|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09598 |
PRK09598 |
phosphoethanolamine--lipid A transferase EptA; |
1-521 |
0e+00 |
|
phosphoethanolamine--lipid A transferase EptA;
Pssm-ID: 236581 [Multi-domain] Cd Length: 522 Bit Score: 889.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 1 MASLFHLKFLKPLSCLQAGLLYSLIFGVLYHFPLFAYVYKESNQVSFIAMMVVVLFCVNGTLFLALGLISASLMRWSAIV 80
Cdd:PRK09598 1 MASLFHLKFLKPLSCLQAGLLYSLLNGVLYHFPLFAYVYKESNQVSFIAMLVVLLFCVNGLLFLLLGLLSRRLMRLSAIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 81 FSWLNSVAFYFISAYKVFLNKSMMGNVLNTNTHEVLGFLSVKLFVFIVVFGVLPGYIIYKIPIKNSSKKAPFLAILALVF 160
Cdd:PRK09598 81 FSLLNSIAFYFINTYKVFLNKSMMGNVLNTNTAESSGFLSVKLFIYIVVLGVLPGYIIYKIPLKNSSKKAPFAAILALVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 161 IFIASALANAKNWLWFDKHAKFIGGLILPFAYSVNAFRVSALKFFAPTIKPL--PLFSPNHSNSFVVLVIGESARKHNYA 238
Cdd:PRK09598 161 IFLASAFANSKNWLWFDKHAKFLGGLILPWSYSVNTFRVSAHKFFAPTIKPLlpPLFSPNHSKSVVVLVIGESARKHNYA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 239 LYGYNKPTTPRLSKRLADNELTLFNATSCATYTTASLECILDSSFKN--NAYENLPTYLTKAGIKVFWYSANDGEKNVKV 316
Cdd:PRK09598 241 LYGYEKPTNPRLSKRLATHELTLFNATSCATYTTASLECILDSSFKNtsNAYENLPTYLTRAGIKVFWRSANDGEPNVKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 317 TSYLKNYELIQKCSNCEaiAPYDESLLYNLPDLLKEHSNENVLLILHLAGSHGPNYDNKVPLNFRVFKPYCSSADLSSCS 396
Cdd:PRK09598 321 TSYLKNYELIQKCPNCE--APYDESLLYNLPELIKASSNENVLLILHLAGSHGPNYDNKYPLNFRVFKPVCSSVELSSCS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 397 KESLINAYDNTIFYNDYLLDKIISMLKKAKQPALMIYLSDHGESLGEEAFYLHGIPKSIAPKEQYEIPFIVYANDLFKKE 476
Cdd:PRK09598 399 KESLINAYDNTIFYNDYLLDKIISMLKNLKQPALMIYLSDHGESLGEGAFYLHGIPKSIAPKEQYEIPFIVWASDSFKKQ 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1151294739 477 HSIIQTQTPINQNVIFHSILGVFeDFKNPSVVYRPSLDLLKHKKE 521
Cdd:PRK09598 479 HSIIQTQTPINQNVIFHSVLGVF-DFKNPSAVYRPSLDLFKHKKE 522
|
|
| OpgE |
COG2194 |
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall ... |
8-517 |
1.90e-127 |
|
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441797 [Multi-domain] Cd Length: 537 Bit Score: 382.28 E-value: 1.90e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 8 KFLKPLSCLQAGLLYSLIFGVLYHFPLFAYVYK----ESNQVSFIAMMVVVLFCvngTLFLALGLISAS-LMRWSAIVFS 82
Cdd:COG2194 2 FLLPRLSPLKLILLLALYFALFLNLPFWGRLLAilplDGVNLLFLLSLPLLLLA---ALNLLLSLLAWRyLFKPLLILLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 83 WLNSVAFYFISAYKVFLNKSMMGNVLNTNTHEVLGFLSVKLFVFIVVFGVLPGYIIYKIPIK-NSSKKAP---FLAILAL 158
Cdd:COG2194 79 LISAAASYFMDFYGVVIDYGMIQNVLETDPAEASELLSPKLILWLLLLGVLPALLLWRVRIRyRPLLRELgqrLALLLLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 159 VFIFIASALANAKNWLWFDKHAKFIGGLILPFAYSVNAFRVSALKFFAPTIKPLPLF------SPNHSNSFVVLVIGESA 232
Cdd:COG2194 159 LLVIVLLALLFYKDYASFFRNHKELRYLINPSNFIYALGKYAKARYFAAPLPLQPLGadaklaAAGAKPTLVVLVVGETA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 233 RKHNYALYGYNKPTTPRLSKRladNELTLF-NATSCATYTTASLECIL-------DSSFKNNAYENLPTYLTKAGIKVFW 304
Cdd:COG2194 239 RADNFSLNGYARDTTPELAKE---KNLVSFrDVTSCGTATAVSVPCMFsrlgradYDPQRALNQENLLDVLQRAGVKVLW 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 305 YSANDGEKNVkvTSYLKNYELIQKCSN--CEAIAPYDESLLYNLPDLLKEHSNeNVLLILHLAGSHGPNYDNKVPLNFRV 382
Cdd:COG2194 316 RDNQSGCKGV--CDRVPTIDLTADNLPplCDGGECLDEVLLDGLDEALADLAG-DKLIVLHQMGSHGPAYYKRYPPEFRK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 383 FKPYCSSADLSSCSKESLINAYDNTIFYNDYLLDKIISMLK--KAKQPALMIYLSDHGESLGEEAFYLHGIPKSIAPKEQ 460
Cdd:COG2194 393 FTPTCDTNDLQNCSREELVNAYDNTILYTDYVLSQVIDLLKakQDRYDTAMLYVSDHGESLGENGLYLHGTPYAIAPDEQ 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1151294739 461 YEIPFIVYANDLFKKEHSI------IQTQTPINQNVIFHSILGVFeDFKNPsvVYRPSLDLLK 517
Cdd:COG2194 473 THVPMIMWLSDGYAQRYGIdfaclkARADKPYSHDNLFHTLLGLL-DVRTS--VYDPELDILA 532
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
224-499 |
4.80e-92 |
|
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase; Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase catalyzes the modification of the lipid A headgroups by phosphoethanolamine (PEA) or 4-amino-arabinose residues. Lipopolysaccharides, also called endotoxins, protect bacterial pathogens from antimicrobial peptides and have roles in virulence. The PEA modified lipid A increases resistance to the cationic cyclic polypeptide antibiotic, polymyxin. Lipid A PEA transferases usually consist of a transmembrane domain anchoring the enzyme to the periplasmic face of the cytoplasmic membrane.
Pssm-ID: 293741 [Multi-domain] Cd Length: 288 Bit Score: 282.59 E-value: 4.80e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 224 VVLVIGESARKHNYALYGYNKPTTPRLSKRlaDNELTLF-NATSCATYTTASLECILdsSFKN-------NAYENLPTYL 295
Cdd:cd16017 5 VVLVIGESARRDHMSLYGYPRDTTPFLSKL--KKNLIVFdNVISCGTSTAVSLPCML--SFANrenydraYYQENLIDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 296 TKAGIKVFWYSANDGEKNV--KVTSYLKNYELIQKCSNCEAIAPYDESLLYNLPDLLKEhSNENVLLILHLAGSHGPnYD 373
Cdd:cd16017 81 KKAGYKTYWISNQGGCGGYdtRISAIAKIETVFTNKGSCNSSNCYDEALLPLLDEALAD-SSKKKLIVLHLMGSHGP-YY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 374 NKVPLNFRVFKPYCSSaDLSSCSKESLINAYDNTIFYNDYLLDKIISMLKKAKQPALMIYLSDHGESLGEEAFYLHGIPK 453
Cdd:cd16017 159 DRYPEEFAKFTPDCDN-ELQSCSKEELINAYDNSILYTDYVLSQIIERLKKKDKDAALIYFSDHGESLGENGLYLHGAPY 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1151294739 454 siAPKEQYEIPFIVYANDLFKKEHSIIQTQ----TPINQNVIFHSILGVF 499
Cdd:cd16017 238 --APKEQYHVPFIIWSSDSYKQRYPVERLRankdRPFSHDNLFHTLLGLL 285
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
224-499 |
7.18e-57 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 191.87 E-value: 7.18e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 224 VVLVIGESARKHNYALYGYNKPTTPRLSkRLADNELTLFNATSCATYTTASLECILDSSFKNNA-------------YEN 290
Cdd:pfam00884 3 VVLVLGESLRAPDLGLYGYPRPTTPFLD-RLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFgsyvstpvglprtEPS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 291 LPTYLTKAGIKV--------FWYSANDGEKN--VKVTSYLKNYELIQKCSNCEAIAP----YDESLLYNLPDLLKEHSnE 356
Cdd:pfam00884 82 LPDLLKRAGYNTgaigkwhlGWYNNQSPCNLgfDKFFGRNTGSDLYADPPDVPYNCSgggvSDEALLDEALEFLDNND-K 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 357 NVLLILHLAGSHGP-NYDNKVPLNFRVFKPycssadlSSCSKESLINAYDNTIFYNDYLLDKIISMLKKAKQ--PALMIY 433
Cdd:pfam00884 161 PFFLVLHTLGSHGPpYYPDRYPEKYATFKP-------SSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLldNTLVVY 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1151294739 434 LSDHGESLGEEAFYLHGIPKSIAPKEQYEIPFIVYANDLFKKEHsiiQTQTPINQNVIFHSILGVF 499
Cdd:pfam00884 234 TSDHGESLGEGGGYLHGGKYDNAPEGGYRVPLLIWSPGGKAKGQ---KSEALVSHVDLFPTILDLA 296
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09598 |
PRK09598 |
phosphoethanolamine--lipid A transferase EptA; |
1-521 |
0e+00 |
|
phosphoethanolamine--lipid A transferase EptA;
Pssm-ID: 236581 [Multi-domain] Cd Length: 522 Bit Score: 889.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 1 MASLFHLKFLKPLSCLQAGLLYSLIFGVLYHFPLFAYVYKESNQVSFIAMMVVVLFCVNGTLFLALGLISASLMRWSAIV 80
Cdd:PRK09598 1 MASLFHLKFLKPLSCLQAGLLYSLLNGVLYHFPLFAYVYKESNQVSFIAMLVVLLFCVNGLLFLLLGLLSRRLMRLSAIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 81 FSWLNSVAFYFISAYKVFLNKSMMGNVLNTNTHEVLGFLSVKLFVFIVVFGVLPGYIIYKIPIKNSSKKAPFLAILALVF 160
Cdd:PRK09598 81 FSLLNSIAFYFINTYKVFLNKSMMGNVLNTNTAESSGFLSVKLFIYIVVLGVLPGYIIYKIPLKNSSKKAPFAAILALVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 161 IFIASALANAKNWLWFDKHAKFIGGLILPFAYSVNAFRVSALKFFAPTIKPL--PLFSPNHSNSFVVLVIGESARKHNYA 238
Cdd:PRK09598 161 IFLASAFANSKNWLWFDKHAKFLGGLILPWSYSVNTFRVSAHKFFAPTIKPLlpPLFSPNHSKSVVVLVIGESARKHNYA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 239 LYGYNKPTTPRLSKRLADNELTLFNATSCATYTTASLECILDSSFKN--NAYENLPTYLTKAGIKVFWYSANDGEKNVKV 316
Cdd:PRK09598 241 LYGYEKPTNPRLSKRLATHELTLFNATSCATYTTASLECILDSSFKNtsNAYENLPTYLTRAGIKVFWRSANDGEPNVKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 317 TSYLKNYELIQKCSNCEaiAPYDESLLYNLPDLLKEHSNENVLLILHLAGSHGPNYDNKVPLNFRVFKPYCSSADLSSCS 396
Cdd:PRK09598 321 TSYLKNYELIQKCPNCE--APYDESLLYNLPELIKASSNENVLLILHLAGSHGPNYDNKYPLNFRVFKPVCSSVELSSCS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 397 KESLINAYDNTIFYNDYLLDKIISMLKKAKQPALMIYLSDHGESLGEEAFYLHGIPKSIAPKEQYEIPFIVYANDLFKKE 476
Cdd:PRK09598 399 KESLINAYDNTIFYNDYLLDKIISMLKNLKQPALMIYLSDHGESLGEGAFYLHGIPKSIAPKEQYEIPFIVWASDSFKKQ 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1151294739 477 HSIIQTQTPINQNVIFHSILGVFeDFKNPSVVYRPSLDLLKHKKE 521
Cdd:PRK09598 479 HSIIQTQTPINQNVIFHSVLGVF-DFKNPSAVYRPSLDLFKHKKE 522
|
|
| OpgE |
COG2194 |
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall ... |
8-517 |
1.90e-127 |
|
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441797 [Multi-domain] Cd Length: 537 Bit Score: 382.28 E-value: 1.90e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 8 KFLKPLSCLQAGLLYSLIFGVLYHFPLFAYVYK----ESNQVSFIAMMVVVLFCvngTLFLALGLISAS-LMRWSAIVFS 82
Cdd:COG2194 2 FLLPRLSPLKLILLLALYFALFLNLPFWGRLLAilplDGVNLLFLLSLPLLLLA---ALNLLLSLLAWRyLFKPLLILLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 83 WLNSVAFYFISAYKVFLNKSMMGNVLNTNTHEVLGFLSVKLFVFIVVFGVLPGYIIYKIPIK-NSSKKAP---FLAILAL 158
Cdd:COG2194 79 LISAAASYFMDFYGVVIDYGMIQNVLETDPAEASELLSPKLILWLLLLGVLPALLLWRVRIRyRPLLRELgqrLALLLLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 159 VFIFIASALANAKNWLWFDKHAKFIGGLILPFAYSVNAFRVSALKFFAPTIKPLPLF------SPNHSNSFVVLVIGESA 232
Cdd:COG2194 159 LLVIVLLALLFYKDYASFFRNHKELRYLINPSNFIYALGKYAKARYFAAPLPLQPLGadaklaAAGAKPTLVVLVVGETA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 233 RKHNYALYGYNKPTTPRLSKRladNELTLF-NATSCATYTTASLECIL-------DSSFKNNAYENLPTYLTKAGIKVFW 304
Cdd:COG2194 239 RADNFSLNGYARDTTPELAKE---KNLVSFrDVTSCGTATAVSVPCMFsrlgradYDPQRALNQENLLDVLQRAGVKVLW 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 305 YSANDGEKNVkvTSYLKNYELIQKCSN--CEAIAPYDESLLYNLPDLLKEHSNeNVLLILHLAGSHGPNYDNKVPLNFRV 382
Cdd:COG2194 316 RDNQSGCKGV--CDRVPTIDLTADNLPplCDGGECLDEVLLDGLDEALADLAG-DKLIVLHQMGSHGPAYYKRYPPEFRK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 383 FKPYCSSADLSSCSKESLINAYDNTIFYNDYLLDKIISMLK--KAKQPALMIYLSDHGESLGEEAFYLHGIPKSIAPKEQ 460
Cdd:COG2194 393 FTPTCDTNDLQNCSREELVNAYDNTILYTDYVLSQVIDLLKakQDRYDTAMLYVSDHGESLGENGLYLHGTPYAIAPDEQ 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1151294739 461 YEIPFIVYANDLFKKEHSI------IQTQTPINQNVIFHSILGVFeDFKNPsvVYRPSLDLLK 517
Cdd:COG2194 473 THVPMIMWLSDGYAQRYGIdfaclkARADKPYSHDNLFHTLLGLL-DVRTS--VYDPELDILA 532
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
224-499 |
4.80e-92 |
|
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase; Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase catalyzes the modification of the lipid A headgroups by phosphoethanolamine (PEA) or 4-amino-arabinose residues. Lipopolysaccharides, also called endotoxins, protect bacterial pathogens from antimicrobial peptides and have roles in virulence. The PEA modified lipid A increases resistance to the cationic cyclic polypeptide antibiotic, polymyxin. Lipid A PEA transferases usually consist of a transmembrane domain anchoring the enzyme to the periplasmic face of the cytoplasmic membrane.
Pssm-ID: 293741 [Multi-domain] Cd Length: 288 Bit Score: 282.59 E-value: 4.80e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 224 VVLVIGESARKHNYALYGYNKPTTPRLSKRlaDNELTLF-NATSCATYTTASLECILdsSFKN-------NAYENLPTYL 295
Cdd:cd16017 5 VVLVIGESARRDHMSLYGYPRDTTPFLSKL--KKNLIVFdNVISCGTSTAVSLPCML--SFANrenydraYYQENLIDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 296 TKAGIKVFWYSANDGEKNV--KVTSYLKNYELIQKCSNCEAIAPYDESLLYNLPDLLKEhSNENVLLILHLAGSHGPnYD 373
Cdd:cd16017 81 KKAGYKTYWISNQGGCGGYdtRISAIAKIETVFTNKGSCNSSNCYDEALLPLLDEALAD-SSKKKLIVLHLMGSHGP-YY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 374 NKVPLNFRVFKPYCSSaDLSSCSKESLINAYDNTIFYNDYLLDKIISMLKKAKQPALMIYLSDHGESLGEEAFYLHGIPK 453
Cdd:cd16017 159 DRYPEEFAKFTPDCDN-ELQSCSKEELINAYDNSILYTDYVLSQIIERLKKKDKDAALIYFSDHGESLGENGLYLHGAPY 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1151294739 454 siAPKEQYEIPFIVYANDLFKKEHSIIQTQ----TPINQNVIFHSILGVF 499
Cdd:cd16017 238 --APKEQYHVPFIIWSSDSYKQRYPVERLRankdRPFSHDNLFHTLLGLL 285
|
|
| PRK11598 |
PRK11598 |
putative metal dependent hydrolase; Provisional |
9-517 |
2.53e-80 |
|
putative metal dependent hydrolase; Provisional
Pssm-ID: 183224 [Multi-domain] Cd Length: 545 Bit Score: 260.76 E-value: 2.53e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 9 FLKPLSClqAGLLYSLIFGVLYHFPLFAYVYKESNQ---------VSFIAMMVVVLFCVNGTLFLALGLISasLMRWSAI 79
Cdd:PRK11598 4 LLKRPSL--NLLTFLLLAAFYITLCLNIAFYKQVLQllpldslhnVLVFASMPVVAFSVINIVFTLLSFPW--LRRPLAC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 80 VFSWLNSVAFYFISAYKVFLNKSMMGNVLNTNTHEVLGFLSVKLFVFIVVFGVLPGYIIYKIPIKNSSKK-----APFLA 154
Cdd:PRK11598 80 LFILVGAAAQYFMMTYGIVIDRSMIQNIFETTPAESFALMTPQMLLWLGLSGVLPALIACWIKIRPATPRwrsvlFRLAN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 155 ILALVFIFIASALANAKNWLWFDKHAKFIGGLILPFAYSVNAFRVSALKFFA--PTIK------PLPLFSPNHSNSFVVL 226
Cdd:PRK11598 160 ILVSVLLILLVAALFYKDYASLFRNNKELVKSLTPSNSIVASWSWYSHQRLAnlPLVRigedahKNPLMQNQKRKNLTIL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 227 VIGESARKHNYALYGYNKPTTPRLSKrlaDNELTLFNATSCATYTTASLECILdSSFKNNAY--------ENLPTYLTKA 298
Cdd:PRK11598 240 VVGETSRAENFSLGGYPRETNPRLAK---DNVIYFPHTTSCGTATAVSVPCMF-SNMPRKHYdeelahhqEGLLDIIQRA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 299 GIKVFWySANDGE--------KNVKVTSYlknyELIQKCSNCEAiapYDESLLYNLPDLLKEHSNENVLlILHLAGSHGP 370
Cdd:PRK11598 316 GINVLW-NDNDGGckgacdrvPHQDVTAL----NLPGQCIDGEC---YDEVLFHGLENYINNLQGDGVI-VLHTIGSHGP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 371 NYDNKVPLNFRVFKPYCSSADLSSCSKESLINAYDNTIFYNDYLLDKIISMLKK--AKQPALMIYLSDHGESLGEEAFYL 448
Cdd:PRK11598 387 TYYNRYPPQFRKFTPTCDTNEIQTCTQQQLVNTYDNTILYVDYIVDKAINLLKQhqDKFNTSLVYLSDHGESLGENGIYL 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1151294739 449 HGIPKSIAPKEQYEIPFIVYANDLFKKEHSIIQT-------QTPINQNVIFHSILGVFEdfkNPSVVYRPSLDLLK 517
Cdd:PRK11598 467 HGLPYAIAPDQQTHVPMLLWLSPDYQKRYGVDQQclqkqaqTQDYSQDNLFSTLLGLTG---VQTKEYQAADDILQ 539
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
224-499 |
7.18e-57 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 191.87 E-value: 7.18e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 224 VVLVIGESARKHNYALYGYNKPTTPRLSkRLADNELTLFNATSCATYTTASLECILDSSFKNNA-------------YEN 290
Cdd:pfam00884 3 VVLVLGESLRAPDLGLYGYPRPTTPFLD-RLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFgsyvstpvglprtEPS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 291 LPTYLTKAGIKV--------FWYSANDGEKN--VKVTSYLKNYELIQKCSNCEAIAP----YDESLLYNLPDLLKEHSnE 356
Cdd:pfam00884 82 LPDLLKRAGYNTgaigkwhlGWYNNQSPCNLgfDKFFGRNTGSDLYADPPDVPYNCSgggvSDEALLDEALEFLDNND-K 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 357 NVLLILHLAGSHGP-NYDNKVPLNFRVFKPycssadlSSCSKESLINAYDNTIFYNDYLLDKIISMLKKAKQ--PALMIY 433
Cdd:pfam00884 161 PFFLVLHTLGSHGPpYYPDRYPEKYATFKP-------SSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLldNTLVVY 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1151294739 434 LSDHGESLGEEAFYLHGIPKSIAPKEQYEIPFIVYANDLFKKEHsiiQTQTPINQNVIFHSILGVF 499
Cdd:pfam00884 234 TSDHGESLGEGGGYLHGGKYDNAPEGGYRVPLLIWSPGGKAKGQ---KSEALVSHVDLFPTILDLA 296
|
|
| PRK11560 |
PRK11560 |
kdo(2)-lipid A phosphoethanolamine 7''-transferase; |
7-473 |
5.88e-44 |
|
kdo(2)-lipid A phosphoethanolamine 7''-transferase;
Pssm-ID: 183198 [Multi-domain] Cd Length: 558 Bit Score: 163.29 E-value: 5.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 7 LKFLKPLSCLQAGLLYSLIFGVLYHFPLFAYVYKESNQ----VSFIAMMVVVLFCVNGTLFLaLGLIS----------AS 72
Cdd:PRK11560 1 MRYIKSLTQQKLSFLLAVYIGLFLNIAVFYRRFDSYAQdftvWKGLSAVVELAATVLVTFFL-LRLLSlfgrrfwrvlAS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 73 LMrwsaIVFSwlnSVAFYFISAYKVFLNKSMMGNVLNTNT---HEVLGFlsvKLFVFIVVFGVLPGYIIYKIPIKNS--- 146
Cdd:PRK11560 80 LL----VLFS---AAASYYMTFFNVVIGYGIIASVMTTDIdlsKEVVGL---HFILWLVAVSALPLILIWNNRCRYTllr 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 147 SKKAPFLAILALVFIFIASALAnaknWL---WFDKHAKF---IGGLILPFAYSVNAFR------VSALKFFAPT------ 208
Cdd:PRK11560 150 QLRTPGQRIRSLAVVVLAGLLV----WApirLLDIQQKKverATGVDLPSYGGVVANSylpsnwLSALGLYAWAqvdess 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 209 -----IKPLPLF----SPNHSNSFVVLVIGESARKHNYALYGYNKPTTPRLSKrlaDNELTLFNATSCATYTTASLECIL 279
Cdd:PRK11560 226 dnnslLNPAKKFtyqaPKGVDDTYVVFIIGETTRWDHMGILGYERNTTPKLAQ---EKNLAAFRGYSCDTATKLSLRCMF 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 280 -------DSSFKNNAYENLPTYLTKAGI---------KVFWYSandgekNVKVTSYLKNyELIQKcSNCEAIAPYDESLL 343
Cdd:PRK11560 303 vreggaeDNPQRTLKEQNVFAVLKQLGFsselfamqsEMWFYN------NTMADNYAYR-EQIGA-EPRNRGKPVDDMLL 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 344 YN-LPDLLKEHSNENVLLILHLAGSHGpNYDNKVPLNFRVFKPYCSSADlSSCSKESLINAYDNTIFYNDYLLDKIISML 422
Cdd:PRK11560 375 VDeMKQSLGRNPDGKHLIILHTKGSHY-NYTQRYPRSFARYQPECIGVD-SGCSKAQLINSYDNSVLYVDHFISSVIDQL 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1151294739 423 KKAKqpALMIYLSDHGESLGEEAfYLHGIPKSIAPKEQYEIPFIVYANDLF 473
Cdd:PRK11560 453 RDKK--AIVFYAADHGESINERE-HLHGTPREMAPPEQFRVPMMVWMSDKY 500
|
|
| EptA_B_N |
pfam08019 |
Phosphoethanolamine transferase EptA/EptB; This entry represents a domain found in a group of ... |
62-199 |
1.66e-32 |
|
Phosphoethanolamine transferase EptA/EptB; This entry represents a domain found in a group of bacterial phosphoethanolamine transferases, including eptA from Helicobacter pylori and eptB from Escherichia coli EC:2.7.8.42. This domain is found immediately N-terminal to the sulphatase domain in many sulphatases.
Pssm-ID: 429788 [Multi-domain] Cd Length: 151 Bit Score: 121.47 E-value: 1.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 62 LFLALGLISAS-LMRWSAIVFSWLNSVAFYFISAYKVFLNKSMMGNVLNTNTHEVLGFLSVKLFVFIVVFGVLPGYIIYK 140
Cdd:pfam08019 5 LNLLLSLLSWRyLLKPLLILLLLLSAAASYFMDTYGVVIDRDMIQNVLETDVAEASDLLSPKLLLYLLLLGVLPALLLWR 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1151294739 141 IPIKNSSKKAPFLA----ILALVFIFIASALANAKNWLWFDKHAKFIGGLILPFAYSVNAFRV 199
Cdd:pfam08019 85 VRIRYRPWLRELLSrlalILVSLLVIGLVAFLFYKDYASFFRNHKELRYLINPTNYIYSTVKY 147
|
|
| PRK10649 |
PRK10649 |
phosphoethanolamine transferase CptA; |
225-477 |
5.10e-25 |
|
phosphoethanolamine transferase CptA;
Pssm-ID: 182617 [Multi-domain] Cd Length: 577 Bit Score: 108.64 E-value: 5.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 225 VLVIGESARKHNYALYGYNKPTTPRLSK-RLADNELTLF-NATSCATYTTASLECILdsSFKNNayENLPTYLTK----- 297
Cdd:PRK10649 240 VLVIGESTQRGRMSLYGYPRETTPELDAlHKTDPGLTVFnNVVTSRPYTIEILQQAL--TFADE--KNPDLYLTQpslmn 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 298 ----AGIKVFWYS-------ANDG----EKNVKVTSYLKNyeliQKCSNCeaiAPYDESLLYNLPDLLKEhSNENVLLIL 362
Cdd:PRK10649 316 mmkqAGYKTFWITnqqtmtaRNTMltvfSRQTDKQYYMNQ----QRTQNA---REYDTNVLKPFSEVLAD-PAPKKFIIV 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 363 HLAGSHgPNYDNKVPLNFRVFK-------PYCSSADLSScskeslINAYDNTIFYNDYLLDKIISMLKKAKQPALMIYLS 435
Cdd:PRK10649 388 HLLGTH-IKYKYRYPENQGKFDdrtghvpPGLNADELES------YNDYDNANLYNDHVVASLIKDFKATDPNGFLVYFS 460
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1151294739 436 DHGESLgeeafYLHGIPKSIAPKE------QYEIPFIVYANDLFKKEH 477
Cdd:PRK10649 461 DHGEEV-----YDTPPHKTQGRNEdnptrhMYTIPFLLWTSEKWQAAH 503
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
24-476 |
3.06e-11 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 65.83 E-value: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 24 LIFGVLYHFPLFAYVYKESNQVSFIAMMVVVLFCVNGTLFLALGLISASLMRWSAIVFSWLNSVAFY----FISAYKVFL 99
Cdd:COG1368 13 LVFLLFNFDLSLGEILQAFLYGLRFILYLLLLLLLLLLLLLPLLFRRPKLRWIYLLLVLLLLLLLLVadilYYRFFGDRL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 100 NKSMMGNVlnTNTHEVLGFLS----VKLFVFIVVFGVLPGYIIY-----KIPIKNSSKKAPFLAILALVFIFIASALANA 170
Cdd:COG1368 93 NFSDLDYL--GDTGEVLGSLLssydLLLLLDLLLLLLLLLLLYRllkklRKSLPWRKRLALLLLLLALLLLGIRLGEDRP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 171 KNWLWFDKHAKFIGGLILPFAYSV-NAFRVSALKFFAP--TIKPLPLFSPNHSNSF----------VVLVIGESARKHNY 237
Cdd:COG1368 171 LNLSDAFSRNNFVNELGLNGPYSFyDALRNNKAPATYSeeEALEIKKYLKSNRPTPnpfgpakkpnVVVILLESFSDFFI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 238 ALYGYNKPTTPRLsKRLADNELTLFNATSCATYTTASLECILDS-----------SFKNNAYENLPTYLTKAGIKVFWYS 306
Cdd:COG1368 251 GALGNGKDVTPFL-DSLAKESLYFGNFYSQGGRTSRGEFAVLTGlpplpggspykRPGQNNFPSLPSILKKQGYETSFFH 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 307 ANDGE--------KNVKVTSYLKNYELIQKCSNceAIAPYDESLLYNLPDLLKEhSNENVLLILHLAGSHGPnYDnkVPL 378
Cdd:COG1368 330 GGDGSfwnrdsfyKNLGFDEFYDREDFDDPFDG--GWGVSDEDLFDKALEELEK-LKKPFFAFLITLSNHGP-YT--LPE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 379 NFRVFKPYcssadlsscsKESLINAYDNTIFYNDYLLDKIISMLKKAK--QPALMIYLSDHGESLGEEAFYLHgipksia 456
Cdd:COG1368 404 EDKKIPDY----------GKTTLNNYLNAVRYADQALGEFIEKLKKSGwyDNTIFVIYGDHGPRSPGKTDYEN------- 466
|
490 500
....*....|....*....|
gi 1151294739 457 PKEQYEIPFIVYANDLFKKE 476
Cdd:COG1368 467 PLERYRVPLLIYSPGLKKPK 486
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
224-476 |
2.78e-08 |
|
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer found in Gram-positive bacteria. It may contain long chains of ribitol or glycerol phosphate. LTA synthase catalyzes the reaction to extend the polymer by the repeated addition of glycerolphosphate (GroP) subunits to the end of the growing chain.
Pssm-ID: 293739 [Multi-domain] Cd Length: 283 Bit Score: 55.00 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 224 VVLVIGESARKHNYALYGYNKPTTPRLsKRLADNEL--TLFNATSCATYTTASLECIL------------DSSFKNNAYE 289
Cdd:cd16015 3 VIVILLESFSDPYIDKDVGGEDLTPNL-NKLAKEGLyfGNFYSPGFGGGTANGEFEVLtglpplplgsgsYTLYKLNPLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 290 NLPTYLTKAGIKVFWYSANDGEkNVKVTSYLKNY---------ELIQKCSNCEAIAPYDESLLYNLPDLLKEHSNENVLL 360
Cdd:cd16015 82 SLPSILKEQGYETIFIHGGDAS-FYNRDSVYPNLgfdefydleDFPDDEKETNGWGVSDESLFDQALEELEELKKKPFFI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 361 ILHLAGSHGPNYDNKVPLNFRVFKPYcssadlsscsKESLINAYDNTIFYNDYLLDKIISMLKKAKQ--PALMIYLSDHG 438
Cdd:cd16015 161 FLVTMSNHGPYDLPEEKKDEPLKVEE----------DKTELENYLNAIHYTDKALGEFIEKLKKSGLyeNTIIVIYGDHL 230
|
250 260 270
....*....|....*....|....*....|....*...
gi 1151294739 439 ESLGEEAFYlhgipKSIAPKEQYEIPFIVYANDLFKKE 476
Cdd:cd16015 231 PSLGSDYDE-----TDEDPLDLYRTPLLIYSPGLKKPK 263
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
412-507 |
4.75e-05 |
|
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293775 [Multi-domain] Cd Length: 468 Bit Score: 45.84 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 412 DYLLDKIISMLKKAKQPALMIYLSDHGESLGEEAFYLHGipkSIAPKEQYEIPFIVYANDlfkKEHSIIQTQTPINQNVI 491
Cdd:cd16156 251 DYEIGRVLDAADEIAEDAWVIYTSDHGDMLGAHKLWAKG---PAVYDEITNIPLIIRGKG---GEKAGTVTDTPVSHIDL 324
|
90
....*....|....*.
gi 1151294739 492 FHSILGVFeDFKNPSV 507
Cdd:cd16156 325 APTILDYA-GIPQPKV 339
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
224-468 |
6.81e-05 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 44.85 E-value: 6.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 224 VVLVIGESARKHNYALYGYNKPTTPRLSkRLADNELTLFNATSCATYTTASLECIL----------DSSFKNNAYENLPT 293
Cdd:cd16148 3 VILIVIDSLRADHLGCYGYDRVTTPNLD-RLAAEGVVFDNHYSGSNPTLPSRFSLFtglypfyhgvWGGPLEPDDPTLAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 294 YLTKAGIKVFWYSANDGEKNVkvTSYLKNYELIQKCSNCEAIAPY-----DESLLYNLPDLLKEH-SNENVLLILHLAGS 367
Cdd:cd16148 82 ILRKAGYYTAAVSSNPHLFGG--PGFDRGFDTFEDFRGQEGDPGEegderAERVTDRALEWLDRNaDDDPFFLFLHYFDP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151294739 368 HGPnydnkvplnFRvfkpycssadlsscskeslinaYDNTIFYNDYLLDKIISMLKK---AKQPALMIyLSDHGESLGEE 444
Cdd:cd16148 160 HEP---------YL----------------------YDAEVRYVDEQIGRLLDKLKElglLEDTLVIV-TSDHGEEFGEH 207
|
250 260
....*....|....*....|....*
gi 1151294739 445 AFYL-HGipkSIAPKEQYEIPFIVY 468
Cdd:cd16148 208 GLYWgHG---SNLYDEQLHVPLIIR 229
|
|
|