|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11598 |
PRK11598 |
putative metal dependent hydrolase; Provisional |
2-546 |
0e+00 |
|
putative metal dependent hydrolase; Provisional
Pssm-ID: 183224 [Multi-domain] Cd Length: 545 Bit Score: 1055.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 2 LKRLLKRPSLNLLAWLLLAAFYISICLNIAFFKQVLQALPLDSLHNVLVFLSMPVVAFSVINIVLTLSSFLWLNRPLACL 81
Cdd:PRK11598 1 LKRLLKRPSLNLLTFLLLAAFYITLCLNIAFYKQVLQLLPLDSLHNVLVFASMPVVAFSVINIVFTLLSFPWLRRPLACL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 82 FILVGAAAQYFIMTYGIVIDRSMIANIIDTTPAESYALMTPQMLLTLGFSGVLAALIACWIKIKPATSRLRSVLFRGANI 161
Cdd:PRK11598 81 FILVGAAAQYFMMTYGIVIDRSMIQNIFETTPAESFALMTPQMLLWLGLSGVLPALIACWIKIRPATPRWRSVLFRLANI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 162 LVSVLLILLVAALFYKDYASLFRNNKELVKSLSPSNSIVASWSWYSHQRLANLPLVRIGEDAHRNPLMQNEKRKNLTILI 241
Cdd:PRK11598 161 LVSVLLILLVAALFYKDYASLFRNNKELVKSLTPSNSIVASWSWYSHQRLANLPLVRIGEDAHKNPLMQNQKRKNLTILV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 242 VGETSRAENFSLNGYPRETNPRLAKDNVVYFPNTASCGTATAVSVPCMFSDMPREHYKEELAQHQEGVLDIIQRAGINVL 321
Cdd:PRK11598 241 VGETSRAENFSLGGYPRETNPRLAKDNVIYFPHTTSCGTATAVSVPCMFSNMPRKHYDEELAHHQEGLLDIIQRAGINVL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 322 WNDNDGGCKGACDRVPHQNVTALNLPDQCINGECYDEVLFHGLEEYINNLQGDGVIVLHTIGSHGPTYYNRYPPQFRKFT 401
Cdd:PRK11598 321 WNDNDGGCKGACDRVPHQDVTALNLPGQCIDGECYDEVLFHGLENYINNLQGDGVIVLHTIGSHGPTYYNRYPPQFRKFT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 402 PTCDTNEIQTCTKEQLVNTYDNTLVYVDYIVDKAINLLKEHQDKFTTSLVYLSDHGESLGENGIYLHGLPYAIAPDSQKQ 481
Cdd:PRK11598 401 PTCDTNEIQTCTQQQLVNTYDNTILYVDYIVDKAINLLKQHQDKFNTSLVYLSDHGESLGENGIYLHGLPYAIAPDQQTH 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446842536 482 VPMLLWLSEDYQKRYQVDQNCLQKQAQTQHYSQDNLFSTLLGLTGVETKYYQAADDILQTCRRVS 546
Cdd:PRK11598 481 VPMLLWLSPDYQKRYGVDQQCLQKQAQTQDYSQDNLFSTLLGLTGVQTKEYQAADDILQPCRRLS 545
|
|
| OpgE |
COG2194 |
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall ... |
22-544 |
0e+00 |
|
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441797 [Multi-domain] Cd Length: 537 Bit Score: 772.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 22 FYISICLNIAFFKQVLQALPLDSlHNVLVFLSMPVVAFSVINIVLTLSSFLWLNRPLACLFILVGAAAQYFIMTYGIVID 101
Cdd:COG2194 18 LYFALFLNLPFWGRLLAILPLDG-VNLLFLLSLPLLLLAALNLLLSLLAWRYLFKPLLILLLLISAAASYFMDFYGVVID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 102 RSMIANIIDTTPAESYALMTPQMLLTLGFSGVLAALIACWIKIKPaTSRLRSVLFRGANILVSVLLILLVAALFYKDYAS 181
Cdd:COG2194 97 YGMIQNVLETDPAEASELLSPKLILWLLLLGVLPALLLWRVRIRY-RPLLRELGQRLALLLLALLVIVLLALLFYKDYAS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 182 LFRNNKELVKSLSPSNSIVASWSWYSHQ-RLANLPLVRIGEDAHRNPlmqNEKRKNLTILIVGETSRAENFSLNGYPRET 260
Cdd:COG2194 176 FFRNHKELRYLINPSNFIYALGKYAKARyFAAPLPLQPLGADAKLAA---AGAKPTLVVLVVGETARADNFSLNGYARDT 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 261 NPRLAKD-NVVYFPNTASCGTATAVSVPCMFSDMPREHYKEELAQHQEGVLDIIQRAGINVLWNDNDGGCKGACDRVPHQ 339
Cdd:COG2194 253 TPELAKEkNLVSFRDVTSCGTATAVSVPCMFSRLGRADYDPQRALNQENLLDVLQRAGVKVLWRDNQSGCKGVCDRVPTI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 340 NVTALNLPDQCINGECYDEVLFHGLEEYINNLQGDGVIVLHTIGSHGPTYYNRYPPQFRKFTPTCDTNEIQTCTKEQLVN 419
Cdd:COG2194 333 DLTADNLPPLCDGGECLDEVLLDGLDEALADLAGDKLIVLHQMGSHGPAYYKRYPPEFRKFTPTCDTNDLQNCSREELVN 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 420 TYDNTLVYVDYIVDKAINLLKEHQDKFTTSLVYLSDHGESLGENGIYLHGLPYAIAPDSQKQVPMLLWLSEDYQKRYQVD 499
Cdd:COG2194 413 AYDNTILYTDYVLSQVIDLLKAKQDRYDTAMLYVSDHGESLGENGLYLHGTPYAIAPDEQTHVPMIMWLSDGYAQRYGID 492
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 446842536 500 QNCLQKQAQtQHYSQDNLFSTLLGLTGVETKYYQAADDILQTCRR 544
Cdd:COG2194 493 FACLKARAD-KPYSHDNLFHTLLGLLDVRTSVYDPELDILAPCRR 536
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
234-528 |
1.72e-124 |
|
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: 366.56 E-value: 1.72e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 234 RKNLTILIVGETSRAENFSLNGYPRETNPRLAK--DNVVYFPNTASCGTATAVSVPCMFSDMPREHYKEelAQHQEGVLD 311
Cdd:cd16017 1 KPKNVVLVIGESARRDHMSLYGYPRDTTPFLSKlkKNLIVFDNVISCGTSTAVSLPCMLSFANRENYDR--AYYQENLID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 312 IIQRAGINVLWNDNDGGCKGACDRVPHQNVTA--LNLPDQCINGECYDEVLFHGLEEYINNLQGDGVIVLHTIGSHGPtY 389
Cdd:cd16017 79 LAKKAGYKTYWISNQGGCGGYDTRISAIAKIEtvFTNKGSCNSSNCYDEALLPLLDEALADSSKKKLIVLHLMGSHGP-Y 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 390 YNRYPPQFRKFTPTCDtNEIQTCTKEQLVNTYDNTLVYVDYIVDKAINLLKEHQDKftTSLVYLSDHGESLGENGIYLHG 469
Cdd:cd16017 158 YDRYPEEFAKFTPDCD-NELQSCSKEELINAYDNSILYTDYVLSQIIERLKKKDKD--AALIYFSDHGESLGENGLYLHG 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446842536 470 LPYaiAPDSQKQVPMLLWLSEDYQKRYQVdqnCLQKQAQTQHYSQDNLFSTLLGLTGVE 528
Cdd:cd16017 235 APY--APKEQYHVPFIIWSSDSYKQRYPV---ERLRANKDRPFSHDNLFHTLLGLLGIK 288
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
239-527 |
9.45e-79 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 249.65 E-value: 9.45e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 239 ILIVGETSRAENFSLNGYPRETNPRLAK--DNVVYFPNTASCGTATAVSVPCMFSDMPREHY------KEELAQHQEGVL 310
Cdd:pfam00884 4 VLVLGESLRAPDLGLYGYPRPTTPFLDRlaEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFgsyvstPVGLPRTEPSLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 311 DIIQRAGINV--------LWNDNDGGCK----GACDRVPHQNVTALN--LPDQCINGECYDEVLFHGLEEYINNLQGDGV 376
Cdd:pfam00884 84 DLLKRAGYNTgaigkwhlGWYNNQSPCNlgfdKFFGRNTGSDLYADPpdVPYNCSGGGVSDEALLDEALEFLDNNDKPFF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 377 IVLHTIGSHGP-TYYNRYPPQFRKFTPtcdtneiQTCTKEQLVNTYDNTLVYVDYIVDKAINLLKEHQDKFTTSLVYLSD 455
Cdd:pfam00884 164 LVLHTLGSHGPpYYPDRYPEKYATFKP-------SSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSD 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446842536 456 HGESLGENGIYLHGLPYAIAPDSQKQVPMLLWLSEDYQKRYQVDqnclqkqaqtQHYSQDNLFSTLLGLTGV 527
Cdd:pfam00884 237 HGESLGEGGGYLHGGKYDNAPEGGYRVPLLIWSPGGKAKGQKSE----------ALVSHVDLFPTILDLAGI 298
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11598 |
PRK11598 |
putative metal dependent hydrolase; Provisional |
2-546 |
0e+00 |
|
putative metal dependent hydrolase; Provisional
Pssm-ID: 183224 [Multi-domain] Cd Length: 545 Bit Score: 1055.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 2 LKRLLKRPSLNLLAWLLLAAFYISICLNIAFFKQVLQALPLDSLHNVLVFLSMPVVAFSVINIVLTLSSFLWLNRPLACL 81
Cdd:PRK11598 1 LKRLLKRPSLNLLTFLLLAAFYITLCLNIAFYKQVLQLLPLDSLHNVLVFASMPVVAFSVINIVFTLLSFPWLRRPLACL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 82 FILVGAAAQYFIMTYGIVIDRSMIANIIDTTPAESYALMTPQMLLTLGFSGVLAALIACWIKIKPATSRLRSVLFRGANI 161
Cdd:PRK11598 81 FILVGAAAQYFMMTYGIVIDRSMIQNIFETTPAESFALMTPQMLLWLGLSGVLPALIACWIKIRPATPRWRSVLFRLANI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 162 LVSVLLILLVAALFYKDYASLFRNNKELVKSLSPSNSIVASWSWYSHQRLANLPLVRIGEDAHRNPLMQNEKRKNLTILI 241
Cdd:PRK11598 161 LVSVLLILLVAALFYKDYASLFRNNKELVKSLTPSNSIVASWSWYSHQRLANLPLVRIGEDAHKNPLMQNQKRKNLTILV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 242 VGETSRAENFSLNGYPRETNPRLAKDNVVYFPNTASCGTATAVSVPCMFSDMPREHYKEELAQHQEGVLDIIQRAGINVL 321
Cdd:PRK11598 241 VGETSRAENFSLGGYPRETNPRLAKDNVIYFPHTTSCGTATAVSVPCMFSNMPRKHYDEELAHHQEGLLDIIQRAGINVL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 322 WNDNDGGCKGACDRVPHQNVTALNLPDQCINGECYDEVLFHGLEEYINNLQGDGVIVLHTIGSHGPTYYNRYPPQFRKFT 401
Cdd:PRK11598 321 WNDNDGGCKGACDRVPHQDVTALNLPGQCIDGECYDEVLFHGLENYINNLQGDGVIVLHTIGSHGPTYYNRYPPQFRKFT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 402 PTCDTNEIQTCTKEQLVNTYDNTLVYVDYIVDKAINLLKEHQDKFTTSLVYLSDHGESLGENGIYLHGLPYAIAPDSQKQ 481
Cdd:PRK11598 401 PTCDTNEIQTCTQQQLVNTYDNTILYVDYIVDKAINLLKQHQDKFNTSLVYLSDHGESLGENGIYLHGLPYAIAPDQQTH 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446842536 482 VPMLLWLSEDYQKRYQVDQNCLQKQAQTQHYSQDNLFSTLLGLTGVETKYYQAADDILQTCRRVS 546
Cdd:PRK11598 481 VPMLLWLSPDYQKRYGVDQQCLQKQAQTQDYSQDNLFSTLLGLTGVQTKEYQAADDILQPCRRLS 545
|
|
| OpgE |
COG2194 |
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall ... |
22-544 |
0e+00 |
|
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441797 [Multi-domain] Cd Length: 537 Bit Score: 772.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 22 FYISICLNIAFFKQVLQALPLDSlHNVLVFLSMPVVAFSVINIVLTLSSFLWLNRPLACLFILVGAAAQYFIMTYGIVID 101
Cdd:COG2194 18 LYFALFLNLPFWGRLLAILPLDG-VNLLFLLSLPLLLLAALNLLLSLLAWRYLFKPLLILLLLISAAASYFMDFYGVVID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 102 RSMIANIIDTTPAESYALMTPQMLLTLGFSGVLAALIACWIKIKPaTSRLRSVLFRGANILVSVLLILLVAALFYKDYAS 181
Cdd:COG2194 97 YGMIQNVLETDPAEASELLSPKLILWLLLLGVLPALLLWRVRIRY-RPLLRELGQRLALLLLALLVIVLLALLFYKDYAS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 182 LFRNNKELVKSLSPSNSIVASWSWYSHQ-RLANLPLVRIGEDAHRNPlmqNEKRKNLTILIVGETSRAENFSLNGYPRET 260
Cdd:COG2194 176 FFRNHKELRYLINPSNFIYALGKYAKARyFAAPLPLQPLGADAKLAA---AGAKPTLVVLVVGETARADNFSLNGYARDT 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 261 NPRLAKD-NVVYFPNTASCGTATAVSVPCMFSDMPREHYKEELAQHQEGVLDIIQRAGINVLWNDNDGGCKGACDRVPHQ 339
Cdd:COG2194 253 TPELAKEkNLVSFRDVTSCGTATAVSVPCMFSRLGRADYDPQRALNQENLLDVLQRAGVKVLWRDNQSGCKGVCDRVPTI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 340 NVTALNLPDQCINGECYDEVLFHGLEEYINNLQGDGVIVLHTIGSHGPTYYNRYPPQFRKFTPTCDTNEIQTCTKEQLVN 419
Cdd:COG2194 333 DLTADNLPPLCDGGECLDEVLLDGLDEALADLAGDKLIVLHQMGSHGPAYYKRYPPEFRKFTPTCDTNDLQNCSREELVN 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 420 TYDNTLVYVDYIVDKAINLLKEHQDKFTTSLVYLSDHGESLGENGIYLHGLPYAIAPDSQKQVPMLLWLSEDYQKRYQVD 499
Cdd:COG2194 413 AYDNTILYTDYVLSQVIDLLKAKQDRYDTAMLYVSDHGESLGENGLYLHGTPYAIAPDEQTHVPMIMWLSDGYAQRYGID 492
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 446842536 500 QNCLQKQAQtQHYSQDNLFSTLLGLTGVETKYYQAADDILQTCRR 544
Cdd:COG2194 493 FACLKARAD-KPYSHDNLFHTLLGLLDVRTSVYDPELDILAPCRR 536
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
234-528 |
1.72e-124 |
|
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: 366.56 E-value: 1.72e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 234 RKNLTILIVGETSRAENFSLNGYPRETNPRLAK--DNVVYFPNTASCGTATAVSVPCMFSDMPREHYKEelAQHQEGVLD 311
Cdd:cd16017 1 KPKNVVLVIGESARRDHMSLYGYPRDTTPFLSKlkKNLIVFDNVISCGTSTAVSLPCMLSFANRENYDR--AYYQENLID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 312 IIQRAGINVLWNDNDGGCKGACDRVPHQNVTA--LNLPDQCINGECYDEVLFHGLEEYINNLQGDGVIVLHTIGSHGPtY 389
Cdd:cd16017 79 LAKKAGYKTYWISNQGGCGGYDTRISAIAKIEtvFTNKGSCNSSNCYDEALLPLLDEALADSSKKKLIVLHLMGSHGP-Y 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 390 YNRYPPQFRKFTPTCDtNEIQTCTKEQLVNTYDNTLVYVDYIVDKAINLLKEHQDKftTSLVYLSDHGESLGENGIYLHG 469
Cdd:cd16017 158 YDRYPEEFAKFTPDCD-NELQSCSKEELINAYDNSILYTDYVLSQIIERLKKKDKD--AALIYFSDHGESLGENGLYLHG 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446842536 470 LPYaiAPDSQKQVPMLLWLSEDYQKRYQVdqnCLQKQAQTQHYSQDNLFSTLLGLTGVE 528
Cdd:cd16017 235 APY--APKEQYHVPFIIWSSDSYKQRYPV---ERLRANKDRPFSHDNLFHTLLGLLGIK 288
|
|
| PRK09598 |
PRK09598 |
phosphoethanolamine--lipid A transferase EptA; |
27-544 |
1.35e-95 |
|
phosphoethanolamine--lipid A transferase EptA;
Pssm-ID: 236581 [Multi-domain] Cd Length: 522 Bit Score: 300.54 E-value: 1.35e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 27 CLNIAFFKQVLQALPLDSLHNV----LVFLSMPVVAFSVINIVLTLSSFLwlNRPLACLFILVGAAAQYFIMTYGIVIDR 102
Cdd:PRK09598 24 LLNGVLYHFPLFAYVYKESNQVsfiaMLVVLLFCVNGLLFLLLGLLSRRL--MRLSAIVFSLLNSIAFYFINTYKVFLNK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 103 SMIANIIDTTPAESYALMTPQMLLTLGFSGVLAALIACWI------KIKPATSRLRSVLFRGANILVSVllillvaalfy 176
Cdd:PRK09598 102 SMMGNVLNTNTAESSGFLSVKLFIYIVVLGVLPGYIIYKIplknssKKAPFAAILALVLIFLASAFANS----------- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 177 KDYASLFRNNKELVKSLSPSNSIVASWSWYSHQRLANL--PLVrigedahrNPLMQNEKRKNLTILIVGETSRAENFSLN 254
Cdd:PRK09598 171 KNWLWFDKHAKFLGGLILPWSYSVNTFRVSAHKFFAPTikPLL--------PPLFSPNHSKSVVVLVIGESARKHNYALY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 255 GYPRETNPRLAK---DNVVYFPNTASCGTATAVSVPCMFSdmprEHYKEELAQHqEGVLDIIQRAGINVLWNDNDGGCKg 331
Cdd:PRK09598 243 GYEKPTNPRLSKrlaTHELTLFNATSCATYTTASLECILD----SSFKNTSNAY-ENLPTYLTRAGIKVFWRSANDGEP- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 332 acdrvPHQNVTALN---LPDQCINGEC-YDEVLFHGLEEYINNLQGDGV-IVLHTIGSHGPTYYNRYPPQFRKFTPTCDT 406
Cdd:PRK09598 317 -----NVKVTSYLKnyeLIQKCPNCEApYDESLLYNLPELIKASSNENVlLILHLAGSHGPNYDNKYPLNFRVFKPVCSS 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 407 NEIQTCTKEQLVNTYDNTLVYVDYIVDKAINLLKehQDKFTTSLVYLSDHGESLGENGIYLHGLPYAIAPDSQKQVPMLL 486
Cdd:PRK09598 392 VELSSCSKESLINAYDNTIFYNDYLLDKIISMLK--NLKQPALMIYLSDHGESLGEGAFYLHGIPKSIAPKEQYEIPFIV 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 487 WLSEDYQKRYQVdqnclqKQAQTQhYSQDNLFSTLLGLTGVETKY--YQAADDILQTCRR 544
Cdd:PRK09598 470 WASDSFKKQHSI------IQTQTP-INQNVIFHSVLGVFDFKNPSavYRPSLDLFKHKKE 522
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
239-527 |
9.45e-79 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 249.65 E-value: 9.45e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 239 ILIVGETSRAENFSLNGYPRETNPRLAK--DNVVYFPNTASCGTATAVSVPCMFSDMPREHY------KEELAQHQEGVL 310
Cdd:pfam00884 4 VLVLGESLRAPDLGLYGYPRPTTPFLDRlaEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFgsyvstPVGLPRTEPSLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 311 DIIQRAGINV--------LWNDNDGGCK----GACDRVPHQNVTALN--LPDQCINGECYDEVLFHGLEEYINNLQGDGV 376
Cdd:pfam00884 84 DLLKRAGYNTgaigkwhlGWYNNQSPCNlgfdKFFGRNTGSDLYADPpdVPYNCSGGGVSDEALLDEALEFLDNNDKPFF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 377 IVLHTIGSHGP-TYYNRYPPQFRKFTPtcdtneiQTCTKEQLVNTYDNTLVYVDYIVDKAINLLKEHQDKFTTSLVYLSD 455
Cdd:pfam00884 164 LVLHTLGSHGPpYYPDRYPEKYATFKP-------SSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSD 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446842536 456 HGESLGENGIYLHGLPYAIAPDSQKQVPMLLWLSEDYQKRYQVDqnclqkqaqtQHYSQDNLFSTLLGLTGV 527
Cdd:pfam00884 237 HGESLGEGGGYLHGGKYDNAPEGGYRVPLLIWSPGGKAKGQKSE----------ALVSHVDLFPTILDLAGI 298
|
|
| EptA_B_N |
pfam08019 |
Phosphoethanolamine transferase EptA/EptB; This entry represents a domain found in a group of ... |
59-209 |
1.18e-46 |
|
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: 159.99 E-value: 1.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 59 FSVINIVLTLSSFLWLNRPLACLFILVGAAAQYFIMTYGIVIDRSMIANIIDTTPAESYALMTPQMLLTLGFSGVLAALI 138
Cdd:pfam08019 2 FAALNLLLSLLSWRYLLKPLLILLLLLSAAASYFMDTYGVVIDRDMIQNVLETDVAEASDLLSPKLLLYLLLLGVLPALL 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446842536 139 ACWIKIKPaTSRLRSVLFRGANILVSVLLILLVAALFYKDYASLFRNNKELVKSLSPSNSIVASWSWYSHQ 209
Cdd:pfam08019 82 LWRVRIRY-RPWLRELLSRLALILVSLLVIGLVAFLFYKDYASFFRNHKELRYLINPTNYIYSTVKYAKHQ 151
|
|
| PRK11560 |
PRK11560 |
kdo(2)-lipid A phosphoethanolamine 7''-transferase; |
22-526 |
2.44e-45 |
|
kdo(2)-lipid A phosphoethanolamine 7''-transferase;
Pssm-ID: 183198 [Multi-domain] Cd Length: 558 Bit Score: 167.91 E-value: 2.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 22 FYISICLNIA-FFKQVLQALPLDSLHNVLVFLSMPVVAFSVINIVLTLSSFL--WLNRPLACLFILVGAAAQYFIMTYGI 98
Cdd:PRK11560 18 VYIGLFLNIAvFYRRFDSYAQDFTVWKGLSAVVELAATVLVTFFLLRLLSLFgrRFWRVLASLLVLFSAAASYYMTFFNV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 99 VIDRSMIANIIDTTPAESYALMTPQMLL-TLGFSGVLAALIacWIKIKPATSrLRSVLFRGANILVSVLLILLVAALF-- 175
Cdd:PRK11560 98 VIGYGIIASVMTTDIDLSKEVVGLHFILwLVAVSALPLILI--WNNRCRYTL-LRQLRTPGQRIRSLAVVVLAGLLVWap 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 176 --YKDYASlfRNNKELVKSLSPSNSIVASWSWYSHQRLANLPLV---RIGEDAHRNPLMQNEKR------KNL----TIL 240
Cdd:PRK11560 175 irLLDIQQ--KKVERATGVDLPSYGGVVANSYLPSNWLSALGLYawaQVDESSDNNSLLNPAKKftyqapKGVddtyVVF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 241 IVGETSRAENFSLNGYPRETNPRLAKD-NVVYFPNTaSCGTATAVSVPCMF------SDMPREHYKEElaqhqeGVLDII 313
Cdd:PRK11560 253 IIGETTRWDHMGILGYERNTTPKLAQEkNLAAFRGY-SCDTATKLSLRCMFvreggaEDNPQRTLKEQ------NVFAVL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 314 QRAGINV--------LWNDNdggckgacdrvphqNVTALNL-------PDQCINGECYDEVLFhgLEEYINNL----QGD 374
Cdd:PRK11560 326 KQLGFSSelfamqseMWFYN--------------NTMADNYayreqigAEPRNRGKPVDDMLL--VDEMKQSLgrnpDGK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 375 GVIVLHTIGSHGpTYYNRYPPQFRKFTPTCdTNEIQTCTKEQLVNTYDNTLVYVDYIVDKAINLLKehqDKfTTSLVYLS 454
Cdd:PRK11560 390 HLIILHTKGSHY-NYTQRYPRSFARYQPEC-IGVDSGCSKAQLINSYDNSVLYVDHFISSVIDQLR---DK-KAIVFYAA 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446842536 455 DHGESLGENGiYLHGLPYAIAPDSQKQVPMLLWLSEDY----QKRYQVDQncLQKQAQ--TQHYsQDNLFSTLLGLTG 526
Cdd:PRK11560 464 DHGESINERE-HLHGTPREMAPPEQFRVPMMVWMSDKYlanpDNAQAFAQ--LKKQADmkVPRR-HVELFDTILGCLG 537
|
|
| PRK10649 |
PRK10649 |
phosphoethanolamine transferase CptA; |
33-493 |
2.02e-19 |
|
phosphoethanolamine transferase CptA;
Pssm-ID: 182617 [Multi-domain] Cd Length: 577 Bit Score: 91.69 E-value: 2.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 33 FKQVLQALPLDSLHNVLVFLsMP---VVAFSVINIVLTLSSFLwlnrplaclfilvgAAAQYFImtYGIVIDRSMIANII 109
Cdd:PRK10649 43 TNGFRDALLFSSLWLIPVFL-FPrriRIIAAVIGVVLWAASLA--------------ALCYYVI--YGQEFSQSVLFVMF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 110 DTTPAESYALMTPQMLLTLGFSGVLAALIAC--WIKIKPATSRLRSVLfrganILVSVLLILLVAALFYKDYASLFRNNK 187
Cdd:PRK10649 106 ETNTNEASEYLSQYFSLKIVLIALAYTAVAVllWTRLRPVYIPWPWRY-----VVSFALLYGLILHPIAMNTFIKHKPFE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 188 ELVKSLSPSNSIVASW----SWYS-HQRLANLPlvRIGEDAHRNPLMQNEKRKNLT-----ILIVGETSRAENFSLNGYP 257
Cdd:PRK10649 181 KTLDKLASRMEPAAPWqfltGYYQyRQQLNSLQ--KLLNENAALPPLANLKDESGNaprtlVLVIGESTQRGRMSLYGYP 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 258 RETNPRLAK-----------DNVVyfpnTASCGTATAVSVPCMFSDmpREHYKEELAQhqEGVLDIIQRAGINVLWNDNd 326
Cdd:PRK10649 259 RETTPELDAlhktdpgltvfNNVV----TSRPYTIEILQQALTFAD--EKNPDLYLTQ--PSLMNMMKQAGYKTFWITN- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 327 ggckgacdrvpHQNVTALN--------LPDQCI--------NGECYDEVLFHGLEEYINNLQGDGVIVLHTIGSHgPTYY 390
Cdd:PRK10649 330 -----------QQTMTARNtmltvfsrQTDKQYymnqqrtqNAREYDTNVLKPFSEVLADPAPKKFIIVHLLGTH-IKYK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 391 NRYPPQFRKFT-------PTCDTNEIQTctkeqlVNTYDNTLVYVDYIVDkaiNLLKEHQDKFTTS-LVYLSDHGE---- 458
Cdd:PRK10649 398 YRYPENQGKFDdrtghvpPGLNADELES------YNDYDNANLYNDHVVA---SLIKDFKATDPNGfLVYFSDHGEevyd 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 446842536 459 -----SLGENgiylHGLP----YAIapdsqkqvPMLLWLSEDYQ 493
Cdd:PRK10649 469 tpphkTQGRN----EDNPtrhmYTI--------PFLLWTSEKWQ 500
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
238-532 |
7.70e-14 |
|
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: 71.81 E-value: 7.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 238 TILIVGETSRAENFSLNGYPRETNP---RLAKDNVVyFPNTASCGTATAVSVPCMFSDM-PREH--YKEELAQHQEGVLD 311
Cdd:cd16148 3 VILIVIDSLRADHLGCYGYDRVTTPnldRLAAEGVV-FDNHYSGSNPTLPSRFSLFTGLyPFYHgvWGGPLEPDDPTLAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 312 IIQRAGIN-VLWNDNDGGCKGAC-DRVPHQNVTALNLPDQCINGECY-DEVLFHGLEEYINNLQGDG--VIVLHTIGSHG 386
Cdd:cd16148 82 ILRKAGYYtAAVSSNPHLFGGPGfDRGFDTFEDFRGQEGDPGEEGDErAERVTDRALEWLDRNADDDpfFLFLHYFDPHE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 387 PtyynryppqFRkftptcdtneiqtctkeqlvntYDNTLVYVDYIVDKAINLLKEHQDKFTTSLVYLSDHGESLGENGIY 466
Cdd:cd16148 162 P---------YL----------------------YDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGLY 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446842536 467 L-HGLPYAiapDSQKQVPMLLWLsEDYQKRYQVDqnclqkqAQTQHYsqDnLFSTLLGLTGVETKYY 532
Cdd:cd16148 211 WgHGSNLY---DEQLHVPLIIRW-PGKEPGKRVD-------ALVSHI--D-IAPTLLDLLGVEPPDY 263
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
32-534 |
1.70e-12 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 70.07 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 32 FFKQVLQALPLDSLHNVLVFLSMPVVAFSVINIVLTLSSFLWLnrpLACLFILVGAAAQYFIMTYGIVIDRSMIANIIDT 111
Cdd:COG1368 27 ILQAFLYGLRFILYLLLLLLLLLLLLLPLLFRRPKLRWIYLLL---VLLLLLLLLVADILYYRFFGDRLNFSDLDYLGDT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 112 TPAESyALMTPQMLLTLGFSGVLAALIACWIKIKPATSRLRSVLFRGANILVSVLLILLVAALFYKDYASLFR--NNKEL 189
Cdd:COG1368 104 GEVLG-SLLSSYDLLLLLDLLLLLLLLLLLYRLLKKLRKSLPWRKRLALLLLLLALLLLGIRLGEDRPLNLSDafSRNNF 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 190 VKSLSPSNSIVASWSWYSHQRLANLPLVRIGE-------DAHRNPLMQNEKRKNLtILIVGETSRAENFSLNGYPRETNP 262
Cdd:COG1368 183 VNELGLNGPYSFYDALRNNKAPATYSEEEALEikkylksNRPTPNPFGPAKKPNV-VVILLESFSDFFIGALGNGKDVTP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 263 ---RLAKDNVvYFPNTASCGTATAVSVPCMFSDMP----REHYKEELAQHQEGVLDIIQRAGI-------NVLWNDNdgg 328
Cdd:COG1368 262 fldSLAKESL-YFGNFYSQGGRTSRGEFAVLTGLPplpgGSPYKRPGQNNFPSLPSILKKQGYetsffhgGDGSFWN--- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 329 ckgaCDRV-PHQNVTAL----NLPDQCING-ECYDEVLFHGLEEYINNLQGDGVIVLHTIGSHGPtyYNrYPPQFRKFTP 402
Cdd:COG1368 338 ----RDSFyKNLGFDEFydreDFDDPFDGGwGVSDEDLFDKALEELEKLKKPFFAFLITLSNHGP--YT-LPEEDKKIPD 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 403 TCDTNeiqtctkeqlVNTYDNTLVYVDYIVDKAINLLKEhQDKFT-TSLVYLSDHGESLGENGIYLHglpyaiaPDSQKQ 481
Cdd:COG1368 411 YGKTT----------LNNYLNAVRYADQALGEFIEKLKK-SGWYDnTIFVIYGDHGPRSPGKTDYEN-------PLERYR 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 446842536 482 VPMLLWLSEDYQKRyQVDQNClqkqaqtqhySQDNLFSTLLGLTGVETKYYQA 534
Cdd:COG1368 473 VPLLIYSPGLKKPK-VIDTVG----------SQIDIAPTLLDLLGIDYPSYYA 514
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
235-524 |
2.27e-11 |
|
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. 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. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.
Pssm-ID: 293732 [Multi-domain] Cd Length: 237 Bit Score: 63.98 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 235 KNLtILIVGETSRAENFSLNGYPRETNPRLA--KDNVVYFP-NTASCGTATAVSVPCMFSdmprehykeelaqhqeGVLD 311
Cdd:cd00016 1 KHV-VLIVLDGLGADDLGKAGNPAPTTPNLKrlASEGATFNfRSVSPPTSSAPNHAALLT----------------GAYP 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 312 IIQRAGInvlWNDNDGGCKGACDRVP--HQNVTALnLPDQCIngecydEVLFHGLEEYINNLQGD--GVIVLHTIGSHGP 387
Cdd:cd00016 64 TLHGYTG---NGSADPELPSRAAGKDedGPTIPEL-LKQAGY------RTGVIGLLKAIDETSKEkpFVLFLHFDGPDGP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 388 TY-YNRYPPqfrkftptcdtneiqtctkeqlvnTYDNTLVYVDYIVDKAINLLKEHQDKFTTSLVYLSDHGESLGENGIY 466
Cdd:cd00016 134 GHaYGPNTP------------------------EYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHGGD 189
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446842536 467 LHGLPYAIAPDSQKQVPMLLWLSedyqkryqvdqNCLQKQAQTQHYSQDNLFSTLLGL 524
Cdd:cd00016 190 PKADGKADKSHTGMRVPFIAYGP-----------GVKKGGVKHELISQYDIAPTLADL 236
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
386-487 |
4.77e-06 |
|
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];
Pssm-ID: 442317 [Multi-domain] Cd Length: 603 Bit Score: 49.52 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 386 GPTYYNRYPPQFRKFTPTCDTNEIQTCTKEQ---LVNTYDNTLVYVDYIVDKAINLLKEHQDKFTTSLVYLSDHGESLGE 462
Cdd:COG3083 391 APHAYSFPADYPKPFQPSEDCNYLALDNESDptpFKNRYRNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFNE 470
|
90 100
....*....|....*....|....*..
gi 446842536 463 NGI--YLHGLPYAiapDSQKQVPMLLW 487
Cdd:COG3083 471 NGQnyWGHNSNFS---RYQLQVPLVIH 494
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
366-528 |
2.13e-04 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 43.71 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 366 EYINNLQGDG---VIVLHTIGSHGPT-----YYNRYPPQFRKFTPTCDTNEIQTCTKEQLVNTYDNTLVYVDYIVDKAIN 437
Cdd:COG3119 139 DFLERQADKDkpfFLYLAFNAPHAPYqapeeYLDKYDGKDIPLPPNLAPRDLTEEELRRARAAYAAMIEEVDDQVGRLLD 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 438 LLKEH-QDKFTTsLVYLSDHGESLGENGIYLH-GLPY--AIapdsqkQVPMLLWLSEDYQKRYQVDQnclqkqaqtQHYS 513
Cdd:COG3119 219 ALEELgLADNTI-VVFTSDNGPSLGEHGLRGGkGTLYegGI------RVPLIVRWPGKIKAGSVSDA---------LVSL 282
|
170
....*....|....*
gi 446842536 514 QDnLFSTLLGLTGVE 528
Cdd:COG3119 283 ID-LLPTLLDLAGVP 296
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
427-528 |
4.22e-03 |
|
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: 39.67 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446842536 427 YVDYIVDKAINLLKEHQDKFTtsLVYLSDHGESLGENGIYLHGlpyAIAPDSQKQVPMLLWlSEDYQKRYQVDQNclqkq 506
Cdd:cd16156 249 FVDYEIGRVLDAADEIAEDAW--VIYTSDHGDMLGAHKLWAKG---PAVYDEITNIPLIIR-GKGGEKAGTVTDT----- 317
|
90 100
....*....|....*....|..
gi 446842536 507 aqtqHYSQDNLFSTLLGLTGVE 528
Cdd:cd16156 318 ----PVSHIDLAPTILDYAGIP 335
|
|
| |
