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Conserved domains on  [gi|1550155691|gb|RVO36572|]
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phosphoethanolamine transferase [Sinorhizobium meliloti]

Protein Classification

phosphoethanolamine transferase( domain architecture ID 11450875)

phosphoethanolamine transferase similar to Escherichia coli OpgE, which catalyzes the addition of a phosphoethanolamine moiety to the osmoregulated periplasmic glucan (OPG) backbone

EC:  2.7.-.-
Gene Ontology:  GO:0005886|GO:0016776|GO:1900727|GO:0008484|GO:0009244

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
OpgE COG2194
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall ...
 17-552 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: 695.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691  17 RIPRPEIGSISLSAIVALYLLLATNNSFWAHASVYFVHARTSLLAFAAALYLALFAIL---TPLSVKYLMKPALVILILV 93
Cdd:COG2194     1 KFLLPRLSPLKLILLLALYFALFLNLPFWGRLLAILPLDGVNLLFLLSLPLLLLAALNlllSLLAWRYLFKPLLILLLLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691  94 SATAAYFADTFGIIIDRDMIGNAAVTTQAEASHLLTFSLARHLLVYAVLPSILIVWVRVRHRRFLPKAAVNFAFVSVSLL 173
Cdd:COG2194    81 SAAASYFMDFYGVVIDYGMIQNVLETDPAEASELLSPKLILWLLLLGVLPALLLWRVRIRYRPLLRELGQRLALLLLALL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 174 VGAGLIYANFATVAYALREHTDLMKRFNPSGPLIATVRYGLSTYRERNLVVRPLGTDAHQgarVAAAGKPVVVVVVAGET 253
Cdd:COG2194   161 VIVLLALLFYKDYASFFRNHKELRYLINPSNFIYALGKYAKARYFAAPLPLQPLGADAKL---AAAGAKPTLVVLVVGET 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 254 ARAMNFSLNGYERETNPELKALR-VVNYRNTTSCGTATAVSLPCMFSVYPRSQYSDWKARSTENLVNVLTRAGVSVSWWD 332
Cdd:COG2194   238 ARADNFSLNGYARDTTPELAKEKnLVSFRDVTSCGTATAVSVPCMFSRLGRADYDPQRALNQENLLDVLQRAGVKVLWRD 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 333 NNTGSKGIADLISFASQTGRKNSPLCNNGECLDEILLGDLDRKLGAAISNSVIVLHQLGSHGPSYYLRYPAAFRRFTPDC 412
Cdd:COG2194   318 NQSGCKGVCDRVPTIDLTADNLPPLCDGGECLDEVLLDGLDEALADLAGDKLIVLHQMGSHGPAYYKRYPPEFRKFTPTC 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 413 RTPELMRCSTAELVNAYDNTILYTDHILASVARLLEKHQDRIAGAMIYMSDHGESLGENGLYLHGAPYVIAPKEQTQVPF 492
Cdd:COG2194   398 DTNDLQNCSREELVNAYDNTILYTDYVLSQVIDLLKAKQDRYDTAMLYVSDHGESLGENGLYLHGTPYAIAPDEQTHVPM 477

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 493 IAWFSEPYQAAMGVDAGCLAKDADKPKSHDNLFHTVLGMMDVETRVYNRDLDAFAACTRP 552
Cdd:COG2194   478 IMWLSDGYAQRYGIDFACLKARADKPYSHDNLFHTLLGLLDVRTSVYDPELDILAPCRRA 537
 
Name Accession Description Interval E-value
OpgE COG2194
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall ...
 17-552 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: 695.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691  17 RIPRPEIGSISLSAIVALYLLLATNNSFWAHASVYFVHARTSLLAFAAALYLALFAIL---TPLSVKYLMKPALVILILV 93
Cdd:COG2194     1 KFLLPRLSPLKLILLLALYFALFLNLPFWGRLLAILPLDGVNLLFLLSLPLLLLAALNlllSLLAWRYLFKPLLILLLLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691  94 SATAAYFADTFGIIIDRDMIGNAAVTTQAEASHLLTFSLARHLLVYAVLPSILIVWVRVRHRRFLPKAAVNFAFVSVSLL 173
Cdd:COG2194    81 SAAASYFMDFYGVVIDYGMIQNVLETDPAEASELLSPKLILWLLLLGVLPALLLWRVRIRYRPLLRELGQRLALLLLALL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 174 VGAGLIYANFATVAYALREHTDLMKRFNPSGPLIATVRYGLSTYRERNLVVRPLGTDAHQgarVAAAGKPVVVVVVAGET 253
Cdd:COG2194   161 VIVLLALLFYKDYASFFRNHKELRYLINPSNFIYALGKYAKARYFAAPLPLQPLGADAKL---AAAGAKPTLVVLVVGET 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 254 ARAMNFSLNGYERETNPELKALR-VVNYRNTTSCGTATAVSLPCMFSVYPRSQYSDWKARSTENLVNVLTRAGVSVSWWD 332
Cdd:COG2194   238 ARADNFSLNGYARDTTPELAKEKnLVSFRDVTSCGTATAVSVPCMFSRLGRADYDPQRALNQENLLDVLQRAGVKVLWRD 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 333 NNTGSKGIADLISFASQTGRKNSPLCNNGECLDEILLGDLDRKLGAAISNSVIVLHQLGSHGPSYYLRYPAAFRRFTPDC 412
Cdd:COG2194   318 NQSGCKGVCDRVPTIDLTADNLPPLCDGGECLDEVLLDGLDEALADLAGDKLIVLHQMGSHGPAYYKRYPPEFRKFTPTC 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 413 RTPELMRCSTAELVNAYDNTILYTDHILASVARLLEKHQDRIAGAMIYMSDHGESLGENGLYLHGAPYVIAPKEQTQVPF 492
Cdd:COG2194   398 DTNDLQNCSREELVNAYDNTILYTDYVLSQVIDLLKAKQDRYDTAMLYVSDHGESLGENGLYLHGTPYAIAPDEQTHVPM 477

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 493 IAWFSEPYQAAMGVDAGCLAKDADKPKSHDNLFHTVLGMMDVETRVYNRDLDAFAACTRP 552
Cdd:COG2194   478 IMWLSDGYAQRYGIDFACLKARADKPYSHDNLFHTLLGLLDVRTSVYDPELDILAPCRRA 537
PRK11598 PRK11598
putative metal dependent hydrolase; Provisional
 15-553 5.80e-174

putative metal dependent hydrolase; Provisional


Pssm-ID: 183224 [Multi-domain]  Cd Length: 545  Bit Score: 504.21  E-value: 5.80e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691  15 IPRIPRPEIGSISLSAIVALYLLLATNNSF----WAHASVYFVHARTSLLAFAAALYLALFAILTPLSVKYLMKPALVIL 90
Cdd:PRK11598    2 KRLLKRPSLNLLTFLLLAAFYITLCLNIAFykqvLQLLPLDSLHNVLVFASMPVVAFSVINIVFTLLSFPWLRRPLACLF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691  91 ILVSATAAYFADTFGIIIDRDMIGNAAVTTQAEASHLLTFSLARHLLVYAVLPSILIVWVRVRHRRFLPKAAV-NFAFVS 169
Cdd:PRK11598   82 ILVGAAAQYFMMTYGIVIDRSMIQNIFETTPAESFALMTPQMLLWLGLSGVLPALIACWIKIRPATPRWRSVLfRLANIL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 170 VSLLV---GAGLIYANFATVayaLREHTDLMKRFNPSGPLIATVRYglstYRERNLVVRPL---GTDAHQGARVAAAGKP 243
Cdd:PRK11598  162 VSVLLillVAALFYKDYASL---FRNNKELVKSLTPSNSIVASWSW----YSHQRLANLPLvriGEDAHKNPLMQNQKRK 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 244 VVVVVVAGETARAMNFSLNGYERETNPELKALRVVNYRNTTSCGTATAVSLPCMFSVYPRSQYSDWKARSTENLVNVLTR 323
Cdd:PRK11598  235 NLTILVVGETSRAENFSLGGYPRETNPRLAKDNVIYFPHTTSCGTATAVSVPCMFSNMPRKHYDEELAHHQEGLLDIIQR 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 324 AGVSVSWWDNNTGSKGIADLISFASQTGRKNSPLCNNGECLDEILLGDLDRKLGAAISNSVIVLHQLGSHGPSYYLRYPA 403
Cdd:PRK11598  315 AGINVLWNDNDGGCKGACDRVPHQDVTALNLPGQCIDGECYDEVLFHGLENYINNLQGDGVIVLHTIGSHGPTYYNRYPP 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 404 AFRRFTPDCRTPELMRCSTAELVNAYDNTILYTDHILASVARLLEKHQDRIAGAMIYMSDHGESLGENGLYLHGAPYVIA 483
Cdd:PRK11598  395 QFRKFTPTCDTNEIQTCTQQQLVNTYDNTILYVDYIVDKAINLLKQHQDKFNTSLVYLSDHGESLGENGIYLHGLPYAIA 474

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1550155691 484 PKEQTQVPFIAWFSEPYQAAMGVDAGCLAKDADKPK-SHDNLFHTVLGMMDVETRVYNRDLDAFAACTRPA 553
Cdd:PRK11598  475 PDQQTHVPMLLWLSPDYQKRYGVDQQCLQKQAQTQDySQDNLFSTLLGLTGVQTKEYQAADDILQPCRRLS 545
LptA cd16017
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ...
 251-535 9.15e-120

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: 355.78  E-value: 9.15e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 251 GETARAMNFSLNGYERETNPELKALR--VVNYRNTTSCGTATAVSLPCMFSVYPRSQYSDWKarSTENLVNVLTRAGVSV 328
Cdd:cd16017    10 GESARRDHMSLYGYPRDTTPFLSKLKknLIVFDNVISCGTSTAVSLPCMLSFANRENYDRAY--YQENLIDLAKKAGYKT 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 329 SWWDNNTGSKGIADLISFASQTGR--KNSPLCNNGECLDEILLGDLDRKLGAAISNSVIVLHQLGSHGPsYYLRYPAAFR 406
Cdd:cd16017    88 YWISNQGGCGGYDTRISAIAKIETvfTNKGSCNSSNCYDEALLPLLDEALADSSKKKLIVLHLMGSHGP-YYDRYPEEFA 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 407 RFTPDCrTPELMRCSTAELVNAYDNTILYTDHILASVARLLEKHQDRiaGAMIYMSDHGESLGENGLYLHGAPYviAPKE 486
Cdd:cd16017   167 KFTPDC-DNELQSCSKEELINAYDNSILYTDYVLSQIIERLKKKDKD--AALIYFSDHGESLGENGLYLHGAPY--APKE 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1550155691 487 QTQVPFIAWFSEPYQAAMGVDagCLAKDADKPKSHDNLFHTVLGMMDVE 535
Cdd:cd16017   242 QYHVPFIIWSSDSYKQRYPVE--RLRANKDRPFSHDNLFHTLLGLLGIK 288
Sulfatase pfam00884
Sulfatase;
251-534 9.17e-62

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 206.12  E-value: 9.17e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 251 GETARAMNFSLNGYERETNPELKALR--VVNYRNTTSCGTATAVSLPCMFSVYPRSQYSDW------KARSTENLVNVLT 322
Cdd:pfam00884   8 GESLRAPDLGLYGYPRPTTPFLDRLAeeGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYvstpvgLPRTEPSLPDLLK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 323 RAGV--------SVSWWDNNTGSKGIADLIsFASQTGR-------KNSPLCNNGECLDEILLGDLDRKLGAAISNSVIVL 387
Cdd:pfam00884  88 RAGYntgaigkwHLGWYNNQSPCNLGFDKF-FGRNTGSdlyadppDVPYNCSGGGVSDEALLDEALEFLDNNDKPFFLVL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 388 HQLGSHGPSYYL-RYPAAFRRFTPDcrtpelmRCSTAELVNAYDNTILYTDHILASVARLLEKHQDRIAGAMIYMSDHGE 466
Cdd:pfam00884 167 HTLGSHGPPYYPdRYPEKYATFKPS-------SCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGE 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1550155691 467 SLGENGLYLHGAPYVIAPKEQTQVPFIAWFSEPYQAAMGVDAgclakdadkPKSHDNLFHTVLGMMDV 534
Cdd:pfam00884 240 SLGEGGGYLHGGKYDNAPEGGYRVPLLIWSPGGKAKGQKSEA---------LVSHVDLFPTILDLAGI 298
 
Name Accession Description Interval E-value
OpgE COG2194
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall ...
 17-552 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: 695.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691  17 RIPRPEIGSISLSAIVALYLLLATNNSFWAHASVYFVHARTSLLAFAAALYLALFAIL---TPLSVKYLMKPALVILILV 93
Cdd:COG2194     1 KFLLPRLSPLKLILLLALYFALFLNLPFWGRLLAILPLDGVNLLFLLSLPLLLLAALNlllSLLAWRYLFKPLLILLLLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691  94 SATAAYFADTFGIIIDRDMIGNAAVTTQAEASHLLTFSLARHLLVYAVLPSILIVWVRVRHRRFLPKAAVNFAFVSVSLL 173
Cdd:COG2194    81 SAAASYFMDFYGVVIDYGMIQNVLETDPAEASELLSPKLILWLLLLGVLPALLLWRVRIRYRPLLRELGQRLALLLLALL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 174 VGAGLIYANFATVAYALREHTDLMKRFNPSGPLIATVRYGLSTYRERNLVVRPLGTDAHQgarVAAAGKPVVVVVVAGET 253
Cdd:COG2194   161 VIVLLALLFYKDYASFFRNHKELRYLINPSNFIYALGKYAKARYFAAPLPLQPLGADAKL---AAAGAKPTLVVLVVGET 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 254 ARAMNFSLNGYERETNPELKALR-VVNYRNTTSCGTATAVSLPCMFSVYPRSQYSDWKARSTENLVNVLTRAGVSVSWWD 332
Cdd:COG2194   238 ARADNFSLNGYARDTTPELAKEKnLVSFRDVTSCGTATAVSVPCMFSRLGRADYDPQRALNQENLLDVLQRAGVKVLWRD 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 333 NNTGSKGIADLISFASQTGRKNSPLCNNGECLDEILLGDLDRKLGAAISNSVIVLHQLGSHGPSYYLRYPAAFRRFTPDC 412
Cdd:COG2194   318 NQSGCKGVCDRVPTIDLTADNLPPLCDGGECLDEVLLDGLDEALADLAGDKLIVLHQMGSHGPAYYKRYPPEFRKFTPTC 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 413 RTPELMRCSTAELVNAYDNTILYTDHILASVARLLEKHQDRIAGAMIYMSDHGESLGENGLYLHGAPYVIAPKEQTQVPF 492
Cdd:COG2194   398 DTNDLQNCSREELVNAYDNTILYTDYVLSQVIDLLKAKQDRYDTAMLYVSDHGESLGENGLYLHGTPYAIAPDEQTHVPM 477

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 493 IAWFSEPYQAAMGVDAGCLAKDADKPKSHDNLFHTVLGMMDVETRVYNRDLDAFAACTRP 552
Cdd:COG2194   478 IMWLSDGYAQRYGIDFACLKARADKPYSHDNLFHTLLGLLDVRTSVYDPELDILAPCRRA 537
PRK11598 PRK11598
putative metal dependent hydrolase; Provisional
 15-553 5.80e-174

putative metal dependent hydrolase; Provisional


Pssm-ID: 183224 [Multi-domain]  Cd Length: 545  Bit Score: 504.21  E-value: 5.80e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691  15 IPRIPRPEIGSISLSAIVALYLLLATNNSF----WAHASVYFVHARTSLLAFAAALYLALFAILTPLSVKYLMKPALVIL 90
Cdd:PRK11598    2 KRLLKRPSLNLLTFLLLAAFYITLCLNIAFykqvLQLLPLDSLHNVLVFASMPVVAFSVINIVFTLLSFPWLRRPLACLF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691  91 ILVSATAAYFADTFGIIIDRDMIGNAAVTTQAEASHLLTFSLARHLLVYAVLPSILIVWVRVRHRRFLPKAAV-NFAFVS 169
Cdd:PRK11598   82 ILVGAAAQYFMMTYGIVIDRSMIQNIFETTPAESFALMTPQMLLWLGLSGVLPALIACWIKIRPATPRWRSVLfRLANIL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 170 VSLLV---GAGLIYANFATVayaLREHTDLMKRFNPSGPLIATVRYglstYRERNLVVRPL---GTDAHQGARVAAAGKP 243
Cdd:PRK11598  162 VSVLLillVAALFYKDYASL---FRNNKELVKSLTPSNSIVASWSW----YSHQRLANLPLvriGEDAHKNPLMQNQKRK 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 244 VVVVVVAGETARAMNFSLNGYERETNPELKALRVVNYRNTTSCGTATAVSLPCMFSVYPRSQYSDWKARSTENLVNVLTR 323
Cdd:PRK11598  235 NLTILVVGETSRAENFSLGGYPRETNPRLAKDNVIYFPHTTSCGTATAVSVPCMFSNMPRKHYDEELAHHQEGLLDIIQR 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 324 AGVSVSWWDNNTGSKGIADLISFASQTGRKNSPLCNNGECLDEILLGDLDRKLGAAISNSVIVLHQLGSHGPSYYLRYPA 403
Cdd:PRK11598  315 AGINVLWNDNDGGCKGACDRVPHQDVTALNLPGQCIDGECYDEVLFHGLENYINNLQGDGVIVLHTIGSHGPTYYNRYPP 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 404 AFRRFTPDCRTPELMRCSTAELVNAYDNTILYTDHILASVARLLEKHQDRIAGAMIYMSDHGESLGENGLYLHGAPYVIA 483
Cdd:PRK11598  395 QFRKFTPTCDTNEIQTCTQQQLVNTYDNTILYVDYIVDKAINLLKQHQDKFNTSLVYLSDHGESLGENGIYLHGLPYAIA 474

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1550155691 484 PKEQTQVPFIAWFSEPYQAAMGVDAGCLAKDADKPK-SHDNLFHTVLGMMDVETRVYNRDLDAFAACTRPA 553
Cdd:PRK11598  475 PDQQTHVPMLLWLSPDYQKRYGVDQQCLQKQAQTQDySQDNLFSTLLGLTGVQTKEYQAADDILQPCRRLS 545
LptA cd16017
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ...
 251-535 9.15e-120

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: 355.78  E-value: 9.15e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 251 GETARAMNFSLNGYERETNPELKALR--VVNYRNTTSCGTATAVSLPCMFSVYPRSQYSDWKarSTENLVNVLTRAGVSV 328
Cdd:cd16017    10 GESARRDHMSLYGYPRDTTPFLSKLKknLIVFDNVISCGTSTAVSLPCMLSFANRENYDRAY--YQENLIDLAKKAGYKT 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 329 SWWDNNTGSKGIADLISFASQTGR--KNSPLCNNGECLDEILLGDLDRKLGAAISNSVIVLHQLGSHGPsYYLRYPAAFR 406
Cdd:cd16017    88 YWISNQGGCGGYDTRISAIAKIETvfTNKGSCNSSNCYDEALLPLLDEALADSSKKKLIVLHLMGSHGP-YYDRYPEEFA 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 407 RFTPDCrTPELMRCSTAELVNAYDNTILYTDHILASVARLLEKHQDRiaGAMIYMSDHGESLGENGLYLHGAPYviAPKE 486
Cdd:cd16017   167 KFTPDC-DNELQSCSKEELINAYDNSILYTDYVLSQIIERLKKKDKD--AALIYFSDHGESLGENGLYLHGAPY--APKE 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1550155691 487 QTQVPFIAWFSEPYQAAMGVDagCLAKDADKPKSHDNLFHTVLGMMDVE 535
Cdd:cd16017   242 QYHVPFIIWSSDSYKQRYPVE--RLRANKDRPFSHDNLFHTLLGLLGIK 288
PRK09598 PRK09598
phosphoethanolamine--lipid A transferase EptA;
80-551 7.72e-105

phosphoethanolamine--lipid A transferase EptA;


Pssm-ID: 236581 [Multi-domain]  Cd Length: 522  Bit Score: 325.97  E-value: 7.72e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691  80 KYLMKPALVILILVSATAAYFADTFGIIIDRDMIGNAAVTTQAEASHLLTFSLARHLLVYAVLPSILIVWVRVRHRrflP 159
Cdd:PRK09598   71 RRLMRLSAIVFSLLNSIAFYFINTYKVFLNKSMMGNVLNTNTAESSGFLSVKLFIYIVVLGVLPGYIIYKIPLKNS---S 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 160 KAAVnFAFVSVSLLVGAGLIYANFATVAYALREHTDLMKRFNPSGPLIATVRYGLSTYRERnlVVRPLGTDAHQGARVAA 239
Cdd:PRK09598  148 KKAP-FAAILALVLIFLASAFANSKNWLWFDKHAKFLGGLILPWSYSVNTFRVSAHKFFAP--TIKPLLPPLFSPNHSKS 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 240 AGKPVVvvvvaGETARAMNFSLNGYERETNPELKALRVVN---YRNTTSCGTATAVSLPCMFS-VYPRSQYSDwkarstE 315
Cdd:PRK09598  225 VVVLVI-----GESARKHNYALYGYEKPTNPRLSKRLATHeltLFNATSCATYTTASLECILDsSFKNTSNAY------E 293

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 316 NLVNVLTRAGVSVSWWDNNTGSKGIAdlisfaSQTGRKNSPL---CNNGEC-LDEILLGDLDRKLGAAISNSV-IVLHQL 390
Cdd:PRK09598  294 NLPTYLTRAGIKVFWRSANDGEPNVK------VTSYLKNYELiqkCPNCEApYDESLLYNLPELIKASSNENVlLILHLA 367

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 391 GSHGPSYYLRYPAAFRRFTPDCRTPELMRCSTAELVNAYDNTILYTDHILASVARLLEKHQDRiaGAMIYMSDHGESLGE 470
Cdd:PRK09598  368 GSHGPNYDNKYPLNFRVFKPVCSSVELSSCSKESLINAYDNTIFYNDYLLDKIISMLKNLKQP--ALMIYLSDHGESLGE 445

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 471 NGLYLHGAPYVIAPKEQTQVPFIAWFSEPYQAAMgvdagcLAKDADKPKSHDNLFHTVLGMMDVET--RVYNRDLDAFAA 548
Cdd:PRK09598  446 GAFYLHGIPKSIAPKEQYEIPFIVWASDSFKKQH------SIIQTQTPINQNVIFHSVLGVFDFKNpsAVYRPSLDLFKH 519


                  ...
gi 1550155691 549 CTR 551
Cdd:PRK09598  520 KKE 522
Sulfatase pfam00884
Sulfatase;
251-534 9.17e-62

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 206.12  E-value: 9.17e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 251 GETARAMNFSLNGYERETNPELKALR--VVNYRNTTSCGTATAVSLPCMFSVYPRSQYSDW------KARSTENLVNVLT 322
Cdd:pfam00884   8 GESLRAPDLGLYGYPRPTTPFLDRLAeeGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYvstpvgLPRTEPSLPDLLK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 323 RAGV--------SVSWWDNNTGSKGIADLIsFASQTGR-------KNSPLCNNGECLDEILLGDLDRKLGAAISNSVIVL 387
Cdd:pfam00884  88 RAGYntgaigkwHLGWYNNQSPCNLGFDKF-FGRNTGSdlyadppDVPYNCSGGGVSDEALLDEALEFLDNNDKPFFLVL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 388 HQLGSHGPSYYL-RYPAAFRRFTPDcrtpelmRCSTAELVNAYDNTILYTDHILASVARLLEKHQDRIAGAMIYMSDHGE 466
Cdd:pfam00884 167 HTLGSHGPPYYPdRYPEKYATFKPS-------SCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGE 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1550155691 467 SLGENGLYLHGAPYVIAPKEQTQVPFIAWFSEPYQAAMGVDAgclakdadkPKSHDNLFHTVLGMMDV 534
Cdd:pfam00884 240 SLGEGGGYLHGGKYDNAPEGGYRVPLLIWSPGGKAKGQKSEA---------LVSHVDLFPTILDLAGI 298
EptA_B_N pfam08019
Phosphoethanolamine transferase EptA/EptB; This entry represents a domain found in a group of ...
 75-212 6.37e-49

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: 166.93  E-value: 6.37e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691  75 TPLSVKYLMKPALVILILVSATAAYFADTFGIIIDRDMIGNAAVTTQAEASHLLTFSLARHLLVYAVLPSILIVWVRVRH 154
Cdd:pfam08019  10 SLLSWRYLLKPLLILLLLLSAAASYFMDTYGVVIDRDMIQNVLETDVAEASDLLSPKLLLYLLLLGVLPALLLWRVRIRY 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1550155691 155 RRFLPKAAVNFAFVSVSLLVGAGLIYANFATVAYALREHTDLMKRFNPSGPLIATVRY 212
Cdd:pfam08019  90 RPWLRELLSRLALILVSLLVIGLVAFLFYKDYASFFRNHKELRYLINPTNYIYSTVKY 147
PRK11560 PRK11560
kdo(2)-lipid A phosphoethanolamine 7''-transferase;
251-530 1.66e-47

kdo(2)-lipid A phosphoethanolamine 7''-transferase;


Pssm-ID: 183198 [Multi-domain]  Cd Length: 558  Bit Score: 174.84  E-value: 1.66e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 251 GETARAMNFSLNGYERETNPEL-KALRVVNYRNTtSCGTATAVSLPCMFSvypRSQYSDWKARST---ENLVNVLTRAGV 326
Cdd:PRK11560  255 GETTRWDHMGILGYERNTTPKLaQEKNLAAFRGY-SCDTATKLSLRCMFV---REGGAEDNPQRTlkeQNVFAVLKQLGF 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 327 SVS--------WWDNNTgskgIADLISFASQTGRKNSplcNNGECLDEILLGD-LDRKLGA-AISNSVIVLHQLGSHGpS 396
Cdd:PRK11560  331 SSElfamqsemWFYNNT----MADNYAYREQIGAEPR---NRGKPVDDMLLVDeMKQSLGRnPDGKHLIILHTKGSHY-N 402

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 397 YYLRYPAAFRRFTPDCRTPElMRCSTAELVNAYDNTILYTDHILASVarlLEKHQDRIAgAMIYMSDHGESLGENGlYLH 476
Cdd:PRK11560  403 YTQRYPRSFARYQPECIGVD-SGCSKAQLINSYDNSVLYVDHFISSV---IDQLRDKKA-IVFYAADHGESINERE-HLH 476

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1550155691 477 GAPYVIAPKEQTQVPFIAWFSEPYQAAMGvDAGCLAK-----DADKPKSHDNLFHTVLG 530
Cdd:PRK11560  477 GTPREMAPPEQFRVPMMVWMSDKYLANPD-NAQAFAQlkkqaDMKVPRRHVELFDTILG 534
PRK10649 PRK10649
phosphoethanolamine transferase CptA;
119-527 1.01e-28

phosphoethanolamine transferase CptA;


Pssm-ID: 182617 [Multi-domain]  Cd Length: 577  Bit Score: 120.58  E-value: 1.01e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 119 TTQAEASHLLT--FSLARHLLVYAVLPSILIVWVRVRHRRF-LPKAAVNFAFVSVSLLVG--AGLIYANFATVAYALreh 193
Cdd:PRK10649  107 TNTNEASEYLSqyFSLKIVLIALAYTAVAVLLWTRLRPVYIpWPWRYVVSFALLYGLILHpiAMNTFIKHKPFEKTL--- 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 194 TDLMKRFNPSGP---LIATVRY-----GLSTYRERNLVVRPLGT--DAHQGArvaaagkPVVVVVVAGETARAMNFSLNG 263
Cdd:PRK10649  184 DKLASRMEPAAPwqfLTGYYQYrqqlnSLQKLLNENAALPPLANlkDESGNA-------PRTLVLVIGESTQRGRMSLYG 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 264 YERETNPELKALRVVN-----YRNTTSCGTATAVSLPCMFSVYPRSQYSDWKARSTenLVNVLTRAGVSVSWWDNN-TGS 337
Cdd:PRK10649  257 YPRETTPELDALHKTDpgltvFNNVVTSRPYTIEILQQALTFADEKNPDLYLTQPS--LMNMMKQAGYKTFWITNQqTMT 334

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 338 KGIADLISFASQTGRK---NSPLCNNGECLDEILLGDLDRKLGAAISNSVIVLHQLGSHgPSYYLRYPAAFRRFT----- 409
Cdd:PRK10649  335 ARNTMLTVFSRQTDKQyymNQQRTQNAREYDTNVLKPFSEVLADPAPKKFIIVHLLGTH-IKYKYRYPENQGKFDdrtgh 413

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 410 -PDCRTPElmrcsTAELVNAYDNTILYTDHILASVARLLEKHQDRiaGAMIYMSDHGE---------SLGENglylHGAP 479
Cdd:PRK10649  414 vPPGLNAD-----ELESYNDYDNANLYNDHVVASLIKDFKATDPN--GFLVYFSDHGEevydtpphkTQGRN----EDNP 482

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1550155691 480 yviaPKEQTQVPFIAWFSEPYQAAMGVDagcLAKDADKPKSHDNLFHT 527
Cdd:PRK10649  483 ----TRHMYTIPFLLWTSEKWQAAHPRD---FSQDVDRKYSLAELIHT 523
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 252-539 1.61e-08

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: 56.02  E-value: 1.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 252 ETARAMNFSLNGYERETNPELKAL--RVVNYRNTTSCGTATAVSLPCMF-SVYPrSQYSDWKARSTEN---LVNVLTRAG 325
Cdd:cd16148     9 DSLRADHLGCYGYDRVTTPNLDRLaaEGVVFDNHYSGSNPTLPSRFSLFtGLYP-FYHGVWGGPLEPDdptLAEILRKAG 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 326 V------SVSWWDNNTG-SKGIADLISFASQTGRKNSPLCNNGECLDEILLGDLDRKLGAaiSNSVIVLHQLGSHGPsyY 398
Cdd:cd16148    88 YytaavsSNPHLFGGPGfDRGFDTFEDFRGQEGDPGEEGDERAERVTDRALEWLDRNADD--DPFFLFLHYFDPHEP--Y 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 399 LrypaafrrftpdcrtpelmrcstaelvnaYDNTILYTDHILASVARLLEKHQDR----IagamIYMSDHGESLGENGLY 474
Cdd:cd16148   164 L-----------------------------YDAEVRYVDEQIGRLLDKLKELGLLedtlV----IVTSDHGEEFGEHGLY 210

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1550155691 475 L-HGAPYviaPKEQTQVPFIAWFsePYQAAMGVDagclakdaDKPKSHDNLFHTVLGMMDVETRVY 539
Cdd:cd16148   211 WgHGSNL---YDEQLHVPLIIRW--PGKEPGKRV--------DALVSHIDIAPTLLDLLGVEPPDY 263
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 251-496 2.49e-07

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: 52.04  E-value: 2.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 251 GETARAMNFSLNGYERETNPELKALR---VVNYRNTTSCGTATAVSLPCMFS-VYP-RSQYSDWKARSTENLVNVLTRAG 325
Cdd:cd00016     8 LDGLGADDLGKAGNPAPTTPNLKRLAsegATFNFRSVSPPTSSAPNHAALLTgAYPtLHGYTGNGSADPELPSRAAGKDE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 326 VSVSWWDNNTGSKGIADLISFasqtgrknsplcnngecLDEILLGDLDRKlgaaisnSVIVLHQLGSHGPSYylrypaAF 405
Cdd:cd00016    88 DGPTIPELLKQAGYRTGVIGL-----------------LKAIDETSKEKP-------FVLFLHFDGPDGPGH------AY 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 406 RRFTPdcrtpelmrcstaelvnAYDNTILYTDHILASVARLLEKHQDRIAGAMIYMSDHGESLGENGLYLHGAPYVIAPK 485
Cdd:cd00016   138 GPNTP-----------------EYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHGGDPKADGKADKSH 200

                         250
                  ....*....|.
gi 1550155691 486 EQTQVPFIAWF 496
Cdd:cd00016   201 TGMRVPFIAYG 211
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
 443-535 1.75e-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: 50.84  E-value: 1.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 443 VARLLEKHQDRIAGAMI-YMSDHGESLGENGLYLHGAPyviAPKEQTQVPFIAWFSEPYQAAMGVDAgclakdadkPKSH 521
Cdd:cd16156   254 IGRVLDAADEIAEDAWViYTSDHGDMLGAHKLWAKGPA---VYDEITNIPLIIRGKGGEKAGTVTDT---------PVSH 321

                          90
                  ....*....|....
gi 1550155691 522 DNLFHTVLGMMDVE 535
Cdd:cd16156   322 IDLAPTILDYAGIP 335
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
395-495 2.82e-03

Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 40.25  E-value: 2.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 395 PSYYLRYPAAFRRFTPDCRTPELMRCSTAELVNAYDNTILYTDHilaSVARLLEKHQDRiaGAM-----IYMSDHGESLG 469
Cdd:COG3119   168 EEYLDKYDGKDIPLPPNLAPRDLTEEELRRARAAYAAMIEEVDD---QVGRLLDALEEL--GLAdntivVFTSDNGPSLG 242

                          90       100
                  ....*....|....*....|....*...
gi 1550155691 470 ENGLYLH-GAPYviapkEQ-TQVPFIAW 495
Cdd:COG3119   243 EHGLRGGkGTLY-----EGgIRVPLIVR 265
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 427-534 7.04e-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: 293759 [Multi-domain]  Cd Length: 311  Bit Score: 38.73  E-value: 7.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550155691 427 NAYDNTILYTDHILASVARLLEKH---QDRIagaMIYMSDHGESLGENGlyLHGAPYViAPKEQTQVPFIawFSEPYQAA 503
Cdd:cd16035   167 NFYYNLIRDVDRQIGRVLDALDASglaDNTI---VVFTSDHGEMGGAHG--LRGKGFN-AYEEALHVPLI--ISHPDLFG 238

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1550155691 504 MGVDAGCLAkdadkpkSHDNLFHTVLGMMDV 534
Cdd:cd16035   239 TGQTTDALT-------SHIDLLPTLLGLAGV 262
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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