|
Name |
Accession |
Description |
Interval |
E-value |
| OpgE |
COG2194 |
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall ... |
5-547 |
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: 735.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 5 LLSFKLNPVQRTWAAAFFFTTIGNIALWQTLWINVDVHNiHNLLFFASLPIFLFCFLSILLTPVMViPYLCRPLLVVLIL 84
Cdd:COG2194 2 FLLPRLSPLKLILLLALYFALFLNLPFWGRLLAILPLDG-VNLLFLLSLPLLLLAALNLLLSLLAW-RYLFKPLLILLLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 85 ISACCSYFMMKYNILIDRSMVQNFFETNQAELTSYLSVPFLSTLFLLGIVPAIILALPSTdNKRGAFRIELWWLAHICIA 164
Cdd:COG2194 80 ISAAASYFMDFYGVVIDYGMIQNVLETDPAEASELLSPKLILWLLLLGVLPALLLWRVRI-RYRPLLRELGQRLALLLLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 165 VVLLAMVTMVFYKDYASLIRNNMQIKDQALPFNFVRNTNGYLKRKYQASSTILQSVGEDAVRPiYSNAPPKLVVVVVGET 244
Cdd:COG2194 159 LLVIVLLALLFYKDYASFFRNHKELRYLINPSNFIYALGKYAKARYFAAPLPLQPLGADAKLA-AAGAKPTLVVLVVGET 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 245 ARAQNFQLNGYSRVTNPYLSRRHDVISFKNVSSCGTATAISLPCMFSRMSRNEYNEVRAASEENLLDILKRTGVEVLWRN 324
Cdd:COG2194 238 ARADNFSLNGYARDTTPELAKEKNLVSFRDVTSCGTATAVSVPCMFSRLGRADYDPQRALNQENLLDVLQRAGVKVLWRD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 325 NNnGGCKGICKRVPTDDMPAMKVIGECvnKDGTCFDEVLLNQLSSRINAMQGDALIVLHQMGSHGPTYFERYPSTSKVFS 404
Cdd:COG2194 318 NQ-SGCKGVCDRVPTIDLTADNLPPLC--DGGECLDEVLLDGLDEALADLAGDKLIVLHQMGSHGPAYYKRYPPEFRKFT 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 405 PTCDSNLIEKCSNKELVNTYDNTLVYTDRMLSKTIELLQRYSGMRDVAMIYLSDHGESLGESGIYLHGTPYIIAPNEQTH 484
Cdd:COG2194 395 PTCDTNDLQNCSREELVNAYDNTILYTDYVLSQVIDLLKAKQDRYDTAMLYVSDHGESLGENGLYLHGTPYAIAPDEQTH 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1787232029 485 IPMFMWFSSSFAQHSKLNLECLTGNADKQYSHDNFYHSILGLFNVKTSVYKPELDMFTLCRQS 547
Cdd:COG2194 475 VPMIMWLSDGYAQRYGIDFACLKARADKPYSHDNLFHTLLGLLDVRTSVYDPELDILAPCRRA 537
|
|
| PRK11598 |
PRK11598 |
putative metal dependent hydrolase; Provisional |
18-547 |
0e+00 |
|
putative metal dependent hydrolase; Provisional
Pssm-ID: 183224 [Multi-domain] Cd Length: 545 Bit Score: 640.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 18 AAAFFFTTIGNIALWQTLWINVDVHNIHNLLFFASLPIFLFCFLSILLTpVMVIPYLCRPLLVVLILISACCSYFMMKYN 97
Cdd:PRK11598 18 LAAFYITLCLNIAFYKQVLQLLPLDSLHNVLVFASMPVVAFSVINIVFT-LLSFPWLRRPLACLFILVGAAAQYFMMTYG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 98 ILIDRSMVQNFFETNQAELTSYLSVPFLSTLFLLGIVPAIILALPSTDNKRGAFRIELWWLAHICIAVVLLAMVTMVFYK 177
Cdd:PRK11598 97 IVIDRSMIQNIFETTPAESFALMTPQMLLWLGLSGVLPALIACWIKIRPATPRWRSVLFRLANILVSVLLILLVAALFYK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 178 DYASLIRNNMQIKDQALPFNFVRNTNGYLKRKYQASSTILQsVGEDAVR-PIYSNAPPK-LVVVVVGETARAQNFQLNGY 255
Cdd:PRK11598 177 DYASLFRNNKELVKSLTPSNSIVASWSWYSHQRLANLPLVR-IGEDAHKnPLMQNQKRKnLTILVVGETSRAENFSLGGY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 256 SRVTNPYLsRRHDVISFKNVSSCGTATAISLPCMFSRMSRNEYNEVRAASEENLLDILKRTGVEVLWRNNNnGGCKGICK 335
Cdd:PRK11598 256 PRETNPRL-AKDNVIYFPHTTSCGTATAVSVPCMFSNMPRKHYDEELAHHQEGLLDIIQRAGINVLWNDND-GGCKGACD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 336 RVPTDDMPAMKVIGECvnKDGTCFDEVLLNQLSSRINAMQGDALIVLHQMGSHGPTYFERYPSTSKVFSPTCDSNLIEKC 415
Cdd:PRK11598 334 RVPHQDVTALNLPGQC--IDGECYDEVLFHGLENYINNLQGDGVIVLHTIGSHGPTYYNRYPPQFRKFTPTCDTNEIQTC 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 416 SNKELVNTYDNTLVYTDRMLSKTIELLQRYSGMRDVAMIYLSDHGESLGESGIYLHGTPYIIAPNEQTHIPMFMWFSSSF 495
Cdd:PRK11598 412 TQQQLVNTYDNTILYVDYIVDKAINLLKQHQDKFNTSLVYLSDHGESLGENGIYLHGLPYAIAPDQQTHVPMLLWLSPDY 491
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1787232029 496 AQHSKLNLECLTGNADKQ-YSHDNFYHSILGLFNVKTSVYKPELDMFTLCRQS 547
Cdd:PRK11598 492 QKRYGVDQQCLQKQAQTQdYSQDNLFSTLLGLTGVQTKEYQAADDILQPCRRL 544
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
234-530 |
8.55e-126 |
|
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: 370.42 E-value: 8.55e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 234 PKLVVVVVGETARAQNFQLNGYSRVTNPYLSRR-HDVISFKNVSSCGTATAISLPCMFSRMSRNEYNevRAASEENLLDI 312
Cdd:cd16017 2 PKNVVLVIGESARRDHMSLYGYPRDTTPFLSKLkKNLIVFDNVISCGTSTAVSLPCMLSFANRENYD--RAYYQENLIDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 313 LKRTGVEVLWRNNNnGGCKGICKRVPTDDMPAMKVIGECVNKDGTCFDEVLLNQLSSRINAMQGDALIVLHQMGSHGPtY 392
Cdd:cd16017 80 AKKAGYKTYWISNQ-GGCGGYDTRISAIAKIETVFTNKGSCNSSNCYDEALLPLLDEALADSSKKKLIVLHLMGSHGP-Y 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 393 FERYPSTSKVFSPTCDsNLIEKCSNKELVNTYDNTLVYTDRMLSKTIELLQRYSgmRDVAMIYLSDHGESLGESGIYLHG 472
Cdd:cd16017 158 YDRYPEEFAKFTPDCD-NELQSCSKEELINAYDNSILYTDYVLSQIIERLKKKD--KDAALIYFSDHGESLGENGLYLHG 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1787232029 473 TPYiiAPNEQTHIPMFMWFSSSFAQhsKLNLECLTGNADKQYSHDNFYHSILGLFNVK 530
Cdd:cd16017 235 APY--APKEQYHVPFIIWSSDSYKQ--RYPVERLRANKDRPFSHDNLFHTLLGLLGIK 288
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
235-529 |
1.11e-68 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 223.84 E-value: 1.11e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 235 KLVVVVVGETARAQNFQLNGYSRVTNPYLSR-RHDVISFKNVSSCGTATAISLPCMFSRMSRNEYNEV------RAASEE 307
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRlAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYvstpvgLPRTEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 308 NLLDILKRTGVEV--------LWRNNN---NGGCKGICKRVPTDDMPAMKVIGECVNKDGTCFDEVLLNQLSSRINAMQG 376
Cdd:pfam00884 81 SLPDLLKRAGYNTgaigkwhlGWYNNQspcNLGFDKFFGRNTGSDLYADPPDVPYNCSGGGVSDEALLDEALEFLDNNDK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 377 DALIVLHQMGSHGP-TYFERYPSTSKVFSPtcdsnliEKCSNKELVNTYDNTLVYTDRMLSKTIELLQRYSGMRDVAMIY 455
Cdd:pfam00884 161 PFFLVLHTLGSHGPpYYPDRYPEKYATFKP-------SSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVY 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1787232029 456 LSDHGESLGESGIYLHGTPYIIAPNEQTHIPMFMWFSSSFAQHSKlnlecltgnADKQYSHDNFYHSILGLFNV 529
Cdd:pfam00884 234 TSDHGESLGEGGGYLHGGKYDNAPEGGYRVPLLIWSPGGKAKGQK---------SEALVSHVDLFPTILDLAGI 298
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| OpgE |
COG2194 |
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall ... |
5-547 |
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: 735.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 5 LLSFKLNPVQRTWAAAFFFTTIGNIALWQTLWINVDVHNiHNLLFFASLPIFLFCFLSILLTPVMViPYLCRPLLVVLIL 84
Cdd:COG2194 2 FLLPRLSPLKLILLLALYFALFLNLPFWGRLLAILPLDG-VNLLFLLSLPLLLLAALNLLLSLLAW-RYLFKPLLILLLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 85 ISACCSYFMMKYNILIDRSMVQNFFETNQAELTSYLSVPFLSTLFLLGIVPAIILALPSTdNKRGAFRIELWWLAHICIA 164
Cdd:COG2194 80 ISAAASYFMDFYGVVIDYGMIQNVLETDPAEASELLSPKLILWLLLLGVLPALLLWRVRI-RYRPLLRELGQRLALLLLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 165 VVLLAMVTMVFYKDYASLIRNNMQIKDQALPFNFVRNTNGYLKRKYQASSTILQSVGEDAVRPiYSNAPPKLVVVVVGET 244
Cdd:COG2194 159 LLVIVLLALLFYKDYASFFRNHKELRYLINPSNFIYALGKYAKARYFAAPLPLQPLGADAKLA-AAGAKPTLVVLVVGET 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 245 ARAQNFQLNGYSRVTNPYLSRRHDVISFKNVSSCGTATAISLPCMFSRMSRNEYNEVRAASEENLLDILKRTGVEVLWRN 324
Cdd:COG2194 238 ARADNFSLNGYARDTTPELAKEKNLVSFRDVTSCGTATAVSVPCMFSRLGRADYDPQRALNQENLLDVLQRAGVKVLWRD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 325 NNnGGCKGICKRVPTDDMPAMKVIGECvnKDGTCFDEVLLNQLSSRINAMQGDALIVLHQMGSHGPTYFERYPSTSKVFS 404
Cdd:COG2194 318 NQ-SGCKGVCDRVPTIDLTADNLPPLC--DGGECLDEVLLDGLDEALADLAGDKLIVLHQMGSHGPAYYKRYPPEFRKFT 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 405 PTCDSNLIEKCSNKELVNTYDNTLVYTDRMLSKTIELLQRYSGMRDVAMIYLSDHGESLGESGIYLHGTPYIIAPNEQTH 484
Cdd:COG2194 395 PTCDTNDLQNCSREELVNAYDNTILYTDYVLSQVIDLLKAKQDRYDTAMLYVSDHGESLGENGLYLHGTPYAIAPDEQTH 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1787232029 485 IPMFMWFSSSFAQHSKLNLECLTGNADKQYSHDNFYHSILGLFNVKTSVYKPELDMFTLCRQS 547
Cdd:COG2194 475 VPMIMWLSDGYAQRYGIDFACLKARADKPYSHDNLFHTLLGLLDVRTSVYDPELDILAPCRRA 537
|
|
| PRK11598 |
PRK11598 |
putative metal dependent hydrolase; Provisional |
18-547 |
0e+00 |
|
putative metal dependent hydrolase; Provisional
Pssm-ID: 183224 [Multi-domain] Cd Length: 545 Bit Score: 640.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 18 AAAFFFTTIGNIALWQTLWINVDVHNIHNLLFFASLPIFLFCFLSILLTpVMVIPYLCRPLLVVLILISACCSYFMMKYN 97
Cdd:PRK11598 18 LAAFYITLCLNIAFYKQVLQLLPLDSLHNVLVFASMPVVAFSVINIVFT-LLSFPWLRRPLACLFILVGAAAQYFMMTYG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 98 ILIDRSMVQNFFETNQAELTSYLSVPFLSTLFLLGIVPAIILALPSTDNKRGAFRIELWWLAHICIAVVLLAMVTMVFYK 177
Cdd:PRK11598 97 IVIDRSMIQNIFETTPAESFALMTPQMLLWLGLSGVLPALIACWIKIRPATPRWRSVLFRLANILVSVLLILLVAALFYK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 178 DYASLIRNNMQIKDQALPFNFVRNTNGYLKRKYQASSTILQsVGEDAVR-PIYSNAPPK-LVVVVVGETARAQNFQLNGY 255
Cdd:PRK11598 177 DYASLFRNNKELVKSLTPSNSIVASWSWYSHQRLANLPLVR-IGEDAHKnPLMQNQKRKnLTILVVGETSRAENFSLGGY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 256 SRVTNPYLsRRHDVISFKNVSSCGTATAISLPCMFSRMSRNEYNEVRAASEENLLDILKRTGVEVLWRNNNnGGCKGICK 335
Cdd:PRK11598 256 PRETNPRL-AKDNVIYFPHTTSCGTATAVSVPCMFSNMPRKHYDEELAHHQEGLLDIIQRAGINVLWNDND-GGCKGACD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 336 RVPTDDMPAMKVIGECvnKDGTCFDEVLLNQLSSRINAMQGDALIVLHQMGSHGPTYFERYPSTSKVFSPTCDSNLIEKC 415
Cdd:PRK11598 334 RVPHQDVTALNLPGQC--IDGECYDEVLFHGLENYINNLQGDGVIVLHTIGSHGPTYYNRYPPQFRKFTPTCDTNEIQTC 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 416 SNKELVNTYDNTLVYTDRMLSKTIELLQRYSGMRDVAMIYLSDHGESLGESGIYLHGTPYIIAPNEQTHIPMFMWFSSSF 495
Cdd:PRK11598 412 TQQQLVNTYDNTILYVDYIVDKAINLLKQHQDKFNTSLVYLSDHGESLGENGIYLHGLPYAIAPDQQTHVPMLLWLSPDY 491
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1787232029 496 AQHSKLNLECLTGNADKQ-YSHDNFYHSILGLFNVKTSVYKPELDMFTLCRQS 547
Cdd:PRK11598 492 QKRYGVDQQCLQKQAQTQdYSQDNLFSTLLGLTGVQTKEYQAADDILQPCRRL 544
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
234-530 |
8.55e-126 |
|
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: 370.42 E-value: 8.55e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 234 PKLVVVVVGETARAQNFQLNGYSRVTNPYLSRR-HDVISFKNVSSCGTATAISLPCMFSRMSRNEYNevRAASEENLLDI 312
Cdd:cd16017 2 PKNVVLVIGESARRDHMSLYGYPRDTTPFLSKLkKNLIVFDNVISCGTSTAVSLPCMLSFANRENYD--RAYYQENLIDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 313 LKRTGVEVLWRNNNnGGCKGICKRVPTDDMPAMKVIGECVNKDGTCFDEVLLNQLSSRINAMQGDALIVLHQMGSHGPtY 392
Cdd:cd16017 80 AKKAGYKTYWISNQ-GGCGGYDTRISAIAKIETVFTNKGSCNSSNCYDEALLPLLDEALADSSKKKLIVLHLMGSHGP-Y 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 393 FERYPSTSKVFSPTCDsNLIEKCSNKELVNTYDNTLVYTDRMLSKTIELLQRYSgmRDVAMIYLSDHGESLGESGIYLHG 472
Cdd:cd16017 158 YDRYPEEFAKFTPDCD-NELQSCSKEELINAYDNSILYTDYVLSQIIERLKKKD--KDAALIYFSDHGESLGENGLYLHG 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1787232029 473 TPYiiAPNEQTHIPMFMWFSSSFAQhsKLNLECLTGNADKQYSHDNFYHSILGLFNVK 530
Cdd:cd16017 235 APY--APKEQYHVPFIIWSSDSYKQ--RYPVERLRANKDRPFSHDNLFHTLLGLLGIK 288
|
|
| PRK09598 |
PRK09598 |
phosphoethanolamine--lipid A transferase EptA; |
41-541 |
5.20e-103 |
|
phosphoethanolamine--lipid A transferase EptA;
Pssm-ID: 236581 [Multi-domain] Cd Length: 522 Bit Score: 320.57 E-value: 5.20e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 41 VHNIHNLLFFASLPIFLFC--FLSILLTpVMVIPYLCRPLLVVLILISACCSYFMMKYNILIDRSMVQNFFETNQAELTS 118
Cdd:PRK09598 39 YKESNQVSFIAMLVVLLFCvnGLLFLLL-GLLSRRLMRLSAIVFSLLNSIAFYFINTYKVFLNKSMMGNVLNTNTAESSG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 119 YLSVPFLSTLFLLGIVPAIIL---ALPSTDNKRgafrielwwLAHICIAVVLlAMVTMVFY--KDYASLIRNNMQIKDQA 193
Cdd:PRK09598 118 FLSVKLFIYIVVLGVLPGYIIykiPLKNSSKKA---------PFAAILALVL-IFLASAFAnsKNWLWFDKHAKFLGGLI 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 194 LPFNFVRNTNGYLKRKYQASStiLQSVGEDAVRPIYSNAppkLVVVVVGETARAQNFQLNGYSRVTNPYLSRRHD--VIS 271
Cdd:PRK09598 188 LPWSYSVNTFRVSAHKFFAPT--IKPLLPPLFSPNHSKS---VVVLVIGESARKHNYALYGYEKPTNPRLSKRLAthELT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 272 FKNVSSCGTATAISLPCMFSRMSRNEYNevraaSEENLLDILKRTGVEVLWRNNNNGGckgicKRVP-TDDMPAMKVIGE 350
Cdd:PRK09598 263 LFNATSCATYTTASLECILDSSFKNTSN-----AYENLPTYLTRAGIKVFWRSANDGE-----PNVKvTSYLKNYELIQK 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 351 CVNKDGTcFDEVLLNQLSSRINAMQGD-ALIVLHQMGSHGPTYFERYPSTSKVFSPTCDSNLIEKCSNKELVNTYDNTLV 429
Cdd:PRK09598 333 CPNCEAP-YDESLLYNLPELIKASSNEnVLLILHLAGSHGPNYDNKYPLNFRVFKPVCSSVELSSCSKESLINAYDNTIF 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 430 YTDRMLSKTIELLQrySGMRDVAMIYLSDHGESLGESGIYLHGTPYIIAPNEQTHIPMFMWFSSSFA-QHSKLnlecltg 508
Cdd:PRK09598 412 YNDYLLDKIISMLK--NLKQPALMIYLSDHGESLGEGAFYLHGIPKSIAPKEQYEIPFIVWASDSFKkQHSII------- 482
|
490 500 510
....*....|....*....|....*....|....*
gi 1787232029 509 NADKQYSHDNFYHSILGLFNVKT--SVYKPELDMF 541
Cdd:PRK09598 483 QTQTPINQNVIFHSVLGVFDFKNpsAVYRPSLDLF 517
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
235-529 |
1.11e-68 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 223.84 E-value: 1.11e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 235 KLVVVVVGETARAQNFQLNGYSRVTNPYLSR-RHDVISFKNVSSCGTATAISLPCMFSRMSRNEYNEV------RAASEE 307
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRlAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYvstpvgLPRTEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 308 NLLDILKRTGVEV--------LWRNNN---NGGCKGICKRVPTDDMPAMKVIGECVNKDGTCFDEVLLNQLSSRINAMQG 376
Cdd:pfam00884 81 SLPDLLKRAGYNTgaigkwhlGWYNNQspcNLGFDKFFGRNTGSDLYADPPDVPYNCSGGGVSDEALLDEALEFLDNNDK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 377 DALIVLHQMGSHGP-TYFERYPSTSKVFSPtcdsnliEKCSNKELVNTYDNTLVYTDRMLSKTIELLQRYSGMRDVAMIY 455
Cdd:pfam00884 161 PFFLVLHTLGSHGPpYYPDRYPEKYATFKP-------SSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVY 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1787232029 456 LSDHGESLGESGIYLHGTPYIIAPNEQTHIPMFMWFSSSFAQHSKlnlecltgnADKQYSHDNFYHSILGLFNV 529
Cdd:pfam00884 234 TSDHGESLGEGGGYLHGGKYDNAPEGGYRVPLLIWSPGGKAKGQK---------SEALVSHVDLFPTILDLAGI 298
|
|
| PRK11560 |
PRK11560 |
kdo(2)-lipid A phosphoethanolamine 7''-transferase; |
76-525 |
3.62e-46 |
|
kdo(2)-lipid A phosphoethanolamine 7''-transferase;
Pssm-ID: 183198 [Multi-domain] Cd Length: 558 Bit Score: 170.61 E-value: 3.62e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 76 RPLLVVLILISACCSYFMMKYNILIDRSMVQNFFETN---QAELTSYlsvPFLSTLFLLGIVPaiiLALPSTDNKRGAFR 152
Cdd:PRK11560 75 RVLASLLVLFSAAASYYMTFFNVVIGYGIIASVMTTDidlSKEVVGL---HFILWLVAVSALP---LILIWNNRCRYTLL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 153 IELWWLAH-ICIAVVLLAMVTMVFY-------KDYASLIRNNMQIKDQA-------LPFNFVRNTNGYLKRKYQASSTIl 217
Cdd:PRK11560 149 RQLRTPGQrIRSLAVVVLAGLLVWApirlldiQQKKVERATGVDLPSYGgvvansyLPSNWLSALGLYAWAQVDESSDN- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 218 QSVGEDAVRPIYSnAPPKL----VVVVVGETARAQNFQLNGYSRVTNPYLSRRHDVISFKNvSSCGTATAISLPCMFSRM 293
Cdd:PRK11560 228 NSLLNPAKKFTYQ-APKGVddtyVVFIIGETTRWDHMGILGYERNTTPKLAQEKNLAAFRG-YSCDTATKLSLRCMFVRE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 294 SRNEYNEVRAASEENLLDILKRTGV---------EVLWRNNNNggckgickrvpTDDMPAMKVIGECVNKDGTCFDEVLL 364
Cdd:PRK11560 306 GGAEDNPQRTLKEQNVFAVLKQLGFsselfamqsEMWFYNNTM-----------ADNYAYREQIGAEPRNRGKPVDDMLL 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 365 -NQLSSRI-NAMQGDALIVLHQMGSHgPTYFERYPSTSKVFSPTCdSNLIEKCSNKELVNTYDNTLVYTDRMLSKTIELL 442
Cdd:PRK11560 375 vDEMKQSLgRNPDGKHLIILHTKGSH-YNYTQRYPRSFARYQPEC-IGVDSGCSKAQLINSYDNSVLYVDHFISSVIDQL 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 443 qrysgmRDVAMI--YLSDHGESLGESGiYLHGTPYIIAPNEQTHIPMFMWFSSSF---AQHSKLnLECLTGNAD--KQYS 515
Cdd:PRK11560 453 ------RDKKAIvfYAADHGESINERE-HLHGTPREMAPPEQFRVPMMVWMSDKYlanPDNAQA-FAQLKKQADmkVPRR 524
|
490
....*....|
gi 1787232029 516 HDNFYHSILG 525
Cdd:PRK11560 525 HVELFDTILG 534
|
|
| EptA_B_N |
pfam08019 |
Phosphoethanolamine transferase EptA/EptB; This entry represents a domain found in a group of ... |
57-209 |
2.42e-40 |
|
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: 143.43 E-value: 2.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 57 LFCFLSILLTPVmVIPYLCRPLLVVLILISACCSYFMMKYNILIDRSMVQNFFETNQAELTSYLSVPFLSTLFLLGIVPA 136
Cdd:pfam08019 1 LFAALNLLLSLL-SWRYLLKPLLILLLLLSAAASYFMDTYGVVIDRDMIQNVLETDVAEASDLLSPKLLLYLLLLGVLPA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1787232029 137 IILALPSTdNKRGAFRIELWWLAHICIAVVLLAMVTMVFYKDYASLIRNNMQIKDQALPFNFVRNTNGYLKRK 209
Cdd:pfam08019 80 LLLWRVRI-RYRPWLRELLSRLALILVSLLVIGLVAFLFYKDYASFFRNHKELRYLINPTNYIYSTVKYAKHQ 151
|
|
| PRK10649 |
PRK10649 |
phosphoethanolamine transferase CptA; |
17-522 |
1.45e-21 |
|
phosphoethanolamine transferase CptA;
Pssm-ID: 182617 [Multi-domain] Cd Length: 577 Bit Score: 98.62 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 17 WAAAFF--FTTIGNIALWQTLWINVDvhNIHNLLFFASLpiflfcflsiLLTPVMVIPYLCRPL----LVVLILIS-ACC 89
Cdd:PRK10649 19 WALLFFwfFSTLLQAIIYISGYSGTN--GFRDALLFSSL----------WLIPVFLFPRRIRIIaaviGVVLWAASlAAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 90 SYFMMkYNILIDRSMVQNFFETNQAELTSYLSVPFLSTLFLLGIVPAIILALPSTdnKRGAFRIELWWLAHICIAVvLLA 169
Cdd:PRK10649 87 CYYVI-YGQEFSQSVLFVMFETNTNEASEYLSQYFSLKIVLIALAYTAVAVLLWT--RLRPVYIPWPWRYVVSFAL-LYG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 170 MVTMVFYKDyaSLIRN--------NMQIK-DQALPFNFVrntNGYlkRKYQASSTILQS-VGEDAVRPIYSN------AP 233
Cdd:PRK10649 163 LILHPIAMN--TFIKHkpfektldKLASRmEPAAPWQFL---TGY--YQYRQQLNSLQKlLNENAALPPLANlkdesgNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 234 PKLVVVVVGETARAQNFQLNGYSRVTNPYLSRRHDVIS----FKNVSSCGTATAISLP--CMFSrmsrNEYNEVRAASEE 307
Cdd:PRK10649 236 PRTLVLVIGESTQRGRMSLYGYPRETTPELDALHKTDPgltvFNNVVTSRPYTIEILQqaLTFA----DEKNPDLYLTQP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 308 NLLDILKRTGVEVLWRNNNnggcKGICKR-----VPTDDMPAMKVIGECVNKDGTCFDEVLLNQLSSrinAMQGDA---L 379
Cdd:PRK10649 312 SLMNMMKQAGYKTFWITNQ----QTMTARntmltVFSRQTDKQYYMNQQRTQNAREYDTNVLKPFSE---VLADPApkkF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 380 IVLHQMGSHgPTYFERYPSTSKVFSPTCDsNLIEKCSNKEL--VNTYDNTLVYTDRMLSktiELLQRYSGMRDVAM-IYL 456
Cdd:PRK10649 385 IIVHLLGTH-IKYKYRYPENQGKFDDRTG-HVPPGLNADELesYNDYDNANLYNDHVVA---SLIKDFKATDPNGFlVYF 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1787232029 457 SDHGESlgesgIYLHGTPYIIAPNEQT------HIPMFMWFSSSF-AQHSKlnleCLTGNADKQYSHDNFYHS 522
Cdd:PRK10649 460 SDHGEE-----VYDTPPHKTQGRNEDNptrhmyTIPFLLWTSEKWqAAHPR----DFSQDVDRKYSLAELIHT 523
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
20-534 |
1.18e-13 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 73.53 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 20 AFFFTTIGNIALWQTLWINVDVHNIHNLLFFaslpIFLFCFLSILLTPVMVIPYLCRPLLVVLILISACCSYFMMKYNIL 99
Cdd:COG1368 16 LLFNFDLSLGEILQAFLYGLRFILYLLLLLL----LLLLLLLPLLFRRPKLRWIYLLLVLLLLLLLLVADILYYRFFGDR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 100 IDRSMVQNFFETnqAELTSYLSVPFLSTLFLLGIVPAIILALPSTDNKRGAFRIELWWLAHICIAVVLLAMVTMVFYKDY 179
Cdd:COG1368 92 LNFSDLDYLGDT--GEVLGSLLSSYDLLLLLDLLLLLLLLLLLYRLLKKLRKSLPWRKRLALLLLLLALLLLGIRLGEDR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 180 ASLIR----NNMQIKDQAL--PFNFVRNTNGYLKRKYQASSTILQ----SVGEDAVRPIYSNAPPKLVVVVVGETARAQN 249
Cdd:COG1368 170 PLNLSdafsRNNFVNELGLngPYSFYDALRNNKAPATYSEEEALEikkyLKSNRPTPNPFGPAKKPNVVVILLESFSDFF 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 250 FQLNGYSRVTNPYLSR-RHDVISFKNVSSCGTATAISLPCM------------FSRMSRNEYNevraaseeNLLDILKRT 316
Cdd:COG1368 250 IGALGNGKDVTPFLDSlAKESLYFGNFYSQGGRTSRGEFAVltglpplpggspYKRPGQNNFP--------SLPSILKKQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 317 GVEVL--------WRN-----NNNGGCKGICKrvptDDMPAMKVIGECVNkdgtcfDEVLLNQLSSRINAMQGDALIVLH 383
Cdd:COG1368 322 GYETSffhggdgsFWNrdsfyKNLGFDEFYDR----EDFDDPFDGGWGVS------DEDLFDKALEELEKLKKPFFAFLI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 384 QMGSHGPtyFErYPSTSKVFSPTcdsnliekcsNKELVNTYDNTLVYTDRMLSKTIELLQRYSGMRDVAMIYLSDHGESL 463
Cdd:COG1368 392 TLSNHGP--YT-LPEEDKKIPDY----------GKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGPRS 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1787232029 464 GESGIYLHgtpyiiaPNEQTHIPMFMWFSSSFAqhsklnleclTGNADKQYSHDNFYHSILGLFNVKTSVY 534
Cdd:COG1368 459 PGKTDYEN-------PLERYRVPLLIYSPGLKK----------PKVIDTVGSQIDIAPTLLDLLGIDYPSY 512
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
424-491 |
1.28e-10 |
|
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: 62.18 E-value: 1.28e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 424 YDNTLVYTDRMLSKTIELLQRYSGMRDVAMIYLSDHGESLGESGIYL--HGTPYiiapNEQTHIPMFMWF 491
Cdd:cd16148 165 YDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGLYWghGSNLY----DEQLHVPLIIRW 230
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
235-503 |
5.00e-06 |
|
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: 48.19 E-value: 5.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 235 KLVVVVVGETARAQNFQLNGYSRVTNPYLSRRHDVISFKNVSSC--GTATAISLPCMFsrMSRNEYN------------- 299
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFNFRSVspPTSSAPNHAALL--TGAYPTLhgytgngsadpel 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 300 EVRAASEE----NLLDILKRTGVEVLWrnnnnggckgickrVPTDDMpamkvigecvnkdgtcFDEVLLNQlssrinamq 375
Cdd:cd00016 79 PSRAAGKDedgpTIPELLKQAGYRTGV--------------IGLLKA----------------IDETSKEK--------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 376 gDALIVLHQMGSHGPTYferypstskvfsptcdsnliekcSNKELVNTYDNTLVYTDRMLSKTIELLQRYSGMRDVAMIY 455
Cdd:cd00016 120 -PFVLFLHFDGPDGPGH-----------------------AYGPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIV 175
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1787232029 456 LSDHGESLGESGIYLHGTPYIIAPNEQTHIPMFMWFSSSFAQHSKLNL 503
Cdd:cd00016 176 TADHGGIDKGHGGDPKADGKADKSHTGMRVPFIAYGPGVKKGGVKHEL 223
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
430-490 |
4.45e-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: 45.61 E-value: 4.45e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1787232029 430 YTDRMLSKTIELLQRYSGMRDVAMIYLSDHGESLGESGIYLHGTPYiiapNEQTHIPMFMW 490
Cdd:cd16037 170 FLDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGERGLWGKSTMY----EESVRVPMIIS 226
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
360-490 |
1.70e-04 |
|
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: 43.83 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 360 DEVLLNQLSSRINAMQGD-ALIVLHQMGSHGPtyferYPSTSKVFSptcdsNLIEKCSNKELVNTYDNTLVYTDRMLSKT 438
Cdd:cd16015 139 DESLFDQALEELEELKKKpFFIFLVTMSNHGP-----YDLPEEKKD-----EPLKVEEDKTELENYLNAIHYTDKALGEF 208
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1787232029 439 IELLQRYSGMRDVAMIYLSDHGeslgeSGIYLHGTPYIIAPNEQTHIPMFMW 490
Cdd:cd16015 209 IEKLKKSGLYENTIIVIYGDHL-----PSLGSDYDETDEDPLDLYRTPLLIY 255
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
388-490 |
2.92e-04 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 43.33 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 388 HGPT-----YFERYPSTSKVFSPTCDSNLIEKCSNKELVNTYDNTLVYTDRMLSKTIELLQRySGMRD---VamIYLSDH 459
Cdd:COG3119 161 HAPYqapeeYLDKYDGKDIPLPPNLAPRDLTEEELRRARAAYAAMIEEVDDQVGRLLDALEE-LGLADntiV--VFTSDN 237
|
90 100 110
....*....|....*....|....*....|...
gi 1787232029 460 GESLGESGIYLH-GTPYiiapnEQ-THIPMFMW 490
Cdd:COG3119 238 GPSLGEHGLRGGkGTLY-----EGgIRVPLIVR 265
|
|
| FUSC |
pfam04632 |
Fusaric acid resistance protein family; This family includes a conserved region found in two ... |
62-175 |
2.21e-03 |
|
Fusaric acid resistance protein family; This family includes a conserved region found in two proteins associated with fusaric acid resistance, from Burkholderia cepacia and Klebsiella oxytoca. These proteins are likely to be membrane transporter proteins.
Pssm-ID: 428044 [Multi-domain] Cd Length: 655 Bit Score: 40.73 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787232029 62 SILLTPVMV-IPYLcrpLLVVLILISACCSYFMmkynilidrSMVQNFFetnqaeltSYLsvpflstlFLL-GIVPAIIl 139
Cdd:pfam04632 62 AVLLVALFVqAPLL---FLLALALWIGLCLALS---------LLDRNFR--------SYA--------FVLaGYTAAII- 112
|
90 100 110
....*....|....*....|....*....|....*.
gi 1787232029 140 ALPSTDNKRGAFRIELWWLAHICIAVVLLAMVTMVF 175
Cdd:pfam04632 113 GLPAVADPEAIFDIAVARVSEISLGILCAALVSALV 148
|
|
| |
