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Conserved domains on  [gi|1470397016|gb|RGY11596|]
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lipid A phosphoethanolamine transferase [Butyricimonas virosa]

Protein Classification

lipid A phosphoethanolamine transferase( domain architecture ID 11173129)

lipid A phosphoethanolamine transferase similar to EptA or EptB, which catalyzes the addition of a phosphoethanolamine moiety to lipid A or Kdo(2)-lipid A, respectively

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 ...
 238-531 1.07e-105

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: 319.57  E-value: 1.07e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 238 RREIYVLVIGEAGRAENWNLWGYHRETNPLL-KTEDNLVLYKDALTQSNTTHKSVPLILSAADACHYEYLYTHKSIVTAF 316
Cdd:cd16017     1 KPKNVVLVIGESARRDHMSLYGYPRDTTPFLsKLKKNLIVFDNVISCGTSTAVSLPCMLSFANRENYDRAYYQENLIDLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 317 KEAGFKTIFLSNQTPNRSFTDYFAEEADIHInvRPQADGGLITVNKFDGEMLPLLQQYVDSLQENLFIVFHSYGSHFNYK 396
Cdd:cd16017    81 KKAGYKTYWISNQGGCGGYDTRISAIAKIET--VFTNKGSCNSSNCYDEALLPLLDEALADSSKKKLIVLHLMGSHGPYY 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 397 ERYPEEFAKFQPANATEVEYKNKDQLINAYDNSILYTDYFLHSLIGILKNSGADATMIYSPDHGEDLLDDNrkRFLHASP 476
Cdd:cd16017   159 DRYPEEFAKFTPDCDNELQSCSKEELINAYDNSILYTDYVLSQIIERLKKKDKDAALIYFSDHGESLGENG--LYLHGAP 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1470397016 477 IPTYYQIHIPFLMWFSDNYIEARPekYEVARYNSNAPIsSNASIFHTLLEMAEIN 531
Cdd:cd16017   237 YAPKEQYHVPFIIWSSDSYKQRYP--VERLRANKDRPF-SHDNLFHTLLGLLGIK 288
EptA_B_N pfam08019
Phosphoethanolamine transferase EptA/EptB; This entry represents a domain found in a group of ...
 65-207 2.11e-15

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: 73.71  E-value: 2.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016  65 LSIYMIVFSLFKRAGIMQLILIPVLILHAFQLVLFYLFGeSVIAVDMFLNLPTTNASEAGELLgNIWPSIIIVCVLYIPV 144
Cdd:pfam08019   2 FAALNLLLSLLSWRYLLKPLLILLLLLSAAASYFMDTYG-VVIDRDMIQNVLETDVAEASDLL-SPKLLLYLLLLGVLPA 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1470397016 145 IALASIAVHHKVRRTAvFRKHMITWGIILFIIGSGLVAFEKH-----RdNSYEVKTDIYPANVMYNLY 207
Cdd:pfam08019  80 LLLWRVRIRYRPWLRE-LLSRLALILVSLLVIGLVAFLFYKDyasffR-NHKELRYLINPTNYIYSTV 145
 
Name Accession Description Interval E-value
LptA cd16017
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ...
 238-531 1.07e-105

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: 319.57  E-value: 1.07e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 238 RREIYVLVIGEAGRAENWNLWGYHRETNPLL-KTEDNLVLYKDALTQSNTTHKSVPLILSAADACHYEYLYTHKSIVTAF 316
Cdd:cd16017     1 KPKNVVLVIGESARRDHMSLYGYPRDTTPFLsKLKKNLIVFDNVISCGTSTAVSLPCMLSFANRENYDRAYYQENLIDLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 317 KEAGFKTIFLSNQTPNRSFTDYFAEEADIHInvRPQADGGLITVNKFDGEMLPLLQQYVDSLQENLFIVFHSYGSHFNYK 396
Cdd:cd16017    81 KKAGYKTYWISNQGGCGGYDTRISAIAKIET--VFTNKGSCNSSNCYDEALLPLLDEALADSSKKKLIVLHLMGSHGPYY 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 397 ERYPEEFAKFQPANATEVEYKNKDQLINAYDNSILYTDYFLHSLIGILKNSGADATMIYSPDHGEDLLDDNrkRFLHASP 476
Cdd:cd16017   159 DRYPEEFAKFTPDCDNELQSCSKEELINAYDNSILYTDYVLSQIIERLKKKDKDAALIYFSDHGESLGENG--LYLHGAP 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1470397016 477 IPTYYQIHIPFLMWFSDNYIEARPekYEVARYNSNAPIsSNASIFHTLLEMAEIN 531
Cdd:cd16017   237 YAPKEQYHVPFIIWSSDSYKQRYP--VERLRANKDRPF-SHDNLFHTLLGLLGIK 288
OpgE COG2194
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall ...
 32-548 1.96e-94

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


Pssm-ID: 441797 [Multi-domain]  Cd Length: 537  Bit Score: 299.08  E-value: 1.96e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016  32 FWLFIALNLvPNFCLLF-TEPLSGLGKLILVLVP---LSIYMIVFSLFKRAGIMQLILIPVLILHAFQLVLFYLFGeSVI 107
Cdd:COG2194    18 LYFALFLNL-PFWGRLLaILPLDGVNLLFLLSLPlllLAALNLLLSLLAWRYLFKPLLILLLLISAAASYFMDFYG-VVI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 108 AVDMFLNLPTTNASEAGELLGniwPSIIIVCVLY--IPVIALASIAVHHKVRRTAVFRKhMITWGIILFIIGSGLVAFEK 185
Cdd:COG2194    96 DYGMIQNVLETDPAEASELLS---PKLILWLLLLgvLPALLLWRVRIRYRPLLRELGQR-LALLLLALLVIVLLALLFYK 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 186 H-----RDNSyEVKTDIYPANVMYNLY-YAcvkWNRSMNYPITSKDFTYEASRDSVHQRREIYVLVIGEAGRAENWNLWG 259
Cdd:COG2194   172 DyasffRNHK-ELRYLINPSNFIYALGkYA---KARYFAAPLPLQPLGADAKLAAAGAKPTLVVLVVGETARADNFSLNG 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 260 YHRETNPLLKTEDNLVLYKDALT-QSNTTHkSVPLILSAADACHYEYLYT--HKSIVTAFKEAGFKTIFLSNQTPNRSFT 336
Cdd:COG2194   248 YARDTTPELAKEKNLVSFRDVTScGTATAV-SVPCMFSRLGRADYDPQRAlnQENLLDVLQRAGVKVLWRDNQSGCKGVC 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 337 DYFAEEADIHINVRPQADGGlitvNKFDGEMLPLLQQYVDSLQENLFIVFHSYGSH-FNYKERYPEEFAKFQPA-NATEV 414
Cdd:COG2194   327 DRVPTIDLTADNLPPLCDGG----ECLDEVLLDGLDEALADLAGDKLIVLHQMGSHgPAYYKRYPPEFRKFTPTcDTNDL 402

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 415 EYKNKDQLINAYDNSILYTDYFLHSLIGILKNSGA--DATMIYSPDHGEDlLDDNRKrFLHASP--IPTYYQIHIPFLMW 490
Cdd:COG2194   403 QNCSREELVNAYDNTILYTDYVLSQVIDLLKAKQDryDTAMLYVSDHGES-LGENGL-YLHGTPyaIAPDEQTHVPMIMW 480

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1470397016 491 FSDNYIEARPEKYEVARYNSNAPISSNaSIFHTLLEMAEINTPYFDASYSLVNPGFAR 548
Cdd:COG2194   481 LSDGYAQRYGIDFACLKARADKPYSHD-NLFHTLLGLLDVRTSVYDPELDILAPCRRA 537
PRK10649 PRK10649
phosphoethanolamine transferase CptA;
30-556 6.49e-52

phosphoethanolamine transferase CptA;


Pssm-ID: 182617 [Multi-domain]  Cd Length: 577  Bit Score: 187.22  E-value: 6.49e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016  30 LLFWLFIAlnlVPNFCLLFTEpLSGLGKLILVLVPLSIYMIVFSLFKRAGIMQLILIPVLILHAFQLVLFYL------FG 103
Cdd:PRK10649   22 LFFWFFST---LLQAIIYISG-YSGTNGFRDALLFSSLWLIPVFLFPRRIRIIAAVIGVVLWAASLAALCYYviygqeFS 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 104 ESVIAVdMFlnlpTTNASEAGELLGNIW-PSIIIVCVLYipviALASIAVHHKVR------RTAVFRKHMITWGIILFII 176
Cdd:PRK10649   98 QSVLFV-MF----ETNTNEASEYLSQYFsLKIVLIALAY----TAVAVLLWTRLRpvyipwPWRYVVSFALLYGLILHPI 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 177 GSGLVAFEKHRDNSYE-VKTDIYPAnVMYNLYYACVKWNRSMNypiTSKDFTYEAS--------RDSVHQRREIYVLVIG 247
Cdd:PRK10649  169 AMNTFIKHKPFEKTLDkLASRMEPA-APWQFLTGYYQYRQQLN---SLQKLLNENAalpplanlKDESGNAPRTLVLVIG 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 248 EAGRAENWNLWGYHRETNP----LLKTEDNLVLYKDALTQSNTTHKSVPLILSAADACHYEYLYTHKSIVTAFKEAGFKT 323
Cdd:PRK10649  245 ESTQRGRMSLYGYPRETTPeldaLHKTDPGLTVFNNVVTSRPYTIEILQQALTFADEKNPDLYLTQPSLMNMMKQAGYKT 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 324 IFLSNQTPN---RSFTDYFAEEADIHI---NVRPQadggliTVNKFDGEMLPLLQQYVDSLQENLFIVFHSYGSHFNYKE 397
Cdd:PRK10649  325 FWITNQQTMtarNTMLTVFSRQTDKQYymnQQRTQ------NAREYDTNVLKPFSEVLADPAPKKFIIVHLLGTHIKYKY 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 398 RYPEEFAKFQPANATEVEYKNKDQL--INAYDNSILYTDYFLHSLIGILKNSGADATMIYSPDHGEDLLDD-NRKRFLHA 474
Cdd:PRK10649  399 RYPENQGKFDDRTGHVPPGLNADELesYNDYDNANLYNDHVVASLIKDFKATDPNGFLVYFSDHGEEVYDTpPHKTQGRN 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 475 SPIPTYYQIHIPFLMWFSDNYIEARPEKYEVARynsNAPISSnASIFHTLLEMAEINTPYFDASYSLVNPGFARRPRmYL 554
Cdd:PRK10649  479 EDNPTRHMYTIPFLLWTSEKWQAAHPRDFSQDV---DRKYSL-AELIHTWSDLAGLSYDGYDPTRSLVNPQFKETPR-WI 553


                  ..
gi 1470397016 555 GD 556
Cdd:PRK10649  554 GN 555
Sulfatase pfam00884
Sulfatase;
242-530 7.85e-42

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 152.58  E-value: 7.85e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 242 YVLVIGEAGRAENWNLWGYHRETNPLLKTE-DNLVLYKDALTQSNTTHKSVPLILSAADACHYEYL--------YTHKSI 312
Cdd:pfam00884   3 VVLVLGESLRAPDLGLYGYPRPTTPFLDRLaEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYvstpvglpRTEPSL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 313 VTAFKEAGFKTI--------FLSNQTPNRSFTDYFAEEADIHINVRPQADGGLITVNKF--DGEMLPLLQQYVDSLQENL 382
Cdd:pfam00884  83 PDLLKRAGYNTGaigkwhlgWYNNQSPCNLGFDKFFGRNTGSDLYADPPDVPYNCSGGGvsDEALLDEALEFLDNNDKPF 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 383 FIVFHSYGSH--FNYKERYPEEFAKFQPANATEveyknkDQLINAYDNSILYTDYFLHSLIGILKNSG--ADATMIYSPD 458
Cdd:pfam00884 163 FLVLHTLGSHgpPYYPDRYPEKYATFKPSSCSE------EQLLNSYDNTLLYTDDAIGRVLDKLEENGllDNTLVVYTSD 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1470397016 459 HGEDLLDDNRKRFLHASPIPTYYQIHIPFLMWFSDNYiearpekyevARYNSNAPISSNASIFHTLLEMAEI 530
Cdd:pfam00884 237 HGESLGEGGGYLHGGKYDNAPEGGYRVPLLIWSPGGK----------AKGQKSEALVSHVDLFPTILDLAGI 298
EptA_B_N pfam08019
Phosphoethanolamine transferase EptA/EptB; This entry represents a domain found in a group of ...
 65-207 2.11e-15

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: 73.71  E-value: 2.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016  65 LSIYMIVFSLFKRAGIMQLILIPVLILHAFQLVLFYLFGeSVIAVDMFLNLPTTNASEAGELLgNIWPSIIIVCVLYIPV 144
Cdd:pfam08019   2 FAALNLLLSLLSWRYLLKPLLILLLLLSAAASYFMDTYG-VVIDRDMIQNVLETDVAEASDLL-SPKLLLYLLLLGVLPA 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1470397016 145 IALASIAVHHKVRRTAvFRKHMITWGIILFIIGSGLVAFEKH-----RdNSYEVKTDIYPANVMYNLY 207
Cdd:pfam08019  80 LLLWRVRIRYRPWLRE-LLSRLALILVSLLVIGLVAFLFYKDyasffR-NHKELRYLINPTNYIYSTV 145
 
Name Accession Description Interval E-value
LptA cd16017
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ...
 238-531 1.07e-105

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: 319.57  E-value: 1.07e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 238 RREIYVLVIGEAGRAENWNLWGYHRETNPLL-KTEDNLVLYKDALTQSNTTHKSVPLILSAADACHYEYLYTHKSIVTAF 316
Cdd:cd16017     1 KPKNVVLVIGESARRDHMSLYGYPRDTTPFLsKLKKNLIVFDNVISCGTSTAVSLPCMLSFANRENYDRAYYQENLIDLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 317 KEAGFKTIFLSNQTPNRSFTDYFAEEADIHInvRPQADGGLITVNKFDGEMLPLLQQYVDSLQENLFIVFHSYGSHFNYK 396
Cdd:cd16017    81 KKAGYKTYWISNQGGCGGYDTRISAIAKIET--VFTNKGSCNSSNCYDEALLPLLDEALADSSKKKLIVLHLMGSHGPYY 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 397 ERYPEEFAKFQPANATEVEYKNKDQLINAYDNSILYTDYFLHSLIGILKNSGADATMIYSPDHGEDLLDDNrkRFLHASP 476
Cdd:cd16017   159 DRYPEEFAKFTPDCDNELQSCSKEELINAYDNSILYTDYVLSQIIERLKKKDKDAALIYFSDHGESLGENG--LYLHGAP 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1470397016 477 IPTYYQIHIPFLMWFSDNYIEARPekYEVARYNSNAPIsSNASIFHTLLEMAEIN 531
Cdd:cd16017   237 YAPKEQYHVPFIIWSSDSYKQRYP--VERLRANKDRPF-SHDNLFHTLLGLLGIK 288
OpgE COG2194
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall ...
 32-548 1.96e-94

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


Pssm-ID: 441797 [Multi-domain]  Cd Length: 537  Bit Score: 299.08  E-value: 1.96e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016  32 FWLFIALNLvPNFCLLF-TEPLSGLGKLILVLVP---LSIYMIVFSLFKRAGIMQLILIPVLILHAFQLVLFYLFGeSVI 107
Cdd:COG2194    18 LYFALFLNL-PFWGRLLaILPLDGVNLLFLLSLPlllLAALNLLLSLLAWRYLFKPLLILLLLISAAASYFMDFYG-VVI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 108 AVDMFLNLPTTNASEAGELLGniwPSIIIVCVLY--IPVIALASIAVHHKVRRTAVFRKhMITWGIILFIIGSGLVAFEK 185
Cdd:COG2194    96 DYGMIQNVLETDPAEASELLS---PKLILWLLLLgvLPALLLWRVRIRYRPLLRELGQR-LALLLLALLVIVLLALLFYK 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 186 H-----RDNSyEVKTDIYPANVMYNLY-YAcvkWNRSMNYPITSKDFTYEASRDSVHQRREIYVLVIGEAGRAENWNLWG 259
Cdd:COG2194   172 DyasffRNHK-ELRYLINPSNFIYALGkYA---KARYFAAPLPLQPLGADAKLAAAGAKPTLVVLVVGETARADNFSLNG 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 260 YHRETNPLLKTEDNLVLYKDALT-QSNTTHkSVPLILSAADACHYEYLYT--HKSIVTAFKEAGFKTIFLSNQTPNRSFT 336
Cdd:COG2194   248 YARDTTPELAKEKNLVSFRDVTScGTATAV-SVPCMFSRLGRADYDPQRAlnQENLLDVLQRAGVKVLWRDNQSGCKGVC 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 337 DYFAEEADIHINVRPQADGGlitvNKFDGEMLPLLQQYVDSLQENLFIVFHSYGSH-FNYKERYPEEFAKFQPA-NATEV 414
Cdd:COG2194   327 DRVPTIDLTADNLPPLCDGG----ECLDEVLLDGLDEALADLAGDKLIVLHQMGSHgPAYYKRYPPEFRKFTPTcDTNDL 402

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 415 EYKNKDQLINAYDNSILYTDYFLHSLIGILKNSGA--DATMIYSPDHGEDlLDDNRKrFLHASP--IPTYYQIHIPFLMW 490
Cdd:COG2194   403 QNCSREELVNAYDNTILYTDYVLSQVIDLLKAKQDryDTAMLYVSDHGES-LGENGL-YLHGTPyaIAPDEQTHVPMIMW 480

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1470397016 491 FSDNYIEARPEKYEVARYNSNAPISSNaSIFHTLLEMAEINTPYFDASYSLVNPGFAR 548
Cdd:COG2194   481 LSDGYAQRYGIDFACLKARADKPYSHD-NLFHTLLGLLDVRTSVYDPELDILAPCRRA 537
PRK10649 PRK10649
phosphoethanolamine transferase CptA;
30-556 6.49e-52

phosphoethanolamine transferase CptA;


Pssm-ID: 182617 [Multi-domain]  Cd Length: 577  Bit Score: 187.22  E-value: 6.49e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016  30 LLFWLFIAlnlVPNFCLLFTEpLSGLGKLILVLVPLSIYMIVFSLFKRAGIMQLILIPVLILHAFQLVLFYL------FG 103
Cdd:PRK10649   22 LFFWFFST---LLQAIIYISG-YSGTNGFRDALLFSSLWLIPVFLFPRRIRIIAAVIGVVLWAASLAALCYYviygqeFS 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 104 ESVIAVdMFlnlpTTNASEAGELLGNIW-PSIIIVCVLYipviALASIAVHHKVR------RTAVFRKHMITWGIILFII 176
Cdd:PRK10649   98 QSVLFV-MF----ETNTNEASEYLSQYFsLKIVLIALAY----TAVAVLLWTRLRpvyipwPWRYVVSFALLYGLILHPI 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 177 GSGLVAFEKHRDNSYE-VKTDIYPAnVMYNLYYACVKWNRSMNypiTSKDFTYEAS--------RDSVHQRREIYVLVIG 247
Cdd:PRK10649  169 AMNTFIKHKPFEKTLDkLASRMEPA-APWQFLTGYYQYRQQLN---SLQKLLNENAalpplanlKDESGNAPRTLVLVIG 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 248 EAGRAENWNLWGYHRETNP----LLKTEDNLVLYKDALTQSNTTHKSVPLILSAADACHYEYLYTHKSIVTAFKEAGFKT 323
Cdd:PRK10649  245 ESTQRGRMSLYGYPRETTPeldaLHKTDPGLTVFNNVVTSRPYTIEILQQALTFADEKNPDLYLTQPSLMNMMKQAGYKT 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 324 IFLSNQTPN---RSFTDYFAEEADIHI---NVRPQadggliTVNKFDGEMLPLLQQYVDSLQENLFIVFHSYGSHFNYKE 397
Cdd:PRK10649  325 FWITNQQTMtarNTMLTVFSRQTDKQYymnQQRTQ------NAREYDTNVLKPFSEVLADPAPKKFIIVHLLGTHIKYKY 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 398 RYPEEFAKFQPANATEVEYKNKDQL--INAYDNSILYTDYFLHSLIGILKNSGADATMIYSPDHGEDLLDD-NRKRFLHA 474
Cdd:PRK10649  399 RYPENQGKFDDRTGHVPPGLNADELesYNDYDNANLYNDHVVASLIKDFKATDPNGFLVYFSDHGEEVYDTpPHKTQGRN 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 475 SPIPTYYQIHIPFLMWFSDNYIEARPEKYEVARynsNAPISSnASIFHTLLEMAEINTPYFDASYSLVNPGFARRPRmYL 554
Cdd:PRK10649  479 EDNPTRHMYTIPFLLWTSEKWQAAHPRDFSQDV---DRKYSL-AELIHTWSDLAGLSYDGYDPTRSLVNPQFKETPR-WI 553


                  ..
gi 1470397016 555 GD 556
Cdd:PRK10649  554 GN 555
PRK11598 PRK11598
putative metal dependent hydrolase; Provisional
 23-544 5.48e-46

putative metal dependent hydrolase; Provisional


Pssm-ID: 183224 [Multi-domain]  Cd Length: 545  Bit Score: 170.24  E-value: 5.48e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016  23 NFVKKPK-------LLFWLFIALNLVPNF------CLLFTEPLSGLGKLILVLVPLSIYMIVFSLFKRAGIMQLILIPVL 89
Cdd:PRK11598    3 RLLKRPSlnlltflLLAAFYITLCLNIAFykqvlqLLPLDSLHNVLVFASMPVVAFSVINIVFTLLSFPWLRRPLACLFI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016  90 ILHAFQLVLFYLFGeSVIAVDMFLNLPTTNASEAGELLGniwPSIIIVCVL--YIPVIALASIavhhKVR------RTAV 161
Cdd:PRK11598   83 LVGAAAQYFMMTYG-IVIDRSMIQNIFETTPAESFALMT---PQMLLWLGLsgVLPALIACWI----KIRpatprwRSVL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 162 FRKHMITWGIILFIigsgLVA--FEKH-----RDNSYEVKTdIYPAN-VMYNLYYACVKWNRSMNYPITSKDftyeASRD 233
Cdd:PRK11598  155 FRLANILVSVLLIL----LVAalFYKDyaslfRNNKELVKS-LTPSNsIVASWSWYSHQRLANLPLVRIGED----AHKN 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 234 SV---HQRREIYVLVIGEAGRAENWNLWGYHRETNPLLKtEDNLVLYKDALTQSNTTHKSVPLILSAADACHY-EYLYTH 309
Cdd:PRK11598  226 PLmqnQKRKNLTILVVGETSRAENFSLGGYPRETNPRLA-KDNVIYFPHTTSCGTATAVSVPCMFSNMPRKHYdEELAHH 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 310 KS-IVTAFKEAGFKTIFLSN---------QTPNRSFTDYfaeeadihinvrpQADGGLITVNKFDGEMLPLLQQYVDSLQ 379
Cdd:PRK11598  305 QEgLLDIIQRAGINVLWNDNdggckgacdRVPHQDVTAL-------------NLPGQCIDGECYDEVLFHGLENYINNLQ 371

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 380 ENLFIVFHSYGSHF-NYKERYPEEFAKFQPA-NATEVEYKNKDQLINAYDNSILYTDYFLHSLIGILK--NSGADATMIY 455
Cdd:PRK11598  372 GDGVIVLHTIGSHGpTYYNRYPPQFRKFTPTcDTNEIQTCTQQQLVNTYDNTILYVDYIVDKAINLLKqhQDKFNTSLVY 451

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 456 SPDHGEDLLDDNrkRFLHASP--IPTYYQIHIPFLMWFSDNY----------IEARPEKYEVARYNsnapissnasIFHT 523
Cdd:PRK11598  452 LSDHGESLGENG--IYLHGLPyaIAPDQQTHVPMLLWLSPDYqkrygvdqqcLQKQAQTQDYSQDN----------LFST 519

                         570       580
                  ....*....|....*....|.
gi 1470397016 524 LLEMAEINTPYFDASYSLVNP 544
Cdd:PRK11598  520 LLGLTGVQTKEYQAADDILQP 540
PRK09598 PRK09598
phosphoethanolamine--lipid A transferase EptA;
58-533 1.40e-42

phosphoethanolamine--lipid A transferase EptA;


Pssm-ID: 236581 [Multi-domain]  Cd Length: 522  Bit Score: 160.33  E-value: 1.40e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016  58 LILVLVPLSIYMIVFSLFKRagIMQLILIPVLILHAFQLVLFYLFGeSVIAVDMFLNLPTTNASEAGELLGniwpsiiIV 137
Cdd:PRK09598   53 VLLFCVNGLLFLLLGLLSRR--LMRLSAIVFSLLNSIAFYFINTYK-VFLNKSMMGNVLNTNTAESSGFLS-------VK 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 138 CVLYIPVIALASIAVHHKVRRTAVFRKHMITWGIILFIIGSGLVA--------FEKHRDN--------SYEVKTDIYPAN 201
Cdd:PRK09598  123 LFIYIVVLGVLPGYIIYKIPLKNSSKKAPFAAILALVLIFLASAFansknwlwFDKHAKFlgglilpwSYSVNTFRVSAH 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 202 vmynLYYACVKwnRSMNYPITSKDftyeasrdsvhQRREIYVLVIGEAGRAENWNLWGYHRETNPLL--KTEDNLVLYKD 279
Cdd:PRK09598  203 ----KFFAPTI--KPLLPPLFSPN-----------HSKSVVVLVIGESARKHNYALYGYEKPTNPRLskRLATHELTLFN 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 280 ALTQSNTTHKSVPLILsaaDACHYEYLYTHKSIVTAFKEAGFKTIFLSNQ--TPNRSFTDYFAEEAdiHINVRPQADGGl 357
Cdd:PRK09598  266 ATSCATYTTASLECIL---DSSFKNTSNAYENLPTYLTRAGIKVFWRSANdgEPNVKVTSYLKNYE--LIQKCPNCEAP- 339

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 358 itvnkFDGEMLPLL-QQYVDSLQENLFIVFHSYGSHF-NYKERYPEEFAKFQP-ANATEVEYKNKDQLINAYDNSILYTD 434
Cdd:PRK09598  340 -----YDESLLYNLpELIKASSNENVLLILHLAGSHGpNYDNKYPLNFRVFKPvCSSVELSSCSKESLINAYDNTIFYND 414

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 435 YFLHSLIGILKNSGADATMIYSPDHGEDLLDDNrkRFLHASP--IPTYYQIHIPFLMWFSDNYIEARpekyevARYNSNA 512
Cdd:PRK09598  415 YLLDKIISMLKNLKQPALMIYLSDHGESLGEGA--FYLHGIPksIAPKEQYEIPFIVWASDSFKKQH------SIIQTQT 486

                         490       500
                  ....*....|....*....|.
gi 1470397016 513 PISSNaSIFHTLLEMAEINTP 533
Cdd:PRK09598  487 PINQN-VIFHSVLGVFDFKNP 506
Sulfatase pfam00884
Sulfatase;
242-530 7.85e-42

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 152.58  E-value: 7.85e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 242 YVLVIGEAGRAENWNLWGYHRETNPLLKTE-DNLVLYKDALTQSNTTHKSVPLILSAADACHYEYL--------YTHKSI 312
Cdd:pfam00884   3 VVLVLGESLRAPDLGLYGYPRPTTPFLDRLaEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYvstpvglpRTEPSL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 313 VTAFKEAGFKTI--------FLSNQTPNRSFTDYFAEEADIHINVRPQADGGLITVNKF--DGEMLPLLQQYVDSLQENL 382
Cdd:pfam00884  83 PDLLKRAGYNTGaigkwhlgWYNNQSPCNLGFDKFFGRNTGSDLYADPPDVPYNCSGGGvsDEALLDEALEFLDNNDKPF 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 383 FIVFHSYGSH--FNYKERYPEEFAKFQPANATEveyknkDQLINAYDNSILYTDYFLHSLIGILKNSG--ADATMIYSPD 458
Cdd:pfam00884 163 FLVLHTLGSHgpPYYPDRYPEKYATFKPSSCSE------EQLLNSYDNTLLYTDDAIGRVLDKLEENGllDNTLVVYTSD 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1470397016 459 HGEDLLDDNRKRFLHASPIPTYYQIHIPFLMWFSDNYiearpekyevARYNSNAPISSNASIFHTLLEMAEI 530
Cdd:pfam00884 237 HGESLGEGGGYLHGGKYDNAPEGGYRVPLLIWSPGGK----------AKGQKSEALVSHVDLFPTILDLAGI 298
PRK11560 PRK11560
kdo(2)-lipid A phosphoethanolamine 7''-transferase;
208-535 1.53e-32

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


Pssm-ID: 183198 [Multi-domain]  Cd Length: 558  Bit Score: 131.70  E-value: 1.53e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 208 YACVKWNRSMNY-----PitSKDFTYEASRDsvhqRREIYVL-VIGEAGRAENWNLWGYHRETNPLLKTEDNLVLYKDal 281
Cdd:PRK11560  216 YAWAQVDESSDNnsllnP--AKKFTYQAPKG----VDDTYVVfIIGETTRWDHMGILGYERNTTPKLAQEKNLAAFRG-- 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 282 TQSNTTHKsvpliLS----------AADACHYeylyTHK--SIVTAFKEAGFKTIFLSNQTP----NRSFTDYFA--EEa 343
Cdd:PRK11560  288 YSCDTATK-----LSlrcmfvreggAEDNPQR----TLKeqNVFAVLKQLGFSSELFAMQSEmwfyNNTMADNYAyrEQ- 357

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 344 dihINVRPQADGglitvnKFDGEMLpLLQQYVDSLQENL----FIVFHSYGSHFNYKERYPEEFAKFQPANATEVEYKNK 419
Cdd:PRK11560  358 ---IGAEPRNRG------KPVDDML-LVDEMKQSLGRNPdgkhLIILHTKGSHYNYTQRYPRSFARYQPECIGVDSGCSK 427

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 420 DQLINAYDNSILYTDYFLHSLIGILKNSgaDATMIYSPDHGEDLlddNRKRFLHASP--IPTYYQIHIPFLMWFSDNYIe 497
Cdd:PRK11560  428 AQLINSYDNSVLYVDHFISSVIDQLRDK--KAIVFYAADHGESI---NEREHLHGTPreMAPPEQFRVPMMVWMSDKYL- 501

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1470397016 498 ARPEkyevarynsnapissNASIFHTLLEMAEINTPYF 535
Cdd:PRK11560  502 ANPD---------------NAQAFAQLKKQADMKVPRR 524
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
 30-576 1.22e-15

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 80.08  E-value: 1.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016  30 LLFWLFIALNLV---PNFCLLFTEPLSGLGKLILVLVPLSIYMIVFSLF-----KRAGIMQLILIPVLILHAFQLVLFYL 101
Cdd:COG1368     7 LLLSLRLVFLLFnfdLSLGEILQAFLYGLRFILYLLLLLLLLLLLLLPLlfrrpKLRWIYLLLVLLLLLLLLVADILYYR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 102 FGESVIAVDMFLNLpttnaSEAGELLGNIWPSIIIVCVLYIPVIALASIAVHHKVRRTAVFRKHMITWGIILFIIGSGLV 181
Cdd:COG1368    87 FFGDRLNFSDLDYL-----GDTGEVLGSLLSSYDLLLLLDLLLLLLLLLLLYRLLKKLRKSLPWRKRLALLLLLLALLLL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 182 A----------FEKHRDNSYEVKTdiYPANVMYNLYYACVKWNRSMNYPITS-------KDFTYEASRDSVHQRREIYVL 244
Cdd:COG1368   162 GirlgedrplnLSDAFSRNNFVNE--LGLNGPYSFYDALRNNKAPATYSEEEaleikkyLKSNRPTPNPFGPAKKPNVVV 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 245 VIGEAGRAENWNLWGYHRETNPLL-KTEDNLVLYKDALTQSNTTHKSVPLILS------AADACHYEYLYTHKSIVTAFK 317
Cdd:COG1368   240 ILLESFSDFFIGALGNGKDVTPFLdSLAKESLYFGNFYSQGGRTSRGEFAVLTglpplpGGSPYKRPGQNNFPSLPSILK 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 318 EAGFKTIFLSNQTP---NRS-------FTDYFAEEadihiNVRPQADGGLITvnkFDGEMLPLLQQYVDSLQENLFIVFH 387
Cdd:COG1368   320 KQGYETSFFHGGDGsfwNRDsfyknlgFDEFYDRE-----DFDDPFDGGWGV---SDEDLFDKALEELEKLKKPFFAFLI 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 388 SYGSHFNYKerYPEEFAKFQPANATEVeyknkdqliNAYDNSILYTDYFLHSLIGILKNSGA--DATMIYSPDH-----G 460
Cdd:COG1368   392 TLSNHGPYT--LPEEDKKIPDYGKTTL---------NNYLNAVRYADQALGEFIEKLKKSGWydNTIFVIYGDHgprspG 460

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 461 EDLLDDNRKRFlhaspiptyyqiHIPFLMWFSDNYieaRPEKYEVarynsnapISSNASIFHTLLEMAEINTP-YFDASY 539
Cdd:COG1368   461 KTDYENPLERY------------RVPLLIYSPGLK---KPKVIDT--------VGSQIDIAPTLLDLLGIDYPsYYAFGR 517

                         570       580       590
                  ....*....|....*....|....*....|....*....
gi 1470397016 540 SLVNPGFARRPRMYLG--DHDQPVNYYEVGLKKQDKEMI 576
Cdd:COG1368   518 DLLSPDTDPFAFRNGGfiTDDYVYVLKTGELTEEDKELE 556
EptA_B_N pfam08019
Phosphoethanolamine transferase EptA/EptB; This entry represents a domain found in a group of ...
 65-207 2.11e-15

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: 73.71  E-value: 2.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016  65 LSIYMIVFSLFKRAGIMQLILIPVLILHAFQLVLFYLFGeSVIAVDMFLNLPTTNASEAGELLgNIWPSIIIVCVLYIPV 144
Cdd:pfam08019   2 FAALNLLLSLLSWRYLLKPLLILLLLLSAAASYFMDTYG-VVIDRDMIQNVLETDVAEASDLL-SPKLLLYLLLLGVLPA 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1470397016 145 IALASIAVHHKVRRTAvFRKHMITWGIILFIIGSGLVAFEKH-----RdNSYEVKTDIYPANVMYNLY 207
Cdd:pfam08019  80 LLLWRVRIRYRPWLRE-LLSRLALILVSLLVIGLVAFLFYKDyasffR-NHKELRYLINPTNYIYSTV 145
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 251-542 1.02e-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: 293767 [Multi-domain]  Cd Length: 271  Bit Score: 53.71  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 251 RAENWNLWGYHRETNPLLkteDNL----VLYKDALTQSNTTHKSVPLILSAADAcHYEYLYTHK------SIVTAFKEAG 320
Cdd:cd16148    12 RADHLGCYGYDRVTTPNL---DRLaaegVVFDNHYSGSNPTLPSRFSLFTGLYP-FYHGVWGGPlepddpTLAEILRKAG 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 321 FKT-IFLSN--QTPNRSFTDYFaeeaDIHINVRPQADGGLITVNKFDGEMLPLLQQYVDSLQ--ENLFIVFHSYGSHFNY 395
Cdd:cd16148    88 YYTaAVSSNphLFGGPGFDRGF----DTFEDFRGQEGDPGEEGDERAERVTDRALEWLDRNAddDPFFLFLHYFDPHEPY 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 396 kerypeefakfqpanateveyknkdqlinAYDNSILYTDYFLHSLIGILKNSG-ADATMIY-SPDHGEdLLDDNRKRFLH 473
Cdd:cd16148   164 -----------------------------LYDAEVRYVDEQIGRLLDKLKELGlLEDTLVIvTSDHGE-EFGEHGLYWGH 213

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1470397016 474 ASPiPTYYQIHIPFLMWFsdnyiearPEKYEVARYNSnapISSNASIFHTLLEMAEINTPYFDASYSLV 542
Cdd:cd16148   214 GSN-LYDEQLHVPLIIRW--------PGKEPGKRVDA---LVSHIDIAPTLLDLLGVEPPDYSDGRSLL 270
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
 290-528 1.14e-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: 50.37  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 290 SVPLILSAADACHYEYLYTHKSIVTAFKEAGFKTIFLSNQTP---NRS-------FTDYFAEEaDIHINVRPQADGGLit 359
Cdd:cd16015    61 GLPPLPLGSGSYTLYKLNPLPSLPSILKEQGYETIFIHGGDAsfyNRDsvypnlgFDEFYDLE-DFPDDEKETNGWGV-- 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 360 vnkFDGEMLPLLQQYVDSLQ-ENLFIVFHSYGSHFNYKerYPEEFAKFqpanatEVEYKNKDQLINAYDNSILYTDYFLH 438
Cdd:cd16015   138 ---SDESLFDQALEELEELKkKPFFIFLVTMSNHGPYD--LPEEKKDE------PLKVEEDKTELENYLNAIHYTDKALG 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470397016 439 SLIGILKNSGA--DATMIYSPDHGEDLLDDNRKRFLHaspIPTYYqiHIPFLMWfsDNYIEARPEKYEVArynsnapisS 516
Cdd:cd16015   207 EFIEKLKKSGLyeNTIIVIYGDHLPSLGSDYDETDED---PLDLY--RTPLLIY--SPGLKKPKKIDRVG---------S 270

                         250
                  ....*....|..
gi 1470397016 517 NASIFHTLLEMA 528
Cdd:cd16015   271 QIDIAPTLLDLL 282
 
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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