549 ASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYsSADPTLLASGSDDGSVKLWSINQGVSIGTIKTKANICCVQFPSE 628

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13277350  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 13277350  13 QAHDDAIWSVAWETNKKenieTVVTGSLDDLVKVWKWRDERLelQWSLEGHQLGVVSVDISHTLPIAASSSLDAHIRLWD 92
Cdd:COG2319 117 TGHTGAVRSVAFSPDGK----TLASGSADGTVRLWDLATGKL--LRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWD 190

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277350  93 LENGKQMKSIDAGPVDAWTLAFSPDSQYLATGTHMGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGII 172
Cdd:COG2319 191 LATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTV 270

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277350 173 NIFDIATGKLLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSS 252
Cdd:COG2319 271 RLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSD 350

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 13277350 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 13277350  36 VTGSLDDLVKVWKWRDERLELQWSLEGHQLGVVSVDISHTLPIAASSSLDAHIRLWDLENGKQMKSIDAGPVDAWTLAFS 115
Cdd:COG2319  50 RLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFS 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277350 116 PDSQYLATGTHMGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGHAMPIRS 195
Cdd:COG2319 130 PDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRS 209

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277350 196 LTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDVGTRTCIHTFFDHQD 275
Cdd:COG2319 210 VAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSG 289

                       250       260
                ....*....|....*....|....*..
gi 13277350 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 13277350  13 QAHDDAIWSVAWETNKKenieTVVTGSLDDLVKVWKWRDERLELQwsLEGHQLGVVSVDISHTLPIAASSSLDAHIRLWD 92
Cdd:cd00200   6 KGHTGGVTCVAFSPDGK----LLATGSGDGTIKVWDLETGELLRT--LKGHTGPVRDVAASADGTYLASGSSDKTIRLWD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277350  93 LENGKQMKSI--DAGPVdaWTLAFSPDSQYLATGTHMGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDG 170
Cdd:cd00200  80 LETGECVRTLtgHTSYV--SSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDG 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277350 171 IINIFDIATGKLLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSS 250
Cdd:cd00200 158 TIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASG 237

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 13277350 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 13277350  36 VTGSLDDLVKVWKWRDERLELQWSLEGHQLGVVSVDISHTLPIAASSSLDAHIRLWDLENGKQMKSIDAGPVDAWTLAFS 115
Cdd:COG2319   8 ALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFS 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277350 116 PDSQYLATGTHMGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGHAMPIRS 195
Cdd:COG2319  88 PDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTS 167

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277350 196 LTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDVGTRTCIHTFFDHQD 275
Cdd:COG2319 168 VAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSG 247

                       250       260
                ....*....|....*....|....*..
gi 13277350 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 13277350  60 LEGHQLGVVSVDISHTLPIAASSSLDAHIRLWDLENGKQMKSIDAGPVDAWTLAFSPDSQYLATGTHMGKVNIFGVESGK 139
Cdd:cd00200   5 LKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGE 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277350 140 KEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYDV 219
Cdd:cd00200  85 CVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277350 220 QHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDVGTRTCIHTFFDHQDQVWGVKYNGNGSKIVSVGDDQEIH 299
Cdd:cd00200 165 RTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIR 244


                ...
gi 13277350 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 13277350   8 LFKQEQAHDDAIWSVAWETNKKenieTVVTGSLDDLVKVWKWRDErlELQWSLEGHQLGVVSVDISHTLPIAASSSLDAH 87
Cdd:cd00200  43 LLRTLKGHTGPVRDVAASADGT----YLASGSSDKTIRLWDLETG--ECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKT 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277350  88 IRLWDLENGKQMKSIDAGPVDAWTLAFSPDSQYLATGTHMGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGA 167
Cdd:cd00200 117 IKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSS 196

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277350 168 IDGIINIFDIATGKLLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHF 247
Cdd:cd00200 197 SDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRL 276

                       250
                ....*....|...
gi 13277350 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 13277350 182 LLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDV 261
Cdd:cd00200   1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 13277350 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 13277350  78 IAASSSLDAHIRLWDLENGKQMKSIDAGPvDAWTLAFSPDSQYL-ATGTHMGKVNIFGVESGKKEYSLDTrGKFILSIAY 156
Cdd:COG3391  82 LYVANSGSGRVSVIDLATGKVVATIPVGG-GPRGLAVDPDGGRLyVADSGNGRVSVIDTATGKVVATIPV-GAGPHGIAV 159

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13277350 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 13277350    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 13277350  78 IAASSSLD--AHIRLWDLENGKQMK-----SIDAGPvdawtlAFSPDSQYLA-TGTHMGKVNIFGVE-SGKKEYSLDTRG 148
Cdd:COG0823   1 LAFTLSRDgnSDIYVVDLDGGEPRRltnspGIDTSP------AWSPDGRRIAfTSDRGGGPQIYVVDaDGGEPRRLTFGG 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13277350 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 13277350   112 LAFSPDSQYLATGTHMGKVNIFGVeSGKKEY--SLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGH 189
Cdd:pfam12894   1 MSWCPTMDLIALATEDGELLLHRL-NWQRVWtlSPDKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSAG 79

                          90
                  ....*....|
gi 13277350   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 13277350  113 AFSPDSQYLATgthmgkvniFGVESGKKE---YSLDTRGK----------FILSIAYSPDGKYLASGAIDGIINIFDIAT 179
Cdd:COG4946  349 AWSPDGKSIAY---------FSDASGEYElyiAPADGSGEpkqltlgdlgRVFNPVWSPDGKKIAFTDNRGRLWVVDLAS 419

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 13277350  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 13277350   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 13277350   80 ASSSLDAHIRLWDLENGKQMKSIDAGPVDAWTLAF-SPDSQYLATGTHMGKVNIFGVESGKKEYSLDTRGKFILSIAYSP 158
Cdd:PLN00181 549 ASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYsSADPTLLASGSDDGSVKLWSINQGVSIGTIKTKANICCVQFPSE 628

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13277350  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 13277350 101 SIDAGPVDAWTLAFSPDSQYL-ATGTHMGKVNIFGVESGKKEYSLDTrGKFILSIAYSPDGKYL-ASGAIDGIINIFDIA 178
Cdd:COG3391  62 LGAAAVADADGADAGADGRRLyVANSGSGRVSVIDLATGKVVATIPV-GGGPRGLAVDPDGGRLyVADSGNGRVSVIDTA 140

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13277350 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 13277350   92 DLENGKQMKSIDAG-PVDAWTLAFSPDSQYLATGTHMGKVNIFGVESGK-KEYSLDTRGKFILSIAYSPDGKYLASGAID 169
Cdd:COG4946  373 PADGSGEPKQLTLGdLGRVFNPVWSPDGKKIAFTDNRGRLWVVDLASGKvRKVDTDGYGDGISDLAWSPDSKWLAYSKPG 452

                         90
                 ....*....|....*.
gi 13277350  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 13277350   52 ERLELQWSLEGHQLGVVsvdishtlpiaassslDAHIRLW--DLENGKQMKsIDAGP--VDAWTLAFSPDSQYLA----T 123
Cdd:COG4946  390 RVFNPVWSPDGKKIAFT----------------DNRGRLWvvDLASGKVRK-VDTDGygDGISDLAWSPDSKWLAyskpG 452

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 13277350  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 13277350  112 LAFSPDSQYLATGTHMGKVNIFGVESGKKE--------YSLDTRGKfILSIAYSPDGK-YLASGAIDGIINIFDIATGKL 182
Cdd:PLN00181 489 IGFDRDGEFFATAGVNKKIKIFECESIIKDgrdihypvVELASRSK-LSGICWNSYIKsQVASSNFEGVVQVWDVARSQL 567

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13277350  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 13277350  112 LAFSP-DSQYLATGTHMGKVNIFGV-ESGKKEYSLD--------TRGKFILSIAYSPDGkYLASGAIDGIINIFDIATGK 181
Cdd:PTZ00421  81 VAFNPfDPQKLFTASEDGTIMGWGIpEEGLTQNISDpivhlqghTKKVGIVSFHPSAMN-VLASAGADMVVNVWDVERGK 159

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 13277350  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 13277350  86 AHIRLWDLENGKQMKSIDAG------PVD------AWtlAFSPDSQYL-ATGTHmgKVNIFGVESGKKEYSLDTRGKFIL 152
Cdd:cd20778 210 GLLDLWKPERGVRRILLDYGkgeeklPVYkmphleGW--AVAGDKAFVpAVGEH--RVLVYDTNDWKFIKSIPLAGQPVF 285

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13277350 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 13277350    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 13277350  87 HIRLWDLENG-KQMKSIDAGPvdawTLAFSPDSQYLATGTHMGKVNIFGVESGKKEYSLdtRGKF---ILSIAYSPD--G 160
Cdd:cd22850 216 QVRLYDTSAGrRPVFSEKPIK----KPEEDLDGHTVYVGDTSGDLALIDIRTGKLLGRL--LGKYggsITGAVRHPElfD 289

                        90       100
                ....*....|....*....|....
gi 13277350 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 13277350 116 PDSQYLATGTHMGKVNIFGVESGKKE-YSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGHA-MPI 193
Cdd:cd22857 190 DDHRKIVTGTGYHQVRLYDTRAQRRPvVSVDFGETPIKAVAEDPDGHTVYVGDTSGDLASIDLRTGKLLGCFKGKCgGSI 269

                        90       100
                ....*....|....*....|....*..
gi 13277350 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 13277350  188 GHAMPIRSLTFSP-DSQLLVTASDDGYIKIYDVQHANLAGTLS-------GHASWVLNVAFCPDDTH-FVSSSSDKSVKV 258
Cdd:PTZ00421  73 GQEGPIIDVAFNPfDPQKLFTASEDGTIMGWGIPEEGLTQNISdpivhlqGHTKKVGIVSFHPSAMNvLASAGADMVVNV 152

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 13277350  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 13277350    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 13277350   143 SLDTRGKfILSIAYSPDGK--YLASGAIDGIINIFDiATGKLLHTLEGHamPIRSLTFSPDSQLLVTA---SDDGYIKIY 217
Cdd:pfam08662  55 ELDKEGP-IHDVAWSPNGKefAVIYGYMPAKVSFFD-LKGNVIHSFGEQ--PRNTIFWSPFGRLVLLAgfgNLAGDIEFW 130

                          90       100       110
                  ....*....|....*....|....*....|
gi 13277350   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 13277350   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 13277350   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 13277350    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 13277350  87 HIRLWDLENGKQ-MKSIDAGPVDAWTLAFSPDSQYLATGTHMGKVNIFGVESGKKEYSLdtRGK---FILSIAYSPDGKY 162
Cdd:cd22857 203 QVRLYDTRAQRRpVVSVDFGETPIKAVAEDPDGHTVYVGDTSGDLASIDLRTGKLLGCF--KGKcggSIRSIARHPELPL 280

                        90       100
                ....*....|....*....|..
gi 13277350 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 13277350     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 13277350   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 13277350 112 LAFSPDSQYL--ATGTHMGKVNIFGVESGKKEYSL----DTRGKFILSIAYSPDGKYLASGA-IDGIINIFDI-ATGKLL 183
Cdd:COG2706  50 LALSPDGRFLyaVNEVDDGGVSAFRIDPADGTLTLlntvSSGGASPCHLSVDPDGRFLFVANyGGGSVSVFPIdADGSLG 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13277350 184 -------HTLEGHAMP------IRSLTFSPDSQLLVtASDDG--YIKIYDVQHANlaGTLSGHASWVLN-------VAFC 241
Cdd:COG2706 130 epvqviqHEGSGPNPErqegphAHSVVFDPDGRFLY-VPDLGtdRIYVYRLDPAT--GKLPEPPEVSLPpgsgprhLAFH 206


                ....*.
gi 13277350 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 13277350   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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