|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11598 |
PRK11598 |
putative metal dependent hydrolase; Provisional |
1-541 |
0e+00 |
|
putative metal dependent hydrolase; Provisional
Pssm-ID: 183224 [Multi-domain] Cd Length: 545 Bit Score: 1022.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 1 MQLIKKLQCNDIKFTLGCALFFTL-LNGLFIQRSWAIIAPSHLHDILFAASVPVVLFCGWVIVFSLLNIPYIRKPLLIVL 79
Cdd:PRK11598 2 KRLLKRPSLNLLTFLLLAAFYITLcLNIAFYKQVLQLLPLDSLHNVLVFASMPVVAFSVINIVFTLLSFPWLRRPLACLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 80 TVGCAAATYFMYTYGAVIDQNMIVNVFETNSQEATALVTPQMILWIVVAGLVPSVVLALTRIRTGK-WWYALLTRVAAML 158
Cdd:PRK11598 82 ILVGAAAQYFMMTYGIVIDRSMIQNIFETTPAESFALMTPQMLLWLGLSGVLPALIACWIKIRPATpRWRSVLFRLANIL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 159 GALLVIILIAALFYKDYASLFRNNKSIVKMVTPANYVSAVVKYSKMRWFaGDQTLVRIGEDAHKGSLIAGQQKKTVLVLV 238
Cdd:PRK11598 162 VSVLLILLVAALFYKDYASLFRNNKELVKSLTPSNSIVASWSWYSHQRL-ANLPLVRIGEDAHKNPLMQNQKRKNLTILV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 239 VGEASRAANYSLNGYGRETNPELKKQDVINFPQASSCGTETAVSVPCMFSGMTRSKYDADLARHQEGLLDVLRHAGVNLL 318
Cdd:PRK11598 241 VGETSRAENFSLGGYPRETNPRLAKDNVIYFPHTTSCGTATAVSVPCMFSNMPRKHYDEELAHHQEGLLDIIQRAGINVL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 319 WRDNDGGCKGACDRVPHTDMTQWNLDQFCKDKSCIDDVNFYRLDNVLDGVKQDTVLVIHLMGSHGPAYYRRYPDNFRKFT 398
Cdd:PRK11598 321 WNDNDGGCKGACDRVPHQDVTALNLPGQCIDGECYDEVLFHGLENYINNLQGDGVIVLHTIGSHGPTYYNRYPPQFRKFT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 399 PTCDTNEIQDCDHQALMNTYDNTILYTDSMVSKTIDALKARQANMNTALIYLSDHGESLGESGIYLHGTPYMLAPEQQTH 478
Cdd:PRK11598 401 PTCDTNEIQTCTQQQLVNTYDNTILYVDYIVDKAINLLKQHQDKFNTSLVYLSDHGESLGENGIYLHGLPYAIAPDQQTH 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278866360 479 IPFMFWLSPDYAKNFGINAQCLRDYAAKNAVSQDNLFSTVLGMMDIKSKVYQQQLDILNGCRQ 541
Cdd:PRK11598 481 VPMLLWLSPDYQKRYGVDQQCLQKQAQTQDYSQDNLFSTLLGLTGVQTKEYQAADDILQPCRR 543
|
|
| OpgE |
COG2194 |
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall ... |
4-541 |
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: 810.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 4 IKKLQCNDIKFTLGCALFFTL-LNGLFIQRSWAIIaPSHLHDILFAASVPVVLFCGWVIVFSLLNIPYIRKPLLIVLTVG 82
Cdd:COG2194 2 FLLPRLSPLKLILLLALYFALfLNLPFWGRLLAIL-PLDGVNLLFLLSLPLLLLAALNLLLSLLAWRYLFKPLLILLLLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 83 CAAATYFMYTYGAVIDQNMIVNVFETNSQEATALVTPQMILWIVVAGLVPSVVLALTRIRTGKWWYALLTRVAAMLGALL 162
Cdd:COG2194 81 SAAASYFMDFYGVVIDYGMIQNVLETDPAEASELLSPKLILWLLLLGVLPALLLWRVRIRYRPLLRELGQRLALLLLALL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 163 VIILIAALFYKDYASLFRNNKSIVKMVTPANYVSAVVKYSKMRWFAGDQTLVRIGEDAHkgsLIAGQQKKTVLVLVVGEA 242
Cdd:COG2194 161 VIVLLALLFYKDYASFFRNHKELRYLINPSNFIYALGKYAKARYFAAPLPLQPLGADAK---LAAAGAKPTLVVLVVGET 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 243 SRAANYSLNGYGRETNPELKKQ-DVINFPQASSCGTETAVSVPCMFSGMTRSKYDADLARHQEGLLDVLRHAGVNLLWRD 321
Cdd:COG2194 238 ARADNFSLNGYARDTTPELAKEkNLVSFRDVTSCGTATAVSVPCMFSRLGRADYDPQRALNQENLLDVLQRAGVKVLWRD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 322 NDGGCKGACDRVPHTDMTQWNLDQFCKDKSCIDDVNFYRLDNVLDGVKQDTVLVIHLMGSHGPAYYRRYPDNFRKFTPTC 401
Cdd:COG2194 318 NQSGCKGVCDRVPTIDLTADNLPPLCDGGECLDEVLLDGLDEALADLAGDKLIVLHQMGSHGPAYYKRYPPEFRKFTPTC 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 402 DTNEIQDCDHQALMNTYDNTILYTDSMVSKTIDALKARQANMNTALIYLSDHGESLGESGIYLHGTPYMLAPEQQTHIPF 481
Cdd:COG2194 398 DTNDLQNCSREELVNAYDNTILYTDYVLSQVIDLLKAKQDRYDTAMLYVSDHGESLGENGLYLHGTPYAIAPDEQTHVPM 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 482 MFWLSPDYAKNFGINAQCLRDYAAKnAVSQDNLFSTVLGMMDIKSKVYQQQLDILNGCRQ 541
Cdd:COG2194 478 IMWLSDGYAQRYGIDFACLKARADK-PYSHDNLFHTLLGLLDVRTSVYDPELDILAPCRR 536
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
231-525 |
5.22e-123 |
|
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: 362.71 E-value: 5.22e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 231 KKTVLVLVVGEASRAANYSLNGYGRETNPELKKQ--DVINFPQASSCGTETAVSVPCMFSGMTRSKYDadLARHQEGLLD 308
Cdd:cd16017 1 KPKNVVLVIGESARRDHMSLYGYPRDTTPFLSKLkkNLIVFDNVISCGTSTAVSLPCMLSFANRENYD--RAYYQENLID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 309 VLRHAGVNLLWRDNDGGCKGACDRVPHTDMTQW--NLDQFCKDKSCIDDVNFYRLDNVLDGVKQDTVLVIHLMGSHGPaY 386
Cdd:cd16017 79 LAKKAGYKTYWISNQGGCGGYDTRISAIAKIETvfTNKGSCNSSNCYDEALLPLLDEALADSSKKKLIVLHLMGSHGP-Y 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 387 YRRYPDNFRKFTPTCDtNEIQDCDHQALMNTYDNTILYTDSMVSKTIDALKarQANMNTALIYLSDHGESLGESGIYLHG 466
Cdd:cd16017 158 YDRYPEEFAKFTPDCD-NELQSCSKEELINAYDNSILYTDYVLSQIIERLK--KKDKDAALIYFSDHGESLGENGLYLHG 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1278866360 467 TPYmlAPEQQTHIPFMFWLSPDYAKNFGInaQCLRDyAAKNAVSQDNLFSTVLGMMDIK 525
Cdd:cd16017 235 APY--APKEQYHVPFIIWSSDSYKQRYPV--ERLRA-NKDRPFSHDNLFHTLLGLLGIK 288
|
|
| PRK09598 |
PRK09598 |
phosphoethanolamine--lipid A transferase EptA; |
1-541 |
2.65e-108 |
|
phosphoethanolamine--lipid A transferase EptA;
Pssm-ID: 236581 [Multi-domain] Cd Length: 522 Bit Score: 333.29 E-value: 2.65e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 1 MQLIKKLQCndikftLGCALFFTLLNGLFIQRSWAIIAPSHLHDILFAASVPVVLFCGWVIVFSLLNI--PYIRKPLLIV 78
Cdd:PRK09598 7 LKFLKPLSC------LQAGLLYSLLNGVLYHFPLFAYVYKESNQVSFIAMLVVLLFCVNGLLFLLLGLlsRRLMRLSAIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 79 LTVGCAAATYFMYTYGAVIDQNMIVNVFETNSQEATALVTPQMILWIVVAGLVPSVVLALTRIRTGKwwyalLTRVAAML 158
Cdd:PRK09598 81 FSLLNSIAFYFINTYKVFLNKSMMGNVLNTNTAESSGFLSVKLFIYIVVLGVLPGYIIYKIPLKNSS-----KKAPFAAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 159 GALlVIILIAALFY--KDYASLFRNNKSIVKMVTPANYVSAVVKYSKMRWFAgdQTLVRIGEDAHKGSliagqQKKTVLV 236
Cdd:PRK09598 156 LAL-VLIFLASAFAnsKNWLWFDKHAKFLGGLILPWSYSVNTFRVSAHKFFA--PTIKPLLPPLFSPN-----HSKSVVV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 237 LVVGEASRAANYSLNGYGRETNPELKKQD---VINFPQASSCGTETAVSVPCMFSGMTRSKYDADlarhqEGLLDVLRHA 313
Cdd:PRK09598 228 LVIGESARKHNYALYGYEKPTNPRLSKRLathELTLFNATSCATYTTASLECILDSSFKNTSNAY-----ENLPTYLTRA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 314 GVNLLWRDNDGGCKgacdRVPHTD-MTQWNLDQFCKDKSC-IDDVNFYRLDNVLDGVKQDTVLVI-HLMGSHGPAYYRRY 390
Cdd:PRK09598 303 GIKVFWRSANDGEP----NVKVTSyLKNYELIQKCPNCEApYDESLLYNLPELIKASSNENVLLIlHLAGSHGPNYDNKY 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 391 PDNFRKFTPTCDTNEIQDCDHQALMNTYDNTILYTDSMVSKTIDALKarQANMNTALIYLSDHGESLGESGIYLHGTPYM 470
Cdd:PRK09598 379 PLNFRVFKPVCSSVELSSCSKESLINAYDNTIFYNDYLLDKIISMLK--NLKQPALMIYLSDHGESLGEGAFYLHGIPKS 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278866360 471 LAPEQQTHIPFMFWLSPDYAKNFGInaqclrdYAAKNAVSQDNLFSTVLGMMDIK--SKVYQQQLDILNGCRQ 541
Cdd:PRK09598 457 IAPKEQYEIPFIVWASDSFKKQHSI-------IQTQTPINQNVIFHSVLGVFDFKnpSAVYRPSLDLFKHKKE 522
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
235-524 |
1.07e-68 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 223.07 E-value: 1.07e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 235 LVLVVGEASRAANYSLNGYGRETNPELKK--QDVINFPQASSCGTETAVSVPCMFSGMTRSKYDA------DLARHQEGL 306
Cdd:pfam00884 3 VVLVLGESLRAPDLGLYGYPRPTTPFLDRlaEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSyvstpvGLPRTEPSL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 307 LDVLRHAGVN--------LLWRDNDGGCK----GACDRVPHTDM--TQWNLDQFCKDKSCIDDVNFYRLDNVLDGVKQDT 372
Cdd:pfam00884 83 PDLLKRAGYNtgaigkwhLGWYNNQSPCNlgfdKFFGRNTGSDLyaDPPDVPYNCSGGGVSDEALLDEALEFLDNNDKPF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 373 VLVIHLMGSHGPAYY-RRYPDNFRKFTPtcdtneiQDCDHQALMNTYDNTILYTDSMVSKTIDALKARQANMNTALIYLS 451
Cdd:pfam00884 163 FLVLHTLGSHGPPYYpDRYPEKYATFKP-------SSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTS 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278866360 452 DHGESLGESGIYLHGTPYMLAPEQQTHIPFMFWLSPDYAKNfginaqclrdYAAKNAVSQDNLFSTVLGMMDI 524
Cdd:pfam00884 236 DHGESLGEGGGYLHGGKYDNAPEGGYRVPLLIWSPGGKAKG----------QKSEALVSHVDLFPTILDLAGI 298
|
|
| EptA_B_N |
pfam08019 |
Phosphoethanolamine transferase EptA/EptB; This entry represents a domain found in a group of ... |
55-205 |
7.05e-61 |
|
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: 197.36 E-value: 7.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 55 LFCGWVIVFSLLNIPYIRKPLLIVLTVGCAAATYFMYTYGAVIDQNMIVNVFETNSQEATALVTPQMILWIVVAGLVPSV 134
Cdd:pfam08019 1 LFAALNLLLSLLSWRYLLKPLLILLLLLSAAASYFMDTYGVVIDRDMIQNVLETDVAEASDLLSPKLLLYLLLLGVLPAL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1278866360 135 VLALTRIRTGKWWYALLTRVAAMLGALLVIILIAALFYKDYASLFRNNKSIVKMVTPANYVSAVVKYSKMR 205
Cdd:pfam08019 81 LLWRVRIRYRPWLRELLSRLALILVSLLVIGLVAFLFYKDYASFFRNHKELRYLINPTNYIYSTVKYAKHQ 151
|
|
| PRK11560 |
PRK11560 |
kdo(2)-lipid A phosphoethanolamine 7''-transferase; |
76-520 |
8.87e-40 |
|
kdo(2)-lipid A phosphoethanolamine 7''-transferase;
Pssm-ID: 183198 [Multi-domain] Cd Length: 558 Bit Score: 152.12 E-value: 8.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 76 LIVLTvgCAAATYFMYTYGAVIDQNMIVNVFETNSQEATALVTPQMILWIVVAGLVPSVVLALTRIR---------TGKW 146
Cdd:PRK11560 80 LLVLF--SAAASYYMTFFNVVIGYGIIASVMTTDIDLSKEVVGLHFILWLVAVSALPLILIWNNRCRytllrqlrtPGQR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 147 WYALLTRVAAmlgallVIILIAALFYKDYASLFRNNKSIVKMVT----------PANYVSAVVKYSKMRWfagdqtlvri 216
Cdd:PRK11560 158 IRSLAVVVLA------GLLVWAPIRLLDIQQKKVERATGVDLPSyggvvansylPSNWLSALGLYAWAQV---------- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 217 GEDAHKGSLIAGQQK----------KTVLVLVVGEASRAANYSLNGYGRETNPELKKQDVINFPQASSCGTETAVSVPCM 286
Cdd:PRK11560 222 DESSDNNSLLNPAKKftyqapkgvdDTYVVFIIGETTRWDHMGILGYERNTTPKLAQEKNLAAFRGYSCDTATKLSLRCM 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 287 F--SGMTrskyDADLAR--HQEGLLDVLRHAGVNL--------LWRDNdggcKGACDRVPHTDMTQwnLDQFCKDKScID 354
Cdd:PRK11560 302 FvrEGGA----EDNPQRtlKEQNVFAVLKQLGFSSelfamqseMWFYN----NTMADNYAYREQIG--AEPRNRGKP-VD 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 355 D---VNfyRLDNVLDGVKQDTVLVI-HLMGSHGpAYYRRYPDNFRKFTPTCdTNEIQDCDHQALMNTYDNTILYTDSMVS 430
Cdd:PRK11560 371 DmllVD--EMKQSLGRNPDGKHLIIlHTKGSHY-NYTQRYPRSFARYQPEC-IGVDSGCSKAQLINSYDNSVLYVDHFIS 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 431 KTIDALKARQAnmntALIYLSDHGESLGESGiYLHGTPYMLAPEQQTHIPFMFWLS------PDYAKNFginAQCLRDYA 504
Cdd:PRK11560 447 SVIDQLRDKKA----IVFYAADHGESINERE-HLHGTPREMAPPEQFRVPMMVWMSdkylanPDNAQAF---AQLKKQAD 518
|
490
....*....|....*.
gi 1278866360 505 AKNAVSQDNLFSTVLG 520
Cdd:PRK11560 519 MKVPRRHVELFDTILG 534
|
|
| PRK10649 |
PRK10649 |
phosphoethanolamine transferase CptA; |
51-489 |
4.90e-29 |
|
phosphoethanolamine transferase CptA;
Pssm-ID: 182617 [Multi-domain] Cd Length: 577 Bit Score: 120.97 E-value: 4.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 51 VPVVLFCGWVIVFSLLnipyirkpLLIVLTVGCAAATYFMYTYGAVIDQNMIVNVFETNSQEATALVTPQMILWIVVAGL 130
Cdd:PRK10649 58 IPVFLFPRRIRIIAAV--------IGVVLWAASLAALCYYVIYGQEFSQSVLFVMFETNTNEASEYLSQYFSLKIVLIAL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 131 VPSVVLAL--TRIRTGKW-WYALLTRVAAMLGALLVIILIAALFYKDyASLFRNNKSIVKMVTPANYVSAVVKYSKMRwf 207
Cdd:PRK10649 130 AYTAVAVLlwTRLRPVYIpWPWRYVVSFALLYGLILHPIAMNTFIKH-KPFEKTLDKLASRMEPAAPWQFLTGYYQYR-- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 208 agdQTLVRIGEDAHKGSLIA---------GQQKKTvLVLVVGEASRAANYSLNGYGRETNPELKK-----------QDVI 267
Cdd:PRK10649 207 ---QQLNSLQKLLNENAALPplanlkdesGNAPRT-LVLVIGESTQRGRMSLYGYPRETTPELDAlhktdpgltvfNNVV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 268 nfpqasscgTETAVSVPCMFSGMTRSKYDA-DLARHQEGLLDVLRHAGVNLLWRDNdggckgacdrvpHTDMTQWN--LD 344
Cdd:PRK10649 283 ---------TSRPYTIEILQQALTFADEKNpDLYLTQPSLMNMMKQAGYKTFWITN------------QQTMTARNtmLT 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 345 QFCKDKSC--------------IDDVNFYRLDNVLDGVKQDTVLVIHLMGSHgPAYYRRYPDNFRKFTPTCDTNEIQDCD 410
Cdd:PRK10649 342 VFSRQTDKqyymnqqrtqnareYDTNVLKPFSEVLADPAPKKFIIVHLLGTH-IKYKYRYPENQGKFDDRTGHVPPGLNA 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 411 HQA-LMNTYDNTILYTDSMVSKTIDALKArqANMNTALIYLSDHGESLGESGIYL-----HGTP--YMLApeqqthIPFM 482
Cdd:PRK10649 421 DELeSYNDYDNANLYNDHVVASLIKDFKA--TDPNGFLVYFSDHGEEVYDTPPHKtqgrnEDNPtrHMYT------IPFL 492
|
....*..
gi 1278866360 483 FWLSPDY 489
Cdd:PRK10649 493 LWTSEKW 499
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
14-531 |
4.43e-18 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 87.40 E-value: 4.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 14 FTLGCALFFTLLNGLFIQRSWAI--IAPSHLHDILFAASVPVVL-FCGWVIVFSLLNIPYIRKP-----LLIVLTVGCAA 85
Cdd:COG1368 2 FLLFLLLLSLRLVFLLFNFDLSLgeILQAFLYGLRFILYLLLLLlLLLLLLLPLLFRRPKLRWIylllvLLLLLLLLVAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 86 ATYFMYtYGAVIDQNMIVNVFETNSQEATALVTPQMILWIVVAGLVPSVVLALTRIRTGKWWYALLTRVAAMLGALLVII 165
Cdd:COG1368 82 ILYYRF-FGDRLNFSDLDYLGDTGEVLGSLLSSYDLLLLLDLLLLLLLLLLLYRLLKKLRKSLPWRKRLALLLLLLALLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 166 LIAALFYKDYASLFR--NNKSIVKM--VTPANYVSAVVKYSKMRWFAGDQTLVRIG---EDAHKGSLIAGQQKKTVLVLV 238
Cdd:COG1368 161 LGIRLGEDRPLNLSDafSRNNFVNElgLNGPYSFYDALRNNKAPATYSEEEALEIKkylKSNRPTPNPFGPAKKPNVVVI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 239 VGEaSRAANY-SLNGYGRETNPELKK--QDVINFPQASSCGTETAVSVPCMFSGMT----RSKYDADLARHQEGLLDVLR 311
Cdd:COG1368 241 LLE-SFSDFFiGALGNGKDVTPFLDSlaKESLYFGNFYSQGGRTSRGEFAVLTGLPplpgGSPYKRPGQNNFPSLPSILK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 312 HAGvnllwrdndggckgacdrvPHT------DMTQWNLDQFCK--------DKSCI-----------DDVNFYRLDNVLD 366
Cdd:COG1368 320 KQG-------------------YETsffhggDGSFWNRDSFYKnlgfdefyDREDFddpfdggwgvsDEDLFDKALEELE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 367 GVKQDTVLVIHLMGSHGPayYRrYPDNFRKFTPTCDTNeiqdcdhqalMNTYDNTILYTDSMVSKTIDALKARQANMNTA 446
Cdd:COG1368 381 KLKKPFFAFLITLSNHGP--YT-LPEEDKKIPDYGKTT----------LNNYLNAVRYADQALGEFIEKLKKSGWYDNTI 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 447 LIYLSDHGESLGESgiylhgTPYMLAPEQQtHIPFMFWlSPDYAKNFGINaqclrdyaakNAVSQDNLFSTVLGMMDIKS 526
Cdd:COG1368 448 FVIYGDHGPRSPGK------TDYENPLERY-RVPLLIY-SPGLKKPKVID----------TVGSQIDIAPTLLDLLGIDY 509
|
....*
gi 1278866360 527 KVYQQ 531
Cdd:COG1368 510 PSYYA 514
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
234-529 |
6.94e-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: 80.67 E-value: 6.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 234 VLVLVVgEASRAANYSLNGYGRETNPELKK--QDVINFPQASSCGTETAVSVPCMFSGMTRSKYDA---DLARHQEGLLD 308
Cdd:cd16148 3 VILIVI-DSLRADHLGCYGYDRVTTPNLDRlaAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVwggPLEPDDPTLAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 309 VLRHAGV------------------------NLLWRDNDGGCKGACDRVPHT--DMTQWnLDQFCKDKsciddvNFYrld 362
Cdd:cd16148 82 ILRKAGYytaavssnphlfggpgfdrgfdtfEDFRGQEGDPGEEGDERAERVtdRALEW-LDRNADDD------PFF--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 363 nvldgvkqdtvLVIHLMGSHGPayYRrypdnfrkftptcdtneiqdcdhqalmntYDNTILYTDSMVSKTIDALKARQAN 442
Cdd:cd16148 152 -----------LFLHYFDPHEP--YL-----------------------------YDAEVRYVDEQIGRLLDKLKELGLL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 443 MNTALIYLSDHGESLGESGIYL--HGTPYmlapEQQTHIPFMFWLsPDYAKNFGINAQclrdyaaknaVSQDNLFSTVLG 520
Cdd:cd16148 190 EDTLVIVTSDHGEEFGEHGLYWghGSNLY----DEQLHVPLIIRW-PGKEPGKRVDAL----------VSHIDIAPTLLD 254
|
....*....
gi 1278866360 521 MMDIKSKVY 529
Cdd:cd16148 255 LLGVEPPDY 263
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
235-522 |
7.23e-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: 59.36 E-value: 7.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 235 LVLVVGEASRAANYSLNGYGRETNPELKKQDvINFP----QASSCGTETAVSVPCMFSGmtRSKYDADLARHQEGLLDVL 310
Cdd:cd00016 3 VVLIVLDGLGADDLGKAGNPAPTTPNLKRLA-SEGAtfnfRSVSPPTSSAPNHAALLTG--AYPTLHGYTGNGSADPELP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 311 RHAGvnllwrdndgGCKGACDRVPHTdMTQWNLDQfckdksciddVNFYRLDNV-LDGVKQDTVLVIHLMGSHGPAYYRR 389
Cdd:cd00016 80 SRAA----------GKDEDGPTIPEL-LKQAGYRT----------GVIGLLKAIdETSKEKPFVLFLHFDGPDGPGHAYG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 390 ypdnfrkftptcdtneiqdcdhqALMNTYDNTILYTDSMVSKTIDALK-ARQANmNTALIYLSDHGESLGESGIYLHGTP 468
Cdd:cd00016 139 -----------------------PNTPEYYDAVEEIDERIGKVLDALKkAGDAD-DTVIIVTADHGGIDKGHGGDPKADG 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1278866360 469 YMLAPEQQTHIPFMFWlSPdYAKNFGINaqclrdyaaKNAVSQDNLFSTVLGMM 522
Cdd:cd00016 195 KADKSHTGMRVPFIAY-GP-GVKKGGVK---------HELISQYDIAPTLADLL 237
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
374-484 |
2.46e-09 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 59.12 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 374 LVIHLMGSHGP-----AYYRRYPDNFRKFTPTCDTNEIQDCDHQALMNTYDNTILYTDSMVSKTIDALKARQANMNTALI 448
Cdd:COG3119 153 LYLAFNAPHAPyqapeEYLDKYDGKDIPLPPNLAPRDLTEEELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVV 232
|
90 100 110
....*....|....*....|....*....|....*..
gi 1278866360 449 YLSDHGESLGESGIYLH-GTPYmlapEQQTHIPFMFW 484
Cdd:COG3119 233 FTSDNGPSLGEHGLRGGkGTLY----EGGIRVPLIVR 265
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
379-523 |
4.71e-08 |
|
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: 54.61 E-value: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 379 MGSHGPayYRRYPDNFRKFTPTCDTNEIqdcdhqalMNTYDNTILYTDSMVSKTIDALKARQANMNTALIYLSDHGeslg 458
Cdd:cd16015 165 MSNHGP--YDLPEEKKDEPLKVEEDKTE--------LENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHL---- 230
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278866360 459 eSGIYLHGTPYMLAPEQQTHIPFMFWlSPDYAKNFGINaqclrdyaakNAVSQDNLFSTVLGMMD 523
Cdd:cd16015 231 -PSLGSDYDETDEDPLDLYRTPLLIY-SPGLKKPKKID----------RVGSQIDIAPTLLDLLG 283
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
424-492 |
2.15e-07 |
|
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: 52.93 E-value: 2.15e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 424 YTDSMVSKTIDALKA-RQANmNTALIYLSDHGESLGESGIYLHGTPYmlapEQQTHIPFMFWlSPDYAKN 492
Cdd:cd16037 170 FLDENIGRVLDALEElGLLD-NTLIIYTSDHGDMLGERGLWGKSTMY----EESVRVPMIIS-GPGIPAG 233
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
384-483 |
7.90e-07 |
|
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: 51.45 E-value: 7.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 384 PAYYRRYPDNFRKFTptcDTNEiqdcDHQALMNTYDNTILYTDSMVSKTIDALKARQANMNTALIYLSDHGESLGESGIY 463
Cdd:cd16033 192 PYIYRRERKRWGVDT---EDEE----DWKEIIAHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLW 264
|
90 100
....*....|....*....|
gi 1278866360 464 LHGtPYMlaPEQQTHIPFMF 483
Cdd:cd16033 265 DKG-PFM--YEETYRIPLII 281
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
426-525 |
9.15e-07 |
|
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: 51.42 E-value: 9.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 426 DSMVSKTIDALKARQANMNTALIYLSDHGESLGESGIYLHGTPYmlapEQQTHIPFMF-WlsPDYAKNFGINAQCLrdya 504
Cdd:cd16034 237 DDNIGRLLDALKELGLLENTIVVFTSDHGDMLGSHGLMNKQVPY----EESIRVPFIIrY--PGKIKAGRVVDLLI---- 306
|
90 100
....*....|....*....|.
gi 1278866360 505 akNAVsqDnLFSTVLGMMDIK 525
Cdd:cd16034 307 --NTV--D-IMPTLLGLCGLP 322
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
424-525 |
1.03e-06 |
|
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: 51.23 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 424 YTDSMVSKTIDALKARQANmnTALIYLSDHGESLGESGIYLHGtPYMLapEQQTHIPFMFWlSPDYAKNFGINaqclrdy 503
Cdd:cd16156 249 FVDYEIGRVLDAADEIAED--AWVIYTSDHGDMLGAHKLWAKG-PAVY--DEITNIPLIIR-GKGGEKAGTVT------- 315
|
90 100
....*....|....*....|..
gi 1278866360 504 aaKNAVSQDNLFSTVLGMMDIK 525
Cdd:cd16156 316 --DTPVSHIDLAPTILDYAGIP 335
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
416-499 |
2.20e-06 |
|
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: 49.51 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 416 NTYDNTILYTDSMVSKTIDALKARQANMNTALIYLSDHGESLGESGiyLHGTPYMlAPEQQTHIPFmFWLSPDYaknFGI 495
Cdd:cd16035 167 NFYYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHG--LRGKGFN-AYEEALHVPL-IISHPDL---FGT 239
|
....
gi 1278866360 496 NAQC 499
Cdd:cd16035 240 GQTT 243
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
422-484 |
2.87e-05 |
|
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: 45.51 E-value: 2.87e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278866360 422 ILYTDSMVSKTIDALKAR-QANmNTALIYLSDHGESLGESGIYL-HGTPYmlapEQQTHIPFMFW 484
Cdd:cd16022 137 VSAIDDQIGRILDALEELgLLD-NTLIVFTSDHGDMLGDHGLRGkKGSLY----EGGIRVPFIVR 196
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
418-481 |
2.01e-04 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 43.89 E-value: 2.01e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278866360 418 YDNTILYTDSMVSKTIDALKARQANMNTALIYLSDHGESLGESGIYLHGTPYmlapEQQTHIPF 481
Cdd:PRK13759 270 YYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHGDMLGDHYLFRKGYPY----EGSAHIPF 329
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
381-482 |
3.02e-04 |
|
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficiency of N-acetylglucosamine-6-sulfatase results in the disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease.
Pssm-ID: 293755 [Multi-domain] Cd Length: 429 Bit Score: 43.29 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 381 SHGPAYYRRYPDNFRKFTPTC--------DTNEiqdcDHQALMNTYDNTILYTDSMVSKTIDALKARQANMNTALIYLSD 452
Cdd:cd16031 198 TFDDDDYAGRPEWAREQRNRIrgvldgrfDTPE----KYQRYMKDYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSD 273
|
90 100 110
....*....|....*....|....*....|....*
gi 1278866360 453 HGESLGEsgiylHG-----TPYmlapEQQTHIPFM 482
Cdd:cd16031 274 NGFFLGE-----HGlfdkrLMY----EESIRVPLI 299
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
424-491 |
3.80e-04 |
|
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the hydrolysis of sulfate ester bonds from a wide variety of substrates, including steroids, carbohydrates and proteins. Iduronate 2-sulfatase is required for the lysosomal degradation of heparan sulfate and dermatan sulfate. Mutations in the iduronate 2-sulfatase gene that result in enzymatic deficiency lead to the sex-linked mucopolysaccharidosis type II, also known as Hunter syndrome.
Pssm-ID: 293754 [Multi-domain] Cd Length: 435 Bit Score: 42.95 E-value: 3.80e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278866360 424 YTDSMVSKTIDALKARQANMNTALIYLSDHGESLGEsgiylHG-----TPYmlapEQQTHIPFMFWlSPDYAK 491
Cdd:cd16030 269 YVDAQVGRVLDALEELGLADNTIVVLWSDHGWHLGE-----HGhwgkhTLF----EEATRVPLIIR-APGVTK 331
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
418-483 |
1.11e-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: 1.11e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278866360 418 YDNTILYTDSMVSKTIDALK-ARQANmNTALIYLSDHGESLGESGIYLHGTPYmlapEQQTHIPFMF 483
Cdd:cd16032 166 YYGMVSYVDDKVGQLLDTLErTGLAD-DTIVIFTSDHGDMLGERGLWYKMSFF----EGSARVPLII 227
|
|
| GPI_EPT_1 |
cd16020 |
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ... |
326-484 |
1.96e-03 |
|
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.
Pssm-ID: 293744 Cd Length: 294 Bit Score: 40.26 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 326 CKGACDRVPHTDMTQWNlDQFCKDKSCIDDVNFYRLDNVLDGVKQDT---------VLVIHLMGshgpayyrrypdnfrk 396
Cdd:cd16020 104 PKGATGGKVLTYIYPEE-DFDSTDASELDEWVFDKVEEFLANASSNKtellnqdglVFFLHLLG---------------- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278866360 397 ftptCDTNEIQdcdHQALMNTYDNTILYTDSMVSKTIDALKARQANMNTALIYLSDHGESlgesgiyLHGTPYMLAPeQQ 476
Cdd:cd16020 167 ----LDTNGHA---HKPYSKEYLENIRYVDKGIEKTYPLIEEYFNDGRTAYIFTSDHGMT-------DWGSHGDGSP-DE 231
|
....*...
gi 1278866360 477 THIPFMFW 484
Cdd:cd16020 232 TETPFIAW 239
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
424-491 |
3.43e-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: 39.67 E-value: 3.43e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1278866360 424 YTDSMVSKTIDALKA--RQANMNTALIYL-SDHGESLGESGIYLHGTPYmlapEQQTHIPFMFwLSPDYAK 491
Cdd:cd16153 176 YGDAQVGRAVEAFKAysLKQDRDYTIVYVtGDHGWHLGEQGILAKFTFW----PQSHRVPLIV-VSSDKLK 241
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
417-462 |
5.70e-03 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 39.14 E-value: 5.70e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1278866360 417 TYDNTILYTDSMVSKTIDALKARQANMNTALIYLSDHGESLGESGI 462
Cdd:cd16150 201 TYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHGDYTGDYGL 246
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
418-484 |
8.44e-03 |
|
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) belongs to the sulfatase family and catalyses the cleavage of N-linked sulfate groups from the GAGs heparin sulfate and heparin. The active site is characterized by the amino-acid sequence motif C(X)PSR that is highly conserved among most sulfatases. The cysteine residue is post-translationally converted to a formylglycine (FGly) residue, which is crucial for the catalytic process. Loss of function of SGSH results a disease called mucopolysaccharidosis type IIIA (Sanfilippo A syndrome), a fatal childhood-onset neurodegenerative disease with mild facial, visceral and skeletal abnormalities.
Pssm-ID: 293751 [Multi-domain] Cd Length: 373 Bit Score: 38.64 E-value: 8.44e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278866360 418 YDNTILYTDSMVSKTIDALKAR-QANmNTALIYLSDHGE-------SLGESGIylhgtpymlapeqqtHIPFMFW 484
Cdd:cd16027 191 YYDEIERLDQQVGEILDELEEDgLLD-NTIVIFTSDHGMpfprakgTLYDSGL---------------RVPLIVR 249
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|
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