|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
79-425 |
7.34e-36 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 136.19 E-value: 7.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411222 79 LNTLKGHGDAVTGLCFSSDGKSLATACADGVIRVFKLDDAssksfKFLRinlPAGGHP---TAVAFADDASSIVvachhm 155
Cdd:COG2319 113 LRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATG-----KLLR---TLTGHSgavTSVAFSPDGKLLA------ 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411222 156 SGSSlymygedkqkDQQGKLplpsikWDhhhIHEKRSVLTISGATAT-YGTA---DGSvVIASCSEGTDIVLWHGKTGRN 231
Cdd:COG2319 179 SGSD----------DGTVRL------WD---LATGKLLRTLTGHTGAvRSVAfspDGK-LLASGSADGTVRLWDLATGKL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411222 232 LGHVDTNQLKNHMAAVSPNGRFLAAAAFTADVKVWEIvyqKDGSVKEVsrvmqLKGHKSAVTWLCFSPNSEQIITASKDG 311
Cdd:COG2319 239 LRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDL---ATGELLRT-----LTGHSGGVNSVAFSPDGKLLASGSDDG 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411222 312 SIRVWNInvryhldEDPKTLKVFPiplcdsgGNPLHYDRLSLCPEGKILA-ASHGSTLQWLCAETGNVLDTAeKAHEGDI 390
Cdd:COG2319 311 TVRLWDL-------ATGKLLRTLT-------GHTGAVRSVAFSPDGKTLAsGSDDGTVRLWDLATGELLRTL-TGHTGAV 375
|
330 340 350
....*....|....*....|....*....|....*
gi 18411222 391 TCISWAPKaitvGERhamvLGTSGDDKKVKLWEAP 425
Cdd:COG2319 376 TSVAFSPD----GRT----LASGSADGTVRLWDLA 402
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
81-423 |
1.11e-27 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 111.27 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411222 81 TLKGHGDAVTGLCFSSDGKSLATACADGVIRVFKLDDASSKSFKflrinlpaGGHP---TAVAFADDASSIVVAchhmsg 157
Cdd:cd00200 4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTL--------KGHTgpvRDVAASADGTYLASG------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411222 158 sslymyGEDKQkdqqgklplpsIK-WDhhhIHEKRSVLTISGATATYGTADGSV---VIASCSEGTDIVLWHGKTGRNL- 232
Cdd:cd00200 70 ------SSDKT-----------IRlWD---LETGECVRTLTGHTSYVSSVAFSPdgrILSSSSRDKTIKVWDVETGKCLt 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411222 233 ---GHVDT-NQLknhmaAVSPNGRFLAAAAFTADVKVWEIVYQKdgsvkevsRVMQLKGHKSAVTWLCFSPNSEQIITAS 308
Cdd:cd00200 130 tlrGHTDWvNSV-----AFSPDGTFVASSSQDGTIKLWDLRTGK--------CVATLTGHTGEVNSVAFSPDGEKLLSSS 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411222 309 KDGSIRVWNINVRYHLdedpKTLKVFPIPLCDsggnplhydrLSLCPEGKILA-ASHGSTLQWLCAETGNVLDTAeKAHE 387
Cdd:cd00200 197 SDGTIKLWDLSTGKCL----GTLRGHENGVNS----------VAFSPDGYLLAsGSEDGTIRVWDLRTGECVQTL-SGHT 261
|
330 340 350
....*....|....*....|....*....|....*.
gi 18411222 388 GDITCISWAPKAITvgerhamvLGTSGDDKKVKLWE 423
Cdd:cd00200 262 NSVTSLAWSPDGKR--------LASGSADGTIRIWD 289
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
282-317 |
7.22e-09 |
|
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: 51.16 E-value: 7.22e-09
10 20 30
....*....|....*....|....*....|....*.
gi 18411222 282 VMQLKGHKSAVTWLCFSPNSEQIITASKDGSIRVWN 317
Cdd:smart00320 5 LKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
280-317 |
9.08e-08 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 48.11 E-value: 9.08e-08
10 20 30
....*....|....*....|....*....|....*...
gi 18411222 280 SRVMQLKGHKSAVTWLCFSPNSEQIITASKDGSIRVWN 317
Cdd:pfam00400 2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| PTZ00420 |
PTZ00420 |
coronin; Provisional |
282-348 |
2.23e-04 |
|
coronin; Provisional
Pssm-ID: 240412 [Multi-domain] Cd Length: 568 Bit Score: 43.40 E-value: 2.23e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18411222 282 VMQLKGHKSAVTWLCFSP-NSEQIITASKDGSIRVWNINvryHLDEDPKTLKvfpIPLCDSGG----------NPLHY 348
Cdd:PTZ00420 67 VIKLKGHTSSILDLQFNPcFSEILASGSEDLTIRVWEIP---HNDESVKEIK---DPQCILKGhkkkisiidwNPMNY 138
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
79-425 |
7.34e-36 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 136.19 E-value: 7.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411222 79 LNTLKGHGDAVTGLCFSSDGKSLATACADGVIRVFKLDDAssksfKFLRinlPAGGHP---TAVAFADDASSIVvachhm 155
Cdd:COG2319 113 LRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATG-----KLLR---TLTGHSgavTSVAFSPDGKLLA------ 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411222 156 SGSSlymygedkqkDQQGKLplpsikWDhhhIHEKRSVLTISGATAT-YGTA---DGSvVIASCSEGTDIVLWHGKTGRN 231
Cdd:COG2319 179 SGSD----------DGTVRL------WD---LATGKLLRTLTGHTGAvRSVAfspDGK-LLASGSADGTVRLWDLATGKL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411222 232 LGHVDTNQLKNHMAAVSPNGRFLAAAAFTADVKVWEIvyqKDGSVKEVsrvmqLKGHKSAVTWLCFSPNSEQIITASKDG 311
Cdd:COG2319 239 LRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDL---ATGELLRT-----LTGHSGGVNSVAFSPDGKLLASGSDDG 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411222 312 SIRVWNInvryhldEDPKTLKVFPiplcdsgGNPLHYDRLSLCPEGKILA-ASHGSTLQWLCAETGNVLDTAeKAHEGDI 390
Cdd:COG2319 311 TVRLWDL-------ATGKLLRTLT-------GHTGAVRSVAFSPDGKTLAsGSDDGTVRLWDLATGELLRTL-TGHTGAV 375
|
330 340 350
....*....|....*....|....*....|....*
gi 18411222 391 TCISWAPKaitvGERhamvLGTSGDDKKVKLWEAP 425
Cdd:COG2319 376 TSVAFSPD----GRT----LASGSADGTVRLWDLA 402
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
79-424 |
2.44e-30 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 121.17 E-value: 2.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411222 79 LNTLKGHGDAVTGLCFSSDGKSLATACADGVIRVFKLDDAssksfKFLRINLPAGGHPTAVAFADDASSIVVAchhmsgs 158
Cdd:COG2319 71 LATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATG-----LLLRTLTGHTGAVRSVAFSPDGKTLASG------- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411222 159 slymyGEDKqkdqqgklplpSIK-WDhhhIHEKRSVLTISGATATYGT----ADGSvVIASCSEGTDIVLWHGKTGRNLG 233
Cdd:COG2319 139 -----SADG-----------TVRlWD---LATGKLLRTLTGHSGAVTSvafsPDGK-LLASGSDDGTVRLWDLATGKLLR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411222 234 HVDTNQLKNHMAAVSPNGRFLAAAAFTADVKVWeivyqkdgSVKEVSRVMQLKGHKSAVTWLCFSPNSEQIITASKDGSI 313
Cdd:COG2319 199 TLTGHTGAVRSVAFSPDGKLLASGSADGTVRLW--------DLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTV 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411222 314 RVWNInvryhldEDPKTLKVFPIplcdsggnplHYDR---LSLCPEGKILA-ASHGSTLQWLCAETGNVLDTAeKAHEGD 389
Cdd:COG2319 271 RLWDL-------ATGELLRTLTG----------HSGGvnsVAFSPDGKLLAsGSDDGTVRLWDLATGKLLRTL-TGHTGA 332
|
330 340 350
....*....|....*....|....*....|....*
gi 18411222 390 ITCISWAPKaitvGERhamvLGTSGDDKKVKLWEA 424
Cdd:COG2319 333 VRSVAFSPD----GKT----LASGSDDGTVRLWDL 359
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
81-423 |
1.11e-27 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 111.27 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411222 81 TLKGHGDAVTGLCFSSDGKSLATACADGVIRVFKLDDASSKSFKflrinlpaGGHP---TAVAFADDASSIVVAchhmsg 157
Cdd:cd00200 4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTL--------KGHTgpvRDVAASADGTYLASG------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411222 158 sslymyGEDKQkdqqgklplpsIK-WDhhhIHEKRSVLTISGATATYGTADGSV---VIASCSEGTDIVLWHGKTGRNL- 232
Cdd:cd00200 70 ------SSDKT-----------IRlWD---LETGECVRTLTGHTSYVSSVAFSPdgrILSSSSRDKTIKVWDVETGKCLt 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411222 233 ---GHVDT-NQLknhmaAVSPNGRFLAAAAFTADVKVWEIVYQKdgsvkevsRVMQLKGHKSAVTWLCFSPNSEQIITAS 308
Cdd:cd00200 130 tlrGHTDWvNSV-----AFSPDGTFVASSSQDGTIKLWDLRTGK--------CVATLTGHTGEVNSVAFSPDGEKLLSSS 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411222 309 KDGSIRVWNINVRYHLdedpKTLKVFPIPLCDsggnplhydrLSLCPEGKILA-ASHGSTLQWLCAETGNVLDTAeKAHE 387
Cdd:cd00200 197 SDGTIKLWDLSTGKCL----GTLRGHENGVNS----------VAFSPDGYLLAsGSEDGTIRVWDLRTGECVQTL-SGHT 261
|
330 340 350
....*....|....*....|....*....|....*.
gi 18411222 388 GDITCISWAPKAITvgerhamvLGTSGDDKKVKLWE 423
Cdd:cd00200 262 NSVTSLAWSPDGKR--------LASGSADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
182-430 |
6.46e-19 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 88.04 E-value: 6.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411222 182 WDHHHIHEKRSVLTISGATATYGTADGSVVIASCSEGTDIVLWHGKTGRNLGHVDTNQLKNHMAAVSPNGRFLAAAAFTA 261
Cdd:COG2319 21 LAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411222 262 DVKVWeivyqkdgSVKEVSRVMQLKGHKSAVTWLCFSPNSEQIITASKDGSIRVWNInvryhldEDPKTLKVFPiplcds 341
Cdd:COG2319 101 TVRLW--------DLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDL-------ATGKLLRTLT------ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411222 342 gGNPLHYDRLSLCPEGKILA-ASHGSTLQWLCAETGNVLDTAeKAHEGDITCISWAPKaitvGERhamvLGTSGDDKKVK 420
Cdd:COG2319 160 -GHSGAVTSVAFSPDGKLLAsGSDDGTVRLWDLATGKLLRTL-TGHTGAVRSVAFSPD----GKL----LASGSADGTVR 229
|
250
....*....|
gi 18411222 421 LWEAPKSQSL 430
Cdd:COG2319 230 LWDLATGKLL 239
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
79-317 |
7.51e-18 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 83.54 E-value: 7.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411222 79 LNTLKGHGDAVTGLCFSSDGKSLATACADGVIRVFKLDdasskSFKFLRInlpAGGHP---TAVAFADDASSIVVACHhm 155
Cdd:cd00200 86 VRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVE-----TGKCLTT---LRGHTdwvNSVAFSPDGTFVASSSQ-- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411222 156 sgsslymygedkqkDQQGKLplpsikWDhhhIHEKRSVLTISG----ATATYGTADGSVVIASCSEGTdIVLWHGKTGRN 231
Cdd:cd00200 156 --------------DGTIKL------WD---LRTGKCVATLTGhtgeVNSVAFSPDGEKLLSSSSDGT-IKLWDLSTGKC 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411222 232 LGhvdtnQLKNHMAAV-----SPNGRFLAAAAFTADVKVWeivyqkdgSVKEVSRVMQLKGHKSAVTWLCFSPNSEQIIT 306
Cdd:cd00200 212 LG-----TLRGHENGVnsvafSPDGYLLASGSEDGTIRVW--------DLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS 278
|
250
....*....|.
gi 18411222 307 ASKDGSIRVWN 317
Cdd:cd00200 279 GSADGTIRIWD 289
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
284-430 |
8.07e-12 |
|
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: 65.43 E-value: 8.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411222 284 QLKGHKSAVTWLCFSPNSEQIITASKDGSIRVWNinvrYHLDEDPKTLKVFPIPLcdsggnplhyDRLSLCPEGK-ILAA 362
Cdd:cd00200 4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWD----LETGELLRTLKGHTGPV----------RDVAASADGTyLASG 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18411222 363 SHGSTLQWLCAETGNVLDTAEkAHEGDITCISWAPKaitvgeRHamVLGTSGDDKKVKLWEAPKSQSL 430
Cdd:cd00200 70 SSDKTIRLWDLETGECVRTLT-GHTSYVSSVAFSPD------GR--ILSSSSRDKTIKVWDVETGKCL 128
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
282-317 |
7.22e-09 |
|
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: 51.16 E-value: 7.22e-09
10 20 30
....*....|....*....|....*....|....*.
gi 18411222 282 VMQLKGHKSAVTWLCFSPNSEQIITASKDGSIRVWN 317
Cdd:smart00320 5 LKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
280-317 |
9.08e-08 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 48.11 E-value: 9.08e-08
10 20 30
....*....|....*....|....*....|....*...
gi 18411222 280 SRVMQLKGHKSAVTWLCFSPNSEQIITASKDGSIRVWN 317
Cdd:pfam00400 2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
79-117 |
2.14e-07 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 52.61 E-value: 2.14e-07
10 20 30
....*....|....*....|....*....|....*....
gi 18411222 79 LNTLKGHGDAVTGLCFSSDGKSLATACADGVIRVFKLDD 117
Cdd:COG2319 365 LRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
79-114 |
2.65e-07 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 46.54 E-value: 2.65e-07
10 20 30
....*....|....*....|....*....|....*.
gi 18411222 79 LNTLKGHGDAVTGLCFSSDGKSLATACADGVIRVFK 114
Cdd:smart00320 5 LKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
79-113 |
2.98e-06 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 43.87 E-value: 2.98e-06
10 20 30
....*....|....*....|....*....|....*
gi 18411222 79 LNTLKGHGDAVTGLCFSSDGKSLATACADGVIRVF 113
Cdd:pfam00400 4 LKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
|
|
| Pgl |
COG2706 |
6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism]; |
77-366 |
4.02e-05 |
|
6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism];
Pssm-ID: 442025 [Multi-domain] Cd Length: 352 Bit Score: 45.28 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411222 77 LDLNTLKGHGDAVTGLCFSSDGKSL--ATACADGVIRVFKLDDASSKsFKFLRINLPAGGHPTAVAFADDASSIVVACHH 154
Cdd:COG2706 35 LTLLGLVAALGNPSFLALSPDGRFLyaVNEVDDGGVSAFRIDPADGT-LTLLNTVSSGGASPCHLSVDPDGRFLFVANYG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411222 155 mSGS-SLYMYGEDkqkdqqGKL--PLPSIKWDHHHIHEKRSvlTISGATATYGTADGSVVIASCSeGTD-IVLWH--GKT 228
Cdd:COG2706 114 -GGSvSVFPIDAD------GSLgePVQVIQHEGSGPNPERQ--EGPHAHSVVFDPDGRFLYVPDL-GTDrIYVYRldPAT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411222 229 GRnLGHVDTNQLKN-----HMaAVSPNGRFLAAA-AFTADVKVWEIVyQKDGSVKEVSRVMQL----KGHKSAvTWLCFS 298
Cdd:COG2706 184 GK-LPEPPEVSLPPgsgprHL-AFHPNGRFAYVInELDSTVSVYAYD-AATGTLTLIQTVSTLpedfTGENWA-ADIHIS 259
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18411222 299 PNSEQIITA-SKDGSIRVwninvrYHLDEDPKTLKvfPIPLCDSGGN-PLHydrLSLCPEGK-ILAASHGS 366
Cdd:COG2706 260 PDGRFLYVSnRGHNSIAV------FAIDADGGKLT--LVGHVPTGGKwPRD---FAIDPDGRfLLVANQKS 319
|
|
| PTZ00420 |
PTZ00420 |
coronin; Provisional |
282-348 |
2.23e-04 |
|
coronin; Provisional
Pssm-ID: 240412 [Multi-domain] Cd Length: 568 Bit Score: 43.40 E-value: 2.23e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18411222 282 VMQLKGHKSAVTWLCFSP-NSEQIITASKDGSIRVWNINvryHLDEDPKTLKvfpIPLCDSGG----------NPLHY 348
Cdd:PTZ00420 67 VIKLKGHTSSILDLQFNPcFSEILASGSEDLTIRVWEIP---HNDESVKEIK---DPQCILKGhkkkisiidwNPMNY 138
|
|
| PTZ00420 |
PTZ00420 |
coronin; Provisional |
214-318 |
5.70e-04 |
|
coronin; Provisional
Pssm-ID: 240412 [Multi-domain] Cd Length: 568 Bit Score: 42.24 E-value: 5.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411222 214 SCSEGTDIVLWHGKTGRNLGHVD-TNQ--------LKNHMAAV---SPNGRF---LAAAAFTADVKVWEIVYQkDGSVKE 278
Cdd:PTZ00420 35 ACSSGFVAVPWEVEGGGLIGAIRlENQmrkppvikLKGHTSSIldlQFNPCFseiLASGSEDLTIRVWEIPHN-DESVKE 113
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 18411222 279 VSRVM-QLKGHKSAVTWLCFSPNSEQIITASK-DGSIRVWNI 318
Cdd:PTZ00420 114 IKDPQcILKGHKKKISIIDWNPMNYYIMCSSGfDSFVNIWDI 155
|
|
| ANAPC4_WD40 |
pfam12894 |
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ... |
295-396 |
7.51e-04 |
|
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC,
Pssm-ID: 403945 [Multi-domain] Cd Length: 91 Bit Score: 38.41 E-value: 7.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411222 295 LCFSPNSEQIITASKDGSIRVWNINVRyhldedpktlKVFPIPLCDSGGNPLHydrLSLCPEGKILAASHGS-TLQWLCA 373
Cdd:pfam12894 1 MSWCPTMDLIALATEDGELLLHRLNWQ----------RVWTLSPDKEDLEVTS---LAWRPDGKLLAVGYSDgTVRLLDA 67
|
90 100
....*....|....*....|...
gi 18411222 374 ETGNVLDTAeKAHEGDITCISWA 396
Cdd:pfam12894 68 ENGKIVHHF-SAGSDLITCLGWG 89
|
|
| FHA_KIF16A_STARD9 |
cd22731 |
forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); ... |
136-230 |
2.56e-03 |
|
forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); StARD9, also called START domain-containing protein 9, or kinesin-like protein KIF16A, is a microtubule-dependent motor protein required for spindle pole assembly during mitosis. It is required to stabilize the pericentriolar material (PCM). The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438783 [Multi-domain] Cd Length: 119 Bit Score: 37.83 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411222 136 PTAVAFADDASSIVVACHHMSGSSLYMYGEDKQKDQQGKLPLPSIKWDHHHIHEKRSVLTISGATATYGTADGSVVIASC 215
Cdd:cd22731 9 PHLIAMDDDILSTGVVLYHLREGTTKIGRSDSEQEQDIVLQGPWIERDHCMIHNECGVVTLRPAQGAQCTVNGREVTESC 88
|
90
....*....|....*..
gi 18411222 216 --SEGTDIVLwhGKTGR 230
Cdd:cd22731 89 rlSQGAVIVL--GKTHK 103
|
|
| ANAPC4_WD40 |
pfam12894 |
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ... |
82-113 |
3.84e-03 |
|
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC,
Pssm-ID: 403945 [Multi-domain] Cd Length: 91 Bit Score: 36.49 E-value: 3.84e-03
10 20 30
....*....|....*....|....*....|..
gi 18411222 82 LKGHGDAVTGLCFSSDGKSLATACADGVIRVF 113
Cdd:pfam12894 34 PDKEDLEVTSLAWRPDGKLLAVGYSDGTVRLL 65
|
|
| YncE |
COG3391 |
DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
86-159 |
6.54e-03 |
|
DNA-binding beta-propeller fold protein YncE [General function prediction only];
Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 38.14 E-value: 6.54e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18411222 86 GDAVTGLCFSSDGKSLATACADG----VIrVFKLDdasSKSFKFLRiNLPAGGHPTAVAFADDASSIVVACHHmSGSS 159
Cdd:COG3391 151 GAGPHGIAVDPDGKRLYVANSGSntvsVI-VSVID---TATGKVVA-TIPVGGGPVGVAVSPDGRRLYVANRG-SNTS 222
|
|
|