|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
49-362 |
1.63e-33 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 133.88 E-value: 1.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741849 49 LLGHFGCVNAIEFSNNGgQWLVSGGDDRRVLLWHMEQAihsrvKPIQLKGEHHSNIFCLAFNSGNTKVFSGGNDEQVILH 128
Cdd:COG2319 116 LTGHTGAVRSVAFSPDG-KTLASGSADGTVRLWDLATG-----KLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLW 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741849 129 DVESSETLDVF-AHEDAVYGLSVSPvNDNIFASSSDDGRVLIWDIRESPhgEPFCLANYPSAFHSVMFNPvEPRLLATAN 207
Cdd:COG2319 190 DLATGKLLRTLtGHTGAVRSVAFSP-DGKLLASGSADGTVRLWDLATGK--LLRTLTGHSGSVRSVAFSP-DGRLLASGS 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741849 208 SKEGVGLWDIRKPQSsLLRYGGNLSlqSAMSVRFNSNGTQLLA------LRrrlppvLYDIHSRLPVFQFdnQGYFNSCT 281
Cdd:COG2319 266 ADGTVRLWDLATGEL-LRTLTGHSG--GVNSVAFSPDGKLLASgsddgtVR------LWDLATGKLLRTL--TGHTGAVR 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741849 282 mkSCCFAGDrDQYILSGSDDFNLYMWripaDPEAGGIGRVvngafmvLKGHRSIVNQVRFNPHTYMICSSGVEKIIKIWS 361
Cdd:COG2319 335 --SVAFSPD-GKTLASGSDDGTVRLW----DLATGELLRT-------LTGHTGAVTSVAFSPDGRTLASGSADGTVRLWD 400
|
.
gi 55741849 362 P 362
Cdd:COG2319 401 L 401
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
49-361 |
4.47e-31 |
|
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: 123.98 E-value: 4.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741849 49 LLGHFGCVNAIEFSNNGgQWLVSGGDDRRVLLWHMEQAIHSRvkpiQLKGeHHSNIFCLAFNSGNTKVFSGGNDEQVILH 128
Cdd:cd00200 5 LKGHTGGVTCVAFSPDG-KLLATGSGDGTIKVWDLETGELLR----TLKG-HTGPVRDVAASADGTYLASGSSDKTIRLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741849 129 DVESSETLDVFA-HEDAVYGLSVSPvNDNIFASSSDDGRVLIWDIRESPhgepfCLANYPSAFHSVM---FNPvEPRLLA 204
Cdd:cd00200 79 DLETGECVRTLTgHTSYVSSVAFSP-DGRILSSSSRDKTIKVWDVETGK-----CLTTLRGHTDWVNsvaFSP-DGTFVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741849 205 TAnSKEG-VGLWDIRKPQSSLLRYGGNLSLQSamsVRFNSNGTQLLA------LRrrlppvLYDIHSRLPVFQFD-NQGY 276
Cdd:cd00200 152 SS-SQDGtIKLWDLRTGKCVATLTGHTGEVNS---VAFSPDGEKLLSsssdgtIK------LWDLSTGKCLGTLRgHENG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741849 277 FNSCtmkscCFAGDRDqYILSGSDDFNLYMWRIpadpeagGIGRVVngafMVLKGHRSIVNQVRFNPHTYMICSSGVEKI 356
Cdd:cd00200 222 VNSV-----AFSPDGY-LLASGSEDGTIRVWDL-------RTGECV----QTLSGHTNSVTSLAWSPDGKRLASGSADGT 284
|
....*
gi 55741849 357 IKIWS 361
Cdd:cd00200 285 IRIWD 289
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
140-171 |
3.02e-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: 41.91 E-value: 3.02e-05
10 20 30
....*....|....*....|....*....|..
gi 55741849 140 AHEDAVYGLSVSPvNDNIFASSSDDGRVLIWD 171
Cdd:smart00320 10 GHTGPVTSVAFSP-DGKYLASGSDDGTIKLWD 40
|
|
| PTZ00420 |
PTZ00420 |
coronin; Provisional |
286-360 |
1.21e-04 |
|
coronin; Provisional
Pssm-ID: 240412 [Multi-domain] Cd Length: 568 Bit Score: 45.71 E-value: 1.21e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55741849 286 CFAgdrdQYILSGSDDFNLYMWRIPADPEAGgigRVVNGAFMVLKGHRSIVNQVRFNPHTYMI-CSSGVEKIIKIW 360
Cdd:PTZ00420 85 CFS----EILASGSEDLTIRVWEIPHNDESV---KEIKDPQCILKGHKKKISIIDWNPMNYYImCSSGFDSFVNIW 153
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
49-81 |
1.61e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 39.64 E-value: 1.61e-04
10 20 30
....*....|....*....|....*....|...
gi 55741849 49 LLGHFGCVNAIEFSNNGgQWLVSGGDDRRVLLW 81
Cdd:pfam00400 7 LEGHTGSVTSLAFSPDG-KLLASGSDDGTVKVW 38
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
49-362 |
1.63e-33 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 133.88 E-value: 1.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741849 49 LLGHFGCVNAIEFSNNGgQWLVSGGDDRRVLLWHMEQAihsrvKPIQLKGEHHSNIFCLAFNSGNTKVFSGGNDEQVILH 128
Cdd:COG2319 116 LTGHTGAVRSVAFSPDG-KTLASGSADGTVRLWDLATG-----KLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLW 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741849 129 DVESSETLDVF-AHEDAVYGLSVSPvNDNIFASSSDDGRVLIWDIRESPhgEPFCLANYPSAFHSVMFNPvEPRLLATAN 207
Cdd:COG2319 190 DLATGKLLRTLtGHTGAVRSVAFSP-DGKLLASGSADGTVRLWDLATGK--LLRTLTGHSGSVRSVAFSP-DGRLLASGS 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741849 208 SKEGVGLWDIRKPQSsLLRYGGNLSlqSAMSVRFNSNGTQLLA------LRrrlppvLYDIHSRLPVFQFdnQGYFNSCT 281
Cdd:COG2319 266 ADGTVRLWDLATGEL-LRTLTGHSG--GVNSVAFSPDGKLLASgsddgtVR------LWDLATGKLLRTL--TGHTGAVR 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741849 282 mkSCCFAGDrDQYILSGSDDFNLYMWripaDPEAGGIGRVvngafmvLKGHRSIVNQVRFNPHTYMICSSGVEKIIKIWS 361
Cdd:COG2319 335 --SVAFSPD-GKTLASGSDDGTVRLW----DLATGELLRT-------LTGHTGAVTSVAFSPDGRTLASGSADGTVRLWD 400
|
.
gi 55741849 362 P 362
Cdd:COG2319 401 L 401
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
49-361 |
4.47e-31 |
|
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: 123.98 E-value: 4.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741849 49 LLGHFGCVNAIEFSNNGgQWLVSGGDDRRVLLWHMEQAIHSRvkpiQLKGeHHSNIFCLAFNSGNTKVFSGGNDEQVILH 128
Cdd:cd00200 5 LKGHTGGVTCVAFSPDG-KLLATGSGDGTIKVWDLETGELLR----TLKG-HTGPVRDVAASADGTYLASGSSDKTIRLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741849 129 DVESSETLDVFA-HEDAVYGLSVSPvNDNIFASSSDDGRVLIWDIRESPhgepfCLANYPSAFHSVM---FNPvEPRLLA 204
Cdd:cd00200 79 DLETGECVRTLTgHTSYVSSVAFSP-DGRILSSSSRDKTIKVWDVETGK-----CLTTLRGHTDWVNsvaFSP-DGTFVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741849 205 TAnSKEG-VGLWDIRKPQSSLLRYGGNLSLQSamsVRFNSNGTQLLA------LRrrlppvLYDIHSRLPVFQFD-NQGY 276
Cdd:cd00200 152 SS-SQDGtIKLWDLRTGKCVATLTGHTGEVNS---VAFSPDGEKLLSsssdgtIK------LWDLSTGKCLGTLRgHENG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741849 277 FNSCtmkscCFAGDRDqYILSGSDDFNLYMWRIpadpeagGIGRVVngafMVLKGHRSIVNQVRFNPHTYMICSSGVEKI 356
Cdd:cd00200 222 VNSV-----AFSPDGY-LLASGSEDGTIRVWDL-------RTGECV----QTLSGHTNSVTSLAWSPDGKRLASGSADGT 284
|
....*
gi 55741849 357 IKIWS 361
Cdd:cd00200 285 IRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
3-362 |
2.44e-30 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 124.64 E-value: 2.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741849 3 RRAGLGGSMRSVVGFLSQRGLHGDPLLTQDFQRRRLRGcRNLYKKDLLGHFGCVNAIEFSNNGgQWLVSGGDDRRVLLWH 82
Cdd:COG2319 29 LLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAA-AGALLATLLGHTAAVLSVAFSPDG-RLLASASADGTVRLWD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741849 83 MEQAihsrvKPIQLKGEHHSNIFCLAFNSGNTKVFSGGNDEQVILHDVESSETLDVF-AHEDAVYGLSVSPvNDNIFASS 161
Cdd:COG2319 107 LATG-----LLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLtGHSGAVTSVAFSP-DGKLLASG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741849 162 SDDGRVLIWDIREsphGEPFC-LANYPSAFHSVMFNPvEPRLLATANSKEGVGLWDIRKPQsSLLRYGGNLSlqSAMSVR 240
Cdd:COG2319 181 SDDGTVRLWDLAT---GKLLRtLTGHTGAVRSVAFSP-DGKLLASGSADGTVRLWDLATGK-LLRTLTGHSG--SVRSVA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741849 241 FNSNGTQLLA------LRrrlppvLYDIHSRLPVFQFDNQgyfnSCTMKSCCFAGDrDQYILSGSDDFNLYMWRIPAdpe 314
Cdd:COG2319 254 FSPDGRLLASgsadgtVR------LWDLATGELLRTLTGH----SGGVNSVAFSPD-GKLLASGSDDGTVRLWDLAT--- 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 55741849 315 aggiGRVVNGafmvLKGHRSIVNQVRFNPHTYMICSSGVEKIIKIWSP 362
Cdd:COG2319 320 ----GKLLRT----LTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDL 359
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
46-171 |
3.19e-14 |
|
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: 74.29 E-value: 3.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741849 46 KKDLLGHFGCVNAIEFSNNGGQwLVSGGDDRRVLLW--HMEQAIHsrvkpiQLKGeHHSNIFCLAFNSGNTKVFSGGNDE 123
Cdd:cd00200 170 VATLTGHTGEVNSVAFSPDGEK-LLSSSSDGTIKLWdlSTGKCLG------TLRG-HENGVNSVAFSPDGYLLASGSEDG 241
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 55741849 124 QVILHDVESSETLDVF-AHEDAVYGLSVSPvNDNIFASSSDDGRVLIWD 171
Cdd:cd00200 242 TIRVWDLRTGECVQTLsGHTNSVTSLAWSP-DGKRLASGSADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
49-132 |
3.26e-09 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 59.92 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741849 49 LLGHFGCVNAIEFSNNGgQWLVSGGDDRRVLLWHMEQAihsrvKPIQLKGEHHSNIFCLAFNSGNTKVFSGGNDEQVILH 128
Cdd:COG2319 326 LTGHTGAVRSVAFSPDG-KTLASGSDDGTVRLWDLATG-----ELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLW 399
|
....
gi 55741849 129 DVES 132
Cdd:COG2319 400 DLAT 403
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
140-171 |
3.02e-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: 41.91 E-value: 3.02e-05
10 20 30
....*....|....*....|....*....|..
gi 55741849 140 AHEDAVYGLSVSPvNDNIFASSSDDGRVLIWD 171
Cdd:smart00320 10 GHTGPVTSVAFSP-DGKYLASGSDDGTIKLWD 40
|
|
| PTZ00420 |
PTZ00420 |
coronin; Provisional |
286-360 |
1.21e-04 |
|
coronin; Provisional
Pssm-ID: 240412 [Multi-domain] Cd Length: 568 Bit Score: 45.71 E-value: 1.21e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55741849 286 CFAgdrdQYILSGSDDFNLYMWRIPADPEAGgigRVVNGAFMVLKGHRSIVNQVRFNPHTYMI-CSSGVEKIIKIW 360
Cdd:PTZ00420 85 CFS----EILASGSEDLTIRVWEIPHNDESV---KEIKDPQCILKGHKKKISIIDWNPMNYYImCSSGFDSFVNIW 153
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
327-361 |
1.56e-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: 39.99 E-value: 1.56e-04
10 20 30
....*....|....*....|....*....|....*
gi 55741849 327 MVLKGHRSIVNQVRFNPHTYMICSSGVEKIIKIWS 361
Cdd:smart00320 6 KTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
49-81 |
1.61e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 39.64 E-value: 1.61e-04
10 20 30
....*....|....*....|....*....|...
gi 55741849 49 LLGHFGCVNAIEFSNNGgQWLVSGGDDRRVLLW 81
Cdd:pfam00400 7 LEGHTGSVTSLAFSPDG-KLLASGSDDGTVKVW 38
|
|
| PLN00181 |
PLN00181 |
protein SPA1-RELATED; Provisional |
19-224 |
1.73e-04 |
|
protein SPA1-RELATED; Provisional
Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 45.46 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741849 19 SQRGLHGDPLLTQ-----DFQRRRLRGcrNLYKKDLLGHFGCVNAIEFSNNGgQWLVSGGDDRRVLLWHME------QAI 87
Cdd:PLN00181 446 SRQGGWIDPFLEGlckylSFSKLRVKA--DLKQGDLLNSSNLVCAIGFDRDG-EFFATAGVNKKIKIFECEsiikdgRDI 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741849 88 HSRVkpIQLKGEhhSNIFCLAFNSG-NTKVFSGGNDEQVILHDVESSETL-DVFAHEDAVYGLSVSPVNDNIFASSSDDG 165
Cdd:PLN00181 523 HYPV--VELASR--SKLSGICWNSYiKSQVASSNFEGVVQVWDVARSQLVtEMKEHEKRVWSIDYSSADPTLLASGSDDG 598
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 55741849 166 RVLIWDIREsphGEPFCLANYPSAFHSVMFNPVEPRLLATANSKEGVGLWDIRKPQSSL 224
Cdd:PLN00181 599 SVKLWSINQ---GVSIGTIKTKANICCVQFPSESGRSLAFGSADHKVYYYDLRNPKLPL 654
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
140-171 |
2.27e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 39.25 E-value: 2.27e-04
10 20 30
....*....|....*....|....*....|..
gi 55741849 140 AHEDAVYGLSVSPvNDNIFASSSDDGRVLIWD 171
Cdd:pfam00400 9 GHTGSVTSLAFSP-DGKLLASGSDDGTVKVWD 39
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
51-82 |
9.34e-04 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 37.68 E-value: 9.34e-04
10 20 30
....*....|....*....|....*....|..
gi 55741849 51 GHFGCVNAIEFSNNGgQWLVSGGDDRRVLLWH 82
Cdd:smart00320 10 GHTGPVTSVAFSPDG-KYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
327-361 |
1.39e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 37.32 E-value: 1.39e-03
10 20 30
....*....|....*....|....*....|....*
gi 55741849 327 MVLKGHRSIVNQVRFNPHTYMICSSGVEKIIKIWS 361
Cdd:pfam00400 5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| YncE |
COG3391 |
DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
59-172 |
1.92e-03 |
|
DNA-binding beta-propeller fold protein YncE [General function prediction only];
Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 40.83 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741849 59 IEFSNNGGQWLVSGGDDRRVLLwhMEQAIHSRVKPIQLKGEHHSnifcLAFNSGNTKVF---SGGNDEQVILH--DVESS 133
Cdd:COG3391 115 LAVDPDGGRLYVADSGNGRVSV--IDTATGKVVATIPVGAGPHG----IAVDPDGKRLYvanSGSNTVSVIVSviDTATG 188
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 55741849 134 ETLDVFAHEDAVYGLSVSPVNDNIF-------ASSSDDGRVLIWDI 172
Cdd:COG3391 189 KVVATIPVGGGPVGVAVSPDGRRLYvanrgsnTSNGGSNTVSVIDL 234
|
|
| 8prop_hemeD1_NirF |
cd20778 |
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ... |
117-175 |
9.09e-03 |
|
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: 39.57 E-value: 9.09e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55741849 117 FSGGNDE--QVIlhDVESSETLDVFAHEDAVYGLSVSPVNDNIFASSSDDGRVLIWDIRES 175
Cdd:cd20778 299 FSGPDNDtvQVI--DTKTLKVVKTLEPGKRVLHMEFTPRGEAVYISVNDDNKVVVYDTRTF 357
|
|
|