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Conserved domains on  [gi|495123759|ref|WP_007848572|]
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phosphoethanolamine transferase [Cronobacter sakazakii]

Protein Classification

phosphoethanolamine transferase( domain architecture ID 10887874)

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 ...
214-483 5.22e-80

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: 251.77  E-value: 5.22e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 214 KYHTYVVVIGESVRRDAVGAFGGQWDNSPFASHV--NGYLFTDYIAASGSTQKSLGLTLNRVV---DNKPQYQDNFVTLA 288
Cdd:cd16017    1 KPKNVVLVIGESARRDHMSLYGYPRDTTPFLSKLkkNLIVFDNVISCGTSTAVSLPCMLSFANrenYDRAYYQENLIDLA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 289 NRAGFQTWWFSNQGQIGEYDTAIASIAKRadeVHFLKSGDFEADKNTRDEALLKMTAQVLAtQRPQPQLIVLHLMGSHPQ 368
Cdd:cd16017   81 KKAGYKTYWISNQGGCGGYDTRISAIAKI---ETVFTNKGSCNSSNCYDEALLPLLDEALA-DSSKKKLIVLHLMGSHGP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 369 ACDRTQGKYDEFV-----------QSKETSCYLYSIRQTDDLLSKLYQQLQNSGQSFSMVYFSDHGLAIKERGKavqYLa 437
Cdd:cd16017  157 YYDRYPEEFAKFTpdcdnelqscsKEELINAYDNSILYTDYVLSQIIERLKKKDKDAALIYFSDHGESLGENGL---YL- 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 495123759 438 HDD--KFQQNFQVPFMVLSSDD--------KAHRIIKARRSANDFLSFFVQWTGIK 483
Cdd:cd16017  233 HGApyAPKEQYHVPFIIWSSDSykqrypveRLRANKDRPFSHDNLFHTLLGLLGIK 288
 
Name Accession Description Interval E-value
LptA cd16017
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ...
214-483 5.22e-80

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: 251.77  E-value: 5.22e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 214 KYHTYVVVIGESVRRDAVGAFGGQWDNSPFASHV--NGYLFTDYIAASGSTQKSLGLTLNRVV---DNKPQYQDNFVTLA 288
Cdd:cd16017    1 KPKNVVLVIGESARRDHMSLYGYPRDTTPFLSKLkkNLIVFDNVISCGTSTAVSLPCMLSFANrenYDRAYYQENLIDLA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 289 NRAGFQTWWFSNQGQIGEYDTAIASIAKRadeVHFLKSGDFEADKNTRDEALLKMTAQVLAtQRPQPQLIVLHLMGSHPQ 368
Cdd:cd16017   81 KKAGYKTYWISNQGGCGGYDTRISAIAKI---ETVFTNKGSCNSSNCYDEALLPLLDEALA-DSSKKKLIVLHLMGSHGP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 369 ACDRTQGKYDEFV-----------QSKETSCYLYSIRQTDDLLSKLYQQLQNSGQSFSMVYFSDHGLAIKERGKavqYLa 437
Cdd:cd16017  157 YYDRYPEEFAKFTpdcdnelqscsKEELINAYDNSILYTDYVLSQIIERLKKKDKDAALIYFSDHGESLGENGL---YL- 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 495123759 438 HDD--KFQQNFQVPFMVLSSDD--------KAHRIIKARRSANDFLSFFVQWTGIK 483
Cdd:cd16017  233 HGApyAPKEQYHVPFIIWSSDSykqrypveRLRANKDRPFSHDNLFHTLLGLLGIK 288
Sulfatase pfam00884
Sulfatase;
217-482 6.35e-50

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 173.38  E-value: 6.35e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759  217 TYVVVIGESVRRDAVGAFGGQWDNSPFASHV--NGYLFTDYIAASGSTQKSLGLTLNR-----------VVDNKPQYQDN 283
Cdd:pfam00884   2 NVVLVLGESLRAPDLGLYGYPRPTTPFLDRLaeEGLLFSNFYSGGTLTAPSRFALLTGlpphnfgsyvsTPVGLPRTEPS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759  284 FVTLANRAGFQT--------WWFSNQG-QIGEYDTAIASIAKRADEVHFLKSGDFEADKNTRDEALLKMTAQVLAtQRPQ 354
Cdd:pfam00884  82 LPDLLKRAGYNTgaigkwhlGWYNNQSpCNLGFDKFFGRNTGSDLYADPPDVPYNCSGGGVSDEALLDEALEFLD-NNDK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759  355 PQLIVLHLMGSH--PQACDRTQGKYDEFV-----QSKETSCYLYSIRQTDDLLSKLYQQLQNSGQ--SFSMVYFSDHGLA 425
Cdd:pfam00884 161 PFFLVLHTLGSHgpPYYPDRYPEKYATFKpsscsEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLldNTLVVYTSDHGES 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 495123759  426 IKERGKAVQYLAHDDKFQQNFQVPFMVLSSDDKAH-RIIKARRSANDFLSFFVQWTGI 482
Cdd:pfam00884 241 LGEGGGYLHGGKYDNAPEGGYRVPLLIWSPGGKAKgQKSEALVSHVDLFPTILDLAGI 298
OpgE COG2194
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall ...
31-457 1.20e-29

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


Pssm-ID: 441797 [Multi-domain]  Cd Length: 537  Bit Score: 122.27  E-value: 1.20e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759  31 NFALGYEFSLLYAIAFCCVLLLLWKTAPRAQKGLLAVCSLVAGLYFPFGQTYGA-PNFNTLLALHATNMEESTELLTiFP 109
Cdd:COG2194   40 GVNLLFLLSLPLLLLAALNLLLSLLAWRYLFKPLLILLLLISAAASYFMDFYGVvIDYGMIQNVLETDPAEASELLS-PK 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 110 WYSYLVSLFIFTLGIIALRRTPQAPSRWQP-----FDSLCLAVSVVSFFVTpvqNQLYGGVF----ALKDSGYPVFRFVK 180
Cdd:COG2194  119 LILWLLLLGVLPALLLWRVRIRYRPLLRELgqrlaLLLLALLVIVLLALLF---YKDYASFFrnhkELRYLINPSNFIYA 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 181 DVVVNNREVLEEQQRMEALSRmkDSwNVLAVAPKYHTYVVVIGESVRRDAVGAFGGQWDNSPFASHVNGYL-FTDYIAAS 259
Cdd:COG2194  196 LGKYAKARYFAAPLPLQPLGA--DA-KLAAAGAKPTLVVLVVGETARADNFSLNGYARDTTPELAKEKNLVsFRDVTSCG 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 260 GSTQKSL-----GLTLNRVVDNKPQYQDNFVTLANRAGFQTWWFSNQ-GQIGEYDTaIASIAKRADevhflKSGDFEADK 333
Cdd:COG2194  273 TATAVSVpcmfsRLGRADYDPQRALNQENLLDVLQRAGVKVLWRDNQsGCKGVCDR-VPTIDLTAD-----NLPPLCDGG 346
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 334 NTRDEALLKMTAQVLAtQRPQPQLIVLHLMGSH--------PQA-------CDRTQGK---YDEFVQSketscYLYSIRQ 395
Cdd:COG2194  347 ECLDEVLLDGLDEALA-DLAGDKLIVLHQMGSHgpayykryPPEfrkftptCDTNDLQncsREELVNA-----YDNTILY 420
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495123759 396 TDDLLSKLYQQLQNSGQSF--SMVYFSDHGLAIKERGKavqYL-AHDDKF--QQNFQVPFMVLSSDD 457
Cdd:COG2194  421 TDYVLSQVIDLLKAKQDRYdtAMLYVSDHGESLGENGL---YLhGTPYAIapDEQTHVPMIMWLSDG 484
PRK10649 PRK10649
phosphoethanolamine transferase CptA;
19-456 1.66e-17

phosphoethanolamine transferase CptA;


Pssm-ID: 182617 [Multi-domain]  Cd Length: 577  Bit Score: 85.53  E-value: 1.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759  19 WIGFY-FLQSLLinfalgyeFSLLYAIAfccVLLLlwktaPRAQKGLLAV-------CSLVA-GLYFPFGQTYGApnfNT 89
Cdd:PRK10649  40 YSGTNgFRDALL--------FSSLWLIP---VFLF-----PRRIRIIAAVigvvlwaASLAAlCYYVIYGQEFSQ---SV 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759  90 LLALHATNMEESTELLT-IFPWYSYLVSLfIFTLGIIAL--RRTP-QAPSRWQPFDSLCLAVSVVsffVTPVQNQLY--- 162
Cdd:PRK10649 101 LFVMFETNTNEASEYLSqYFSLKIVLIAL-AYTAVAVLLwtRLRPvYIPWPWRYVVSFALLYGLI---LHPIAMNTFikh 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 163 ------GGVFALKDSGYPVFRFVKDV------VVNNREVLEEQQRMEALSRMKDSwnvLAVAPKyhTYVVVIGESVRRDA 230
Cdd:PRK10649 177 kpfektLDKLASRMEPAAPWQFLTGYyqyrqqLNSLQKLLNENAALPPLANLKDE---SGNAPR--TLVLVIGESTQRGR 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 231 VGAFGGQWDNSP-----FASHVNGYLFTDYIAASGSTQKSL--GLTLNRVvDNKPQY--QDNFVTLANRAGFQTWWFSNQ 301
Cdd:PRK10649 252 MSLYGYPRETTPeldalHKTDPGLTVFNNVVTSRPYTIEILqqALTFADE-KNPDLYltQPSLMNMMKQAGYKTFWITNQ 330
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 302 GQIGEYDTAIASIAKRADEVHFLKSgdfEADKNTR--DEALLKMTAQVLATQRPQpQLIVLHLMGSH-------PQACDR 372
Cdd:PRK10649 331 QTMTARNTMLTVFSRQTDKQYYMNQ---QRTQNAReyDTNVLKPFSEVLADPAPK-KFIIVHLLGTHikykyryPENQGK 406
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 373 ---TQGKYDEFVQSKETSCY-LY--SIRQTDDLLSKLYQQLQNSGQSFSMVYFSDHGLAI-KERGKAVQYLAHDDKFQQN 445
Cdd:PRK10649 407 fddRTGHVPPGLNADELESYnDYdnANLYNDHVVASLIKDFKATDPNGFLVYFSDHGEEVyDTPPHKTQGRNEDNPTRHM 486
                        490
                 ....*....|.
gi 495123759 446 FQVPFMVLSSD 456
Cdd:PRK10649 487 YTIPFLLWTSE 497
 
Name Accession Description Interval E-value
LptA cd16017
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ...
214-483 5.22e-80

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: 251.77  E-value: 5.22e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 214 KYHTYVVVIGESVRRDAVGAFGGQWDNSPFASHV--NGYLFTDYIAASGSTQKSLGLTLNRVV---DNKPQYQDNFVTLA 288
Cdd:cd16017    1 KPKNVVLVIGESARRDHMSLYGYPRDTTPFLSKLkkNLIVFDNVISCGTSTAVSLPCMLSFANrenYDRAYYQENLIDLA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 289 NRAGFQTWWFSNQGQIGEYDTAIASIAKRadeVHFLKSGDFEADKNTRDEALLKMTAQVLAtQRPQPQLIVLHLMGSHPQ 368
Cdd:cd16017   81 KKAGYKTYWISNQGGCGGYDTRISAIAKI---ETVFTNKGSCNSSNCYDEALLPLLDEALA-DSSKKKLIVLHLMGSHGP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 369 ACDRTQGKYDEFV-----------QSKETSCYLYSIRQTDDLLSKLYQQLQNSGQSFSMVYFSDHGLAIKERGKavqYLa 437
Cdd:cd16017  157 YYDRYPEEFAKFTpdcdnelqscsKEELINAYDNSILYTDYVLSQIIERLKKKDKDAALIYFSDHGESLGENGL---YL- 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 495123759 438 HDD--KFQQNFQVPFMVLSSDD--------KAHRIIKARRSANDFLSFFVQWTGIK 483
Cdd:cd16017  233 HGApyAPKEQYHVPFIIWSSDSykqrypveRLRANKDRPFSHDNLFHTLLGLLGIK 288
Sulfatase pfam00884
Sulfatase;
217-482 6.35e-50

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 173.38  E-value: 6.35e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759  217 TYVVVIGESVRRDAVGAFGGQWDNSPFASHV--NGYLFTDYIAASGSTQKSLGLTLNR-----------VVDNKPQYQDN 283
Cdd:pfam00884   2 NVVLVLGESLRAPDLGLYGYPRPTTPFLDRLaeEGLLFSNFYSGGTLTAPSRFALLTGlpphnfgsyvsTPVGLPRTEPS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759  284 FVTLANRAGFQT--------WWFSNQG-QIGEYDTAIASIAKRADEVHFLKSGDFEADKNTRDEALLKMTAQVLAtQRPQ 354
Cdd:pfam00884  82 LPDLLKRAGYNTgaigkwhlGWYNNQSpCNLGFDKFFGRNTGSDLYADPPDVPYNCSGGGVSDEALLDEALEFLD-NNDK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759  355 PQLIVLHLMGSH--PQACDRTQGKYDEFV-----QSKETSCYLYSIRQTDDLLSKLYQQLQNSGQ--SFSMVYFSDHGLA 425
Cdd:pfam00884 161 PFFLVLHTLGSHgpPYYPDRYPEKYATFKpsscsEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLldNTLVVYTSDHGES 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 495123759  426 IKERGKAVQYLAHDDKFQQNFQVPFMVLSSDDKAH-RIIKARRSANDFLSFFVQWTGI 482
Cdd:pfam00884 241 LGEGGGYLHGGKYDNAPEGGYRVPLLIWSPGGKAKgQKSEALVSHVDLFPTILDLAGI 298
OpgE COG2194
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall ...
31-457 1.20e-29

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


Pssm-ID: 441797 [Multi-domain]  Cd Length: 537  Bit Score: 122.27  E-value: 1.20e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759  31 NFALGYEFSLLYAIAFCCVLLLLWKTAPRAQKGLLAVCSLVAGLYFPFGQTYGA-PNFNTLLALHATNMEESTELLTiFP 109
Cdd:COG2194   40 GVNLLFLLSLPLLLLAALNLLLSLLAWRYLFKPLLILLLLISAAASYFMDFYGVvIDYGMIQNVLETDPAEASELLS-PK 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 110 WYSYLVSLFIFTLGIIALRRTPQAPSRWQP-----FDSLCLAVSVVSFFVTpvqNQLYGGVF----ALKDSGYPVFRFVK 180
Cdd:COG2194  119 LILWLLLLGVLPALLLWRVRIRYRPLLRELgqrlaLLLLALLVIVLLALLF---YKDYASFFrnhkELRYLINPSNFIYA 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 181 DVVVNNREVLEEQQRMEALSRmkDSwNVLAVAPKYHTYVVVIGESVRRDAVGAFGGQWDNSPFASHVNGYL-FTDYIAAS 259
Cdd:COG2194  196 LGKYAKARYFAAPLPLQPLGA--DA-KLAAAGAKPTLVVLVVGETARADNFSLNGYARDTTPELAKEKNLVsFRDVTSCG 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 260 GSTQKSL-----GLTLNRVVDNKPQYQDNFVTLANRAGFQTWWFSNQ-GQIGEYDTaIASIAKRADevhflKSGDFEADK 333
Cdd:COG2194  273 TATAVSVpcmfsRLGRADYDPQRALNQENLLDVLQRAGVKVLWRDNQsGCKGVCDR-VPTIDLTAD-----NLPPLCDGG 346
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 334 NTRDEALLKMTAQVLAtQRPQPQLIVLHLMGSH--------PQA-------CDRTQGK---YDEFVQSketscYLYSIRQ 395
Cdd:COG2194  347 ECLDEVLLDGLDEALA-DLAGDKLIVLHQMGSHgpayykryPPEfrkftptCDTNDLQncsREELVNA-----YDNTILY 420
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495123759 396 TDDLLSKLYQQLQNSGQSF--SMVYFSDHGLAIKERGKavqYL-AHDDKF--QQNFQVPFMVLSSDD 457
Cdd:COG2194  421 TDYVLSQVIDLLKAKQDRYdtAMLYVSDHGESLGENGL---YLhGTPYAIapDEQTHVPMIMWLSDG 484
PRK10649 PRK10649
phosphoethanolamine transferase CptA;
19-456 1.66e-17

phosphoethanolamine transferase CptA;


Pssm-ID: 182617 [Multi-domain]  Cd Length: 577  Bit Score: 85.53  E-value: 1.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759  19 WIGFY-FLQSLLinfalgyeFSLLYAIAfccVLLLlwktaPRAQKGLLAV-------CSLVA-GLYFPFGQTYGApnfNT 89
Cdd:PRK10649  40 YSGTNgFRDALL--------FSSLWLIP---VFLF-----PRRIRIIAAVigvvlwaASLAAlCYYVIYGQEFSQ---SV 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759  90 LLALHATNMEESTELLT-IFPWYSYLVSLfIFTLGIIAL--RRTP-QAPSRWQPFDSLCLAVSVVsffVTPVQNQLY--- 162
Cdd:PRK10649 101 LFVMFETNTNEASEYLSqYFSLKIVLIAL-AYTAVAVLLwtRLRPvYIPWPWRYVVSFALLYGLI---LHPIAMNTFikh 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 163 ------GGVFALKDSGYPVFRFVKDV------VVNNREVLEEQQRMEALSRMKDSwnvLAVAPKyhTYVVVIGESVRRDA 230
Cdd:PRK10649 177 kpfektLDKLASRMEPAAPWQFLTGYyqyrqqLNSLQKLLNENAALPPLANLKDE---SGNAPR--TLVLVIGESTQRGR 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 231 VGAFGGQWDNSP-----FASHVNGYLFTDYIAASGSTQKSL--GLTLNRVvDNKPQY--QDNFVTLANRAGFQTWWFSNQ 301
Cdd:PRK10649 252 MSLYGYPRETTPeldalHKTDPGLTVFNNVVTSRPYTIEILqqALTFADE-KNPDLYltQPSLMNMMKQAGYKTFWITNQ 330
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 302 GQIGEYDTAIASIAKRADEVHFLKSgdfEADKNTR--DEALLKMTAQVLATQRPQpQLIVLHLMGSH-------PQACDR 372
Cdd:PRK10649 331 QTMTARNTMLTVFSRQTDKQYYMNQ---QRTQNAReyDTNVLKPFSEVLADPAPK-KFIIVHLLGTHikykyryPENQGK 406
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 373 ---TQGKYDEFVQSKETSCY-LY--SIRQTDDLLSKLYQQLQNSGQSFSMVYFSDHGLAI-KERGKAVQYLAHDDKFQQN 445
Cdd:PRK10649 407 fddRTGHVPPGLNADELESYnDYdnANLYNDHVVASLIKDFKATDPNGFLVYFSDHGEEVyDTPPHKTQGRNEDNPTRHM 486
                        490
                 ....*....|.
gi 495123759 446 FQVPFMVLSSD 456
Cdd:PRK10649 487 YTIPFLLWTSE 497
PRK09598 PRK09598
phosphoethanolamine--lipid A transferase EptA;
216-470 2.08e-15

phosphoethanolamine--lipid A transferase EptA;


Pssm-ID: 236581 [Multi-domain]  Cd Length: 522  Bit Score: 78.67  E-value: 2.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 216 HTYVV-VIGESVRRDAVGAFGGQWDNSPFAS---HVNGYLFTDYIAASGSTQKSLGLTLNRVVDNKPQYQDNFVTLANRA 291
Cdd:PRK09598 223 KSVVVlVIGESARKHNYALYGYEKPTNPRLSkrlATHELTLFNATSCATYTTASLECILDSSFKNTSNAYENLPTYLTRA 302
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 292 GFQTWWFSNQGqiGEYDTAIASiakradevhFLKSGDFEAD-KNTR---DEALLKMTAQVLATQRPQPQLIVLHLMGSHP 367
Cdd:PRK09598 303 GIKVFWRSAND--GEPNVKVTS---------YLKNYELIQKcPNCEapyDESLLYNLPELIKASSNENVLLILHLAGSHG 371
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 368 QACDRTQGKYDEFVQ-----------SKET--SCYLYSIRQTDDLLSKLYQQLQNSGQSFSMVYFSDHGLAIKERGKAVQ 434
Cdd:PRK09598 372 PNYDNKYPLNFRVFKpvcssvelsscSKESliNAYDNTIFYNDYLLDKIISMLKNLKQPALMIYLSDHGESLGEGAFYLH 451
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 495123759 435 YLAHDDKFQQNFQVPFMVLSSDD--KAHRIIKARRSAN 470
Cdd:PRK09598 452 GIPKSIAPKEQYEIPFIVWASDSfkKQHSIIQTQTPIN 489
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
219-473 1.88e-11

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: 64.63  E-value: 1.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 219 VVVIGESVRRDAVGAFGGQWDNSPF--ASHVNGYLFTDYIAASG---------STQKSLGLTLNRVVDNKPQYQDNFVTL 287
Cdd:cd16015    4 IVILLESFSDPYIDKDVGGEDLTPNlnKLAKEGLYFGNFYSPGFgggtangefEVLTGLPPLPLGSGSYTLYKLNPLPSL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 288 ANragfqtwWFSNQGqigeYDTAI-----ASIAKRA--------DEVHFLKsgDFEADKNTR------DEALLKMTAQVL 348
Cdd:cd16015   84 PS-------ILKEQG----YETIFihggdASFYNRDsvypnlgfDEFYDLE--DFPDDEKETngwgvsDESLFDQALEEL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 349 ATQRPQPQLIVLHLMGSHP---QACDRTQGKYDEFVQSKETSCYLYSIRQTDDLLSKLYQQLQNSGQS----FsmVYFSD 421
Cdd:cd16015  151 EELKKKPFFIFLVTMSNHGpydLPEEKKDEPLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYentiI--VIYGD 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 495123759 422 HGLAIKErgkavQYLAHDDKFQQNFQVPFMVLSSDDKAHRIIKARRSANDFL 473
Cdd:cd16015  229 HLPSLGS-----DYDETDEDPLDLYRTPLLIYSPGLKKPKKIDRVGSQIDIA 275
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
22-473 4.18e-11

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 65.44  E-value: 4.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759  22 FYFLQSLLINFALGYEFSLLYAIAFCCVLLLLWKTAPRAQKGLLAVCSLVAGLYF---PFGQTYGAP-NFNTLLALhaTN 97
Cdd:COG1368   25 GEILQAFLYGLRFILYLLLLLLLLLLLLLPLLFRRPKLRWIYLLLVLLLLLLLLVadiLYYRFFGDRlNFSDLDYL--GD 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759  98 MEESTELLTIFPWYSYLVSLFIFTLGIIALRRTPQAPSRWQPFDSLcLAVSVVSFFVTPVQNQLYGGVFALKDSGYPVFR 177
Cdd:COG1368  103 TGEVLGSLLSSYDLLLLLDLLLLLLLLLLLYRLLKKLRKSLPWRKR-LALLLLLLALLLLGIRLGEDRPLNLSDAFSRNN 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 178 FVKDVVVN-------------NREVLEEQQRMEALSRMKDSWNVLAVAPKYHTY--VVVIGESVRRDAVGAFGGQWDNSP 242
Cdd:COG1368  182 FVNELGLNgpysfydalrnnkAPATYSEEEALEIKKYLKSNRPTPNPFGPAKKPnvVVILLESFSDFFIGALGNGKDVTP 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 243 F-ASHV-NGYLFTDYIAASGSTQKSLGLTLNRVVDNKPQY------QDNFVTLA---NRAGFQT---------WW----- 297
Cdd:COG1368  262 FlDSLAkESLYFGNFYSQGGRTSRGEFAVLTGLPPLPGGSpykrpgQNNFPSLPsilKKQGYETsffhggdgsFWnrdsf 341
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 298 FSNQGqigeYDtaiasiakradevHFLKSGDFEADKNT----RDEALLKMTAQVLATQrPQPQLIVLHLMGSH-----PQ 368
Cdd:COG1368  342 YKNLG----FD-------------EFYDREDFDDPFDGgwgvSDEDLFDKALEELEKL-KKPFFAFLITLSNHgpytlPE 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 369 ACDRTQGKYDEFVQSketscYLYSIRQTDDLLSKLYQQLQNSGQS----FsmVYFSDHGLAIKERGKAVQYLahddkfqQ 444
Cdd:COG1368  404 EDKKIPDYGKTTLNN-----YLNAVRYADQALGEFIEKLKKSGWYdntiF--VIYGDHGPRSPGKTDYENPL-------E 469
                        490       500
                 ....*....|....*....|....*....
gi 495123759 445 NFQVPFMVLSSDDKAHRIIKARRSANDFL 473
Cdd:COG1368  470 RYRVPLLIYSPGLKKPKVIDTVGSQIDIA 498
PRK11560 PRK11560
kdo(2)-lipid A phosphoethanolamine 7''-transferase;
204-456 7.97e-08

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


Pssm-ID: 183198 [Multi-domain]  Cd Length: 558  Bit Score: 55.05  E-value: 7.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 204 DSWNVLAVAPKYH---------TYVV-VIGESVRRDAVGAFGGQWDNSP-FASHVNGYLFTDYiAASGSTQKSLGLTLNR 272
Cdd:PRK11560 226 DNNSLLNPAKKFTyqapkgvddTYVVfIIGETTRWDHMGILGYERNTTPkLAQEKNLAAFRGY-SCDTATKLSLRCMFVR 304
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 273 V--VDNKPQY----QDNFVTLaNRAGFQTWWFSNQGQIGEYDTAIA-SIAKR----ADEVHFLKSGDfeadkntrDEALL 341
Cdd:PRK11560 305 EggAEDNPQRtlkeQNVFAVL-KQLGFSSELFAMQSEMWFYNNTMAdNYAYReqigAEPRNRGKPVD--------DMLLV 375
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 342 KMTAQVLAtQRPQ-PQLIVLHLMGSH---PQACDRTQGKYDEFVQSKETSC--------YLYSIRQTDDLLSKLYQQLQN 409
Cdd:PRK11560 376 DEMKQSLG-RNPDgKHLIILHTKGSHynyTQRYPRSFARYQPECIGVDSGCskaqlinsYDNSVLYVDHFISSVIDQLRD 454
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 495123759 410 sgQSFSMVYFSDHGLAIKER----GKAVQYLAhddkfQQNFQVPFMVLSSD 456
Cdd:PRK11560 455 --KKAIVFYAADHGESINERehlhGTPREMAP-----PEQFRVPMMVWMSD 498
PRK11598 PRK11598
putative metal dependent hydrolase; Provisional
358-461 2.03e-05

putative metal dependent hydrolase; Provisional


Pssm-ID: 183224 [Multi-domain]  Cd Length: 545  Bit Score: 47.36  E-value: 2.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 358 IVLHLMGSH-PQACDRTQGKYDEFVQSKET----SC--------YLYSIRQTDDLLSKLYQQLQNSGQSF--SMVYFSDH 422
Cdd:PRK11598 376 IVLHTIGSHgPTYYNRYPPQFRKFTPTCDTneiqTCtqqqlvntYDNTILYVDYIVDKAINLLKQHQDKFntSLVYLSDH 455
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 495123759 423 GLAIKERGKAVQYLAHDDKFQQNFQVPFMVLSSDDKAHR 461
Cdd:PRK11598 456 GESLGENGIYLHGLPYAIAPDQQTHVPMLLWLSPDYQKR 494
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
271-482 5.25e-04

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293760 [Multi-domain]  Cd Length: 321  Bit Score: 42.14  E-value: 5.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 271 NRVVDNKPQYQDNFVTLANRAGfqtwwfsNQGqigeYDTAiaSIAKradeVHFLKSGD---FEADKNTRDEAL--LKMTA 345
Cdd:cd16037   65 TGVWDNADPYDGDVPSWGHALR-------AAG----YETV--LIGK----LHFRGEDQrhgFRYDRDVTEAAVdwLREEA 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495123759 346 QvlatqRPQPQLIVLHLMGSH-PQACDrtQGKYDEFVQsKETSCYLYSIRQTDDLLSKLYQQLQNSGQS--FSMVYFSDH 422
Cdd:cd16037  128 A-----DDKPWFLFVGFVAPHfPLIAP--QEFYDLYVR-RARAAYYGLVEFLDENIGRVLDALEELGLLdnTLIIYTSDH 199
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495123759 423 GLAIKERG---KAVQYlahddkfQQNFQVPfMVLSSDD-KAHRIIKARRSANDFLSFFVQWTGI 482
Cdd:cd16037  200 GDMLGERGlwgKSTMY-------EESVRVP-MIISGPGiPAGKRVKTPVSLVDLAPTILEAAGA 255
 
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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