|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1-330 |
2.64e-154 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 438.58 E-value: 2.64e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 1 LEGHGSSVLSVAFSPDGQRVASGSDDKTIKIWDTASGTGTQTLEGHGGSVWSVAFTPDGQRVASGSDDKTIKIWDAASGT 80
Cdd:COG2319 74 LLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 81 CTQTLEGHGGRVQSVAFSPDGQRVASGSDDHTIKIRDAASGTCTQTLEGHGSSVLSVAFSPDGQRVASGSGDKTIKIWDT 160
Cdd:COG2319 154 LLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDL 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 161 ASGTCTQTLEGHGDSVWSVAFSPDGQRVASGSIDDTIKIWDAASGTCTQTLEGHGGWVHSVAFSPDGQRVASGSIDGTIK 240
Cdd:COG2319 234 ATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVR 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 241 IWDAASGTCTQTLEGHGGWVQSVAFSPDGQRVASGSSDKTIKIWDTASGTCTQTLEGHGGWVQSVAFSPDGQRVASGSSD 320
Cdd:COG2319 314 LWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSAD 393
|
330
....*....|
gi 281410787 321 NTIKIWDTAS 330
Cdd:COG2319 394 GTVRLWDLAT 403
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1-336 |
5.78e-142 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 407.37 E-value: 5.78e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 1 LEGHGSSVLSVAFSPDGQRVASGSDDKTIKIWDTASGTGTQTLEGHGGSVWSVAFTPDGQRVASGSDDKTIKIWDAASGT 80
Cdd:COG2319 32 LLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 81 CTQTLEGHGGRVQSVAFSPDGQRVASGSDDHTIKIRDAASGTCTQTLEGHGSSVLSVAFSPDGQRVASGSGDKTIKIWDT 160
Cdd:COG2319 112 LLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 161 ASGTCTQTLEGHGDSVWSVAFSPDGQRVASGSIDDTIKIWDAASGTCTQTLEGHGGWVHSVAFSPDGQRVASGSIDGTIK 240
Cdd:COG2319 192 ATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVR 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 241 IWDAASGTCTQTLEGHGGWVQSVAFSPDGQRVASGSSDKTIKIWDTASGTCTQTLEGHGGWVQSVAFSPDGQRVASGSSD 320
Cdd:COG2319 272 LWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDD 351
|
330
....*....|....*.
gi 281410787 321 NTIKIWDTASGTCTQT 336
Cdd:COG2319 352 GTVRLWDLATGELLRT 367
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
12-336 |
9.96e-125 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 363.46 E-value: 9.96e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 12 AFSPDGQRVASGSDDKTIKIWDTASGTGTQTLEGHGGSVWSVAFTPDGQRVASGSDDKTIKIWDAASGTCTQTLEGHGGR 91
Cdd:COG2319 1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 92 VQSVAFSPDGQRVASGSDDHTIKIRDAASGTCTQTLEGHGSSVLSVAFSPDGQRVASGSGDKTIKIWDTASGTCTQTLEG 171
Cdd:COG2319 81 VLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 172 HGDSVWSVAFSPDGQRVASGSIDDTIKIWDAASGTCTQTLEGHGGWVHSVAFSPDGQRVASGSIDGTIKIWDAASGTCTQ 251
Cdd:COG2319 161 HSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 252 TLEGHGGWVQSVAFSPDGQRVASGSSDKTIKIWDTASGTCTQTLEGHGGWVQSVAFSPDGQRVASGSSDNTIKIWDTASG 331
Cdd:COG2319 241 TLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATG 320
|
....*
gi 281410787 332 TCTQT 336
Cdd:COG2319 321 KLLRT 325
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
40-327 |
8.56e-119 |
|
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: 344.32 E-value: 8.56e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 40 TQTLEGHGGSVWSVAFTPDGQRVASGSDDKTIKIWDAASGTCTQTLEGHGGRVQSVAFSPDGQRVASGSDDHTIKIRDAA 119
Cdd:cd00200 2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 120 SGTCTQTLEGHGSSVLSVAFSPDGQRVASGSGDKTIKIWDTASGTCTQTLEGHGDSVWSVAFSPDGQRVASGSIDDTIKI 199
Cdd:cd00200 82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 200 WDAASGTCTQTLEGHGGWVHSVAFSPDGQRVASGSIDGTIKIWDAASGTCTQTLEGHGGWVQSVAFSPDGQRVASGSSDK 279
Cdd:cd00200 162 WDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 281410787 280 TIKIWDTASGTCTQTLEGHGGWVQSVAFSPDGQRVASGSSDNTIKIWD 327
Cdd:cd00200 242 TIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1-285 |
7.94e-117 |
|
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: 339.31 E-value: 7.94e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 1 LEGHGSSVLSVAFSPDGQRVASGSDDKTIKIWDTASGTGTQTLEGHGGSVWSVAFTPDGQRVASGSDDKTIKIWDAASGT 80
Cdd:cd00200 5 LKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 81 CTQTLEGHGGRVQSVAFSPDGQRVASGSDDHTIKIRDAASGTCTQTLEGHGSSVLSVAFSPDGQRVASGSGDKTIKIWDT 160
Cdd:cd00200 85 CVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 161 ASGTCTQTLEGHGDSVWSVAFSPDGQRVASGSIDDTIKIWDAASGTCTQTLEGHGGWVHSVAFSPDGQRVASGSIDGTIK 240
Cdd:cd00200 165 RTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIR 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 281410787 241 IWDAASGTCTQTLEGHGGWVQSVAFSPDGQRVASGSSDKTIKIWD 285
Cdd:cd00200 245 VWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
81-336 |
2.16e-100 |
|
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: 297.32 E-value: 2.16e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 81 CTQTLEGHGGRVQSVAFSPDGQRVASGSDDHTIKIRDAASGTCTQTLEGHGSSVLSVAFSPDGQRVASGSGDKTIKIWDT 160
Cdd:cd00200 1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 161 ASGTCTQTLEGHGDSVWSVAFSPDGQRVASGSIDDTIKIWDAASGTCTQTLEGHGGWVHSVAFSPDGQRVASGSIDGTIK 240
Cdd:cd00200 81 ETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 241 IWDAASGTCTQTLEGHGGWVQSVAFSPDGQRVASGSSDKTIKIWDTASGTCTQTLEGHGGWVQSVAFSPDGQRVASGSSD 320
Cdd:cd00200 161 LWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSED 240
|
250
....*....|....*.
gi 281410787 321 NTIKIWDTASGTCTQT 336
Cdd:cd00200 241 GTIRVWDLRTGECVQT 256
|
|
| PLN00181 |
PLN00181 |
protein SPA1-RELATED; Provisional |
19-203 |
3.60e-16 |
|
protein SPA1-RELATED; Provisional
Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 79.36 E-value: 3.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 19 RVASGSDDKTIKIWDTASGTGTQTLEGHGGSVWSVAF-TPDGQRVASGSDDKTIKIWDAASGTCTQTLEGHgGRVQSVAF 97
Cdd:PLN00181 547 QVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYsSADPTLLASGSDDGSVKLWSINQGVSIGTIKTK-ANICCVQF 625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 98 SPD-GQRVASGSDDHTI---KIRDAASGTCTQTleGHGSSVLSVAFSpDGQRVASGSGDKTIKIWD---TASG---TCTQ 167
Cdd:PLN00181 626 PSEsGRSLAFGSADHKVyyyDLRNPKLPLCTMI--GHSKTVSYVRFV-DSSTLVSSSTDNTLKLWDlsmSISGineTPLH 702
|
170 180 190
....*....|....*....|....*....|....*.
gi 281410787 168 TLEGHGDSVWSVAFSPDGQRVASGSIDDTIKIWDAA 203
Cdd:PLN00181 703 SFMGHTNVKNFVGLSVSDGYIATGSETNEVFVYHKA 738
|
|
| PLN00181 |
PLN00181 |
protein SPA1-RELATED; Provisional |
92-329 |
4.45e-16 |
|
protein SPA1-RELATED; Provisional
Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 79.36 E-value: 4.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 92 VQSVAFSPDGQRVASGSDDHTIKIRDAAS------GTCTQTLEGHGSSVLSVAF--SPDGQRVASGSGDKTIKIWDTASG 163
Cdd:PLN00181 486 VCAIGFDRDGEFFATAGVNKKIKIFECESiikdgrDIHYPVVELASRSKLSGICwnSYIKSQVASSNFEGVVQVWDVARS 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 164 TCTQTLEGHGDSVWSVAF-SPDGQRVASGSIDDTIKIWDAASGTCTQTLEGHGGwVHSVAFSPD-GQRVASGSIDGTIKI 241
Cdd:PLN00181 566 QLVTEMKEHEKRVWSIDYsSADPTLLASGSDDGSVKLWSINQGVSIGTIKTKAN-ICCVQFPSEsGRSLAFGSADHKVYY 644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 242 WDAASGT---CTQTleGHGGWVQSVAFSpDGQRVASGSSDKTIKIWD---TASG---TCTQTLEGHGGWVQSVAFSPDGQ 312
Cdd:PLN00181 645 YDLRNPKlplCTMI--GHSKTVSYVRFV-DSSTLVSSSTDNTLKLWDlsmSISGineTPLHSFMGHTNVKNFVGLSVSDG 721
|
250
....*....|....*..
gi 281410787 313 RVASGSSDNTIKIWDTA 329
Cdd:PLN00181 722 YIATGSETNEVFVYHKA 738
|
|
| COG4946 |
COG4946 |
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ... |
89-227 |
3.06e-15 |
|
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown];
Pssm-ID: 443973 [Multi-domain] Cd Length: 1072 Bit Score: 76.62 E-value: 3.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 89 GGRVQSVAFSPDGQRVASGSD---DHTIKIRDAASGTCTQTLEgHGSS--VLSVAFSPDGQRVASGSGDKTIKIWDTASG 163
Cdd:COG4946 342 GVRERLPAWSPDGKSIAYFSDasgEYELYIAPADGSGEPKQLT-LGDLgrVFNPVWSPDGKKIAFTDNRGRLWVVDLASG 420
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281410787 164 TCTQTLEG-HGDSVWSVAFSPDGQRVASGSIDDT----IKIWDAASGTCTQTLEGhGGWVHSVAFSPDG 227
Cdd:COG4946 421 KVRKVDTDgYGDGISDLAWSPDSKWLAYSKPGPNqlsqIFLYDVETGKTVQLTDG-RYDDGSPAFSPDG 488
|
|
| YncE |
COG3391 |
DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
132-331 |
8.10e-15 |
|
DNA-binding beta-propeller fold protein YncE [General function prediction only];
Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 72.80 E-value: 8.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 132 SSVLSVAFSPDGQRVASGSGDKTIKIWDTASGTCTQ-TLEGHGDSVWSVAFSPDGQRV-ASGSIDDTIKIWDAASGTCTQ 209
Cdd:COG3391 25 VAALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLgLGAAAVADADGADAGADGRRLyVANSGSGRVSVIDLATGKVVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 210 TLEgHGGWVHSVAFSPDGQRV-ASGSIDGTIKIWDAASGTCTQTLEGhGGWVQSVAFSPDGQR--VASGSSDKTIKI--- 283
Cdd:COG3391 105 TIP-VGGGPRGLAVDPDGGRLyVADSGNGRVSVIDTATGKVVATIPV-GAGPHGIAVDPDGKRlyVANSGSNTVSVIvsv 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 281410787 284 WDTASGTCTQTLEGhGGWVQSVAFSPDGQRV--------ASGSSDNTIKIWDTASG 331
Cdd:COG3391 183 IDTATGKVVATIPV-GGGPVGVAVSPDGRRLyvanrgsnTSNGGSNTVSVIDLATL 237
|
|
| COG4946 |
COG4946 |
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ... |
13-335 |
1.47e-14 |
|
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown];
Pssm-ID: 443973 [Multi-domain] Cd Length: 1072 Bit Score: 74.69 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 13 FSPDGQRVA-SGSDDKTIKIW--DTASGTGTQtLEGHGGSVWSVAFTPDGQRV--ASGSDDKTIKIW-----DAASGTCT 82
Cdd:COG4946 68 FSPDGKWIAfTSDYDGNTDVYvmPAEGGEPKR-LTYHPANDRVVGWTPDGKSVlfASNRGSPPSRSNqlytvPVDGGLPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 83 QTLEGhggRVQSVAFSPDGQRVA----SGSDDHT----------IKIRDAASGTCTQTLEGHGSSV-----------LS- 136
Cdd:COG4946 147 RLPLP---PAGDGSFSPDGKKLAytriGREFRTWkryrggtagdIWIYDLGTGEFTRLTDFGGNDRnpmwigdriyfLSd 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 137 ------V-AFSPDGQ-------------RVASGSGDK-------TIKIWDTASGTcTQTLE--GHGDSVW---------- 177
Cdd:COG4946 224 rdgtfnLySYDPDGKdlrqlthfkdfdvRFPSTDGGRivyeqggDLYLLDLASGE-PRKLNitLAGDFPQrrprwvdvsg 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 178 ---SVAFSPDGQRVAsgsiddtikiwdaasgtctqtLEGHGgWVHSV---------------------AFSPDGQRVASG 233
Cdd:COG4946 303 yltSFALSPDGKRVA---------------------FEARG-EVFTVpaekgptrnltntpgvrerlpAWSPDGKSIAYF 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 234 S-IDGTIKIW--DAASGTCTQTL-EGHGGWVQSVAFSPDGQRVASGSSDKTIKIWDTASGTCTQTLEG-HGGWVQSVAFS 308
Cdd:COG4946 361 SdASGEYELYiaPADGSGEPKQLtLGDLGRVFNPVWSPDGKKIAFTDNRGRLWVVDLASGKVRKVDTDgYGDGISDLAWS 440
|
410 420 430
....*....|....*....|....*....|.
gi 281410787 309 PDGQRVA-SGSSDNT---IKIWDTASGTCTQ 335
Cdd:COG4946 441 PDSKWLAySKPGPNQlsqIFLYDVETGKTVQ 471
|
|
| COG4946 |
COG4946 |
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ... |
11-311 |
6.03e-14 |
|
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown];
Pssm-ID: 443973 [Multi-domain] Cd Length: 1072 Bit Score: 72.76 E-value: 6.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 11 VAFSPDGQRVAS--------------GSDDKTIKIWDTASGTGTQTLEgHGGS----VWS---VAFTpdgqrvasgSD-D 68
Cdd:COG4946 156 GSFSPDGKKLAYtrigrefrtwkryrGGTAGDIWIYDLGTGEFTRLTD-FGGNdrnpMWIgdrIYFL---------SDrD 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 69 KTIKIW--DAASGTCTQ-T---------LEGHGGRVqsvAFSPDGQ----RVASGSDdHTIKIRdaASGTCTQTLEGH-- 130
Cdd:COG4946 226 GTFNLYsyDPDGKDLRQlThfkdfdvrfPSTDGGRI---VYEQGGDlyllDLASGEP-RKLNIT--LAGDFPQRRPRWvd 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 131 -GSSVLSVAFSPDGQRVAsgsgdktikiwdtasgtctqtLEGHGDSVW--------------------SVAFSPDGQRVA 189
Cdd:COG4946 300 vSGYLTSFALSPDGKRVA---------------------FEARGEVFTvpaekgptrnltntpgvrerLPAWSPDGKSIA 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 190 -----SGSidDTIKIWDAASGTCTQTL-EGHGGWVHSVAFSPDGQRVASGSIDGTIKIWDAASGTCTQTLEG-HGGWVQS 262
Cdd:COG4946 359 yfsdaSGE--YELYIAPADGSGEPKQLtLGDLGRVFNPVWSPDGKKIAFTDNRGRLWVVDLASGKVRKVDTDgYGDGISD 436
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 281410787 263 VAFSPDGQRVASGSSDKT----IKIWDTASGTCTQTLEGhGGWVQSVAFSPDG 311
Cdd:COG4946 437 LAWSPDSKWLAYSKPGPNqlsqIFLYDVETGKTVQLTDG-RYDDGSPAFSPDG 488
|
|
| YncE |
COG3391 |
DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
95-289 |
1.09e-13 |
|
DNA-binding beta-propeller fold protein YncE [General function prediction only];
Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 69.72 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 95 VAFSPDGQRVASGSDDHTIKIRDAASGTCTQTLEGHGSSVLSVAFS-PDGQRV-ASGSGDKTIKIWDTASGTCTQTLEgH 172
Cdd:COG3391 30 LGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAgADGRRLyVANSGSGRVSVIDLATGKVVATIP-V 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 173 GDSVWSVAFSPDGQRV-ASGSIDDTIKIWDAASGTCTQTLEGhGGWVHSVAFSPDGQRV-----ASGSIDGTIKIWDAAS 246
Cdd:COG3391 109 GGGPRGLAVDPDGGRLyVADSGNGRVSVIDTATGKVVATIPV-GAGPHGIAVDPDGKRLyvansGSNTVSVIVSVIDTAT 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 281410787 247 GTCTQTLEGhGGWVQSVAFSPDGQRV--------ASGSSDKTIKIWDTASG 289
Cdd:COG3391 188 GKVVATIPV-GGGPVGVAVSPDGRRLyvanrgsnTSNGGSNTVSVIDLATL 237
|
|
| COG4946 |
COG4946 |
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ... |
10-185 |
1.81e-13 |
|
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown];
Pssm-ID: 443973 [Multi-domain] Cd Length: 1072 Bit Score: 71.22 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 10 SVAFSPDGQRVA---------SGSDDKTIK-IwdtasgtgTQTlegHGGSVWSVAFTPDGQRVA-----SGSDDktikIW 74
Cdd:COG4946 306 SFALSPDGKRVAfeargevftVPAEKGPTRnL--------TNT---PGVRERLPAWSPDGKSIAyfsdaSGEYE----LY 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 75 --DAASGTCTQTL-EGHGGRVQSVAFSPDGQRVASGSDDHTIKIRDAASGTCTQTLEG-HGSSVLSVAFSPDGQRVA--- 147
Cdd:COG4946 371 iaPADGSGEPKQLtLGDLGRVFNPVWSPDGKKIAFTDNRGRLWVVDLASGKVRKVDTDgYGDGISDLAWSPDSKWLAysk 450
|
170 180 190
....*....|....*....|....*....|....*....
gi 281410787 148 -SGSGDKTIKIWDTASGTCTQTLEGHGDSvWSVAFSPDG 185
Cdd:COG4946 451 pGPNQLSQIFLYDVETGKTVQLTDGRYDD-GSPAFSPDG 488
|
|
| PTZ00421 |
PTZ00421 |
coronin; Provisional |
3-160 |
2.73e-11 |
|
coronin; Provisional
Pssm-ID: 173611 [Multi-domain] Cd Length: 493 Bit Score: 64.14 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 3 GHGSSVLSVAFSP-DGQRVASGSDDKTIKIWDTASGTGTQT-------LEGHGGSVWSVAFTPDGQRV-ASGSDDKTIKI 73
Cdd:PTZ00421 73 GQEGPIIDVAFNPfDPQKLFTASEDGTIMGWGIPEEGLTQNisdpivhLQGHTKKVGIVSFHPSAMNVlASAGADMVVNV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 74 WDAASGTCTQTLEGHGGRVQSVAFSPDGQRVASGSDDHTIKIRDAASGTCTQTLEGHGSS-------------VLSVAFS 140
Cdd:PTZ00421 153 WDVERGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRDGTIVSSVEAHASAksqrclwakrkdlIITLGCS 232
|
170 180
....*....|....*....|
gi 281410787 141 PDGQRvasgsgdkTIKIWDT 160
Cdd:PTZ00421 233 KSQQR--------QIMLWDT 244
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
204-243 |
4.05e-11 |
|
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: 57.32 E-value: 4.05e-11
10 20 30 40
....*....|....*....|....*....|....*....|
gi 281410787 204 SGTCTQTLEGHGGWVHSVAFSPDGQRVASGSIDGTIKIWD 243
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| COG4946 |
COG4946 |
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ... |
46-335 |
7.34e-11 |
|
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown];
Pssm-ID: 443973 [Multi-domain] Cd Length: 1072 Bit Score: 63.52 E-value: 7.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 46 HGGSVWSVAFTPDGQRVA-SGSDDKTIKIW--DAASGTCTQtLEGHGGRVQSVAFSPDGQRVASGSDDHTIKIR------ 116
Cdd:COG4946 59 HPGYESFPRFSPDGKWIAfTSDYDGNTDVYvmPAEGGEPKR-LTYHPANDRVVGWTPDGKSVLFASNRGSPPSRsnqlyt 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 117 -DAASGTCTQTLEGHGSSVlsvAFSPDGQRVAS--------------GSGDKTIKIWDTASGTCTQTLEG---------H 172
Cdd:COG4946 138 vPVDGGLPERLPLPPAGDG---SFSPDGKKLAYtrigrefrtwkryrGGTAGDIWIYDLGTGEFTRLTDFggndrnpmwI 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 173 GDSV------------WSvaFSPDGQ-------------RVASGSiDDTI------KIW--DAASGT-----------CT 208
Cdd:COG4946 215 GDRIyflsdrdgtfnlYS--YDPDGKdlrqlthfkdfdvRFPSTD-GGRIvyeqggDLYllDLASGEprklnitlagdFP 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 209 QTLEGH---GGWVHSVAFSPDGQRVAS---GSI------DGTIK-IwdaasgtcTQTLEGHggwVQSVAFSPDGQRVASg 275
Cdd:COG4946 292 QRRPRWvdvSGYLTSFALSPDGKRVAFearGEVftvpaeKGPTRnL--------TNTPGVR---ERLPAWSPDGKSIAY- 359
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281410787 276 SSDKT----IKIWDTASGTCTQTL-EGHGGWVQSVAFSPDGQRVASGSSDNTIKIWDTASGTCTQ 335
Cdd:COG4946 360 FSDASgeyeLYIAPADGSGEPKQLtLGDLGRVFNPVWSPDGKKIAFTDNRGRLWVVDLASGKVRK 424
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
288-327 |
9.46e-11 |
|
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: 56.17 E-value: 9.46e-11
10 20 30 40
....*....|....*....|....*....|....*....|
gi 281410787 288 SGTCTQTLEGHGGWVQSVAFSPDGQRVASGSSDNTIKIWD 327
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
246-285 |
9.84e-11 |
|
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: 56.17 E-value: 9.84e-11
10 20 30 40
....*....|....*....|....*....|....*....|
gi 281410787 246 SGTCTQTLEGHGGWVQSVAFSPDGQRVASGSSDKTIKIWD 285
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| PTZ00421 |
PTZ00421 |
coronin; Provisional |
179-328 |
1.07e-10 |
|
coronin; Provisional
Pssm-ID: 173611 [Multi-domain] Cd Length: 493 Bit Score: 62.60 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 179 VAFSP-DGQRVASGSIDDTIKIWDAASGTCTQT-------LEGHGGWVHSVAFSPDGQRV-ASGSIDGTIKIWDAASGTC 249
Cdd:PTZ00421 81 VAFNPfDPQKLFTASEDGTIMGWGIPEEGLTQNisdpivhLQGHTKKVGIVSFHPSAMNVlASAGADMVVNVWDVERGKA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 250 TQTLEGHGGWVQSVAFSPDGQRVASGSSDKTIKIWDTASGTCTQTLEGHGG-------W------VQSVAFSPDGQRvas 316
Cdd:PTZ00421 161 VEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRDGTIVSSVEAHASaksqrclWakrkdlIITLGCSKSQQR--- 237
|
170
....*....|..
gi 281410787 317 gssdnTIKIWDT 328
Cdd:PTZ00421 238 -----QIMLWDT 244
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
120-159 |
1.73e-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: 55.40 E-value: 1.73e-10
10 20 30 40
....*....|....*....|....*....|....*....|
gi 281410787 120 SGTCTQTLEGHGSSVLSVAFSPDGQRVASGSGDKTIKIWD 159
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
162-201 |
3.65e-10 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 54.63 E-value: 3.65e-10
10 20 30 40
....*....|....*....|....*....|....*....|
gi 281410787 162 SGTCTQTLEGHGDSVWSVAFSPDGQRVASGSIDDTIKIWD 201
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
205-243 |
3.75e-10 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 54.27 E-value: 3.75e-10
10 20 30
....*....|....*....|....*....|....*....
gi 281410787 205 GTCTQTLEGHGGWVHSVAFSPDGQRVASGSIDGTIKIWD 243
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| PTZ00421 |
PTZ00421 |
coronin; Provisional |
213-332 |
5.82e-10 |
|
coronin; Provisional
Pssm-ID: 173611 [Multi-domain] Cd Length: 493 Bit Score: 60.29 E-value: 5.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 213 GHGGWVHSVAFSP-DGQRVASGSIDGTIKIWDAASGTCTQT-------LEGHGGWVQSVAFSPDGQRV-ASGSSDKTIKI 283
Cdd:PTZ00421 73 GQEGPIIDVAFNPfDPQKLFTASEDGTIMGWGIPEEGLTQNisdpivhLQGHTKKVGIVSFHPSAMNVlASAGADMVVNV 152
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 281410787 284 WDTASGTCTQTLEGHGGWVQSVAFSPDGQRVASGSSDNTIKIWDTASGT 332
Cdd:PTZ00421 153 WDVERGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRDGT 201
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
247-285 |
7.55e-10 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 53.50 E-value: 7.55e-10
10 20 30
....*....|....*....|....*....|....*....
gi 281410787 247 GTCTQTLEGHGGWVQSVAFSPDGQRVASGSSDKTIKIWD 285
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
289-327 |
8.41e-10 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 53.50 E-value: 8.41e-10
10 20 30
....*....|....*....|....*....|....*....
gi 281410787 289 GTCTQTLEGHGGWVQSVAFSPDGQRVASGSSDNTIKIWD 327
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
163-201 |
9.46e-10 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 53.12 E-value: 9.46e-10
10 20 30
....*....|....*....|....*....|....*....
gi 281410787 163 GTCTQTLEGHGDSVWSVAFSPDGQRVASGSIDDTIKIWD 201
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| PTZ00421 |
PTZ00421 |
coronin; Provisional |
87-244 |
9.98e-10 |
|
coronin; Provisional
Pssm-ID: 173611 [Multi-domain] Cd Length: 493 Bit Score: 59.52 E-value: 9.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 87 GHGGRVQSVAFSP-DGQRVASGSDDHTIKIRDAASGTCTQT-------LEGHGSSVLSVAFSPDGQRV-ASGSGDKTIKI 157
Cdd:PTZ00421 73 GQEGPIIDVAFNPfDPQKLFTASEDGTIMGWGIPEEGLTQNisdpivhLQGHTKKVGIVSFHPSAMNVlASAGADMVVNV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 158 WDTASGTCTQTLEGHGDSVWSVAFSPDGQRVASGSIDDTIKIWDAASGTCTQTLEGHGG-------W------VHSVAFS 224
Cdd:PTZ00421 153 WDVERGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRDGTIVSSVEAHASaksqrclWakrkdlIITLGCS 232
|
170 180
....*....|....*....|
gi 281410787 225 PDGQRvasgsidgTIKIWDA 244
Cdd:PTZ00421 233 KSQQR--------QIMLWDT 244
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
121-159 |
1.12e-09 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 53.12 E-value: 1.12e-09
10 20 30
....*....|....*....|....*....|....*....
gi 281410787 121 GTCTQTLEGHGSSVLSVAFSPDGQRVASGSGDKTIKIWD 159
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| YncE |
COG3391 |
DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
5-121 |
1.37e-09 |
|
DNA-binding beta-propeller fold protein YncE [General function prediction only];
Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 57.78 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 5 GSSVLSVAFSPDGQRV-ASGSDDKTIKIWDTASGTGTQTLEGhGGSVWSVAFTPDGQR--VASGSDDKTIKI---WDAAS 78
Cdd:COG3391 109 GGGPRGLAVDPDGGRLyVADSGNGRVSVIDTATGKVVATIPV-GAGPHGIAVDPDGKRlyVANSGSNTVSVIvsvIDTAT 187
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 281410787 79 GTCTQTLEGhGGRVQSVAFSPDGQRV--------ASGSDDHTIKIRDAASG 121
Cdd:COG3391 188 GKVVATIPV-GGGPVGVAVSPDGRRLyvanrgsnTSNGGSNTVSVIDLATL 237
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
36-75 |
2.07e-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: 52.31 E-value: 2.07e-09
10 20 30 40
....*....|....*....|....*....|....*....|
gi 281410787 36 SGTGTQTLEGHGGSVWSVAFTPDGQRVASGSDDKTIKIWD 75
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| Pgl |
COG2706 |
6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism]; |
67-336 |
2.28e-09 |
|
6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism];
Pssm-ID: 442025 [Multi-domain] Cd Length: 352 Bit Score: 57.99 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 67 DDKTIKIW--DAASGTCTQ-TLEGHGGRVQSVAFSPDGQR--VASGSDDHTI---KIrDAASGTCTQ--TLEGHGSSVLS 136
Cdd:COG2706 19 ESEGIYVFrlDTATGELTLlGLVAALGNPSFLALSPDGRFlyAVNEVDDGGVsafRI-DPADGTLTLlnTVSSGGASPCH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 137 VAFSPDGQRVASGS-GDKTIKIWDTAS----GTCTQTLEGHGDSVW----------SVAFSPDGQRVAS---GSidDTIK 198
Cdd:COG2706 98 LSVDPDGRFLFVANyGGGSVSVFPIDAdgslGEPVQVIQHEGSGPNperqegphahSVVFDPDGRFLYVpdlGT--DRIY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 199 IW--DAASGTctqtLEGHGGWV--------HsVAFSPDGQRV-ASGSIDGTIKI--WDAASG--TCTQTL----EGHGGW 259
Cdd:COG2706 176 VYrlDPATGK----LPEPPEVSlppgsgprH-LAFHPNGRFAyVINELDSTVSVyaYDAATGtlTLIQTVstlpEDFTGE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 260 VQS--VAFSPDGQRV-ASGSSDKTIKIW----DTASGTCTQTLEGHGGWVQSVAFSPDGQRV-ASGSSDNTIKIW--DTA 329
Cdd:COG2706 251 NWAadIHISPDGRFLyVSNRGHNSIAVFaidaDGGKLTLVGHVPTGGKWPRDFAIDPDGRFLlVANQKSDNITVFriDAD 330
|
....*..
gi 281410787 330 SGTCTQT 336
Cdd:COG2706 331 TGKLTPT 337
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
40-75 |
7.32e-09 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 50.81 E-value: 7.32e-09
10 20 30
....*....|....*....|....*....|....*.
gi 281410787 40 TQTLEGHGGSVWSVAFTPDGQRVASGSDDKTIKIWD 75
Cdd:pfam00400 4 LKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1-33 |
9.11e-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: 50.39 E-value: 9.11e-09
10 20 30
....*....|....*....|....*....|...
gi 281410787 1 LEGHGSSVLSVAFSPDGQRVASGSDDKTIKIWD 33
Cdd:smart00320 8 LKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
78-117 |
1.92e-08 |
|
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: 49.62 E-value: 1.92e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 281410787 78 SGTCTQTLEGHGGRVQSVAFSPDGQRVASGSDDHTIKIRD 117
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1-33 |
2.92e-08 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 49.27 E-value: 2.92e-08
10 20 30
....*....|....*....|....*....|...
gi 281410787 1 LEGHGSSVLSVAFSPDGQRVASGSDDKTIKIWD 33
Cdd:pfam00400 7 LEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| YncE |
COG3391 |
DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
174-336 |
3.08e-08 |
|
DNA-binding beta-propeller fold protein YncE [General function prediction only];
Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 53.54 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 174 DSVWSVAFSPDGQRVASGSIDDTIKIWDAASGTCTQTLEGHGGWVHSVAFS-PDGQRV-ASGSIDGTIKIWDAASGTCTQ 251
Cdd:COG3391 25 VAALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAgADGRRLyVANSGSGRVSVIDLATGKVVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 252 TLEgHGGWVQSVAFSPDGQRV-ASGSSDKTIKIWDTASGTCTQTLEGhGGWVQSVAFSPDGQR--VASGSSDNTIKI--- 325
Cdd:COG3391 105 TIP-VGGGPRGLAVDPDGGRLyVADSGNGRVSVIDTATGKVVATIPV-GAGPHGIAVDPDGKRlyVANSGSNTVSVIvsv 182
|
170
....*....|.
gi 281410787 326 WDTASGTCTQT 336
Cdd:COG3391 183 IDTATGKVVAT 193
|
|
| TolB |
COG0823 |
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ... |
104-242 |
5.37e-08 |
|
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440585 [Multi-domain] Cd Length: 158 Bit Score: 51.60 E-value: 5.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 104 VASGSDDHTIKIRDAASGTCTQtLEGHGSSVLSVAFSPDGQRVA---SGSGDKTIKIWDTASGTcTQTLEGHGDSVWSVA 180
Cdd:COG0823 4 TLSRDGNSDIYVVDLDGGEPRR-LTNSPGIDTSPAWSPDGRRIAftsDRGGGPQIYVVDADGGE-PRRLTFGGGYNASPS 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281410787 181 FSPDGQRVA-SGSIDDTIKIW--DAASGTCTQTLEGHggwvHSVAFSPDGQRVA-SGSIDGTIKIW 242
Cdd:COG0823 82 WSPDGKRLAfVSRSDGRFDIYvlDLDGGAPRRLTDGP----GSPSWSPDGRRIVfSSDRGGRPDLY 143
|
|
| TolB |
COG0823 |
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ... |
179-326 |
7.74e-08 |
|
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440585 [Multi-domain] Cd Length: 158 Bit Score: 51.21 E-value: 7.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 179 VAFSpdgqRVASGSIDdtIKIWDAASGTCTQtLEGHGGWVHSVAFSPDGQRVA-SGSIDGTIKIW--DAASGTcTQTLEG 255
Cdd:COG0823 1 LAFT----LSRDGNSD--IYVVDLDGGEPRR-LTNSPGIDTSPAWSPDGRRIAfTSDRGGGPQIYvvDADGGE-PRRLTF 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281410787 256 HGGWVQSVAFSPDGQRVA-SGSSDKTIKIW--DTASGTCTQTLEGHGgwvqSVAFSPDGQRVA-SGSSDNTIKIW 326
Cdd:COG0823 73 GGGYNASPSWSPDGKRLAfVSRSDGRFDIYvlDLDGGAPRRLTDGPG----SPSWSPDGRRIVfSSDRGGRPDLY 143
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
79-117 |
1.17e-07 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 47.34 E-value: 1.17e-07
10 20 30
....*....|....*....|....*....|....*....
gi 281410787 79 GTCTQTLEGHGGRVQSVAFSPDGQRVASGSDDHTIKIRD 117
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| PLN00181 |
PLN00181 |
protein SPA1-RELATED; Provisional |
1-161 |
1.79e-07 |
|
protein SPA1-RELATED; Provisional
Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 52.78 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 1 LEGHGSSVLSVAFSP-DGQRVASGSDDKTIKIWDTASGTGTQTLEGHgGSVWSVAFTPD-GQRVASGSDDKTIKIWDAAS 78
Cdd:PLN00181 571 MKEHEKRVWSIDYSSaDPTLLASGSDDGSVKLWSINQGVSIGTIKTK-ANICCVQFPSEsGRSLAFGSADHKVYYYDLRN 649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 79 GT---CTQTleGHGGRVQSVAFSpDGQRVASGSDDHTIKIRD---AASG---TCTQTLEGHGSSVLSVAFSPDGQRVASG 149
Cdd:PLN00181 650 PKlplCTMI--GHSKTVSYVRFV-DSSTLVSSSTDNTLKLWDlsmSISGineTPLHSFMGHTNVKNFVGLSVSDGYIATG 726
|
170
....*....|..
gi 281410787 150 SGDKTIKIWDTA 161
Cdd:PLN00181 727 SETNEVFVYHKA 738
|
|
| COG4946 |
COG4946 |
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ... |
8-101 |
2.25e-07 |
|
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown];
Pssm-ID: 443973 [Multi-domain] Cd Length: 1072 Bit Score: 52.35 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 8 VLSVAFSPDGQRVASGSDDKTIKIWDTASGTGTQTLEG-HGGSVWSVAFTPDGQRVASGSDDKT----IKIWDAASGTCT 82
Cdd:COG4946 391 VFNPVWSPDGKKIAFTDNRGRLWVVDLASGKVRKVDTDgYGDGISDLAWSPDSKWLAYSKPGPNqlsqIFLYDVETGKTV 470
|
90
....*....|....*....
gi 281410787 83 QTLEGhGGRVQSVAFSPDG 101
Cdd:COG4946 471 QLTDG-RYDDGSPAFSPDG 488
|
|
| TolB |
COG0823 |
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ... |
20-159 |
2.40e-07 |
|
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: 49.67 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 20 VASGSDDKTIKIWDTASGTGTQtLEGHGGSVWSVAFTPDGQRVASGSDDKT---IKIWDAASGTcTQTLEGHGGRVQSVA 96
Cdd:COG0823 4 TLSRDGNSDIYVVDLDGGEPRR-LTNSPGIDTSPAWSPDGRRIAFTSDRGGgpqIYVVDADGGE-PRRLTFGGGYNASPS 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281410787 97 FSPDGQRVA--SGSDDHT-IKIRDAASGTCTQTLEGHGssvlSVAFSPDGQRVA---SGSGDKTIKIWD 159
Cdd:COG0823 82 WSPDGKRLAfvSRSDGRFdIYVLDLDGGAPRRLTDGPG----SPSWSPDGRRIVfssDRGGRPDLYVVD 146
|
|
| PTZ00421 |
PTZ00421 |
coronin; Provisional |
1-93 |
6.70e-07 |
|
coronin; Provisional
Pssm-ID: 173611 [Multi-domain] Cd Length: 493 Bit Score: 50.66 E-value: 6.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 1 LEGHGSSVLSVAFSPDGQRV-ASGSDDKTIKIWDTASGTGTQTLEGHGGSVWSVAFTPDGQRVASGSDDKTIKIWDAASG 79
Cdd:PTZ00421 121 LQGHTKKVGIVSFHPSAMNVlASAGADMVVNVWDVERGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRDG 200
|
90
....*....|....*
gi 281410787 80 TCTQTLEGH-GGRVQ 93
Cdd:PTZ00421 201 TIVSSVEAHaSAKSQ 215
|
|
| TolB |
COG0823 |
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ... |
1-105 |
1.34e-05 |
|
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: 44.66 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 1 LEGHGSSVLSVAFSPDGQRVASGSDDKTIK-IWD-TASGTGTQTLEGHGGSVWSVAFTPDGQRVA-SGSDDKTIKIW--D 75
Cdd:COG0823 26 LTNSPGIDTSPAWSPDGRRIAFTSDRGGGPqIYVvDADGGEPRRLTFGGGYNASPSWSPDGKRLAfVSRSDGRFDIYvlD 105
|
90 100 110
....*....|....*....|....*....|
gi 281410787 76 AASGTCTQTLEGHGgrvqSVAFSPDGQRVA 105
Cdd:COG0823 106 LDGGAPRRLTDGPG----SPSWSPDGRRIV 131
|
|
| 8prop_hemeD1_NirF |
cd20778 |
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ... |
151-230 |
1.95e-05 |
|
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; Denitrification is a process that enables biofilm formation of the opportunistic human pathogen Pseudomonas aeruginosa, making it more resilient to antibiotics and highly adaptable to different habitats. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO3- -> NO2- -> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic cytochrome cd1 (nitrite reductase) NirS via its maturation factor NirF. The nirFDLGHJE genes encode proteins required for heme d1 biosynthesis. NirS, NirF, and NirN, the monomeric dihydro-heme d1 dehydrogenase form a stable complex during nitrite reductase maturation. The nitrite reductase NirS is bound to the denitrification supercomplex via NorB, while the electron donor system NirM and the enzyme maturation machinery NirN-NirF-NirQ, interacting with NirS, are bound via NorC.
Pssm-ID: 467722 [Multi-domain] Cd Length: 381 Bit Score: 45.74 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 151 GDKTIKIWDTASGTCTQTLEGHGDSVWSVAfSPDGQRVA---SGSIDDTIKIWDAASGTCTQTLEgHGGWVHSVAFSPDG 227
Cdd:cd20778 259 GEHRVLVYDTNDWKFIKSIPLAGQPVFAVA-RPDGRYVWvnfSGPDNDTVQVIDTKTLKVVKTLE-PGKRVLHMEFTPRG 336
|
...
gi 281410787 228 QRV 230
Cdd:cd20778 337 EAV 339
|
|
| 8prop_hemeD1_NirF |
cd20778 |
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ... |
51-162 |
3.64e-05 |
|
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; Denitrification is a process that enables biofilm formation of the opportunistic human pathogen Pseudomonas aeruginosa, making it more resilient to antibiotics and highly adaptable to different habitats. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO3- -> NO2- -> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic cytochrome cd1 (nitrite reductase) NirS via its maturation factor NirF. The nirFDLGHJE genes encode proteins required for heme d1 biosynthesis. NirS, NirF, and NirN, the monomeric dihydro-heme d1 dehydrogenase form a stable complex during nitrite reductase maturation. The nitrite reductase NirS is bound to the denitrification supercomplex via NorB, while the electron donor system NirM and the enzyme maturation machinery NirN-NirF-NirQ, interacting with NirS, are bound via NorC.
Pssm-ID: 467722 [Multi-domain] Cd Length: 381 Bit Score: 44.97 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 51 WSVAftpDGQRVASGSDDKTIKIWDAASGTCTQTLEGHGGRVQSVAfSPDGQRVA---SGSDDHTIKIRDAASGTCTQTL 127
Cdd:cd20778 246 WAVA---GDKAFVPAVGEHRVLVYDTNDWKFIKSIPLAGQPVFAVA-RPDGRYVWvnfSGPDNDTVQVIDTKTLKVVKTL 321
|
90 100 110
....*....|....*....|....*....|....*.
gi 281410787 128 EgHGSSVLSVAFSPDGQRV-ASGSGDKTIKIWDTAS 162
Cdd:cd20778 322 E-PGKRVLHMEFTPRGEAVyISVNDDNKVVVYDTRT 356
|
|
| ANAPC4_WD40 |
pfam12894 |
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ... |
72-140 |
4.36e-05 |
|
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: 41.49 E-value: 4.36e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281410787 72 KIWDAAsgtctqtLEGHGGRVQSVAFSPDGQRVASGSDDHTIKIRDAASGTCTQTLEGHGSSVLSVAFS 140
Cdd:pfam12894 28 RVWTLS-------PDKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSAGSDLITCLGWG 89
|
|
| 8prop_hemeD1_NirF |
cd20778 |
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ... |
4-78 |
7.15e-05 |
|
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; Denitrification is a process that enables biofilm formation of the opportunistic human pathogen Pseudomonas aeruginosa, making it more resilient to antibiotics and highly adaptable to different habitats. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO3- -> NO2- -> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic cytochrome cd1 (nitrite reductase) NirS via its maturation factor NirF. The nirFDLGHJE genes encode proteins required for heme d1 biosynthesis. NirS, NirF, and NirN, the monomeric dihydro-heme d1 dehydrogenase form a stable complex during nitrite reductase maturation. The nitrite reductase NirS is bound to the denitrification supercomplex via NorB, while the electron donor system NirM and the enzyme maturation machinery NirN-NirF-NirQ, interacting with NirS, are bound via NorC.
Pssm-ID: 467722 [Multi-domain] Cd Length: 381 Bit Score: 44.20 E-value: 7.15e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281410787 4 HGSSVLSVAfSPDGQRVA---SGSDDKTIKIWDTASGTGTQTLEgHGGSVWSVAFTPDGQRV-ASGSDDKTIKIWDAAS 78
Cdd:cd20778 280 AGQPVFAVA-RPDGRYVWvnfSGPDNDTVQVIDTKTLKVVKTLE-PGKRVLHMEFTPRGEAVyISVNDDNKVVVYDTRT 356
|
|
| PQQ_ABC_repeats |
TIGR03866 |
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family ... |
26-268 |
9.20e-05 |
|
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family consist of seven repeats each of the YVTN family beta-propeller repeat (see TIGR02276). Members occur invariably as part of a transport operon that is associated with PQQ-dependent catabolism of alcohols such as phenylethanol.
Pssm-ID: 274824 [Multi-domain] Cd Length: 310 Bit Score: 43.49 E-value: 9.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 26 DKTIKIWDTASGTGTQTLEGhGGSVWSVAFTPDGQRV-ASGSDDKTIKIWDAASGTCTQTLEGhGGRVQSVAFSPDGQRV 104
Cdd:TIGR03866 20 DNTISVIDTATLKVTRTFPV-GQRPRGITFSKDGKLLyVCASDSDTIQVIDPATGEVLHTLPS-GPDPEQFALHPNGKIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 105 -ASGSDDHTIKIRDAASGTCTQTL------EGhgssvlsVAFSPDGQRVASGSGDKTIKIW-DTASGTCT-QTLEGHGDS 175
Cdd:TIGR03866 98 yIANEDDALVTVIDIETRKVLAQIdvgvepEG-------MAVSPDGKIVVNTSETTNMAHWiDTATYEIVdNTLVDARPR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 176 vwSVAFSPDGQRV-ASGSIDDTIKIWDAAS----GTCTQTLEG-HGGWVHSV--AFSPDGQR--VASGSIDgTIKIWDAA 245
Cdd:TIGR03866 171 --FAEFTADGKELwVSSEIGGTVTVIDVATrkviKKITFAIPGvHPEKVQPVgiKLTKDGKTafVALGPAN-RVAVVDAK 247
|
250 260
....*....|....*....|...
gi 281410787 246 SGTCTQTLEgHGGWVQSVAFSPD 268
Cdd:TIGR03866 248 TYEVLDYLL-VGQRVWQLAFTPD 269
|
|
| COG4946 |
COG4946 |
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ... |
223-336 |
1.38e-04 |
|
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown];
Pssm-ID: 443973 [Multi-domain] Cd Length: 1072 Bit Score: 43.87 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 223 FSPDGQRVA-SGSIDGTIKIW--DAASGTCTQtLEGHGGWVQSVAFSPDGQRVASGSSDKTIKIW-------DTASGTCT 292
Cdd:COG4946 68 FSPDGKWIAfTSDYDGNTDVYvmPAEGGEPKR-LTYHPANDRVVGWTPDGKSVLFASNRGSPPSRsnqlytvPVDGGLPE 146
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 281410787 293 QTLEGHGGWVqsvAFSPDGQRVA--------------SGSSDNTIKIWDTASGTCTQT 336
Cdd:COG4946 147 RLPLPPAGDG---SFSPDGKKLAytrigrefrtwkryRGGTAGDIWIYDLGTGEFTRL 201
|
|
| ANAPC4_WD40 |
pfam12894 |
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ... |
198-266 |
1.42e-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: 40.34 E-value: 1.42e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281410787 198 KIWDAAsgtctqtLEGHGGWVHSVAFSPDGQRVASGSIDGTIKIWDAASGTCTQTLEGHGGWVQSVAFS 266
Cdd:pfam12894 28 RVWTLS-------PDKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSAGSDLITCLGWG 89
|
|
| PLN00181 |
PLN00181 |
protein SPA1-RELATED; Provisional |
218-336 |
1.52e-04 |
|
protein SPA1-RELATED; Provisional
Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 43.54 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 218 VHSVAFSPDGQRVASGSIDGTIKIWDAASgTCTQTLEGHGGWVQSVAFSPDG---------QRVASGSSDKTIKIWDTAS 288
Cdd:PLN00181 486 VCAIGFDRDGEFFATAGVNKKIKIFECES-IIKDGRDIHYPVVELASRSKLSgicwnsyikSQVASSNFEGVVQVWDVAR 564
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 281410787 289 GTCTQTLEGHGGWVQSVAFSP-DGQRVASGSSDNTIKIWDTASGTCTQT 336
Cdd:PLN00181 565 SQLVTEMKEHEKRVWSIDYSSaDPTLLASGSDDGSVKLWSINQGVSIGT 613
|
|
| PTZ00421 |
PTZ00421 |
coronin; Provisional |
255-336 |
1.68e-04 |
|
coronin; Provisional
Pssm-ID: 173611 [Multi-domain] Cd Length: 493 Bit Score: 43.34 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 255 GHGGWVQSVAFSP-DGQRVASGSSDKTIKIWDTASGTCTQT-------LEGHGGWVQSVAFSPDGQRV-ASGSSDNTIKI 325
Cdd:PTZ00421 73 GQEGPIIDVAFNPfDPQKLFTASEDGTIMGWGIPEEGLTQNisdpivhLQGHTKKVGIVSFHPSAMNVlASAGADMVVNV 152
|
90
....*....|.
gi 281410787 326 WDTASGTCTQT 336
Cdd:PTZ00421 153 WDVERGKAVEV 163
|
|
| TolB |
COG0823 |
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ... |
230-335 |
2.34e-04 |
|
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: 41.20 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 230 VASGSIDGTIKIW--DAASGTCTQtLEGHGGWVQSVAFSPDGQRVA-----SGSSDktIKIWDTASGTcTQTLEGHGGWV 302
Cdd:COG0823 2 AFTLSRDGNSDIYvvDLDGGEPRR-LTNSPGIDTSPAWSPDGRRIAftsdrGGGPQ--IYVVDADGGE-PRRLTFGGGYN 77
|
90 100 110
....*....|....*....|....*....|....*.
gi 281410787 303 QSVAFSPDGQRVA-SGSSDNTIKIW--DTASGTCTQ 335
Cdd:COG0823 78 ASPSWSPDGKRLAfVSRSDGRFDIYvlDLDGGAPRR 113
|
|
| 8prop_hemeD1_NirF |
cd20778 |
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ... |
263-330 |
2.48e-04 |
|
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; Denitrification is a process that enables biofilm formation of the opportunistic human pathogen Pseudomonas aeruginosa, making it more resilient to antibiotics and highly adaptable to different habitats. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO3- -> NO2- -> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic cytochrome cd1 (nitrite reductase) NirS via its maturation factor NirF. The nirFDLGHJE genes encode proteins required for heme d1 biosynthesis. NirS, NirF, and NirN, the monomeric dihydro-heme d1 dehydrogenase form a stable complex during nitrite reductase maturation. The nitrite reductase NirS is bound to the denitrification supercomplex via NorB, while the electron donor system NirM and the enzyme maturation machinery NirN-NirF-NirQ, interacting with NirS, are bound via NorC.
Pssm-ID: 467722 [Multi-domain] Cd Length: 381 Bit Score: 42.66 E-value: 2.48e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281410787 263 VAFSPDGQRVA---SGSSDKTIKIWDTASGTCTQTLEgHGGWVQSVAFSPDGQRV-ASGSSDNTIKIWDTAS 330
Cdd:cd20778 286 AVARPDGRYVWvnfSGPDNDTVQVIDTKTLKVVKTLE-PGKRVLHMEFTPRGEAVyISVNDDNKVVVYDTRT 356
|
|
| DPPIV_N |
pfam00930 |
Dipeptidyl peptidase IV (DPP IV) N-terminal region; This family is an alignment of the region ... |
98-309 |
3.14e-04 |
|
Dipeptidyl peptidase IV (DPP IV) N-terminal region; This family is an alignment of the region to the N-terminal side of the active site. The Prosite motif does not correspond to this Pfam entry.
Pssm-ID: 395744 [Multi-domain] Cd Length: 352 Bit Score: 41.92 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 98 SPDGQRV-----------ASGSDDHTIkiRDAASGTCTQTLEGHGssVLSVA-FSPDGQRVASGSgDKTIKIWDTASGTC 165
Cdd:pfam00930 1 SPDGKYLllatnytknwrHSYTADYYI--YDLETNRVEPLPPGEG--KIQDAkWSPDGDRLAFVR-DNNLYVRELATGKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 166 TQ-TLEG-----HGDSVW-----------SVAFSPDGQRVASGSIDDT-IKIWDAASgtctQTLEGHGGWVHSVAFSpdg 227
Cdd:pfam00930 76 IQiTSDGsdgifNGVADWvyeeevlgsnsAVWWSPDGSRLAFLRFDESeVPIITLPY----YTDEGPGPEVREIKYP--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 228 qrvASGSIDGTIK--IWDAASGTCTQT-----LEGHGGWVQSVAFSPDG----QRVASGSSDKTIKIWDTASGTCTQTL- 295
Cdd:pfam00930 149 ---KAGAPNPTVElfVYDLASGKTVEVvppddLSDADYYITRVKWVPDGkllvQWLNRDQNRLKVVLCDAETGRTVVILe 225
|
250
....*....|....*..
gi 281410787 296 EGHGGWV---QSVAFSP 309
Cdd:pfam00930 226 ETSDGWVelhQDPHFIK 242
|
|
| 8prop_hemeD1_NirF |
cd20778 |
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ... |
25-120 |
4.74e-04 |
|
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: 41.50 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 25 DDKTIKIWDTASGTGTQTLEGHGGSVWSVAfTPDGQRVA---SGSDDKTIKIWDAASGTCTQTLEgHGGRVQSVAFSPDG 101
Cdd:cd20778 259 GEHRVLVYDTNDWKFIKSIPLAGQPVFAVA-RPDGRYVWvnfSGPDNDTVQVIDTKTLKVVKTLE-PGKRVLHMEFTPRG 336
|
90 100
....*....|....*....|
gi 281410787 102 QRV-ASGSDDHTIKIRDAAS 120
Cdd:cd20778 337 EAVyISVNDDNKVVVYDTRT 356
|
|
| PTZ00420 |
PTZ00420 |
coronin; Provisional |
127-296 |
5.03e-04 |
|
coronin; Provisional
Pssm-ID: 240412 [Multi-domain] Cd Length: 568 Bit Score: 41.86 E-value: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 127 LEGHGSSVLSVAFSP-DGQRVASGSGDKTIKIW----------DTASGTCtqTLEGHGDSVWSVAFSPDGQRV-ASGSID 194
Cdd:PTZ00420 70 LKGHTSSILDLQFNPcFSEILASGSEDLTIRVWeiphndesvkEIKDPQC--ILKGHKKKISIIDWNPMNYYImCSSGFD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 195 DTIKIWDAA--------------------------SGTCTqtleghGGWVHSVafSPDGQRVASgsidgTIKIWDAASGT 248
Cdd:PTZ00420 148 SFVNIWDIEnekrafqinmpkklsslkwnikgnllSGTCV------GKHMHII--DPRKQEIAS-----SFHIHDGGKNT 214
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 281410787 249 CTQTLEGHGG---WVQSVAFSPDGQRvasgssdkTIKIWD---TASGTCTQTLE 296
Cdd:PTZ00420 215 KNIWIDGLGGddnYILSTGFSKNNMR--------EMKLWDlknTTSALVTMSID 260
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
5-227 |
7.12e-04 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 40.77 E-value: 7.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 5 GSSVLSVAFSPDGQRVASGSDDKTIKIWDTASGTGTQTLEGHGGSVWSVAFTPDGQRVASGSDDKTIKIWDAASGTCTQT 84
Cdd:COG4257 16 GSGPRDVAVDPDGAVWFTDQGGGRIGRLDPATGEFTEYPLGGGSGPHGIAVDPDGNLWFTDNGNNRIGRIDPKTGEITTF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 85 -LEGHGGRVQSVAFSPDGQRVASGSDDHTIKIRDAASGTCTQTLEGHGSSVLS-VAFSPDGQR-VASGSGDKTIKIwDTA 161
Cdd:COG4257 96 aLPGGGSNPHGIAFDPDGNLWFTDQGGNRIGRLDPATGEVTEFPLPTGGAGPYgIAVDPDGNLwVTDFGANAIGRI-DPD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281410787 162 SGTCTQ-TLEGHGDSVWSVAFSPDGQRVASGSIDDTIKIWDAASGTCTQ-TLEGHGGWVHSVAFSPDG 227
Cdd:COG4257 175 TGTLTEyALPTPGAGPRGLAVDPDGNLWVADTGSGRIGRFDPKTGTVTEyPLPGGGARPYGVAVDGDG 242
|
|
| ANAPC4_WD40 |
pfam12894 |
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ... |
127-180 |
9.95e-04 |
|
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC,
Pssm-ID: 403945 [Multi-domain] Cd Length: 91 Bit Score: 37.64 E-value: 9.95e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 281410787 127 LEGHGSSVLSVAFSPDGQRVASGSGDKTIKIWDTASGTCTQTLEGHGDSV----WSVA 180
Cdd:pfam12894 34 PDKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSAGSDLItclgWGEN 91
|
|
| ANAPC4_WD40 |
pfam12894 |
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ... |
282-333 |
1.09e-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: 37.64 E-value: 1.09e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 281410787 282 KIWDTAsgtctqtLEGHGGWVQSVAFSPDGQRVASGSSDNTIKIWDTASGTC 333
Cdd:pfam12894 28 RVWTLS-------PDKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKI 72
|
|
| Pgl |
COG2706 |
6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism]; |
5-210 |
1.24e-03 |
|
6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism];
Pssm-ID: 442025 [Multi-domain] Cd Length: 352 Bit Score: 40.27 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 5 GSSVLSVAFSPDGQR--VASGSDDK--TIKIWDTAS-GTGTQTLEGHGGSVW----------SVAFTPDGQRVAS---GS 66
Cdd:COG2706 92 GASPCHLSVDPDGRFlfVANYGGGSvsVFPIDADGSlGEPVQVIQHEGSGPNperqegphahSVVFDPDGRFLYVpdlGT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 67 DdkTIKIW--DAASGT-----CTQTLEGHGGRvqSVAFSPDGQRV-ASGSDDHTIKI--RDAASG--TCTQTL----EGH 130
Cdd:COG2706 172 D--RIYVYrlDPATGKlpeppEVSLPPGSGPR--HLAFHPNGRFAyVINELDSTVSVyaYDAATGtlTLIQTVstlpEDF 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 131 GSSVLS--VAFSPDGQRV-ASGSGDKTIKIW----DTASGTCTQTLEGHGDSVWSVAFSPDGQRV-ASGSIDDTIKIW-- 200
Cdd:COG2706 248 TGENWAadIHISPDGRFLyVSNRGHNSIAVFaidaDGGKLTLVGHVPTGGKWPRDFAIDPDGRFLlVANQKSDNITVFri 327
|
250
....*....|
gi 281410787 201 DAASGTCTQT 210
Cdd:COG2706 328 DADTGKLTPT 337
|
|
| NBCH_WD40 |
pfam20426 |
Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at ... |
146-238 |
1.60e-03 |
|
Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at the C-terminus of neurobeachin-like proteins.
Pssm-ID: 466575 [Multi-domain] Cd Length: 350 Bit Score: 40.06 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 146 VASGSGDKTIKIWDTASGTCTQTLEGHGDSVWSVAFSPDGQRVASGSIDDTIKIWDAASGTC-------TQT-------- 210
Cdd:pfam20426 97 ISCGNWENSFQVISLNDGRMVQSIRQHKDVVSCVAVTSDGSILATGSYDTTVMVWEVLRGRSsekrsrnTQTefprkdhv 176
|
90 100 110
....*....|....*....|....*....|....*.
gi 281410787 211 --------LEGHGGWVHSVAFSPDGQRVASGSIDGT 238
Cdd:pfam20426 177 iaetpfhiLCGHDDIITCLYVSVELDIVISGSKDGT 212
|
|
| PTZ00420 |
PTZ00420 |
coronin; Provisional |
1-75 |
1.68e-03 |
|
coronin; Provisional
Pssm-ID: 240412 [Multi-domain] Cd Length: 568 Bit Score: 39.93 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 1 LEGHGSSVLSVAFSP-DGQRVASGSDDKTIKIWDTASGTGTQT--------LEGHGGSVWSVAFTPDGQRVASGSD-DKT 70
Cdd:PTZ00420 70 LKGHTSSILDLQFNPcFSEILASGSEDLTIRVWEIPHNDESVKeikdpqciLKGHKKKISIIDWNPMNYYIMCSSGfDSF 149
|
....*
gi 281410787 71 IKIWD 75
Cdd:PTZ00420 150 VNIWD 154
|
|
| Ge1_WD40 |
pfam16529 |
WD40 region of Ge1, enhancer of mRNA-decapping protein; Ge1_WD40 is the N-terminal region of ... |
222-295 |
2.09e-03 |
|
WD40 region of Ge1, enhancer of mRNA-decapping protein; Ge1_WD40 is the N-terminal region of Ge-1 or enhancer of mRNA-decapping proteins. WD40-repeat regions are involved in protein-protein interactions.
Pssm-ID: 465162 [Multi-domain] Cd Length: 328 Bit Score: 39.36 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 222 AFSPDGQRVASGSIDGTIKIW-----DAASGTCTQTLEGHGGWVQSVAF-------SPDGQ----RVASGSSDKTIKIWD 285
Cdd:pfam16529 193 AFSPDGTALATASLDGEVKFFqiylfDNRNPRCLHEWKPHDGKPLSSLFfldnhkkPPEVQfwrfAITGADNNSELKLWS 272
|
90
....*....|
gi 281410787 286 TASGTCTQTL 295
Cdd:pfam16529 273 CESWTCLQTI 282
|
|
| 8prop_hemeD1_NirF |
cd20778 |
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ... |
199-288 |
3.02e-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: 39.19 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 199 IWDAASGTCTQTLEGHGGWVHSVAfSPDGQRVA---SGSIDGTIKIWDAASGTCTQTLEgHGGWVQSVAFSPDGQRV-AS 274
Cdd:cd20778 265 VYDTNDWKFIKSIPLAGQPVFAVA-RPDGRYVWvnfSGPDNDTVQVIDTKTLKVVKTLE-PGKRVLHMEFTPRGEAVyIS 342
|
90
....*....|....
gi 281410787 275 GSSDKTIKIWDTAS 288
Cdd:cd20778 343 VNDDNKVVVYDTRT 356
|
|
| ANAPC4_WD40 |
pfam12894 |
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ... |
240-308 |
3.06e-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: 3.06e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281410787 240 KIWDAAsgtctqtLEGHGGWVQSVAFSPDGQRVASGSSDKTIKIWDTASGTCTQTLEGHGGWVQSVAFS 308
Cdd:pfam12894 28 RVWTLS-------PDKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSAGSDLITCLGWG 89
|
|
| ANAPC4_WD40 |
pfam12894 |
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ... |
30-98 |
3.21e-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: 3.21e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281410787 30 KIWDTAsgtgtqtLEGHGGSVWSVAFTPDGQRVASGSDDKTIKIWDAASGTCTQTLEGHGGRVQSVAFS 98
Cdd:pfam12894 28 RVWTLS-------PDKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSAGSDLITCLGWG 89
|
|
| COG4946 |
COG4946 |
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ... |
2-59 |
4.61e-03 |
|
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown];
Pssm-ID: 443973 [Multi-domain] Cd Length: 1072 Bit Score: 38.87 E-value: 4.61e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281410787 2 EGHGSSVLSVAFSPDGQRVASGSDDKT----IKIWDTASGTGTQTLEGhGGSVWSVAFTPDG 59
Cdd:COG4946 428 DGYGDGISDLAWSPDSKWLAYSKPGPNqlsqIFLYDVETGKTVQLTDG-RYDDGSPAFSPDG 488
|
|
| Ge1_WD40 |
pfam16529 |
WD40 region of Ge1, enhancer of mRNA-decapping protein; Ge1_WD40 is the N-terminal region of ... |
264-336 |
5.09e-03 |
|
WD40 region of Ge1, enhancer of mRNA-decapping protein; Ge1_WD40 is the N-terminal region of Ge-1 or enhancer of mRNA-decapping proteins. WD40-repeat regions are involved in protein-protein interactions.
Pssm-ID: 465162 [Multi-domain] Cd Length: 328 Bit Score: 38.21 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281410787 264 AFSPDGQRVASGSSDKTIKIW-----DTASGTCTQTLEGHGGWVQSVAF-------SPDGQ---RVASGSSDNT-IKIWD 327
Cdd:pfam16529 193 AFSPDGTALATASLDGEVKFFqiylfDNRNPRCLHEWKPHDGKPLSSLFfldnhkkPPEVQfwrFAITGADNNSeLKLWS 272
|
....*....
gi 281410787 328 TASGTCTQT 336
Cdd:pfam16529 273 CESWTCLQT 281
|
|
| ANAPC4_WD40 |
pfam12894 |
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ... |
156-224 |
8.29e-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: 35.33 E-value: 8.29e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281410787 156 KIWDTAsgtctqtLEGHGDSVWSVAFSPDGQRVASGSIDDTIKIWDAASGTCTQTLEGHGGWVHSVAFS 224
Cdd:pfam12894 28 RVWTLS-------PDKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSAGSDLITCLGWG 89
|
|
| |
