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Conserved domains on  [gi|90111552|ref|NP_417641|]
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putative hydrolase YhbX [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

phosphoethanolamine transferase( domain architecture ID 13592986)

phosphoethanolamine transferase similar to Escherichia coli MCR-1 and MCR-2, which confer resistance to colistin, a 'last-line' antibiotic against extensively resistant gram-negative pathogens and are plasmid-encoded membrane-bound phosphoethanolamine transferases that catalyze phosphoethanolamine transfer onto bacterial lipid A

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LptA cd16017
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ...
 222-489 1.65e-92

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: 284.52  E-value: 1.65e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552 222 IDTYVLIVGESVRVDNMSLYGYTRSTTPQVEAQRKQIKLFNQAISGAPYTALSVPLSLTADSVLSHDIHNYPDNIINMAN 301
Cdd:cd16017   2 PKNVVLVIGESARRDHMSLYGYPRDTTPFLSKLKKNLIVFDNVISCGTSTAVSLPCMLSFANRENYDRAYYQENLIDLAK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552 302 QAGFQTFWLSSQSAFRQNGTAVTSIAMRAMETVYV------RGFDELLLPHLSQALqQNTQQKKLIVLHLNGSHEPACSA 375
Cdd:cd16017  82 KAGYKTYWISNQGGCGGYDTRISAIAKIETVFTNKgscnssNCYDEALLPLLDEAL-ADSSKKKLIVLHLMGSHGPYYDR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552 376 YPQSSAVFQPQDDQD----------ACYDNSIHYTDSLLGQVFELLK--DRRASVMYFADHGLERdpTKKNVYFHGGREA 443
Cdd:cd16017 161 YPEEFAKFTPDCDNElqscskeeliNAYDNSILYTDYVLSQIIERLKkkDKDAALIYFSDHGESL--GENGLYLHGAPYA 238

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 90111552 444 SQQAYHVPMFIWYSPVL----GDGVDRTTENNIFSTAYNNYLINAWMGVT 489
Cdd:cd16017 239 PKEQYHVPFIIWSSDSYkqryPVERLRANKDRPFSHDNLFHTLLGLLGIK 288
EptA_B_N super family cl38254
Phosphoethanolamine transferase EptA/EptB; This entry represents a domain found in a group of ...
 41-165 1.94e-03

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.


The actual alignment was detected with superfamily member pfam08019:

Pssm-ID: 429788 [Multi-domain]  Cd Length: 151  Bit Score: 39.04  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552    41 LLFFVLTILVVKRIsslpLRLLVAapFVLLTAAdmsISLYSWCTFGTTFNDGFAISVLQSDPDEVVKMLGM-YIPYLCAF 119
Cdd:pfam08019   4 ALNLLLSLLSWRYL----LKPLLI--LLLLLSA---AASYFMDTYGVVIDRDMIQNVLETDVAEASDLLSPkLLLYLLLL 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 90111552   120 AFL-SLLFLAVIIKYDVSLPTKKVTGILL---LIVISGSLFsacqFAYKD 165
Cdd:pfam08019  75 GVLpALLLWRVRIRYRPWLRELLSRLALIlvsLLVIGLVAF----LFYKD 120
 
Name Accession Description Interval E-value
LptA cd16017
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ...
 222-489 1.65e-92

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: 284.52  E-value: 1.65e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552 222 IDTYVLIVGESVRVDNMSLYGYTRSTTPQVEAQRKQIKLFNQAISGAPYTALSVPLSLTADSVLSHDIHNYPDNIINMAN 301
Cdd:cd16017   2 PKNVVLVIGESARRDHMSLYGYPRDTTPFLSKLKKNLIVFDNVISCGTSTAVSLPCMLSFANRENYDRAYYQENLIDLAK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552 302 QAGFQTFWLSSQSAFRQNGTAVTSIAMRAMETVYV------RGFDELLLPHLSQALqQNTQQKKLIVLHLNGSHEPACSA 375
Cdd:cd16017  82 KAGYKTYWISNQGGCGGYDTRISAIAKIETVFTNKgscnssNCYDEALLPLLDEAL-ADSSKKKLIVLHLMGSHGPYYDR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552 376 YPQSSAVFQPQDDQD----------ACYDNSIHYTDSLLGQVFELLK--DRRASVMYFADHGLERdpTKKNVYFHGGREA 443
Cdd:cd16017 161 YPEEFAKFTPDCDNElqscskeeliNAYDNSILYTDYVLSQIIERLKkkDKDAALIYFSDHGESL--GENGLYLHGAPYA 238

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 90111552 444 SQQAYHVPMFIWYSPVL----GDGVDRTTENNIFSTAYNNYLINAWMGVT 489
Cdd:cd16017 239 PKEQYHVPFIIWSSDSYkqryPVERLRANKDRPFSHDNLFHTLLGLLGIK 288
OpgE COG2194
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall ...
 41-458 2.44e-62

Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441797 [Multi-domain]  Cd Length: 537  Bit Score: 213.56  E-value: 2.44e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552  41 LLFFVLTILVVKRisslpLRLLVAAPFVLLTAAdmsISLYSWcTFGTTFNDGFAISVLQSDPDEVVKMLGMY-IPYLCAF 119
Cdd:COG2194  56 ALNLLLSLLAWRY-----LFKPLLILLLLISAA---ASYFMD-FYGVVIDYGMIQNVLETDPAEASELLSPKlILWLLLL 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552 120 AFL-SLLFLAVIIKYDV---SLPTKKVTGILLLIVISGSLFSACQ-FAYKDAKNK---KAFSPYILASRFATYtpffnln 191
Cdd:COG2194 127 GVLpALLLWRVRIRYRPllrELGQRLALLLLALLVIVLLALLFYKdYASFFRNHKelrYLINPSNFIYALGKY------- 199

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552 192 YFALAAKEHQRLLSIANTVPYFQLSVRDTgidTYVLIVGESVRVDNMSLYGYTRSTTPQVeAQRKQIKLFNQAISGAPYT 271
Cdd:COG2194 200 AKARYFAAPLPLQPLGADAKLAAAGAKPT---LVVLVVGETARADNFSLNGYARDTTPEL-AKEKNLVSFRDVTSCGTAT 275

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552 272 ALSVP--LSLTADSVLSHDIHNYPDNIINMANQAGFQTFWLSSQSAFRqnGTA--VTSIAMRAME-TVYVRG---FDELL 343
Cdd:COG2194 276 AVSVPcmFSRLGRADYDPQRALNQENLLDVLQRAGVKVLWRDNQSGCK--GVCdrVPTIDLTADNlPPLCDGgecLDEVL 353

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552 344 LPHLSQALQQNtQQKKLIVLHLNGSHEPACSA-YPQSSAVFQP----QDDQDaC--------YDNSIHYTDSLLGQVFEL 410
Cdd:COG2194 354 LDGLDEALADL-AGDKLIVLHQMGSHGPAYYKrYPPEFRKFTPtcdtNDLQN-CsreelvnaYDNTILYTDYVLSQVIDL 431

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 90111552 411 LKDRR----ASVMYFADHG--L-ErdptkKNVYFHG--GREASQQAYHVPMFIWYSP 458
Cdd:COG2194 432 LKAKQdrydTAMLYVSDHGesLgE-----NGLYLHGtpYAIAPDEQTHVPMIMWLSD 483
Sulfatase pfam00884
Sulfatase;
224-463 6.36e-52

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 179.16  E-value: 6.36e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552   224 TYVLIVGESVRVDNMSLYGYTRSTTPQVEAQRKQIKLFNQAISGAPYTALSVPLSLTADSVLSHD--------IHNYPDN 295
Cdd:pfam00884   2 NVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGsyvstpvgLPRTEPS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552   296 IINMANQAGFQT--------FWLSSQS-------AFRQNGTAVTSIAMRAMETVYVRG---FDELLLPHLSQALQQNtQQ 357
Cdd:pfam00884  82 LPDLLKRAGYNTgaigkwhlGWYNNQSpcnlgfdKFFGRNTGSDLYADPPDVPYNCSGggvSDEALLDEALEFLDNN-DK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552   358 KKLIVLHLNGSHEP--ACSAYPQSSAVFQP----QDDQDACYDNSIHYTDSLLGQVFELLK----DRRASVMYFADHGLE 427
Cdd:pfam00884 161 PFFLVLHTLGSHGPpyYPDRYPEKYATFKPsscsEEQLLNSYDNTLLYTDDAIGRVLDKLEenglLDNTLVVYTSDHGES 240

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 90111552   428 RDPTKKNVYFHGGREASQQAYHVPMFIWYSPVLGDG 463
Cdd:pfam00884 241 LGEGGGYLHGGKYDNAPEGGYRVPLLIWSPGGKAKG 276
PRK10649 PRK10649
phosphoethanolamine transferase CptA;
60-458 8.90e-34

phosphoethanolamine transferase CptA;


Pssm-ID: 182617 [Multi-domain]  Cd Length: 577  Bit Score: 135.22  E-value: 8.90e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552   60 RLLVAAPFVLLTAADMsISLYSWCTFGTTFNDGFAISVLQSDPDEVVKMLGMYIPYLCAFAFLS------LLFLAVIIKY 133
Cdd:PRK10649  68 RIIAAVIGVVLWAASL-AALCYYVIYGQEFSQSVLFVMFETNTNEASEYLSQYFSLKIVLIALAytavavLLWTRLRPVY 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552  134 dVSLPTKKVTGILLLIVISGSLFSACQFAYKDAKNKKAFSpyiLASRFATYTPF-FNLNYFALAAK--EHQRLLSIANTV 210
Cdd:PRK10649 147 -IPWPWRYVVSFALLYGLILHPIAMNTFIKHKPFEKTLDK---LASRMEPAAPWqFLTGYYQYRQQlnSLQKLLNENAAL 222

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552  211 PYFQlSVRDTGID---TYVLIVGESVRVDNMSLYGYTRSTTPQVEAQRK---QIKLFNQAISGAPYTALSVPLSLTADSV 284
Cdd:PRK10649 223 PPLA-NLKDESGNaprTLVLVIGESTQRGRMSLYGYPRETTPELDALHKtdpGLTVFNNVVTSRPYTIEILQQALTFADE 301

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552  285 LSHDIHNYPDNIINMANQAGFQTFWLSSQSAFRQNGTAVTSIAMRAMETVYV--------RGFDELLLPHLSQALqQNTQ 356
Cdd:PRK10649 302 KNPDLYLTQPSLMNMMKQAGYKTFWITNQQTMTARNTMLTVFSRQTDKQYYMnqqrtqnaREYDTNVLKPFSEVL-ADPA 380

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552  357 QKKLIVLHLNGSHEPACSAYPQSSAVFQPQ--------DDQDA----CYDNSIHYTDSLLGQVFELLK--DRRASVMYFA 422
Cdd:PRK10649 381 PKKFIIVHLLGTHIKYKYRYPENQGKFDDRtghvppglNADELesynDYDNANLYNDHVVASLIKDFKatDPNGFLVYFS 460

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 90111552  423 DHGLErdptkknVYFHG-----GREA---SQQAYHVPMFIWYSP 458
Cdd:PRK10649 461 DHGEE-------VYDTPphktqGRNEdnpTRHMYTIPFLLWTSE 497
EptA_B_N pfam08019
Phosphoethanolamine transferase EptA/EptB; This entry represents a domain found in a group of ...
 41-165 1.94e-03

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: 39.04  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552    41 LLFFVLTILVVKRIsslpLRLLVAapFVLLTAAdmsISLYSWCTFGTTFNDGFAISVLQSDPDEVVKMLGM-YIPYLCAF 119
Cdd:pfam08019   4 ALNLLLSLLSWRYL----LKPLLI--LLLLLSA---AASYFMDTYGVVIDRDMIQNVLETDVAEASDLLSPkLLLYLLLL 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 90111552   120 AFL-SLLFLAVIIKYDVSLPTKKVTGILL---LIVISGSLFsacqFAYKD 165
Cdd:pfam08019  75 GVLpALLLWRVRIRYRPWLRELLSRLALIlvsLLVIGLVAF----LFYKD 120
 
Name Accession Description Interval E-value
LptA cd16017
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ...
 222-489 1.65e-92

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: 284.52  E-value: 1.65e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552 222 IDTYVLIVGESVRVDNMSLYGYTRSTTPQVEAQRKQIKLFNQAISGAPYTALSVPLSLTADSVLSHDIHNYPDNIINMAN 301
Cdd:cd16017   2 PKNVVLVIGESARRDHMSLYGYPRDTTPFLSKLKKNLIVFDNVISCGTSTAVSLPCMLSFANRENYDRAYYQENLIDLAK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552 302 QAGFQTFWLSSQSAFRQNGTAVTSIAMRAMETVYV------RGFDELLLPHLSQALqQNTQQKKLIVLHLNGSHEPACSA 375
Cdd:cd16017  82 KAGYKTYWISNQGGCGGYDTRISAIAKIETVFTNKgscnssNCYDEALLPLLDEAL-ADSSKKKLIVLHLMGSHGPYYDR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552 376 YPQSSAVFQPQDDQD----------ACYDNSIHYTDSLLGQVFELLK--DRRASVMYFADHGLERdpTKKNVYFHGGREA 443
Cdd:cd16017 161 YPEEFAKFTPDCDNElqscskeeliNAYDNSILYTDYVLSQIIERLKkkDKDAALIYFSDHGESL--GENGLYLHGAPYA 238

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 90111552 444 SQQAYHVPMFIWYSPVL----GDGVDRTTENNIFSTAYNNYLINAWMGVT 489
Cdd:cd16017 239 PKEQYHVPFIIWSSDSYkqryPVERLRANKDRPFSHDNLFHTLLGLLGIK 288
OpgE COG2194
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall ...
 41-458 2.44e-62

Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441797 [Multi-domain]  Cd Length: 537  Bit Score: 213.56  E-value: 2.44e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552  41 LLFFVLTILVVKRisslpLRLLVAAPFVLLTAAdmsISLYSWcTFGTTFNDGFAISVLQSDPDEVVKMLGMY-IPYLCAF 119
Cdd:COG2194  56 ALNLLLSLLAWRY-----LFKPLLILLLLISAA---ASYFMD-FYGVVIDYGMIQNVLETDPAEASELLSPKlILWLLLL 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552 120 AFL-SLLFLAVIIKYDV---SLPTKKVTGILLLIVISGSLFSACQ-FAYKDAKNK---KAFSPYILASRFATYtpffnln 191
Cdd:COG2194 127 GVLpALLLWRVRIRYRPllrELGQRLALLLLALLVIVLLALLFYKdYASFFRNHKelrYLINPSNFIYALGKY------- 199

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552 192 YFALAAKEHQRLLSIANTVPYFQLSVRDTgidTYVLIVGESVRVDNMSLYGYTRSTTPQVeAQRKQIKLFNQAISGAPYT 271
Cdd:COG2194 200 AKARYFAAPLPLQPLGADAKLAAAGAKPT---LVVLVVGETARADNFSLNGYARDTTPEL-AKEKNLVSFRDVTSCGTAT 275

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552 272 ALSVP--LSLTADSVLSHDIHNYPDNIINMANQAGFQTFWLSSQSAFRqnGTA--VTSIAMRAME-TVYVRG---FDELL 343
Cdd:COG2194 276 AVSVPcmFSRLGRADYDPQRALNQENLLDVLQRAGVKVLWRDNQSGCK--GVCdrVPTIDLTADNlPPLCDGgecLDEVL 353

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552 344 LPHLSQALQQNtQQKKLIVLHLNGSHEPACSA-YPQSSAVFQP----QDDQDaC--------YDNSIHYTDSLLGQVFEL 410
Cdd:COG2194 354 LDGLDEALADL-AGDKLIVLHQMGSHGPAYYKrYPPEFRKFTPtcdtNDLQN-CsreelvnaYDNTILYTDYVLSQVIDL 431

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 90111552 411 LKDRR----ASVMYFADHG--L-ErdptkKNVYFHG--GREASQQAYHVPMFIWYSP 458
Cdd:COG2194 432 LKAKQdrydTAMLYVSDHGesLgE-----NGLYLHGtpYAIAPDEQTHVPMIMWLSD 483
Sulfatase pfam00884
Sulfatase;
224-463 6.36e-52

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 179.16  E-value: 6.36e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552   224 TYVLIVGESVRVDNMSLYGYTRSTTPQVEAQRKQIKLFNQAISGAPYTALSVPLSLTADSVLSHD--------IHNYPDN 295
Cdd:pfam00884   2 NVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGsyvstpvgLPRTEPS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552   296 IINMANQAGFQT--------FWLSSQS-------AFRQNGTAVTSIAMRAMETVYVRG---FDELLLPHLSQALQQNtQQ 357
Cdd:pfam00884  82 LPDLLKRAGYNTgaigkwhlGWYNNQSpcnlgfdKFFGRNTGSDLYADPPDVPYNCSGggvSDEALLDEALEFLDNN-DK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552   358 KKLIVLHLNGSHEP--ACSAYPQSSAVFQP----QDDQDACYDNSIHYTDSLLGQVFELLK----DRRASVMYFADHGLE 427
Cdd:pfam00884 161 PFFLVLHTLGSHGPpyYPDRYPEKYATFKPsscsEEQLLNSYDNTLLYTDDAIGRVLDKLEenglLDNTLVVYTSDHGES 240

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 90111552   428 RDPTKKNVYFHGGREASQQAYHVPMFIWYSPVLGDG 463
Cdd:pfam00884 241 LGEGGGYLHGGKYDNAPEGGYRVPLLIWSPGGKAKG 276
PRK10649 PRK10649
phosphoethanolamine transferase CptA;
60-458 8.90e-34

phosphoethanolamine transferase CptA;


Pssm-ID: 182617 [Multi-domain]  Cd Length: 577  Bit Score: 135.22  E-value: 8.90e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552   60 RLLVAAPFVLLTAADMsISLYSWCTFGTTFNDGFAISVLQSDPDEVVKMLGMYIPYLCAFAFLS------LLFLAVIIKY 133
Cdd:PRK10649  68 RIIAAVIGVVLWAASL-AALCYYVIYGQEFSQSVLFVMFETNTNEASEYLSQYFSLKIVLIALAytavavLLWTRLRPVY 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552  134 dVSLPTKKVTGILLLIVISGSLFSACQFAYKDAKNKKAFSpyiLASRFATYTPF-FNLNYFALAAK--EHQRLLSIANTV 210
Cdd:PRK10649 147 -IPWPWRYVVSFALLYGLILHPIAMNTFIKHKPFEKTLDK---LASRMEPAAPWqFLTGYYQYRQQlnSLQKLLNENAAL 222

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552  211 PYFQlSVRDTGID---TYVLIVGESVRVDNMSLYGYTRSTTPQVEAQRK---QIKLFNQAISGAPYTALSVPLSLTADSV 284
Cdd:PRK10649 223 PPLA-NLKDESGNaprTLVLVIGESTQRGRMSLYGYPRETTPELDALHKtdpGLTVFNNVVTSRPYTIEILQQALTFADE 301

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552  285 LSHDIHNYPDNIINMANQAGFQTFWLSSQSAFRQNGTAVTSIAMRAMETVYV--------RGFDELLLPHLSQALqQNTQ 356
Cdd:PRK10649 302 KNPDLYLTQPSLMNMMKQAGYKTFWITNQQTMTARNTMLTVFSRQTDKQYYMnqqrtqnaREYDTNVLKPFSEVL-ADPA 380

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552  357 QKKLIVLHLNGSHEPACSAYPQSSAVFQPQ--------DDQDA----CYDNSIHYTDSLLGQVFELLK--DRRASVMYFA 422
Cdd:PRK10649 381 PKKFIIVHLLGTHIKYKYRYPENQGKFDDRtghvppglNADELesynDYDNANLYNDHVVASLIKDFKatDPNGFLVYFS 460

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 90111552  423 DHGLErdptkknVYFHG-----GREA---SQQAYHVPMFIWYSP 458
Cdd:PRK10649 461 DHGEE-------VYDTPphktqGRNEdnpTRHMYTIPFLLWTSE 497
PRK11560 PRK11560
kdo(2)-lipid A phosphoethanolamine 7''-transferase;
223-489 1.55e-31

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


Pssm-ID: 183198 [Multi-domain]  Cd Length: 558  Bit Score: 128.23  E-value: 1.55e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552  223 DTYVL-IVGESVRVDNMSLYGYTRSTTPQVeAQRKQIKLFnQAISgapyTALSVPLSLTADSVLSHDIHNYP------DN 295
Cdd:PRK11560 247 DTYVVfIIGETTRWDHMGILGYERNTTPKL-AQEKNLAAF-RGYS----CDTATKLSLRCMFVREGGAEDNPqrtlkeQN 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552  296 IINMANQAGFQTFWLSSQS-AFRQNGTAVTSIAMRAMETVYVRGF-----DELLLPHLSQALQQNTQQKKLIVLHLNGSH 369
Cdd:PRK11560 321 VFAVLKQLGFSSELFAMQSeMWFYNNTMADNYAYREQIGAEPRNRgkpvdDMLLVDEMKQSLGRNPDGKHLIILHTKGSH 400

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552  370 EPACSAYPQSSAVFQPQ----DDQdaC--------YDNSIHYTDSLLGQVFELLKDRRASVMYFADHGlerDPTKKNVYF 437
Cdd:PRK11560 401 YNYTQRYPRSFARYQPEcigvDSG--CskaqlinsYDNSVLYVDHFISSVIDQLRDKKAIVFYAADHG---ESINEREHL 475

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 90111552  438 HGG-RE-ASQQAYHVPMFIWYSpvlgdgvDRTTENNIFSTAYNNYLINAWMGVT 489
Cdd:PRK11560 476 HGTpREmAPPEQFRVPMMVWMS-------DKYLANPDNAQAFAQLKKQADMKVP 522
PRK09598 PRK09598
phosphoethanolamine--lipid A transferase EptA;
14-458 3.17e-31

phosphoethanolamine--lipid A transferase EptA;


Pssm-ID: 236581 [Multi-domain]  Cd Length: 522  Bit Score: 127.20  E-value: 3.17e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552   14 HWLLYlcviVFGITNLVASSGAHMVQRLLFFV--LTILVVKRISSLPLRLlVAAPFVLLTaadmSISLYSWCTFGTTFND 91
Cdd:PRK09598  31 HFPLF----AYVYKESNQVSFIAMLVVLLFCVngLLFLLLGLLSRRLMRL-SAIVFSLLN----SIAFYFINTYKVFLNK 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552   92 GFAISVLQSDPDEVVK----MLGMYIpylcafAFLSLLFLAVIIKydvsLPTKKVTGILLLIVISGSLFSACQFAYKDA- 166
Cdd:PRK09598 102 SMMGNVLNTNTAESSGflsvKLFIYI------VVLGVLPGYIIYK----IPLKNSSKKAPFAAILALVLIFLASAFANSk 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552  167 ------KNKKAFSPYILASRFATYTP-FFNLNYFAlaaKEHQRLLSIAnTVPYFQLSVrdtgidtYVLIVGESVRVDNMS 239
Cdd:PRK09598 172 nwlwfdKHAKFLGGLILPWSYSVNTFrVSAHKFFA---PTIKPLLPPL-FSPNHSKSV-------VVLVIGESARKHNYA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552  240 LYGYTRSTTPQVEAQRKQ--IKLFNqAISGAPYTALSVplsltaDSVLSHDIHNYP---DNIINMANQAGFQTFWLSSQS 314
Cdd:PRK09598 241 LYGYEKPTNPRLSKRLATheLTLFN-ATSCATYTTASL------ECILDSSFKNTSnayENLPTYLTRAGIKVFWRSAND 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552  315 AfrQNGTAVTSIAMRAMETVYVRG----FDELLLPHLSQALQQNTQQKKLIVLHLNGSHEPACSA-YPQSSAVFQP---Q 386
Cdd:PRK09598 314 G--EPNVKVTSYLKNYELIQKCPNceapYDESLLYNLPELIKASSNENVLLILHLAGSHGPNYDNkYPLNFRVFKPvcsS 391

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552  387 DDQDAC--------YDNSIHYTDSLLGQVFELLKD--RRASVMYFADHGleRDPTKKNVYFHGGRE--ASQQAYHVPMFI 454
Cdd:PRK09598 392 VELSSCskeslinaYDNTIFYNDYLLDKIISMLKNlkQPALMIYLSDHG--ESLGEGAFYLHGIPKsiAPKEQYEIPFIV 469


                 ....
gi 90111552  455 WYSP 458
Cdd:PRK09598 470 WASD 473
PRK11598 PRK11598
putative metal dependent hydrolase; Provisional
 47-475 1.49e-25

putative metal dependent hydrolase; Provisional


Pssm-ID: 183224 [Multi-domain]  Cd Length: 545  Bit Score: 110.54  E-value: 1.49e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552   47 TILVVKRISSLP-LRLLVAAPFVLLTAAdmsiSLYSWCTFGTTFNDGFAISVLQSDPDEVVKMLgmyIPYLCAFAFLSLL 125
Cdd:PRK11598  60 VINIVFTLLSFPwLRRPLACLFILVGAA----AQYFMMTYGIVIDRSMIQNIFETTPAESFALM---TPQMLLWLGLSGV 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552  126 FLAVI---IKYDVSLPTKKVTGI--------LLLIVISGSLFsacqfaYKD-----AKNK---KAFSP--YILAS-RFAT 183
Cdd:PRK11598 133 LPALIacwIKIRPATPRWRSVLFrlanilvsVLLILLVAALF------YKDyaslfRNNKelvKSLTPsnSIVASwSWYS 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552  184 YTPFFNLNYFALAAKEHQrllsiantVPYFQLSVRDTGIdtyVLIVGESVRVDNMSLYGYTRSTTPQVeaQRKQIKLFNQ 263
Cdd:PRK11598 207 HQRLANLPLVRIGEDAHK--------NPLMQNQKRKNLT---ILVVGETSRAENFSLGGYPRETNPRL--AKDNVIYFPH 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552  264 AISGAPYTALSVPLSLTA------DSVLSHdihnYPDNIINMANQAGFQTFWlssqsafRQNG----TAVTSIAMRAMET 333
Cdd:PRK11598 274 TTSCGTATAVSVPCMFSNmprkhyDEELAH----HQEGLLDIIQRAGINVLW-------NDNDggckGACDRVPHQDVTA 342

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552  334 VYVRGF-------DELLLPHLSQALQqNTQQKKLIVLHLNGSHEPA-CSAYPQSSAVFQP-------QD-DQDA---CYD 394
Cdd:PRK11598 343 LNLPGQcidgecyDEVLFHGLENYIN-NLQGDGVIVLHTIGSHGPTyYNRYPPQFRKFTPtcdtneiQTcTQQQlvnTYD 421

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552  395 NSIHYTDSLLGQVFELLKDRRA----SVMYFADHG--LERDptkkNVYFHGGRE--ASQQAYHVPMFIWYSPvlgD---- 462
Cdd:PRK11598 422 NTILYVDYIVDKAINLLKQHQDkfntSLVYLSDHGesLGEN----GIYLHGLPYaiAPDQQTHVPMLLWLSP---Dyqkr 494

                        490       500
                 ....*....|....*....|....*
gi 90111552  463 -GVDRT-----------TENNIFST 475
Cdd:PRK11598 495 yGVDQQclqkqaqtqdySQDNLFST 519
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 226-456 1.03e-15

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: 77.20  E-value: 1.03e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552 226 VLIVGESVRVDNMSLYGYTRSTTPQVEAQRKQIKLFNQAISGAPYTALSVPLSLTADSVLSHDIHNYPDN-----IINMA 300
Cdd:cd16148   4 ILIVIDSLRADHLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVWGGPLEpddptLAEIL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552 301 NQAGFQT------FWLSSQSAFRQngTAVTSIAMRAMETVYVRG---FDELLLPHLSQALQQNTQQKK-LIVLHLNGSHE 370
Cdd:cd16148  84 RKAGYYTaavssnPHLFGGPGFDR--GFDTFEDFRGQEGDPGEEgdeRAERVTDRALEWLDRNADDDPfFLFLHYFDPHE 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552 371 PacsaypqssavFQpqddqdacYDNSIHYTDSLLGQVFELLKDRRAS----VMYFADHG---LERDptkkNVYFHGGREA 443
Cdd:cd16148 162 P-----------YL--------YDAEVRYVDEQIGRLLDKLKELGLLedtlVIVTSDHGeefGEHG----LYWGHGSNLY 218

                       250
                ....*....|...
gi 90111552 444 SQQAyHVPMFIWY 456
Cdd:cd16148 219 DEQL-HVPLIIRW 230
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
 41-468 1.24e-10

Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 63.90  E-value: 1.24e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552  41 LLFFVLTILVVKRISSLPLRLLVAAPFVLLTAADMsisLYsWCTFGTTFNdgfaISVLQ--SDPDEVVKML---GMYIPY 115
Cdd:COG1368  48 LLLLLLPLLFRRPKLRWIYLLLVLLLLLLLLVADI---LY-YRFFGDRLN----FSDLDylGDTGEVLGSLlssYDLLLL 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552 116 LCAFAFLSLLFLAVIIKYDVSLPTKKVTGILLLIVISGSLFSACQFAYKDAKN-KKAFSPYILASRFATYTPF------F 188
Cdd:COG1368 120 LDLLLLLLLLLLLYRLLKKLRKSLPWRKRLALLLLLLALLLLGIRLGEDRPLNlSDAFSRNNFVNELGLNGPYsfydalR 199

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552 189 NLNYFALAAKEhqRLLSIANTVPYFQLSVRDTGIDTY---VLIVGESVRVDNMSLYGYTRSTTPQVEAQRKQIKLFNQAI 265
Cdd:COG1368 200 NNKAPATYSEE--EALEIKKYLKSNRPTPNPFGPAKKpnvVVILLESFSDFFIGALGNGKDVTPFLDSLAKESLYFGNFY 277

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552 266 SGAPYTALSVPLSLT------ADSVLSHDIHNYPDNIINMANQAGFQT---------FWlSSQSAFRQNGTAvTSIAMRA 330
Cdd:COG1368 278 SQGGRTSRGEFAVLTglpplpGGSPYKRPGQNNFPSLPSILKKQGYETsffhggdgsFW-NRDSFYKNLGFD-EFYDRED 355

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552 331 METVYVRGF---DELLLphlSQALQQNTQQKKLIVLHLN--GSHEPacSAYPQSSAVFQPQDDQD-ACYDNSIHYTDSLL 404
Cdd:COG1368 356 FDDPFDGGWgvsDEDLF---DKALEELEKLKKPFFAFLItlSNHGP--YTLPEEDKKIPDYGKTTlNNYLNAVRYADQAL 430

                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111552 405 GQVFELLKDRRAS----VMYFADHGLerdptkkNVYFHGGREASQQAYHVPMFIWYSPVLGDGVDRTT 468
Cdd:COG1368 431 GEFIEKLKKSGWYdntiFVIYGDHGP-------RSPGKTDYENPLERYRVPLLIYSPGLKKPKVIDTV 491
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
 289-477 9.65e-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: 47.29  E-value: 9.65e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552 289 IHNYP---DNIINMANQAGFQTFWlsSQSAFRQNgtavtsiamramETVYVRGF--DELLLPHLSQALQQNTQQKKLIVL 363
Cdd:cd16015  97 IHGGDasfYNRDSVYPNLGFDEFY--DLEDFPDD------------EKETNGWGvsDESLFDQALEELEELKKKPFFIFL 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552 364 HLNGSHEP--ACSAYPQSSAVFQPQDDQDACYDNSIHYTDSLLGQVFELLKDRRAS----VMYFADHGlerdpTKKNVYF 437
Cdd:cd16015 163 VTMSNHGPydLPEEKKDEPLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYentiIVIYGDHL-----PSLGSDY 237

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 90111552 438 HGGREASQQAYHVPMFIWyspvLGDGVDRTTENNIFSTAY 477
Cdd:cd16015 238 DETDEDPLDLYRTPLLIY----SPGLKKPKKIDRVGSQID 273
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 226-475 9.74e-06

alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.


Pssm-ID: 293732 [Multi-domain]  Cd Length: 237  Bit Score: 47.03  E-value: 9.74e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552 226 VLIVGESVRVDNMSLYGYTRSTTPQVEAQRKQIKLFN-QAISGAPYTALSVPLSLTADSVLSHDIHNYPDNIINMANQAG 304
Cdd:cd00016   4 VLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFNfRSVSPPTSSAPNHAALLTGAYPTLHGYTGNGSADPELPSRAA 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552 305 -----FQTFWlssqSAFRQNGTAVTSIamrametvyvrgfdelllpHLSQALQQNTQQKK-LIVLHLNGSHEPACSAYPQ 378
Cdd:cd00016  84 gkdedGPTIP----ELLKQAGYRTGVI-------------------GLLKAIDETSKEKPfVLFLHFDGPDGPGHAYGPN 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552 379 SSAvfqpqddqdacYDNSIHYTDSLLGQVFELLKDRR----ASVMYFADHGLErdptkknVYFHGGREAS---QQAYH-- 449
Cdd:cd00016 141 TPE-----------YYDAVEEIDERIGKVLDALKKAGdaddTVIIVTADHGGI-------DKGHGGDPKAdgkADKSHtg 202

                       250       260       270
                ....*....|....*....|....*....|
gi 90111552 450 --VPMFIWYSPVLGDGVDR--TTENNIFST 475
Cdd:cd00016 203 mrVPFIAYGPGVKKGGVKHelISQYDIAPT 232
EptA_B_N pfam08019
Phosphoethanolamine transferase EptA/EptB; This entry represents a domain found in a group of ...
 41-165 1.94e-03

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: 39.04  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111552    41 LLFFVLTILVVKRIsslpLRLLVAapFVLLTAAdmsISLYSWCTFGTTFNDGFAISVLQSDPDEVVKMLGM-YIPYLCAF 119
Cdd:pfam08019   4 ALNLLLSLLSWRYL----LKPLLI--LLLLLSA---AASYFMDTYGVVIDRDMIQNVLETDVAEASDLLSPkLLLYLLLL 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 90111552   120 AFL-SLLFLAVIIKYDVSLPTKKVTGILL---LIVISGSLFsacqFAYKD 165
Cdd:pfam08019  75 GVLpALLLWRVRIRYRPWLRELLSRLALIlvsLLVIGLVAF----LFYKD 120
 
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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