|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11598 |
PRK11598 |
putative metal dependent hydrolase; Provisional |
2-544 |
0e+00 |
|
putative metal dependent hydrolase; Provisional
Pssm-ID: 183224 [Multi-domain] Cd Length: 545 Bit Score: 1069.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 2 LKHLFKRPTLGLISWLLLISFYLATFLNIAFYKQVLQELPLDSVRNVLVFLSMPVVAFSVMNIVLTLASFLWLNRLVACV 81
Cdd:PRK11598 1 LKRLLKRPSLNLLTFLLLAAFYITLCLNIAFYKQVLQLLPLDSLHNVLVFASMPVVAFSVINIVFTLLSFPWLRRPLACL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 82 FILVGASAQYFIMTYGIIIDRSMIANMMDTTPAETFALLTPQMLITLGVSGILAALIACWVRIKPIAPAMRSVLFRGANI 161
Cdd:PRK11598 81 FILVGAAAQYFMMTYGIVIDRSMIQNIFETTPAESFALMTPQMLLWLGLSGVLPALIACWIKIRPATPRWRSVLFRLANI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 162 LISALLIVLVAAFFYKDYASLFRNNKELVKSLSPSNSIVATSSWYSHQRLAHLPLVRIGEDAHRNPLMVKEKRKNLTIVV 241
Cdd:PRK11598 161 LVSVLLILLVAALFYKDYASLFRNNKELVKSLTPSNSIVASWSWYSHQRLANLPLVRIGEDAHKNPLMQNQKRKNLTILV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 242 LGETSRGDNFSLSGYSRQTNPLLEKDDVVYFPRTTSCGTATAVSVPCMFSGMPRAHYDEELAQHQEGVLDIIQRAGINVL 321
Cdd:PRK11598 241 VGETSRAENFSLGGYPRETNPRLAKDNVIYFPHTTSCGTATAVSVPCMFSNMPRKHYDEELAHHQEGLLDIIQRAGINVL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 322 WNDNDGGCKGACDRVPHQNMTKLNLPGQCIDGECYDDVLFHGLEEYINNLQGDGVIVLHTIGSHGPTYYNRYPAQFKKFT 401
Cdd:PRK11598 321 WNDNDGGCKGACDRVPHQDVTALNLPGQCIDGECYDEVLFHGLENYINNLQGDGVIVLHTIGSHGPTYYNRYPPQFRKFT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 402 PTCDTNEIQTCSQQQLVNTYDNTILYVDYIVDKAINILKEHQDNFTTSLVYLSDHGESLGENGIYLHGLPYSIAPDTQKH 481
Cdd:PRK11598 401 PTCDTNEIQTCTQQQLVNTYDNTILYVDYIVDKAINLLKQHQDKFNTSLVYLSDHGESLGENGIYLHGLPYAIAPDQQTH 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517907629 482 VPMLLWLSEDYQQRYQVSQTCLQKRAGSEDFSQDNLFSTLLGLTGVQTQKYQAADDILQPCRG 544
Cdd:PRK11598 481 VPMLLWLSPDYQKRYGVDQQCLQKQAQTQDYSQDNLFSTLLGLTGVQTKEYQAADDILQPCRR 543
|
|
| 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: 782.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 6 FKRPTLGLISWLLLISFYLATFLNIAFYKQVLQELPLDSVrNVLVFLSMPVVAFSVMNIVLTLASFLWLNRLVACVFILV 85
Cdd:COG2194 2 FLLPRLSPLKLILLLALYFALFLNLPFWGRLLAILPLDGV-NLLFLLSLPLLLLAALNLLLSLLAWRYLFKPLLILLLLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 86 GASAQYFIMTYGIIIDRSMIANMMDTTPAETFALLTPQMLITLGVSGILAALIACWVRIKPiAPAMRSVLFRGANILISA 165
Cdd:COG2194 81 SAAASYFMDFYGVVIDYGMIQNVLETDPAEASELLSPKLILWLLLLGVLPALLLWRVRIRY-RPLLRELGQRLALLLLAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 166 LLIVLVAAFFYKDYASLFRNNKELVKSLSPSNSIVATSSWYSHQ-RLAHLPLVRIGEDAHRNPlmvKEKRKNLTIVVLGE 244
Cdd:COG2194 160 LVIVLLALLFYKDYASFFRNHKELRYLINPSNFIYALGKYAKARyFAAPLPLQPLGADAKLAA---AGAKPTLVVLVVGE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 245 TSRGDNFSLSGYSRQTNPLLEKD-DVVYFPRTTSCGTATAVSVPCMFSGMPRAHYDEELAQHQEGVLDIIQRAGINVLWN 323
Cdd:COG2194 237 TARADNFSLNGYARDTTPELAKEkNLVSFRDVTSCGTATAVSVPCMFSRLGRADYDPQRALNQENLLDVLQRAGVKVLWR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 324 DNDGGCKGACDRVPHQNMTKLNLPGQCIDGECYDDVLFHGLEEYINNLQGDGVIVLHTIGSHGPTYYNRYPAQFKKFTPT 403
Cdd:COG2194 317 DNQSGCKGVCDRVPTIDLTADNLPPLCDGGECLDEVLLDGLDEALADLAGDKLIVLHQMGSHGPAYYKRYPPEFRKFTPT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 404 CDTNEIQTCSQQQLVNTYDNTILYVDYIVDKAINILKEHQDNFTTSLVYLSDHGESLGENGIYLHGLPYSIAPDTQKHVP 483
Cdd:COG2194 397 CDTNDLQNCSREELVNAYDNTILYTDYVLSQVIDLLKAKQDRYDTAMLYVSDHGESLGENGLYLHGTPYAIAPDEQTHVP 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517907629 484 MLLWLSEDYQQRYQVSQTCLQKRAgSEDFSQDNLFSTLLGLTGVQTQKYQAADDILQPCRG 544
Cdd:COG2194 477 MIMWLSDGYAQRYGIDFACLKARA-DKPYSHDNLFHTLLGLLDVRTSVYDPELDILAPCRR 536
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
234-528 |
4.18e-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: 4.18e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 234 RKNLTIVVLGETSRGDNFSLSGYSRQTNPLL--EKDDVVYFPRTTSCGTATAVSVPCMFSGMPRAHYDEelAQHQEGVLD 311
Cdd:cd16017 1 KPKNVVLVIGESARRDHMSLYGYPRDTTPFLskLKKNLIVFDNVISCGTSTAVSLPCMLSFANRENYDR--AYYQENLID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 312 IIQRAGINVLWNDNDGGCKGACDRVPHQNM--TKLNLPGQCIDGECYDDVLFHGLEEYINNLQGDGVIVLHTIGSHGPtY 389
Cdd:cd16017 79 LAKKAGYKTYWISNQGGCGGYDTRISAIAKieTVFTNKGSCNSSNCYDEALLPLLDEALADSSKKKLIVLHLMGSHGP-Y 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 390 YNRYPAQFKKFTPTCDtNEIQTCSQQQLVNTYDNTILYVDYIVDKAINILKEHQDNftTSLVYLSDHGESLGENGIYLHG 469
Cdd:cd16017 158 YDRYPEEFAKFTPDCD-NELQSCSKEELINAYDNSILYTDYVLSQIIERLKKKDKD--AALIYFSDHGESLGENGLYLHG 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 517907629 470 LPYsiAPDTQKHVPMLLWLSEDYQQRYQVsqtCLQKRAGSEDFSQDNLFSTLLGLTGVQ 528
Cdd:cd16017 235 APY--APKEQYHVPFIIWSSDSYKQRYPV---ERLRANKDRPFSHDNLFHTLLGLLGIK 288
|
|
| PRK09598 |
PRK09598 |
phosphoethanolamine--lipid A transferase EptA; |
4-540 |
2.53e-96 |
|
phosphoethanolamine--lipid A transferase EptA;
Pssm-ID: 236581 [Multi-domain] Cd Length: 522 Bit Score: 302.47 E-value: 2.53e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 4 HLFKRPTLGLISWLLLISFYLATFLNIAFYKQVLQELPLDSVRNVLVFLsMPVVAFSVMNIVLTLASFLwlNRLVACVFI 83
Cdd:PRK09598 6 HLKFLKPLSCLQAGLLYSLLNGVLYHFPLFAYVYKESNQVSFIAMLVVL-LFCVNGLLFLLLGLLSRRL--MRLSAIVFS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 84 LVGASAQYFIMTYGIIIDRSMIANMMDTTPAETFALLTPQMLITLGVSGILAAliacWVRIKpiAPAMRSVLFRGANILI 163
Cdd:PRK09598 83 LLNSIAFYFINTYKVFLNKSMMGNVLNTNTAESSGFLSVKLFIYIVVLGVLPG----YIIYK--IPLKNSSKKAPFAAIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 164 SALLIVLVAAFF-YKDYASLFRNNKELVKSLSPSNSIVATSSWYSHQRLAhlPLVRIgedaHRNPLMVKEKRKNLTIVVL 242
Cdd:PRK09598 157 ALVLIFLASAFAnSKNWLWFDKHAKFLGGLILPWSYSVNTFRVSAHKFFA--PTIKP----LLPPLFSPNHSKSVVVLVI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 243 GETSRGDNFSLSGYSRQTNPLLEK---DDVVYFPRTTSCGTATAVSVPCMFSgmpraHYDEELAQHQEGVLDIIQRAGIN 319
Cdd:PRK09598 231 GESARKHNYALYGYEKPTNPRLSKrlaTHELTLFNATSCATYTTASLECILD-----SSFKNTSNAYENLPTYLTRAGIK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 320 VLWNDNDGGCKgacdRVPHQN-MTKLNLPGQCIDGEC-YDDVLFHGLEEYINNLQGDGV-IVLHTIGSHGPTYYNRYPAQ 396
Cdd:PRK09598 306 VFWRSANDGEP----NVKVTSyLKNYELIQKCPNCEApYDESLLYNLPELIKASSNENVlLILHLAGSHGPNYDNKYPLN 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 397 FKKFTPTCDTNEIQTCSQQQLVNTYDNTILYVDYIVDKAINILKEHQDNFTtsLVYLSDHGESLGENGIYLHGLPYSIAP 476
Cdd:PRK09598 382 FRVFKPVCSSVELSSCSKESLINAYDNTIFYNDYLLDKIISMLKNLKQPAL--MIYLSDHGESLGEGAFYLHGIPKSIAP 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517907629 477 DTQKHVPMLLWLSEDYQQRYQVSQTclqkragSEDFSQDNLFSTLLGLTGVQTQK--YQAADDILQ 540
Cdd:PRK09598 460 KEQYEIPFIVWASDSFKKQHSIIQT-------QTPINQNVIFHSVLGVFDFKNPSavYRPSLDLFK 518
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
239-527 |
1.46e-75 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 241.17 E-value: 1.46e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 239 IVVLGETSRGDNFSLSGYSRQTNPLLEK--DDVVYFPRTTSCGTATAVSVPCMFSGMPRAHYD------EELAQHQEGVL 310
Cdd:pfam00884 4 VLVLGESLRAPDLGLYGYPRPTTPFLDRlaEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGsyvstpVGLPRTEPSLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 311 DIIQRAGINV--------LWNDNDGGCK----GACDRVPHQNMTKLN--LPGQCIDGECYDDVLFHGLEEYINNLQGDGV 376
Cdd:pfam00884 84 DLLKRAGYNTgaigkwhlGWYNNQSPCNlgfdKFFGRNTGSDLYADPpdVPYNCSGGGVSDEALLDEALEFLDNNDKPFF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 377 IVLHTIGSHGP-TYYNRYPAQFKKFTPtcdtneiQTCSQQQLVNTYDNTILYVDYIVDKAINILKEHQDNFTTSLVYLSD 455
Cdd:pfam00884 164 LVLHTLGSHGPpYYPDRYPEKYATFKP-------SSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSD 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517907629 456 HGESLGENGIYLHGLPYSIAPDTQKHVPMLLWLSEDYQQRYQVSQtclqkragseDFSQDNLFSTLLGLTGV 527
Cdd:pfam00884 237 HGESLGEGGGYLHGGKYDNAPEGGYRVPLLIWSPGGKAKGQKSEA----------LVSHVDLFPTILDLAGI 298
|
|
| EptA_B_N |
pfam08019 |
Phosphoethanolamine transferase EptA/EptB; This entry represents a domain found in a group of ... |
59-209 |
9.23e-53 |
|
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: 176.17 E-value: 9.23e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 59 FSVMNIVLTLASFLWLNRLVACVFILVGASAQYFIMTYGIIIDRSMIANMMDTTPAETFALLTPQMLITLGVSGILAALI 138
Cdd:pfam08019 2 FAALNLLLSLLSWRYLLKPLLILLLLLSAAASYFMDTYGVVIDRDMIQNVLETDVAEASDLLSPKLLLYLLLLGVLPALL 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517907629 139 ACWVRIKPiAPAMRSVLFRGANILISALLIVLVAAFFYKDYASLFRNNKELVKSLSPSNSIVATSSWYSHQ 209
Cdd:pfam08019 82 LWRVRIRY-RPWLRELLSRLALILVSLLVIGLVAFLFYKDYASFFRNHKELRYLINPTNYIYSTVKYAKHQ 151
|
|
| PRK11560 |
PRK11560 |
kdo(2)-lipid A phosphoethanolamine 7''-transferase; |
18-526 |
2.38e-47 |
|
kdo(2)-lipid A phosphoethanolamine 7''-transferase;
Pssm-ID: 183198 [Multi-domain] Cd Length: 558 Bit Score: 173.30 E-value: 2.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 18 LLISFYLATFLNIA-FYKQVLQELPLDSVRNVLVFLSMPVVAFSVMNIVLTLASFL--WLNRLVACVFILVGASAQYFIM 94
Cdd:PRK11560 14 FLLAVYIGLFLNIAvFYRRFDSYAQDFTVWKGLSAVVELAATVLVTFFLLRLLSLFgrRFWRVLASLLVLFSAAASYYMT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 95 TYGIIIDRSMIANMMDTTPAETFALLTPQMLI-TLGVSGILAALIacWVRikpiapAMRSVLFRGANIL---ISALLIVL 170
Cdd:PRK11560 94 FFNVVIGYGIIASVMTTDIDLSKEVVGLHFILwLVAVSALPLILI--WNN------RCRYTLLRQLRTPgqrIRSLAVVV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 171 VAAFFYKDYASLFRNNKELVKSLS----PSNSIVATSSWYSHQRLAHLPLV---RIGEDAHRNPLMVKEKR--------- 234
Cdd:PRK11560 166 LAGLLVWAPIRLLDIQQKKVERATgvdlPSYGGVVANSYLPSNWLSALGLYawaQVDESSDNNSLLNPAKKftyqapkgv 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 235 KNLTIV-VLGETSRGDNFSLSGYSRQTNPLL--EKDDVVYfpRTTSCGTATAVSVPCMFSgmpRAHYDEELAQH---QEG 308
Cdd:PRK11560 246 DDTYVVfIIGETTRWDHMGILGYERNTTPKLaqEKNLAAF--RGYSCDTATKLSLRCMFV---REGGAEDNPQRtlkEQN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 309 VLDIIQRAGINV--------LWNDNdggcKGACDRVPHQNMT---KLNlpgqciDGECYDDVLFhgLEEYINNL----QG 373
Cdd:PRK11560 321 VFAVLKQLGFSSelfamqseMWFYN----NTMADNYAYREQIgaePRN------RGKPVDDMLL--VDEMKQSLgrnpDG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 374 DGVIVLHTIGSHGpTYYNRYPAQFKKFTPTCdTNEIQTCSQQQLVNTYDNTILYVDYIVDKAINILKEHQdnftTSLVYL 453
Cdd:PRK11560 389 KHLIILHTKGSHY-NYTQRYPRSFARYQPEC-IGVDSGCSKAQLINSYDNSVLYVDHFISSVIDQLRDKK----AIVFYA 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517907629 454 SDHGESLGENGiYLHGLPYSIAPDTQKHVPMLLWLSEDYQQRYQVSQTCLQKRAGSED---FSQDNLFSTLLGLTG 526
Cdd:PRK11560 463 ADHGESINERE-HLHGTPREMAPPEQFRVPMMVWMSDKYLANPDNAQAFAQLKKQADMkvpRRHVELFDTILGCLG 537
|
|
| PRK10649 |
PRK10649 |
phosphoethanolamine transferase CptA; |
68-494 |
5.23e-23 |
|
phosphoethanolamine transferase CptA;
Pssm-ID: 182617 [Multi-domain] Cd Length: 577 Bit Score: 102.86 E-value: 5.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 68 LASFLWL---------NRLVACV--FILVGAS----AQYFImtYGIIIDRSMIANMMDTTPAETFALLT----PQMLITL 128
Cdd:PRK10649 51 LFSSLWLipvflfprrIRIIAAVigVVLWAASlaalCYYVI--YGQEFSQSVLFVMFETNTNEASEYLSqyfsLKIVLIA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 129 GVSGILAALIacWVRIKPIApamrsvLFRGANILISALLIVLVAAF-FYKD----YASLFRNNKELVKSLSPSNSIVATS 203
Cdd:PRK10649 129 LAYTAVAVLL--WTRLRPVY------IPWPWRYVVSFALLYGLILHpIAMNtfikHKPFEKTLDKLASRMEPAAPWQFLT 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 204 SWYS-HQRLAHL-PLVRigEDAHRNPLmvkekrKNL---------TIV-VLGETSRGDNFSLSGYSRQTNPLLEKddvvy 271
Cdd:PRK10649 201 GYYQyRQQLNSLqKLLN--ENAALPPL------ANLkdesgnaprTLVlVIGESTQRGRMSLYGYPRETTPELDA----- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 272 fPRTTSCGTATAVSVPCmfsgmPRAHYDEELAQ--------HQEGVL------DIIQRAGINVLWNDNdggckgacdrvp 337
Cdd:PRK10649 268 -LHKTDPGLTVFNNVVT-----SRPYTIEILQQaltfadekNPDLYLtqpslmNMMKQAGYKTFWITN------------ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 338 HQNMTKLN-----LPGQCID-----------GECYDDVLFHGLEEYINNLQGDGVIVLHTIGSHgPTYYNRYPAQFKKFT 401
Cdd:PRK10649 330 QQTMTARNtmltvFSRQTDKqyymnqqrtqnAREYDTNVLKPFSEVLADPAPKKFIIVHLLGTH-IKYKYRYPENQGKFD 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 402 PTCDT-NEIQTCSQQQLVNTYDNTILYVDYIVDKAINILKEHQDN-FttsLVYLSDHGESLgengiylhglpYSIAP-DT 478
Cdd:PRK10649 409 DRTGHvPPGLNADELESYNDYDNANLYNDHVVASLIKDFKATDPNgF---LVYFSDHGEEV-----------YDTPPhKT 474
|
490 500
....*....|....*....|....*..
gi 517907629 479 Q--------KH---VPMLLWLSEDYQQ 494
Cdd:PRK10649 475 QgrnednptRHmytIPFLLWTSEKWQA 501
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
10-541 |
2.24e-16 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 82.01 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 10 TLGLISWLLLISFYLATFLNIAFYKQVLQELpLDSVRNVLVFLSMPVVAFSV--MNIVLTLASFLWLNRLVACVFILVGA 87
Cdd:COG1368 1 FFLLFLLLLSLRLVFLLFNFDLSLGEILQAF-LYGLRFILYLLLLLLLLLLLllPLLFRRPKLRWIYLLLVLLLLLLLLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 88 SAQYFIMTYGIIIDRSMIANMMDTTPAETFaLLTPQMLITLGVSGILAALIACWVRIKPIAPAMRSVLFRGANILISALL 167
Cdd:COG1368 80 ADILYYRFFGDRLNFSDLDYLGDTGEVLGS-LLSSYDLLLLLDLLLLLLLLLLLYRLLKKLRKSLPWRKRLALLLLLLAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 168 IVLVAAFFYKDYASLFR--NNKELVKSLSPSNSIVATSSWYSHQRLAHLPLVRIGE-------DAHRNPLMVKEKRKNLt 238
Cdd:COG1368 159 LLLGIRLGEDRPLNLSDafSRNNFVNELGLNGPYSFYDALRNNKAPATYSEEEALEikkylksNRPTPNPFGPAKKPNV- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 239 IVVLGEtSRGDNFSLSGYSRQ-----TNPLLEKDdvVYFPRTTSCGTATAVSVPCMFSGMP----RAHYDEELAQHQEGV 309
Cdd:COG1368 238 VVILLE-SFSDFFIGALGNGKdvtpfLDSLAKES--LYFGNFYSQGGRTSRGEFAVLTGLPplpgGSPYKRPGQNNFPSL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 310 LDIIQRAGI-------NVLWNDNdggckgaCDRV-PHQNMTKLnlpgqcIDGECY-----------DDVLFHGLEEYINN 370
Cdd:COG1368 315 PSILKKQGYetsffhgGDGSFWN-------RDSFyKNLGFDEF------YDREDFddpfdggwgvsDEDLFDKALEELEK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 371 LQGDGVIVLHTIGSHGPtyYNrYPAQFKKFTPTCDTNeiqtcsqqqlVNTYDNTILYVDYIVDKAINILKEHQ--DNftT 448
Cdd:COG1368 382 LKKPFFAFLITLSNHGP--YT-LPEEDKKIPDYGKTT----------LNNYLNAVRYADQALGEFIEKLKKSGwyDN--T 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 449 SLVYLSDHGESLGENGIYLHglpysiaPDTQKHVPMLLWlSEDYQQRYQVSQTClqkragsedfSQDNLFSTLLGLTGVQ 528
Cdd:COG1368 447 IFVIYGDHGPRSPGKTDYEN-------PLERYRVPLLIY-SPGLKKPKVIDTVG----------SQIDIAPTLLDLLGID 508
|
570
....*....|....
gi 517907629 529 TQKYQAA-DDILQP 541
Cdd:COG1368 509 YPSYYAFgRDLLSP 522
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
363-524 |
3.91e-10 |
|
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: 60.13 E-value: 3.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 363 GLEEYINNLQGD--GVIVLHTIGSHGPTYYnrypaqFKKFTPTcdtneiqtcsqqqlvntYDNTILYVDYIVDKAINILK 440
Cdd:cd00016 107 GLLKAIDETSKEkpFVLFLHFDGPDGPGHA------YGPNTPE-----------------YYDAVEEIDERIGKVLDALK 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 441 EHQDNFTTSLVYLSDHGESLGENGIYLHGLPYSIAPDTQKHVPMLLWlsedyqqryqvSQTCLQKRAGSEDFSQDNLFST 520
Cdd:cd00016 164 KAGDADDTVIIVTADHGGIDKGHGGDPKADGKADKSHTGMRVPFIAY-----------GPGVKKGGVKHELISQYDIAPT 232
|
....
gi 517907629 521 LLGL 524
Cdd:cd00016 233 LADL 236
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
238-488 |
4.01e-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: 60.64 E-value: 4.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 238 TIVVLGETSRGDNFSLSGYSRQTNPLLEK--DDVVYFPRTTSCGTATAVSVPCMFSGMPRAHYDEELAQHQEGVL---DI 312
Cdd:cd16148 3 VILIVIDSLRADHLGCYGYDRVTTPNLDRlaAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVWGGPLEPDDPtlaEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 313 IQRAGIN-VLWNDNDGGCKGAC-DRVPHQNMTKLNLPGQCIDGECY-DDVLFHGLEEYINNLQGDG--VIVLHTIGSHGP 387
Cdd:cd16148 83 LRKAGYYtAAVSSNPHLFGGPGfDRGFDTFEDFRGQEGDPGEEGDErAERVTDRALEWLDRNADDDpfFLFLHYFDPHEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 388 tyYNrypaqfkkftptcdtneiqtcsqqqlvntYDNTILYVDYIVDKAINILKEHQ--DNftTSLVYLSDHGESLGENGI 465
Cdd:cd16148 163 --YL-----------------------------YDAEVRYVDEQIGRLLDKLKELGllED--TLVIVTSDHGEEFGEHGL 209
|
250 260
....*....|....*....|....
gi 517907629 466 YL-HGLPYSiapDTQKHVPMLLWL 488
Cdd:cd16148 210 YWgHGSNLY---DEQLHVPLIIRW 230
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
386-487 |
6.43e-07 |
|
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];
Pssm-ID: 442317 [Multi-domain] Cd Length: 603 Bit Score: 52.21 E-value: 6.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 386 GPTYYNRYPAQFKKFTPTCDTNEIQTCSQQQ---LVNTYDNTILYVDYIVDKAINILKEHQDNFTTSLVYLSDHGESLGE 462
Cdd:COG3083 391 APHAYSFPADYPKPFQPSEDCNYLALDNESDptpFKNRYRNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFNE 470
|
90 100
....*....|....*....|....*..
gi 517907629 463 NGI--YLHGLPYSiapDTQKHVPMLLW 487
Cdd:COG3083 471 NGQnyWGHNSNFS---RYQLQVPLVIH 494
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
356-526 |
2.21e-06 |
|
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: 49.60 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 356 YDDVLFHGLEEYINNLQGDGV-IVLHTIGSHGPtyYNrYPAQFKKFTPTCDTNEiqtcsqqQLVNTYDNTILYVDYIVDK 434
Cdd:cd16015 138 SDESLFDQALEELEELKKKPFfIFLVTMSNHGP--YD-LPEEKKDEPLKVEEDK-------TELENYLNAIHYTDKALGE 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 435 AINILKE--HQDNftTSLVYLSDHGESLGENGIYLHGLPYsiapdTQKHVPMLLWLSEDYQQRYQvsqtclqkragSEDF 512
Cdd:cd16015 208 FIEKLKKsgLYEN--TIIVIYGDHLPSLGSDYDETDEDPL-----DLYRTPLLIYSPGLKKPKKI-----------DRVG 269
|
170
....*....|....
gi 517907629 513 SQDNLFSTLLGLTG 526
Cdd:cd16015 270 SQIDIAPTLLDLLG 283
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
356-487 |
2.12e-05 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 46.80 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 356 YDDVLFHGLEEYINNLQGDG---VIVLHTIGSHGPT-----YYNRYPAQFKKFTPTCDTNEIQTCSQQQLVNTYDNTILY 427
Cdd:COG3119 129 LTDLLTDKAIDFLERQADKDkpfFLYLAFNAPHAPYqapeeYLDKYDGKDIPLPPNLAPRDLTEEELRRARAAYAAMIEE 208
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517907629 428 VDYIVDKAINILKEH--QDNftTSLVYLSDHGESLGENGIYLH-GLPY--SIapdtqkHVPMLLW 487
Cdd:COG3119 209 VDDQVGRLLDALEELglADN--TIVVFTSDNGPSLGEHGLRGGkGTLYegGI------RVPLIVR 265
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
427-532 |
2.43e-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: 293772 [Multi-domain] Cd Length: 282 Bit Score: 40.05 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 427 YVDYIVDKAINILKEH-----QDNftTSLVYLSDHGESLGENGIYLHGLPYsiapDTQKHVPMLLwlsedyqqryqVSQT 501
Cdd:cd16153 176 YGDAQVGRAVEAFKAYslkqdRDY--TIVYVTGDHGWHLGEQGILAKFTFW----PQSHRVPLIV-----------VSSD 238
|
90 100 110
....*....|....*....|....*....|....
gi 517907629 502 CLQKRAGS--EDFSQD-NLFSTLLGLTGVQTQKY 532
Cdd:cd16153 239 KLKAPAGKvrHDFVEFvDLAPTLLAAAGVDVDAP 272
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
427-487 |
3.32e-03 |
|
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293775 [Multi-domain] Cd Length: 468 Bit Score: 40.06 E-value: 3.32e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517907629 427 YVDYIVDKAINILKEHQDNFTtsLVYLSDHGESLGENGIYLHGlpySIAPDTQKHVPMLLW 487
Cdd:cd16156 249 FVDYEIGRVLDAADEIAEDAW--VIYTSDHGDMLGAHKLWAKG---PAVYDEITNIPLIIR 304
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
387-527 |
3.40e-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: 293758 [Multi-domain] Cd Length: 399 Bit Score: 39.86 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 387 PTYYNRYPAQFKKFTPTCDTNEIQTCSQQQLVNTYDNTILYVDYIVDKAINILKE--HQDNftTSLVYLSDHGESLGENG 464
Cdd:cd16034 195 EEYLDMYDPKKLLLRPNVPEDKKEEAGLREDLRGYYAMITALDDNIGRLLDALKElgLLEN--TIVVFTSDHGDMLGSHG 272
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517907629 465 IYLHGLPY--SIapdtqkHVPMLLwlsedyqqRYQvsqtCLQKRAGSEDF---SQDnLFSTLLGLTGV 527
Cdd:cd16034 273 LMNKQVPYeeSI------RVPFII--------RYP----GKIKAGRVVDLlinTVD-IMPTLLGLCGL 321
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
425-487 |
6.04e-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: 38.57 E-value: 6.04e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517907629 425 ILYVDYIVDKAINILKEHQ--DNftTSLVYLSDHGESLGENGIYL-HGLPY--SIapdtqkHVPMLLW 487
Cdd:cd16022 137 VSAIDDQIGRILDALEELGllDN--TLIVFTSDHGDMLGDHGLRGkKGSLYegGI------RVPFIVR 196
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
387-484 |
6.36e-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: 39.13 E-value: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517907629 387 PTYYNRYPAQFKKFTptcDTNEIQtcsqQQLVNTYDNTILYVDYIVDKAINILKEH--QDNftTSLVYLSDHGESLGENG 464
Cdd:cd16033 192 PYIYRRERKRWGVDT---EDEEDW----KEIIAHYWGYITLIDDAIGRILDALEELglADD--TLVIFTSDHGDALGAHR 262
|
90 100
....*....|....*....|
gi 517907629 465 IYLHGLPYsiaPDTQKHVPM 484
Cdd:cd16033 263 LWDKGPFM---YEETYRIPL 279
|
|
| |
