|
Name |
Accession |
Description |
Interval |
E-value |
| OpgE |
COG2194 |
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall ... |
25-539 |
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: 788.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 25 NWPVLLHFYDILSNIEHFkIGFVVSIPFLLVAALNFVFMPFSIRFLMKPFFAFLFVTGSIASYTMMKYRVLFDGDMIQNI 104
Cdd:COG2194 25 NLPFWGRLLAILPLDGVN-LLFLLSLPLLLLAALNLLLSLLAWRYLFKPLLILLLLISAAASYFMDFYGVVIDYGMIQNV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 105 FETNQSEAFAYVNAPIIIWVLLTGLLPAALIFFVKIEYAStWYKGIAQRLLSMFFSLVIVGIIAALYYQDYASIGRNNQT 184
Cdd:COG2194 104 LETDPAEASELLSPKLILWLLLLGVLPALLLWRVRIRYRP-LLRELGQRLALLLLALLVIVLLALLFYKDYASFFRNHKE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 185 LNREIVPANFMYSTSKYLYRRYMAEPIPFVTLGDDATRVTKKDKPTLMFLVVGETARGKNFSMNGYEKDTNPFTSKSGGV 264
Cdd:COG2194 183 LRYLINPSNFIYALGKYAKARYFAAPLPLQPLGADAKLAAAGAKPTLVVLVVGETARADNFSLNGYARDTTPELAKEKNL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 265 ISFNDVRSCGTATAVSVPCMFSNMGRKEFDDNRARNSEGLLDVLQKTGISIFWKENDGGCKGVCDRVPNIEIKPKDHPKF 344
Cdd:COG2194 263 VSFRDVTSCGTATAVSVPCMFSRLGRADYDPQRALNQENLLDVLQRAGVKVLWRDNQSGCKGVCDRVPTIDLTADNLPPL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 345 CDKNTCYDEVVLQDLDSEIAQMKGDKLVGFHLIGSHGPTYYKRYPDAHRQFTPDCPRSDIENCTDEELTNTYDNTIRYTD 424
Cdd:COG2194 343 CDGGECLDEVLLDGLDEALADLAGDKLIVLHQMGSHGPAYYKRYPPEFRKFTPTCDTNDLQNCSREELVNAYDNTILYTD 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 425 FVIAEMIAKLKTYEDKYNTALLYVSDHGESLGAMGLYLHGTPYKFAPDDQTRVPMQVWMSPGFTKEKGVDMACLQQKaAD 504
Cdd:COG2194 423 YVLSQVIDLLKAKQDRYDTAMLYVSDHGESLGENGLYLHGTPYAIAPDEQTHVPMIMWLSDGYAQRYGIDFACLKAR-AD 501
|
490 500 510
....*....|....*....|....*....|....*
gi 756832308 505 TRYSHDNIFSSVLGIWDVKTSVYEKGLDIFSQCRT 539
Cdd:COG2194 502 KPYSHDNLFHTLLGLLDVRTSVYDPELDILAPCRR 536
|
|
| PRK11598 |
PRK11598 |
putative metal dependent hydrolase; Provisional |
46-541 |
0e+00 |
|
putative metal dependent hydrolase; Provisional
Pssm-ID: 183224 [Multi-domain] Cd Length: 545 Bit Score: 613.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 46 FVVSIPFLLVAALNFVFMPFSIRFLMKPFFAFLFVTGSIASYTMMKYRVLFDGDMIQNIFETNQSEAFAYVNAPIIIWVL 125
Cdd:PRK11598 49 VFASMPVVAFSVINIVFTLLSFPWLRRPLACLFILVGAAAQYFMMTYGIVIDRSMIQNIFETTPAESFALMTPQMLLWLG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 126 LTGLLPAALIFFVKIEYASTWYKGIAQRLLSMFFSLVIVGIIAALYYQDYASIGRNNQTLNREIVPANFMYSTSKYLYRR 205
Cdd:PRK11598 129 LSGVLPALIACWIKIRPATPRWRSVLFRLANILVSVLLILLVAALFYKDYASLFRNNKELVKSLTPSNSIVASWSWYSHQ 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 206 YMAEpIPFVTLGDDATRV---TKKDKPTLMFLVVGETARGKNFSMNGYEKDTNPFTSKSGgVISFNDVRSCGTATAVSVP 282
Cdd:PRK11598 209 RLAN-LPLVRIGEDAHKNplmQNQKRKNLTILVVGETSRAENFSLGGYPRETNPRLAKDN-VIYFPHTTSCGTATAVSVP 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 283 CMFSNMGRKEFDDNRARNSEGLLDVLQKTGISIFWKENDGGCKGVCDRVPNIEIKPKDHPKFCDKNTCYDEVVLQDLDSE 362
Cdd:PRK11598 287 CMFSNMPRKHYDEELAHHQEGLLDIIQRAGINVLWNDNDGGCKGACDRVPHQDVTALNLPGQCIDGECYDEVLFHGLENY 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 363 IAQMKGDKLVGFHLIGSHGPTYYKRYPDAHRQFTPDCPRSDIENCTDEELTNTYDNTIRYTDFVIAEMIAKLKTYEDKYN 442
Cdd:PRK11598 367 INNLQGDGVIVLHTIGSHGPTYYNRYPPQFRKFTPTCDTNEIQTCTQQQLVNTYDNTILYVDYIVDKAINLLKQHQDKFN 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 443 TALLYVSDHGESLGAMGLYLHGTPYKFAPDDQTRVPMQVWMSPGFTKEKGVDMACLQQKAADTRYSHDNIFSSVLGIWDV 522
Cdd:PRK11598 447 TSLVYLSDHGESLGENGIYLHGLPYAIAPDQQTHVPMLLWLSPDYQKRYGVDQQCLQKQAQTQDYSQDNLFSTLLGLTGV 526
|
490
....*....|....*....
gi 756832308 523 KTSVYEKGLDIFSQCRTVQ 541
Cdd:PRK11598 527 QTKEYQAADDILQPCRRLS 545
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
228-523 |
2.27e-119 |
|
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: 353.47 E-value: 2.27e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 228 KPTLMFLVVGETARGKNFSMNGYEKDTNPFTSK-SGGVISFNDVRSCGTATAVSVPCMFSNMGRKEFDdnRARNSEGLLD 306
Cdd:cd16017 1 KPKNVVLVIGESARRDHMSLYGYPRDTTPFLSKlKKNLIVFDNVISCGTSTAVSLPCMLSFANRENYD--RAYYQENLID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 307 VLQKTGISIFWKENDGGCKGVCDRVPNI--EIKPKDHPKFCDKNTCYDEVVLQDLDSEIAQMKGDKLVGFHLIGSHGPtY 384
Cdd:cd16017 79 LAKKAGYKTYWISNQGGCGGYDTRISAIakIETVFTNKGSCNSSNCYDEALLPLLDEALADSSKKKLIVLHLMGSHGP-Y 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 385 YKRYPDAHRQFTPDCpRSDIENCTDEELTNTYDNTIRYTDFVIAEMIAKLKtyEDKYNTALLYVSDHGESLGAMGLYLHG 464
Cdd:cd16017 158 YDRYPEEFAKFTPDC-DNELQSCSKEELINAYDNSILYTDYVLSQIIERLK--KKDKDAALIYFSDHGESLGENGLYLHG 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 756832308 465 TPYkfAPDDQTRVPMQVWMSPGFTKEKGVdmaCLQQKAADTRYSHDNIFSSVLGIWDVK 523
Cdd:cd16017 235 APY--APKEQYHVPFIIWSSDSYKQRYPV---ERLRANKDRPFSHDNLFHTLLGLLGIK 288
|
|
| PRK09598 |
PRK09598 |
phosphoethanolamine--lipid A transferase EptA; |
25-534 |
3.70e-97 |
|
phosphoethanolamine--lipid A transferase EptA;
Pssm-ID: 236581 [Multi-domain] Cd Length: 522 Bit Score: 304.40 E-value: 3.70e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 25 NWPVLLHFYdilSNIEHFKIGFVVSIPFLLVAALNFVFMPFSIRFLMKPFFAFLFVTGSIASYTMMKYRVLFDGDMIQNI 104
Cdd:PRK09598 31 HFPLFAYVY---KESNQVSFIAMLVVLLFCVNGLLFLLLGLLSRRLMRLSAIVFSLLNSIAFYFINTYKVFLNKSMMGNV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 105 FETNQSEAFAYVNAPIIIWVLLTGLLPAALIFFVKIEYAStwYKGIAQRLLSMFFSLVIVGIIAAlyyQDYASIGRNNQT 184
Cdd:PRK09598 108 LNTNTAESSGFLSVKLFIYIVVLGVLPGYIIYKIPLKNSS--KKAPFAAILALVLIFLASAFANS---KNWLWFDKHAKF 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 185 LNREIVPANFMYSTSKYLYRRYMAEPIPfvTLGDDATrvTKKDKPTLMFLVVGETARGKNFSMNGYEKDTNPFTSK--SG 262
Cdd:PRK09598 183 LGGLILPWSYSVNTFRVSAHKFFAPTIK--PLLPPLF--SPNHSKSVVVLVIGESARKHNYALYGYEKPTNPRLSKrlAT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 263 GVISFNDVRSCGTATAVSVPCMFSNMGrkefdDNRARNSEGLLDVLQKTGISIFWKENDGGckgvcdrVPNIEIKP---- 338
Cdd:PRK09598 259 HELTLFNATSCATYTTASLECILDSSF-----KNTSNAYENLPTYLTRAGIKVFWRSANDG-------EPNVKVTSylkn 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 339 KDHPKFCDKNTC-YDEVVLQDLDSEIAQMKGDK-LVGFHLIGSHGPTYYKRYPDAHRQFTPDCPRSDIENCTDEELTNTY 416
Cdd:PRK09598 327 YELIQKCPNCEApYDESLLYNLPELIKASSNENvLLILHLAGSHGPNYDNKYPLNFRVFKPVCSSVELSSCSKESLINAY 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 417 DNTIRYTDFVIAEMIAKLKtyEDKYNTALLYVSDHGESLGAMGLYLHGTPYKFAPDDQTRVPMQVWMSPGFTKEKGVdma 496
Cdd:PRK09598 407 DNTIFYNDYLLDKIISMLK--NLKQPALMIYLSDHGESLGEGAFYLHGIPKSIAPKEQYEIPFIVWASDSFKKQHSI--- 481
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 756832308 497 cLQqkaADTRYSHDNIFSSVLGIWDVKT--SVYEKGLDIF 534
Cdd:PRK09598 482 -IQ---TQTPINQNVIFHSVLGVFDFKNpsAVYRPSLDLF 517
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
233-518 |
3.70e-61 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 203.42 E-value: 3.70e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 233 FLVVGETARGKNFSMNGYEKDTNPFTSK-SGGVISFNDVRSCGTATAVSVPCMFSNMGRKEFD------DNRARNSEGLL 305
Cdd:pfam00884 4 VLVLGESLRAPDLGLYGYPRPTTPFLDRlAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGsyvstpVGLPRTEPSLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 306 DVLQKTGI--------SIFWKENDGGCK----GVCDRVPNIE--IKPKDHPKFCDKNTCYDEVVLQDLDSEIAQMKGDKL 371
Cdd:pfam00884 84 DLLKRAGYntgaigkwHLGWYNNQSPCNlgfdKFFGRNTGSDlyADPPDVPYNCSGGGVSDEALLDEALEFLDNNDKPFF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 372 VGFHLIGSHGP-TYYKRYPDAHRQFTPdcprsdiENCTDEELTNTYDNTIRYTDFVIAEMIAKLKTYEDKYNTALLYVSD 450
Cdd:pfam00884 164 LVLHTLGSHGPpYYPDRYPEKYATFKP-------SSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSD 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 756832308 451 HGESLGAMGLYLHGTPYKFAPDDQTRVPMQVWMSPGFtkekgvdmacLQQKAADTRYSHDNIFSSVLG 518
Cdd:pfam00884 237 HGESLGEGGGYLHGGKYDNAPEGGYRVPLLIWSPGGK----------AKGQKSEALVSHVDLFPTILD 294
|
|
| EptA_B_N |
pfam08019 |
Phosphoethanolamine transferase EptA/EptB; This entry represents a domain found in a group of ... |
54-205 |
4.80e-60 |
|
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: 195.43 E-value: 4.80e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 54 LVAALNFVFMPFSIRFLMKPFFAFLFVTGSIASYTMMKYRVLFDGDMIQNIFETNQSEAFAYVNAPIIIWVLLTGLLPAA 133
Cdd:pfam08019 1 LFAALNLLLSLLSWRYLLKPLLILLLLLSAAASYFMDTYGVVIDRDMIQNVLETDVAEASDLLSPKLLLYLLLLGVLPAL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 756832308 134 LIFFVKIEYAStWYKGIAQRLLSMFFSLVIVGIIAALYYQDYASIGRNNQTLNREIVPANFMYSTSKYLYRR 205
Cdd:pfam08019 81 LLWRVRIRYRP-WLRELLSRLALILVSLLVIGLVAFLFYKDYASFFRNHKELRYLINPTNYIYSTVKYAKHQ 151
|
|
| PRK11560 |
PRK11560 |
kdo(2)-lipid A phosphoethanolamine 7''-transferase; |
25-518 |
8.21e-44 |
|
kdo(2)-lipid A phosphoethanolamine 7''-transferase;
Pssm-ID: 183198 [Multi-domain] Cd Length: 558 Bit Score: 163.29 E-value: 8.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 25 NWPVLLHFYDILSniEHFKIGFVVSIPFLLVAALNFVFmpFSIRFLM---KPFF---AFLFVTGSI-ASYTMMKYRVLFD 97
Cdd:PRK11560 25 NIAVFYRRFDSYA--QDFTVWKGLSAVVELAATVLVTF--FLLRLLSlfgRRFWrvlASLLVLFSAaASYYMTFFNVVIG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 98 GDMIQNIFETNQSEAFAYVNAPIIIWVLLTGLLPAALIFFVKIEYAS-TWYKGIAQRLLSMFFSLVIVGII-AALYYQDY 175
Cdd:PRK11560 101 YGIIASVMTTDIDLSKEVVGLHFILWLVAVSALPLILIWNNRCRYTLlRQLRTPGQRIRSLAVVVLAGLLVwAPIRLLDI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 176 ASiGRNNQTLNREI-----------VPANFMYSTSKYLYRRYmAEPIPFVTLGDDATRVT----KKDKPTLMFLVVGETA 240
Cdd:PRK11560 181 QQ-KKVERATGVDLpsyggvvansyLPSNWLSALGLYAWAQV-DESSDNNSLLNPAKKFTyqapKGVDDTYVVFIIGETT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 241 RGKNFSMNGYEKDTNPFTSKSGGVISFNDVrSCGTATAVSVPCMFSNMGRKEFDDNRARNSEGLLDVLQKTGIS--IF-- 316
Cdd:PRK11560 259 RWDHMGILGYERNTTPKLAQEKNLAAFRGY-SCDTATKLSLRCMFVREGGAEDNPQRTLKEQNVFAVLKQLGFSseLFam 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 317 ----WKENDGGCKGVCDRvPNIEIKPKDHPKFCDkntcyDEVVLQDLDSEIAQM-KGDKLVGFHLIGSHGpTYYKRYPDA 391
Cdd:PRK11560 338 qsemWFYNNTMADNYAYR-EQIGAEPRNRGKPVD-----DMLLVDEMKQSLGRNpDGKHLIILHTKGSHY-NYTQRYPRS 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 392 HRQFTPDCPRSDiENCTDEELTNTYDNTIRYTDFVIAEMIAKLKtyeDKyNTALLYVSDHGESLGAmGLYLHGTPYKFAP 471
Cdd:PRK11560 411 FARYQPECIGVD-SGCSKAQLINSYDNSVLYVDHFISSVIDQLR---DK-KAIVFYAADHGESINE-REHLHGTPREMAP 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 756832308 472 DDQTRVPMQVWMSPGF----TKEKGVDMACLQQKAADTRYsHDNIFSSVLG 518
Cdd:PRK11560 485 PEQFRVPMMVWMSDKYlanpDNAQAFAQLKKQADMKVPRR-HVELFDTILG 534
|
|
| PRK10649 |
PRK10649 |
phosphoethanolamine transferase CptA; |
92-485 |
2.11e-20 |
|
phosphoethanolamine transferase CptA;
Pssm-ID: 182617 [Multi-domain] Cd Length: 577 Bit Score: 94.77 E-value: 2.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 92 YRVLFDGDMIQNIFETNQSEAFAYVNAPIIIWVLLTGLLPAALIFFVKIEYASTWYKGIAQRLLSMffsLVIVGIIAALY 171
Cdd:PRK10649 92 YGQEFSQSVLFVMFETNTNEASEYLSQYFSLKIVLIALAYTAVAVLLWTRLRPVYIPWPWRYVVSF---ALLYGLILHPI 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 172 YQDYASIGRN-NQTLNR---EIVPAN-FMYSTSKYLYRRYMA---------EPIPFVTLGDDATrvtkKDKPTLMFLVVG 237
Cdd:PRK10649 169 AMNTFIKHKPfEKTLDKlasRMEPAApWQFLTGYYQYRQQLNslqkllnenAALPPLANLKDES----GNAPRTLVLVIG 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 238 ETARGKNFSMNGYEKDTNPFTSK----SGGVISFNDVRSCGTAT--AVSVPCMFSNmgRKEFDDNRARNSegLLDVLQKT 311
Cdd:PRK10649 245 ESTQRGRMSLYGYPRETTPELDAlhktDPGLTVFNNVVTSRPYTieILQQALTFAD--EKNPDLYLTQPS--LMNMMKQA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 312 GISIFWKENDggcKGVCDRVPNIEI--KPKDHPKFCDKNTC-----YDEVVLQDLDSEIAQMKGDKLVGFHLIGSHgPTY 384
Cdd:PRK10649 321 GYKTFWITNQ---QTMTARNTMLTVfsRQTDKQYYMNQQRTqnareYDTNVLKPFSEVLADPAPKKFIIVHLLGTH-IKY 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 385 YKRYPDAHRQFT------PDCPRSDienctDEELTNTYDNTIRYTDFVIAEMIAKLKTYEDkyNTALLYVSDHGESLgam 458
Cdd:PRK10649 397 KYRYPENQGKFDdrtghvPPGLNAD-----ELESYNDYDNANLYNDHVVASLIKDFKATDP--NGFLVYFSDHGEEV--- 466
|
410 420 430
....*....|....*....|....*....|....
gi 756832308 459 glyLHGTPYKFA---PDDQTR----VPMQVWMSP 485
Cdd:PRK10649 467 ---YDTPPHKTQgrnEDNPTRhmytIPFLLWTSE 497
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
416-494 |
4.21e-09 |
|
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: 57.56 E-value: 4.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 416 YDNTIRYTDFVIAEMIAKLKTYEDKYNTALLYVSDHGESLGAMGLYL--HGTPYkfapDDQTRVPMQVWmSPGFTKEKGV 493
Cdd:cd16148 165 YDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGLYWghGSNLY----DEQLHVPLIIR-WPGKEPGKRV 239
|
.
gi 756832308 494 D 494
Cdd:cd16148 240 D 240
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
32-535 |
7.09e-09 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 58.51 E-value: 7.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 32 FYDILSNIEHFKIGFVVSIPFLLVAALNFVFMPFSIRFL------MKPFFAFLFVTGSIASY----TMMKYR---VLFDG 98
Cdd:COG1368 15 FLLFNFDLSLGEILQAFLYGLRFILYLLLLLLLLLLLLLpllfrrPKLRWIYLLLVLLLLLLllvaDILYYRffgDRLNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 99 DMIQNIFETNQSEAFAyVNAPIIIWVLLTGLLPAALIFFVKIEYASTWYKGIAQRLLSMFFSLVIVGIIAALYYQDYASI 178
Cdd:COG1368 95 SDLDYLGDTGEVLGSL-LSSYDLLLLLDLLLLLLLLLLLYRLLKKLRKSLPWRKRLALLLLLLALLLLGIRLGEDRPLNL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 179 GR--NNQTLNREIV---PANFMYSTSKYLYRRYM-----AEPIPFVTLGDDATRVTKKDKPTLMFLVVGETARGKNFSMN 248
Cdd:COG1368 174 SDafSRNNFVNELGlngPYSFYDALRNNKAPATYseeeaLEIKKYLKSNRPTPNPFGPAKKPNVVVILLESFSDFFIGAL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 249 GYEKDTNPFT---SKSGgvISFNDVRSCGTATAVSVPCMFSNM----GRKEFDDNRARNSEGLLDVLQKTGI-SIFWKEN 320
Cdd:COG1368 254 GNGKDVTPFLdslAKES--LYFGNFYSQGGRTSRGEFAVLTGLpplpGGSPYKRPGQNNFPSLPSILKKQGYeTSFFHGG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 321 DGG---CKGVcdrVPNIEI-KPKDHPKFCDKNT----CYDEVVLQDLDSEIAQMKGDKLVGFHLIGSHGPtyYKrYPDAH 392
Cdd:COG1368 332 DGSfwnRDSF---YKNLGFdEFYDREDFDDPFDggwgVSDEDLFDKALEELEKLKKPFFAFLITLSNHGP--YT-LPEED 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 393 RQFTPdcprsdiencTDEELTNTYDNTIRYTDFVIAEMIAKLKTYEDKYNTALLYVSDHGESLGamglylHGTPYKFAPD 472
Cdd:COG1368 406 KKIPD----------YGKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGPRSP------GKTDYENPLE 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 756832308 473 DQtRVPMqVWMSPGFTKEKGVDMAClqqkaadtrySHDNIFSSVLGIWDVKTSVYEK-GLDIFS 535
Cdd:COG1368 470 RY-RVPL-LIYSPGLKKPKVIDTVG----------SQIDIAPTLLDLLGIDYPSYYAfGRDLLS 521
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
413-520 |
1.69e-08 |
|
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: 55.50 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 413 TNTYDNTIRYTDFVIAEMIAKLKTYEDKYNTALLYVSDHGESLGAMGLYLHGTPYKFAPDDQTRVPMQVWmSPGFTKekg 492
Cdd:cd00016 141 TPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHGGDPKADGKADKSHTGMRVPFIAY-GPGVKK--- 216
|
90 100
....*....|....*....|....*...
gi 756832308 493 vdmaclqQKAADTRYSHDNIFSSVLGIW 520
Cdd:cd00016 217 -------GGVKHELISQYDIAPTLADLL 237
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
380-493 |
1.10e-06 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 51.03 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 380 HGPT-----YYKRYPDAHRQFTPDCPRSDIENCTDEELTNTYDNTIRYTDFVIAEMIAKLKT--YEDkyNTALLYVSDHG 452
Cdd:COG3119 161 HAPYqapeeYLDKYDGKDIPLPPNLAPRDLTEEELRRARAAYAAMIEEVDDQVGRLLDALEElgLAD--NTIVVFTSDNG 238
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 756832308 453 ESLGAMGLYLH-GTPYkfapDDQTRVPMQVWmSPGFTKEKGV 493
Cdd:COG3119 239 PSLGEHGLRGGkGTLY----EGGIRVPLIVR-WPGKIKAGSV 275
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
422-487 |
1.08e-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: 293760 [Multi-domain] Cd Length: 321 Bit Score: 47.54 E-value: 1.08e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 756832308 422 YTDFVIAEMIAKLKTYEDKYNTALLYVSDHGESLGAMGLYLHGTPYkfapDDQTRVPMQVWmSPGF 487
Cdd:cd16037 170 FLDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGERGLWGKSTMY----EESVRVPMIIS-GPGI 230
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
422-523 |
1.38e-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: 47.76 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 422 YTDFVIAEMIAKLKTYEDkyNTALLYVSDHGESLGAMGLYLHGTPykfAPDDQTRVPMQVWMsPGFTKEKGVDmaclqqk 501
Cdd:cd16156 249 FVDYEIGRVLDAADEIAE--DAWVIYTSDHGDMLGAHKLWAKGPA---VYDEITNIPLIIRG-KGGEKAGTVT------- 315
|
90 100
....*....|....*....|..
gi 756832308 502 aaDTRYSHDNIFSSVLGIWDVK 523
Cdd:cd16156 316 --DTPVSHIDLAPTILDYAGIP 335
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
351-518 |
1.83e-05 |
|
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: 46.52 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 351 YDEVVLQDLDSEIAQMKGDKLVGFHL-IGSHGPtyYKrYPDAHRQFTPDCPrsdiencTDEELTNTYDNTIRYTDFVIAE 429
Cdd:cd16015 138 SDESLFDQALEELEELKKKPFFIFLVtMSNHGP--YD-LPEEKKDEPLKVE-------EDKTELENYLNAIHYTDKALGE 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 430 MIAKLKTYEDKYNTALLYVSDHGeslgaMGLYLHGTPYKFAPDDQTRVPMqVWMSPGFTKEKGVDMAClqqkaadtrySH 509
Cdd:cd16015 208 FIEKLKKSGLYENTIIVIYGDHL-----PSLGSDYDETDEDPLDLYRTPL-LIYSPGLKKPKKIDRVG----------SQ 271
|
....*....
gi 756832308 510 DNIFSSVLG 518
Cdd:cd16015 272 IDIAPTLLD 280
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
382-498 |
3.37e-04 |
|
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: 293758 [Multi-domain] Cd Length: 399 Bit Score: 42.94 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 382 PTYYKRYPDAHRQFTPDCPrsdiencTDEELTNTYDNTIRY-------TDFVIAEMIAKLKT---YEdkyNTALLYVSDH 451
Cdd:cd16034 195 EEYLDMYDPKKLLLRPNVP-------EDKKEEAGLREDLRGyyamitaLDDNIGRLLDALKElglLE---NTIVVFTSDH 264
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 756832308 452 GESLGAMGLYLHGTPYkfapDDQTRVPMQV-WmsPGFTKEKGVDMACL 498
Cdd:cd16034 265 GDMLGSHGLMNKQVPY----EESIRVPFIIrY--PGKIKAGRVVDLLI 306
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
412-479 |
5.57e-04 |
|
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: 293759 [Multi-domain] Cd Length: 311 Bit Score: 42.19 E-value: 5.57e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 412 LTNTYDNTIRYTDFVIAEMIAKLKTYEDKYNTALLYVSDHGESLGAMGLyLH--GTPYkfapDDQTRVPM 479
Cdd:cd16035 165 FRNFYYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHGL-RGkgFNAY----EEALHVPL 229
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
393-489 |
7.98e-04 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 41.96 E-value: 7.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756832308 393 RQFTPDCPRSDIencTDEELTNT---YDNTIRYTDFVIAEMIAKLKTYEDKYNTALLYVSDHGESLGAMGLYLHGTPYkf 469
Cdd:PRK13759 247 EGGSIDALRGNL---GEEYARRAraaYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHGDMLGDHYLFRKGYPY-- 321
|
90 100
....*....|....*....|
gi 756832308 470 apDDQTRVPMQVWMSPGFTK 489
Cdd:PRK13759 322 --EGSAHIPFIIYDPGGLLA 339
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
420-494 |
2.25e-03 |
|
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: 293757 [Multi-domain] Cd Length: 411 Bit Score: 40.67 E-value: 2.25e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 756832308 420 IRYTDFVIAEMIAKLK---TYEdkyNTALLYVSDHGESLGAMGLYLHGTpykFAPDDQTRVPMQVWMsPGFTKEKGVD 494
Cdd:cd16033 223 ITLIDDAIGRILDALEelgLAD---DTLVIFTSDHGDALGAHRLWDKGP---FMYEETYRIPLIIKW-PGVIAAGQVV 293
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
420-486 |
2.40e-03 |
|
sulfatase; 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: 293746 [Multi-domain] Cd Length: 236 Bit Score: 39.73 E-value: 2.40e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 756832308 420 IRYTDFVIAEMIAKLKTYEDKYNTALLYVSDHGESLGAMGLYL-HGTPYkfapDDQTRVPMqVWMSPG 486
Cdd:cd16022 137 VSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLRGkKGSLY----EGGIRVPF-IVRWPG 199
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
411-478 |
9.68e-03 |
|
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: 293769 [Multi-domain] Cd Length: 423 Bit Score: 38.37 E-value: 9.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 756832308 411 ELTNTYDNTIRYTDFVIAEMIAKLKTYEDKYNTALLYVSDHGESLGAMGLyLHGTPYKFApDDQTRVP 478
Cdd:cd16150 197 ELRATYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHGDYTGDYGL-VEKWPNTFE-DCLTRVP 262
|
|
| |
