|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
19-332 |
6.66e-24 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 102.68 E-value: 6.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PM9_A 19 AWSHDKiPLLVSGtvsgtvdanfSTDSSLELWSLlaaDSEKPIASLQVDSKF-NDLDWSHNNKIIAGALDNGSLELYSTN 97
Cdd:COG2319 127 AFSPDG-KTLASG----------SADGTVRLWDL---ATGKLLRTLTGHSGAvTSVAFSPDGKLLASGSDDGTVRLWDLA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PM9_A 98 EANnainSMARFSNHSSSVKTVKFNAkQDNVLASGGNNGEIFIWDMNkctespsnyTPLTPGQSMSSVDEVISLAWNQSl 177
Cdd:COG2319 193 TGK----LLRTLTGHTGAVRSVAFSP-DGKLLASGSADGTVRLWDLA---------TGKLLRTLTGHSGSVRSVAFSPD- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PM9_A 178 AHVFASAGSSNFASIWDLKAKKEVIHLSytspnsGIKQQLSVVEWHPkNSTRVATAtgsDNDPSILIWDLRNaNTPLQTL 257
Cdd:COG2319 258 GRLLASGSADGTVRLWDLATGELLRTLT------GHSGGVNSVAFSP-DGKLLASG---SDDGTVRLWDLAT-GKLLRTL 326
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
2PM9_A 258 nQGHQKGILSLDWcHQDEHLLLSSGRDNTVLLWNPESAEQLSQFPARGNWCFKTKFAPEApDLFACASFDNKIEV 332
Cdd:COG2319 327 -TGHTGAVRSVAF-SPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDG-RTLASGSADGTVRL 398
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
22-332 |
2.46e-21 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 93.17 E-value: 2.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PM9_A 22 HDKIPLLVSGtvsgtvdanfSTDSSLELWSLlaaDSEKPIASLQVDSKF-NDLDWS-HNNKIIAGALDNgSLELYSTNEA 99
Cdd:cd00200 18 SPDGKLLATG----------SGDGTIKVWDL---ETGELLRTLKGHTGPvRDVAASaDGTYLASGSSDK-TIRLWDLETG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PM9_A 100 NNAInsmaRFSNHSSSVKTVKFNAKqDNVLASGGNNGEIFIWDMNKCTESPSnytplTPGQSmssvDEVISLAWNQSLAH 179
Cdd:cd00200 84 ECVR----TLTGHTSYVSSVAFSPD-GRILSSSSRDKTIKVWDVETGKCLTT-----LRGHT----DWVNSVAFSPDGTF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PM9_A 180 VfASAGSSNFASIWDLKAKKEVIHLSytspnsGIKQQLSVVEWHPKNStRVATATGsdnDPSILIWDLRNAnTPLQTLnQ 259
Cdd:cd00200 150 V-ASSSQDGTIKLWDLRTGKCVATLT------GHTGEVNSVAFSPDGE-KLLSSSS---DGTIKLWDLSTG-KCLGTL-R 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
2PM9_A 260 GHQKGILSLDWcHQDEHLLLSSGRDNTVLLWNPESAEQLSQFPARGNWCFKTKFAPEAPDLFACaSFDNKIEV 332
Cdd:cd00200 217 GHENGVNSVAF-SPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASG-SADGTIRI 287
|
|
| PLN00181 |
PLN00181 |
protein SPA1-RELATED; Provisional |
156-337 |
7.27e-07 |
|
protein SPA1-RELATED; Provisional
Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 51.63 E-value: 7.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PM9_A 156 LTPGQSMSSVDEVISLAWNQSlAHVFASAGSSNFASIWDLKA-KKEVIHLSYTSPNSGIKQQLSVVEWHPKNSTRVATat 234
Cdd:PLN00181 474 LKQGDLLNSSNLVCAIGFDRD-GEFFATAGVNKKIKIFECESiIKDGRDIHYPVVELASRSKLSGICWNSYIKSQVAS-- 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PM9_A 235 gSDNDPSILIWDLrnANTPLQTLNQGHQKGILSLDWCHQDEHLLLSSGRDNTVLLWNPESAEQLSQFPARGNWCFkTKFA 314
Cdd:PLN00181 551 -SNFEGVVQVWDV--ARSQLVTEMKEHEKRVWSIDYSSADPTLLASGSDDGSVKLWSINQGVSIGTIKTKANICC-VQFP 626
|
170 180
....*....|....*....|...
2PM9_A 315 PEAPDLFACASFDNKIEVQTLQN 337
Cdd:PLN00181 627 SESGRSLAFGSADHKVYYYDLRN 649
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
252-291 |
1.07e-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: 39.22 E-value: 1.07e-04
10 20 30 40
....*....|....*....|....*....|....*....|
2PM9_A 252 TPLQTLnQGHQKGILSLDWcHQDEHLLLSSGRDNTVLLWN 291
Cdd:smart00320 3 ELLKTL-KGHTGPVTSVAF-SPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
251-291 |
2.00e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 38.48 E-value: 2.00e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
2PM9_A 251 NTPLQTLnQGHQKGILSLDWcHQDEHLLLSSGRDNTVLLWN 291
Cdd:pfam00400 1 GKLLKTL-EGHTGSVTSLAF-SPDGKLLASGSDDGTVKVWD 39
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
19-332 |
6.66e-24 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 102.68 E-value: 6.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PM9_A 19 AWSHDKiPLLVSGtvsgtvdanfSTDSSLELWSLlaaDSEKPIASLQVDSKF-NDLDWSHNNKIIAGALDNGSLELYSTN 97
Cdd:COG2319 127 AFSPDG-KTLASG----------SADGTVRLWDL---ATGKLLRTLTGHSGAvTSVAFSPDGKLLASGSDDGTVRLWDLA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PM9_A 98 EANnainSMARFSNHSSSVKTVKFNAkQDNVLASGGNNGEIFIWDMNkctespsnyTPLTPGQSMSSVDEVISLAWNQSl 177
Cdd:COG2319 193 TGK----LLRTLTGHTGAVRSVAFSP-DGKLLASGSADGTVRLWDLA---------TGKLLRTLTGHSGSVRSVAFSPD- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PM9_A 178 AHVFASAGSSNFASIWDLKAKKEVIHLSytspnsGIKQQLSVVEWHPkNSTRVATAtgsDNDPSILIWDLRNaNTPLQTL 257
Cdd:COG2319 258 GRLLASGSADGTVRLWDLATGELLRTLT------GHSGGVNSVAFSP-DGKLLASG---SDDGTVRLWDLAT-GKLLRTL 326
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
2PM9_A 258 nQGHQKGILSLDWcHQDEHLLLSSGRDNTVLLWNPESAEQLSQFPARGNWCFKTKFAPEApDLFACASFDNKIEV 332
Cdd:COG2319 327 -TGHTGAVRSVAF-SPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDG-RTLASGSADGTVRL 398
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
22-332 |
2.46e-21 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 93.17 E-value: 2.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PM9_A 22 HDKIPLLVSGtvsgtvdanfSTDSSLELWSLlaaDSEKPIASLQVDSKF-NDLDWS-HNNKIIAGALDNgSLELYSTNEA 99
Cdd:cd00200 18 SPDGKLLATG----------SGDGTIKVWDL---ETGELLRTLKGHTGPvRDVAASaDGTYLASGSSDK-TIRLWDLETG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PM9_A 100 NNAInsmaRFSNHSSSVKTVKFNAKqDNVLASGGNNGEIFIWDMNKCTESPSnytplTPGQSmssvDEVISLAWNQSLAH 179
Cdd:cd00200 84 ECVR----TLTGHTSYVSSVAFSPD-GRILSSSSRDKTIKVWDVETGKCLTT-----LRGHT----DWVNSVAFSPDGTF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PM9_A 180 VfASAGSSNFASIWDLKAKKEVIHLSytspnsGIKQQLSVVEWHPKNStRVATATGsdnDPSILIWDLRNAnTPLQTLnQ 259
Cdd:cd00200 150 V-ASSSQDGTIKLWDLRTGKCVATLT------GHTGEVNSVAFSPDGE-KLLSSSS---DGTIKLWDLSTG-KCLGTL-R 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
2PM9_A 260 GHQKGILSLDWcHQDEHLLLSSGRDNTVLLWNPESAEQLSQFPARGNWCFKTKFAPEAPDLFACaSFDNKIEV 332
Cdd:cd00200 217 GHENGVNSVAF-SPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASG-SADGTIRI 287
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
42-291 |
5.86e-21 |
|
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: 92.01 E-value: 5.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PM9_A 42 STDSSLELWSLlaaDSEKPIASL-QVDSKFNDLDWSHNNKIIAGALDNGSLELYSTNEANNAINsmarFSNHSSSVKTVK 120
Cdd:cd00200 70 SSDKTIRLWDL---ETGECVRTLtGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTT----LRGHTDWVNSVA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PM9_A 121 FNaKQDNVLASGGNNGEIFIWDMN--KCTESPSNYTpltpgqsmssvDEVISLAWNQSLAHvFASAGSSNFASIWDLKAK 198
Cdd:cd00200 143 FS-PDGTFVASSSQDGTIKLWDLRtgKCVATLTGHT-----------GEVNSVAFSPDGEK-LLSSSSDGTIKLWDLSTG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PM9_A 199 KEVihLSYTSPNSGIkqqLSVVeWHPKNSTrvatATGSDNDPSILIWDLRNAnTPLQTLnQGHQKGILSLDWcHQDEHLL 278
Cdd:cd00200 210 KCL--GTLRGHENGV---NSVA-FSPDGYL----LASGSEDGTIRVWDLRTG-ECVQTL-SGHTNSVTSLAW-SPDGKRL 276
|
250
....*....|...
2PM9_A 279 LSSGRDNTVLLWN 291
Cdd:cd00200 277 ASGSADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
19-294 |
9.05e-21 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 93.44 E-value: 9.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PM9_A 19 AWSHDKiPLLVSGtvsgtvdanfSTDSSLELWSLlaaDSEKPIASLQVDSKF-NDLDWSHNNKIIAGALDNGSLELYSTN 97
Cdd:COG2319 169 AFSPDG-KLLASG----------SDDGTVRLWDL---ATGKLLRTLTGHTGAvRSVAFSPDGKLLASGSADGTVRLWDLA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PM9_A 98 EANnainSMARFSNHSSSVKTVKFNAkQDNVLASGGNNGEIFIWDmnkcTESPSNYTPLTPGQsmssvDEVISLAWNQSl 177
Cdd:COG2319 235 TGK----LLRTLTGHSGSVRSVAFSP-DGRLLASGSADGTVRLWD----LATGELLRTLTGHS-----GGVNSVAFSPD- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PM9_A 178 AHVFASAGSSNFASIWDLKAKKEVIHLSytspnsGIKQQLSVVEWHPkNSTRVATAtGSDNdpSILIWDLRNaNTPLQTL 257
Cdd:COG2319 300 GKLLASGSDDGTVRLWDLATGKLLRTLT------GHTGAVRSVAFSP-DGKTLASG-SDDG--TVRLWDLAT-GELLRTL 368
|
250 260 270
....*....|....*....|....*....|....*..
2PM9_A 258 nQGHQKGILSLDWcHQDEHLLLSSGRDNTVLLWNPES 294
Cdd:COG2319 369 -TGHTGAVTSVAF-SPDGRTLASGSADGTVRLWDLAT 403
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
112-332 |
1.37e-20 |
|
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: 91.24 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PM9_A 112 HSSSVKTVKFNAKQdNVLASGGNNGEIFIWDMNKCTESPSNYTPLtpgqsmSSVDEVISLAWNQSLahvfASAGSSNFAS 191
Cdd:cd00200 8 HTGGVTCVAFSPDG-KLLATGSGDGTIKVWDLETGELLRTLKGHT------GPVRDVAASADGTYL----ASGSSDKTIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PM9_A 192 IWDLKAKKEVI----HLSYT-----SPNSGI----KQQLSVVEWHPKNSTRVAT-------------------ATGSDND 239
Cdd:cd00200 77 LWDLETGECVRtltgHTSYVssvafSPDGRIlsssSRDKTIKVWDVETGKCLTTlrghtdwvnsvafspdgtfVASSSQD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PM9_A 240 PSILIWDLRNaNTPLQTLnQGHQKGILSLDWcHQDEHLLLSSGRDNTVLLWNPESAEQLSQFPARGNWCFKTKFAPEaPD 319
Cdd:cd00200 157 GTIKLWDLRT-GKCVATL-TGHTGEVNSVAF-SPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPD-GY 232
|
250
....*....|...
2PM9_A 320 LFACASFDNKIEV 332
Cdd:cd00200 233 LLASGSEDGTIRV 245
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
166-332 |
2.08e-12 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 68.40 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PM9_A 166 DEVISLAWnQSLAHVFASAGSSNFASIWDLKAKKEVIHLSytspnsGIKQQLSVVEWHPkNSTRVATATGsdnDPSILIW 245
Cdd:COG2319 79 AAVLSVAF-SPDGRLLASASADGTVRLWDLATGLLLRTLT------GHTGAVRSVAFSP-DGKTLASGSA---DGTVRLW 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PM9_A 246 DLRNAnTPLQTLNqGHQKGILSLDWcHQDEHLLLSSGRDNTVLLWNPESAEQLSQFPARGNWCFKTKFAPEApDLFACAS 325
Cdd:COG2319 148 DLATG-KLLRTLT-GHSGAVTSVAF-SPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDG-KLLASGS 223
|
....*..
2PM9_A 326 FDNKIEV 332
Cdd:COG2319 224 ADGTVRL 230
|
|
| PLN00181 |
PLN00181 |
protein SPA1-RELATED; Provisional |
156-337 |
7.27e-07 |
|
protein SPA1-RELATED; Provisional
Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 51.63 E-value: 7.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PM9_A 156 LTPGQSMSSVDEVISLAWNQSlAHVFASAGSSNFASIWDLKA-KKEVIHLSYTSPNSGIKQQLSVVEWHPKNSTRVATat 234
Cdd:PLN00181 474 LKQGDLLNSSNLVCAIGFDRD-GEFFATAGVNKKIKIFECESiIKDGRDIHYPVVELASRSKLSGICWNSYIKSQVAS-- 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PM9_A 235 gSDNDPSILIWDLrnANTPLQTLNQGHQKGILSLDWCHQDEHLLLSSGRDNTVLLWNPESAEQLSQFPARGNWCFkTKFA 314
Cdd:PLN00181 551 -SNFEGVVQVWDV--ARSQLVTEMKEHEKRVWSIDYSSADPTLLASGSDDGSVKLWSINQGVSIGTIKTKANICC-VQFP 626
|
170 180
....*....|....*....|...
2PM9_A 315 PEAPDLFACASFDNKIEVQTLQN 337
Cdd:PLN00181 627 SESGRSLAFGSADHKVYYYDLRN 649
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
259-337 |
3.57e-05 |
|
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: 45.40 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PM9_A 259 QGHQKGILSLDWcHQDEHLLLSSGRDNTVLLWNPESAEQL------SQFPARGNWCFKTKFapeapdlFACASFDNKIEV 332
Cdd:cd00200 6 KGHTGGVTCVAF-SPDGKLLATGSGDGTIKVWDLETGELLrtlkghTGPVRDVAASADGTY-------LASGSSDKTIRL 77
|
....*
2PM9_A 333 QTLQN 337
Cdd:cd00200 78 WDLET 82
|
|
| PLN00181 |
PLN00181 |
protein SPA1-RELATED; Provisional |
111-291 |
3.72e-05 |
|
protein SPA1-RELATED; Provisional
Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 45.85 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PM9_A 111 NHSSSVKTVKFNaKQDNVLASGGNNGEIFIWDMNKCTESpsNYTPLTPGQSMSSVDEVISLAWNQSLAHVFASAGSSNFA 190
Cdd:PLN00181 481 NSSNLVCAIGFD-RDGEFFATAGVNKKIKIFECESIIKD--GRDIHYPVVELASRSKLSGICWNSYIKSQVASSNFEGVV 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PM9_A 191 SIWDL----------KAKKEVIHLSYTSPNSGI----KQQLSVVEWHPKNSTRVATATGSDN------------------ 238
Cdd:PLN00181 558 QVWDVarsqlvtemkEHEKRVWSIDYSSADPTLlasgSDDGSVKLWSINQGVSIGTIKTKANiccvqfpsesgrslafgs 637
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
2PM9_A 239 -DPSILIWDLRNANTPLQTLnQGHQKGILSLDWChqDEHLLLSSGRDNTVLLWN 291
Cdd:PLN00181 638 aDHKVYYYDLRNPKLPLCTM-IGHSKTVSYVRFV--DSSTLVSSSTDNTLKLWD 688
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
252-291 |
1.07e-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: 39.22 E-value: 1.07e-04
10 20 30 40
....*....|....*....|....*....|....*....|
2PM9_A 252 TPLQTLnQGHQKGILSLDWcHQDEHLLLSSGRDNTVLLWN 291
Cdd:smart00320 3 ELLKTL-KGHTGPVTSVAF-SPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
251-291 |
2.00e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 38.48 E-value: 2.00e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
2PM9_A 251 NTPLQTLnQGHQKGILSLDWcHQDEHLLLSSGRDNTVLLWN 291
Cdd:pfam00400 1 GKLLKTL-EGHTGSVTSLAF-SPDGKLLASGSDDGTVKVWD 39
|
|
| PTZ00420 |
PTZ00420 |
coronin; Provisional |
108-235 |
2.17e-03 |
|
coronin; Provisional
Pssm-ID: 240412 [Multi-domain] Cd Length: 568 Bit Score: 40.32 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PM9_A 108 RFSNHSSSVKTVKFNAKQDNVLASGGNNGEIFIWDMNKCTESPSNYTplTPGQSMSSVDEVIS-LAWNQSLAHVFASAGS 186
Cdd:PTZ00420 69 KLKGHTSSILDLQFNPCFSEILASGSEDLTIRVWEIPHNDESVKEIK--DPQCILKGHKKKISiIDWNPMNYYIMCSSGF 146
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
2PM9_A 187 SNFASIWDLKAKKEVIHLSytspnsgIKQQLSVVEWHPKNSTRVATATG 235
Cdd:PTZ00420 147 DSFVNIWDIENEKRAFQIN-------MPKKLSSLKWNIKGNLLSGTCVG 188
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
104-142 |
3.33e-03 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 34.98 E-value: 3.33e-03
10 20 30
....*....|....*....|....*....|....*....
2PM9_A 104 NSMARFSNHSSSVKTVKFNaKQDNVLASGGNNGEIFIWD 142
Cdd:smart00320 3 ELLKTLKGHTGPVTSVAFS-PDGKYLASGSDDGTIKLWD 40
|
|
| PTZ00421 |
PTZ00421 |
coronin; Provisional |
66-283 |
3.99e-03 |
|
coronin; Provisional
Pssm-ID: 173611 [Multi-domain] Cd Length: 493 Bit Score: 39.49 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PM9_A 66 VDSKFNDLDwshNNKIIAgALDNGSLELYSTNE---ANNAINSMARFSNHSSSVKTVKFNAKQDNVLASGGNNGEIFIWD 142
Cdd:PTZ00421 79 IDVAFNPFD---PQKLFT-ASEDGTIMGWGIPEeglTQNISDPIVHLQGHTKKVGIVSFHPSAMNVLASAGADMVVNVWD 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PM9_A 143 MNKCT--ESPSNYTpltpgqsmssvDEVISLAWNQSlAHVFASAGSSNFASIWDLKAKKEVihlSYTSPNSGIKQQLSVv 220
Cdd:PTZ00421 155 VERGKavEVIKCHS-----------DQITSLEWNLD-GSLLCTTSKDKKLNIIDPRDGTIV---SSVEAHASAKSQRCL- 218
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
2PM9_A 221 eWHPKNSTRVATATGSDNDPSILIWDLRNANTPLQTLNQgHQKGILSLDWCHQDEHLLLSSGR 283
Cdd:PTZ00421 219 -WAKRKDLIITLGCSKSQQRQIMLWDTRKMASPYSTVDL-DQSSALFIPFFDEDTNLLYIGSK 279
|
|
| 8prop_hemeD1_NirF |
cd20778 |
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ... |
235-305 |
4.00e-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: 4.00e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
2PM9_A 235 GSDNDPSILIWDLRNANTpLQTLNQGhqKGILSLDWCHQDEHLLLSSGRDNTVLLWNPESAEQLSQFPARG 305
Cdd:cd20778 300 SGPDNDTVQVIDTKTLKV-VKTLEPG--KRVLHMEFTPRGEAVYISVNDDNKVVVYDTRTFREIKEVPAKK 367
|
|
| |
