|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11598 |
PRK11598 |
putative metal dependent hydrolase; Provisional |
1-545 |
0e+00 |
|
putative metal dependent hydrolase; Provisional
Pssm-ID: 183224 [Multi-domain] Cd Length: 545 Bit Score: 1058.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 1 MWLRQRLRCNSLGFTLATALFFTLFQNALFLHRAWSYITFDSVHSVIFAASMPVVIFCALNIIFSVLTVPYLRKPLIIFF 80
Cdd:PRK11598 2 KRLLKRPSLNLLTFLLLAAFYITLCLNIAFYKQVLQLLPLDSLHNVLVFASMPVVAFSVINIVFTLLSFPWLRRPLACLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 81 LLGSAAANYFMFSYGVVIDGNMMQNAFETNPQEATALLTPRMGLWLALLGILPAVAVCFTQIRQTRPWWYMVGLRAANVM 160
Cdd:PRK11598 82 ILVGAAAQYFMMTYGIVIDRSMIQNIFETTPAESFALMTPQMLLWLGLSGVLPALIACWIKIRPATPRWRSVLFRLANIL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 161 LSLAVILIVAALFYKDYASLIRNNKSVVKMLTPSNFVAGTIKFTEQRYFtRNLPLVKIGEDARKGPLIAGQAKKTLVILV 240
Cdd:PRK11598 162 VSVLLILLVAALFYKDYASLFRNNKELVKSLTPSNSIVASWSWYSHQRL-ANLPLVRIGEDAHKNPLMQNQKRKNLTILV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 241 VGETARAENFSLGGYQRETNPRLKQDDVIYFKNASSCGTETAISVPCMFSNMPRKEYDATQATHQEGMLDVLAHAGVSVL 320
Cdd:PRK11598 241 VGETSRAENFSLGGYPRETNPRLAKDNVIYFPHTTSCGTATAVSVPCMFSNMPRKHYDEELAHHQEGLLDIIQRAGINVL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 321 WRDNDGGCKGACDRVPHIDMTKLKLPQDCDGEVCMDNALLYKLNDYINGLKDDGVIVLHQMGSHGPAYYRRSTPEFQTFS 400
Cdd:PRK11598 321 WNDNDGGCKGACDRVPHQDVTALNLPGQCIDGECYDEVLFHGLENYINNLQGDGVIVLHTIGSHGPTYYNRYPPQFRKFT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 401 PTCNSNQIQDCSHEQLVNTYDNSILYTDAMLDATIKLLRQYDDRFNTALVYLSDHGESLGENGMYLHGTPYVFAPSQQTH 480
Cdd:PRK11598 401 PTCDTNEIQTCTQQQLVNTYDNTILYVDYIVDKAINLLKQHQDKFNTSLVYLSDHGESLGENGIYLHGLPYAIAPDQQTH 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727193019 481 VPFLMWMSADYQRNFGVDRQCLNALAEKDDVSQDNLFHTLLGMLNVQSREYQSRLDILQPCRNAA 545
Cdd:PRK11598 481 VPMLLWLSPDYQKRYGVDQQCLQKQAQTQDYSQDNLFSTLLGLTGVQTKEYQAADDILQPCRRLS 545
|
|
| OpgE |
COG2194 |
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall ... |
6-544 |
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: 832.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 6 RLRCNSLGFTLATALFFTLFQNALFLHRAWSYITFDSvHSVIFAASMPVVIFCALNIIFSVLTVPYLRKPLIIFFLLGSA 85
Cdd:COG2194 4 LPRLSPLKLILLLALYFALFLNLPFWGRLLAILPLDG-VNLLFLLSLPLLLLAALNLLLSLLAWRYLFKPLLILLLLISA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 86 AANYFMFSYGVVIDGNMMQNAFETNPQEATALLTPRMGLWLALLGILPAVAVCFTQIRQtRPWWYMVGLRAANVMLSLAV 165
Cdd:COG2194 83 AASYFMDFYGVVIDYGMIQNVLETDPAEASELLSPKLILWLLLLGVLPALLLWRVRIRY-RPLLRELGQRLALLLLALLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 166 ILIVAALFYKDYASLIRNNKSVVKMLTPSNFVAGTIKFTEQRYFTRNLPLVKIGEDARkgpLIAGQAKKTLVILVVGETA 245
Cdd:COG2194 162 IVLLALLFYKDYASFFRNHKELRYLINPSNFIYALGKYAKARYFAAPLPLQPLGADAK---LAAAGAKPTLVVLVVGETA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 246 RAENFSLGGYQRETNPRL-KQDDVIYFKNASSCGTETAISVPCMFSNMPRKEYDATQATHQEGMLDVLAHAGVSVLWRDN 324
Cdd:COG2194 239 RADNFSLNGYARDTTPELaKEKNLVSFRDVTSCGTATAVSVPCMFSRLGRADYDPQRALNQENLLDVLQRAGVKVLWRDN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 325 DGGCKGACDRVPHIDMTKLKLPQDCDGEVCMDNALLYKLNDYINGLKDDGVIVLHQMGSHGPAYYRRSTPEFQTFSPTCN 404
Cdd:COG2194 319 QSGCKGVCDRVPTIDLTADNLPPLCDGGECLDEVLLDGLDEALADLAGDKLIVLHQMGSHGPAYYKRYPPEFRKFTPTCD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 405 SNQIQDCSHEQLVNTYDNSILYTDAMLDATIKLLRQYDDRFNTALVYLSDHGESLGENGMYLHGTPYVFAPSQQTHVPFL 484
Cdd:COG2194 399 TNDLQNCSREELVNAYDNTILYTDYVLSQVIDLLKAKQDRYDTAMLYVSDHGESLGENGLYLHGTPYAIAPDEQTHVPMI 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 485 MWMSADYQRNFGVDRQCLNALAEKdDVSQDNLFHTLLGMLNVQSREYQSRLDILQPCRNA 544
Cdd:COG2194 479 MWLSDGYAQRYGIDFACLKARADK-PYSHDNLFHTLLGLLDVRTSVYDPELDILAPCRRA 537
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
233-527 |
4.42e-122 |
|
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: 360.40 E-value: 4.42e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 233 KKTLVILVVGETARAENFSLGGYQRETNPRLKQ--DDVIYFKNASSCGTETAISVPCMFSNMPRKEYDatQATHQEGMLD 310
Cdd:cd16017 1 KPKNVVLVIGESARRDHMSLYGYPRDTTPFLSKlkKNLIVFDNVISCGTSTAVSLPCMLSFANRENYD--RAYYQENLID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 311 VLAHAGVSVLWRDNDGGCKGACDRVPHIDM--TKLKLPQDCDGEVCMDNALLYKLNDYINGLKDDGVIVLHQMGSHGPaY 388
Cdd:cd16017 79 LAKKAGYKTYWISNQGGCGGYDTRISAIAKieTVFTNKGSCNSSNCYDEALLPLLDEALADSSKKKLIVLHLMGSHGP-Y 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 389 YRRSTPEFQTFSPTCNsNQIQDCSHEQLVNTYDNSILYTDAMLDATIKLLRQYDDrfNTALVYLSDHGESLGENGMYLHG 468
Cdd:cd16017 158 YDRYPEEFAKFTPDCD-NELQSCSKEELINAYDNSILYTDYVLSQIIERLKKKDK--DAALIYFSDHGESLGENGLYLHG 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 727193019 469 TPYvfAPSQQTHVPFLMWMSADYQRNFGVDRQclnALAEKDDVSQDNLFHTLLGMLNVQ 527
Cdd:cd16017 235 APY--APKEQYHVPFIIWSSDSYKQRYPVERL---RANKDRPFSHDNLFHTLLGLLGIK 288
|
|
| PRK09598 |
PRK09598 |
phosphoethanolamine--lipid A transferase EptA; |
1-539 |
1.09e-109 |
|
phosphoethanolamine--lipid A transferase EptA;
Pssm-ID: 236581 [Multi-domain] Cd Length: 522 Bit Score: 337.14 E-value: 1.09e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 1 MWLRQRLRCNSLGFtLATALFFTLFQNALFlhrawSYItFDSVHSVIFAASMPVVIFCALNIIFSVLTV--PYLRKPLII 78
Cdd:PRK09598 7 LKFLKPLSCLQAGL-LYSLLNGVLYHFPLF-----AYV-YKESNQVSFIAMLVVLLFCVNGLLFLLLGLlsRRLMRLSAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 79 FFLLGSAAANYFMFSYGVVIDGNMMQNAFETNPQEATALLTPRMGLWLALLGILPAVAVCFTQIRQTRpwwymvglRAAN 158
Cdd:PRK09598 80 VFSLLNSIAFYFINTYKVFLNKSMMGNVLNTNTAESSGFLSVKLFIYIVVLGVLPGYIIYKIPLKNSS--------KKAP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 159 VMLSLAVILIVAALFYKDYASLI---RNNKSVVKMLTPSNFVAGTIKFTEQRYFTrnlPLVKIgedaRKGPLIAGQAKKT 235
Cdd:PRK09598 152 FAAILALVLIFLASAFANSKNWLwfdKHAKFLGGLILPWSYSVNTFRVSAHKFFA---PTIKP----LLPPLFSPNHSKS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 236 LVILVVGETARAENFSLGGYQRETNPRLKQ---DDVIYFKNASSCGTETAISVPCMFSNmprkEYDATQATHqEGMLDVL 312
Cdd:PRK09598 225 VVVLVIGESARKHNYALYGYEKPTNPRLSKrlaTHELTLFNATSCATYTTASLECILDS----SFKNTSNAY-ENLPTYL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 313 AHAGVSVLWRDNDGGckgacdrVPHIDMT----KLKLPQDCDGEVC-MDNALLYKLNDYINGLKDDGV-IVLHQMGSHGP 386
Cdd:PRK09598 300 TRAGIKVFWRSANDG-------EPNVKVTsylkNYELIQKCPNCEApYDESLLYNLPELIKASSNENVlLILHLAGSHGP 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 387 AYYRRSTPEFQTFSPTCNSNQIQDCSHEQLVNTYDNSILYTDAMLDATIKLLRQYDDRfnTALVYLSDHGESLGENGMYL 466
Cdd:PRK09598 373 NYDNKYPLNFRVFKPVCSSVELSSCSKESLINAYDNTIFYNDYLLDKIISMLKNLKQP--ALMIYLSDHGESLGEGAFYL 450
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727193019 467 HGTPYVFAPSQQTHVPFLMWMSADYQRNfgvdrqcLNALAEKDDVSQDNLFHTLLGMLNVQSRE--YQSRLDILQ 539
Cdd:PRK09598 451 HGIPKSIAPKEQYEIPFIVWASDSFKKQ-------HSIIQTQTPINQNVIFHSVLGVFDFKNPSavYRPSLDLFK 518
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
237-526 |
1.28e-63 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 209.97 E-value: 1.28e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 237 VILVVGETARAENFSLGGYQRETNPRLKQ--DDVIYFKNASSCGTETAISVPCMFSNMPRKEYDATQ------ATHQEGM 308
Cdd:pfam00884 3 VVLVLGESLRAPDLGLYGYPRPTTPFLDRlaEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVstpvglPRTEPSL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 309 LDVLAHAGV--------SVLWRDNDGGCK----GACDRVPHIDMTKLKLPQD--CDGEVCMDNALLYKLNDYINGLKDDG 374
Cdd:pfam00884 83 PDLLKRAGYntgaigkwHLGWYNNQSPCNlgfdKFFGRNTGSDLYADPPDVPynCSGGGVSDEALLDEALEFLDNNDKPF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 375 VIVLHQMGSHGPAYY-RRSTPEFQTFSPtcnsnqiQDCSHEQLVNTYDNSILYTDAMLDATIKLLRQYDDRFNTALVYLS 453
Cdd:pfam00884 163 FLVLHTLGSHGPPYYpDRYPEKYATFKP-------SSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTS 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 727193019 454 DHGESLGENGMYLHGTPYVFAPSQQTHVPFLMWMSADYQRnFGVDRQclnalaekdDVSQDNLFHTLLGMLNV 526
Cdd:pfam00884 236 DHGESLGEGGGYLHGGKYDNAPEGGYRVPLLIWSPGGKAK-GQKSEA---------LVSHVDLFPTILDLAGI 298
|
|
| EptA_B_N |
pfam08019 |
Phosphoethanolamine transferase EptA/EptB; This entry represents a domain found in a group of ... |
56-203 |
3.54e-59 |
|
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: 193.12 E-value: 3.54e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 56 IFCALNIIFSVLTVPYLRKPLIIFFLLGSAAANYFMFSYGVVIDGNMMQNAFETNPQEATALLTPRMGLWLALLGILPAV 135
Cdd:pfam08019 1 LFAALNLLLSLLSWRYLLKPLLILLLLLSAAASYFMDTYGVVIDRDMIQNVLETDVAEASDLLSPKLLLYLLLLGVLPAL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727193019 136 AVCFTQIRqTRPWWYMVGLRAANVMLSLAVILIVAALFYKDYASLIRNNKSVVKMLTPSNFVAGTIKF 203
Cdd:pfam08019 81 LLWRVRIR-YRPWLRELLSRLALILVSLLVIGLVAFLFYKDYASFFRNHKELRYLINPTNYIYSTVKY 147
|
|
| PRK11560 |
PRK11560 |
kdo(2)-lipid A phosphoethanolamine 7''-transferase; |
19-528 |
8.48e-47 |
|
kdo(2)-lipid A phosphoethanolamine 7''-transferase;
Pssm-ID: 183198 [Multi-domain] Cd Length: 558 Bit Score: 171.76 E-value: 8.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 19 ALFFTLFQN-ALFLHRAWSYITFDSVHSVIFAASMPVVIFCALNIIFSVLTVPYLR--KPLIIFFLLGSAAANYFMFSYG 95
Cdd:PRK11560 17 AVYIGLFLNiAVFYRRFDSYAQDFTVWKGLSAVVELAATVLVTFFLLRLLSLFGRRfwRVLASLLVLFSAAASYYMTFFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 96 VVIDGNMMQNAFETNPQEATALLTPRMGLWLALLGILPAVAVCFTQIRQT--------RPWWymvglRAANVMLsLAVIL 167
Cdd:PRK11560 97 VVIGYGIIASVMTTDIDLSKEVVGLHFILWLVAVSALPLILIWNNRCRYTllrqlrtpGQRI-----RSLAVVV-LAGLL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 168 IVAALFYKDYASLIRNNKSVVKMLT----------PSNFVAGTIKFTEQRYF----TRNL--PLVKIGEDARKGpliagq 231
Cdd:PRK11560 171 VWAPIRLLDIQQKKVERATGVDLPSyggvvansylPSNWLSALGLYAWAQVDessdNNSLlnPAKKFTYQAPKG------ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 232 AKKTLVILVVGETARAENFSLGGYQRETNPRL-KQDDVIYFKnASSCGTETAISVPCMF------SNMPR---KEYDATQ 301
Cdd:PRK11560 245 VDDTYVVFIIGETTRWDHMGILGYERNTTPKLaQEKNLAAFR-GYSCDTATKLSLRCMFvreggaEDNPQrtlKEQNVFA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 302 ATHQEGMLDVLaHAGVSVLWRDNdggcKGACDRVPHIDMTKLKlpQDCDGEVCMDNALLYKLNDYINGlKDDG--VIVLH 379
Cdd:PRK11560 324 VLKQLGFSSEL-FAMQSEMWFYN----NTMADNYAYREQIGAE--PRNRGKPVDDMLLVDEMKQSLGR-NPDGkhLIILH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 380 QMGSHGpAYYRRSTPEFQTFSPTCNSnqIQD-CSHEQLVNTYDNSILYTDAMLDATIKLLRqydDRfnTALV-YLSDHGE 457
Cdd:PRK11560 396 TKGSHY-NYTQRYPRSFARYQPECIG--VDSgCSKAQLINSYDNSVLYVDHFISSVIDQLR---DK--KAIVfYAADHGE 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727193019 458 SLGENgMYLHGTPYVFAPSQQTHVPFLMWMSADYQRNFGvDRQCLNALAEKDDVS----QDNLFHTLLGMLNVQS 528
Cdd:PRK11560 468 SINER-EHLHGTPREMAPPEQFRVPMMVWMSDKYLANPD-NAQAFAQLKKQADMKvprrHVELFDTILGCLGYTS 540
|
|
| PRK10649 |
PRK10649 |
phosphoethanolamine transferase CptA; |
76-500 |
2.85e-19 |
|
phosphoethanolamine transferase CptA;
Pssm-ID: 182617 [Multi-domain] Cd Length: 577 Bit Score: 91.31 E-value: 2.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 76 LIIFFLLGS--AAANYFmFSYGVVIDGNMMQNAFETNPQEATALLTPRMGLWLALLGIL-PAVAVC-FTQIRQTR-PWwy 150
Cdd:PRK10649 73 VIGVVLWAAslAALCYY-VIYGQEFSQSVLFVMFETNTNEASEYLSQYFSLKIVLIALAyTAVAVLlWTRLRPVYiPW-- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 151 mvglRAANVmlsLAVILIVAALFYKDYASLIRNNKSVVKML----------TPSNFVAGTIKFTEQRYFTRNLplvkIGE 220
Cdd:PRK10649 150 ----PWRYV---VSFALLYGLILHPIAMNTFIKHKPFEKTLdklasrmepaAPWQFLTGYYQYRQQLNSLQKL----LNE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 221 DARKGPL-----IAGQAKKTLViLVVGETARAENFSLGGYQRETNPRL---KQDD--VIYFKNASSCGTET--AISVPCM 288
Cdd:PRK10649 219 NAALPPLanlkdESGNAPRTLV-LVIGESTQRGRMSLYGYPRETTPELdalHKTDpgLTVFNNVVTSRPYTieILQQALT 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 289 FSNMPRKEYDATQAThqegMLDVLAHAGVSVLWRDNdggckgacdrvpHIDMTK-----LKLPQDCDGEVCMD-----NA 358
Cdd:PRK10649 298 FADEKNPDLYLTQPS----LMNMMKQAGYKTFWITN------------QQTMTArntmlTVFSRQTDKQYYMNqqrtqNA 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 359 LLYK---LNDYINGLKDDG---VIVLHQMGSHgPAYYRRSTPEFQTFS-------PTCNSNQIQdcsheqLVNTYDNSIL 425
Cdd:PRK10649 362 REYDtnvLKPFSEVLADPApkkFIIVHLLGTH-IKYKYRYPENQGKFDdrtghvpPGLNADELE------SYNDYDNANL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 426 YTDAMLDATIKLLRQYDDrfNTALVYLSDHGE---------SLGEN------GMYlhgtpyvfapsqqtHVPFLMWMSAD 490
Cdd:PRK10649 435 YNDHVVASLIKDFKATDP--NGFLVYFSDHGEevydtpphkTQGRNednptrHMY--------------TIPFLLWTSEK 498
|
490
....*....|....
gi 727193019 491 YQ----RNFGVDRQ 500
Cdd:PRK10649 499 WQaahpRDFSQDVD 512
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
237-486 |
2.42e-17 |
|
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: 82.21 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 237 VILVVGETARAENFSLGGYQRETNPRLKQ--DDVIYFKNASSCGTETAISVPCMFSNMPRKEYDATQATHQEG---MLDV 311
Cdd:cd16148 3 VILIVIDSLRADHLGCYGYDRVTTPNLDRlaAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVWGGPLEPDdptLAEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 312 LAHAGV------SVLWRDNDGG-CKGACDRVPHIDM-TKLKLPQDCDGEVCMDNALlyklnDYINGLKDDG--VIVLHQM 381
Cdd:cd16148 83 LRKAGYytaavsSNPHLFGGPGfDRGFDTFEDFRGQeGDPGEEGDERAERVTDRAL-----EWLDRNADDDpfFLFLHYF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 382 GSHGPayYRrstpefqtfsptcnsnqiqdcsheqlvntYDNSILYTDAMLDATIKLLRQYDDRFNTALVYLSDHGESLGE 461
Cdd:cd16148 158 DPHEP--YL-----------------------------YDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGE 206
|
250 260
....*....|....*....|....*..
gi 727193019 462 NGMYL--HGTPYvfapSQQTHVPFLMW 486
Cdd:cd16148 207 HGLYWghGSNLY----DEQLHVPLIIR 229
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
14-533 |
9.55e-14 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 73.92 E-value: 9.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 14 FTLATALFFTLFQNALFLHRAWSYITFDSVHSVIFAAsmpVVIFCALNIIFSVLTVPYLRKP---LIIFFLLGSAAANYF 90
Cdd:COG1368 7 LLLSLRLVFLLFNFDLSLGEILQAFLYGLRFILYLLL---LLLLLLLLLLPLLFRRPKLRWIyllLVLLLLLLLLVADIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 91 MFSY-GVVIDGNMMQNAfeTNPQEATA-LLTPRMGLWLALLGILPAVAVCFTQIRQTRPWWYMVGLRAANVMLSLAVILI 168
Cdd:COG1368 84 YYRFfGDRLNFSDLDYL--GDTGEVLGsLLSSYDLLLLLDLLLLLLLLLLLYRLLKKLRKSLPWRKRLALLLLLLALLLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 169 VAALFYKDYASLIR--NNKSVVKML---TPSNFVAGTIKFTEQRYFTRN--LPLVKIGEDARKGPLIAGQAKKTLVILVV 241
Cdd:COG1368 162 GIRLGEDRPLNLSDafSRNNFVNELglnGPYSFYDALRNNKAPATYSEEeaLEIKKYLKSNRPTPNPFGPAKKPNVVVIL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 242 GETARAENFSLGGYQRETNPRLKQ--DDVIYFKNASSCGTETAISVPCMFSNMP----RKEYDATQATHQEGMLDVLA-- 313
Cdd:COG1368 242 LESFSDFFIGALGNGKDVTPFLDSlaKESLYFGNFYSQGGRTSRGEFAVLTGLPplpgGSPYKRPGQNNFPSLPSILKkq 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 314 -------HAGVSVLW-RDNDGGCKGaCDRVphIDMTKLKLPQDcDGEVCMDNALLYKLNDYINGLKDDGVIVLHQMGSHG 385
Cdd:COG1368 322 gyetsffHGGDGSFWnRDSFYKNLG-FDEF--YDREDFDDPFD-GGWGVSDEDLFDKALEELEKLKKPFFAFLITLSNHG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 386 PayyrrstpefqtFSPTCNSNQIQDcSHEQLVNTYDNSILYTDAMLDATIKLLRQYDDRFNTALVYLSDHGESLGENGMY 465
Cdd:COG1368 398 P------------YTLPEEDKKIPD-YGKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGPRSPGKTDY 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 466 LHgtpyvfaPSQQTHVPFLMWMSADYQrnfgvdrqclnalAEKDD--VSQDNLFHTLLGMLNVQSREYQS 533
Cdd:COG1368 465 EN-------PLERYRVPLLIYSPGLKK-------------PKVIDtvGSQIDIAPTLLDLLGIDYPSYYA 514
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
237-486 |
8.35e-09 |
|
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: 56.27 E-value: 8.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 237 VILVVGETARAENFSLGGYQRETNPRLK--QDDVIYFK-NASSCGTETAISVPCMFSNMPRKEYDATQathqEGMLDVLA 313
Cdd:cd00016 3 VVLIVLDGLGADDLGKAGNPAPTTPNLKrlASEGATFNfRSVSPPTSSAPNHAALLTGAYPTLHGYTG----NGSADPEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 314 HAGVSVLWrdndggckGACDRVPHIdmtkLKlpqDCDGEVCMdnallYKLNDYIN--GLKDDGVIVLHQMGSHGPAYYRR 391
Cdd:cd00016 79 PSRAAGKD--------EDGPTIPEL----LK---QAGYRTGV-----IGLLKAIDetSKEKPFVLFLHFDGPDGPGHAYG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 392 STPEfqtfsptcnsnqiqdcsheqlvnTYDNSILYTDAMLDATIKLLRQYDDRFNTALVYLSDHGESLGENGMYLHGTPY 471
Cdd:cd00016 139 PNTP-----------------------EYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHGGDPKADGK 195
|
250
....*....|....*
gi 727193019 472 VFAPSQQTHVPFLMW 486
Cdd:cd00016 196 ADKSHTGMRVPFIAY 210
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
426-486 |
1.10e-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: 1.10e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727193019 426 YTDAMLDATIKLLRQYDDRFNTALVYLSDHGESLGENGMYLHGTPYvfapSQQTHVPFLMW 486
Cdd:cd16037 170 FLDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGERGLWGKSTMY----EESVRVPMIIS 226
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
418-526 |
1.87e-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: 293759 [Multi-domain] Cd Length: 311 Bit Score: 46.82 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 418 NTYDNSILYTDAMLDATIKLLRQYDDRFNTALVYLSDHGESLGENGMyLH--GTPYvfapSQQTHVPFLMwmsadyqRN- 494
Cdd:cd16035 167 NFYYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHGL-RGkgFNAY----EEALHVPLII-------SHp 234
|
90 100 110
....*....|....*....|....*....|....
gi 727193019 495 --FGVDRQClNALAekddvSQDNLFHTLLGMLNV 526
Cdd:cd16035 235 dlFGTGQTT-DALT-----SHIDLLPTLLGLAGV 262
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
433-526 |
2.17e-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: 293758 [Multi-domain] Cd Length: 399 Bit Score: 46.79 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 433 ATIKLLRQYDdrfNTALVYLSDHGESLGENGMYLHGTPYvfapSQQTHVPFLMWMSADYQRNfGVDRQCLNalaekddvS 512
Cdd:cd16034 245 DALKELGLLE---NTIVVFTSDHGDMLGSHGLMNKQVPY----EESIRVPFIIRYPGKIKAG-RVVDLLIN--------T 308
|
90
....*....|....
gi 727193019 513 QDnLFHTLLGMLNV 526
Cdd:cd16034 309 VD-IMPTLLGLCGL 321
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
415-486 |
6.80e-05 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 45.25 E-value: 6.80e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 727193019 415 QLVNTYDNSILYTDAMLDATIKLLRQYDDRFNTALVYLSDHGESLGENGMYLH-GTPYvfAPSqqTHVPFLMW 486
Cdd:COG3119 197 RARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHGLRGGkGTLY--EGG--IRVPLIVR 265
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
356-525 |
1.17e-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: 44.21 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 356 DNALLYKLNDYINGLKDDGV-IVLHQMGSHGPayyrrstpeFQTFSPTCNSNQIQDCSHEQLvNTYDNSILYTDAMLDAT 434
Cdd:cd16015 139 DESLFDQALEELEELKKKPFfIFLVTMSNHGP---------YDLPEEKKDEPLKVEEDKTEL-ENYLNAIHYTDKALGEF 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727193019 435 IKLLRQYDDRFNTALVYLSDHGESLGENGMYLHGTPYvfapsQQTHVPFLMWmSADYQRNFGVDRqclnalaekdDVSQD 514
Cdd:cd16015 209 IEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDEDPL-----DLYRTPLLIY-SPGLKKPKKIDR----------VGSQI 272
|
170
....*....|.
gi 727193019 515 NLFHTLLGMLN 525
Cdd:cd16015 273 DIAPTLLDLLG 283
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
435-486 |
2.34e-04 |
|
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: 42.81 E-value: 2.34e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 727193019 435 IKLLRQYDDRFNTALVYLSDHGESLGENGMYL-HGTPYVFApsqqTHVPFLMW 486
Cdd:cd16022 148 LDALEELGLLDNTLIVFTSDHGDMLGDHGLRGkKGSLYEGG----IRVPFIVR 196
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
420-484 |
5.85e-04 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 42.35 E-value: 5.85e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727193019 420 YDNSILYTDAMLDATIKLLRQYDDRFNTALVYLSDHGESLGENGMYLHGTPYvfapSQQTHVPFL 484
Cdd:PRK13759 270 YYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHGDMLGDHYLFRKGYPY----EGSAHIPFI 330
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
420-471 |
1.09e-03 |
|
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from choline. The symbiotic soil bacterium Rhizobium meliloti can synthesize glycine betaine from choline-O-sulphate and choline to protect itself from osmotic stress. This biosynthetic pathway is encoded by the betICBA locus, which comprises a regulatory gene, betI, and three structural genes, betC (choline sulfatase), betB (betaine aldehyde dehydrogenase), and betA (choline dehydrogenase). betICBA genes constitute a single operon.
Pssm-ID: 293756 [Multi-domain] Cd Length: 327 Bit Score: 41.41 E-value: 1.09e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 727193019 420 YDNSILYTDAMLDATIKLLRQYDDRFNTALVYLSDHGESLGENGMYLHGTPY 471
Cdd:cd16032 166 YYGMVSYVDDKVGQLLDTLERTGLADDTIVIFTSDHGDMLGERGLWYKMSFF 217
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
430-485 |
1.19e-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: 41.44 E-value: 1.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727193019 430 MLDATI-KLLR------QYDdrfNTALVYLSDHGESLGENGMYLHGtpyvFAPSQQT-HVPFLM 485
Cdd:cd16033 225 LIDDAIgRILDaleelgLAD---DTLVIFTSDHGDALGAHRLWDKG----PFMYEETyRIPLII 281
|
|
| |
