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Conserved domains on  [gi|1394421524|ref|WP_110014420|]
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MULTISPECIES: phosphoethanolamine--lipid A transferase EptA [Idiomarina]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK09598 super family cl35866
phosphoethanolamine--lipid A transferase EptA;
12-520 1.24e-179

phosphoethanolamine--lipid A transferase EptA;


The actual alignment was detected with superfamily member PRK09598:

Pssm-ID: 236581 [Multi-domain]  Cd Length: 522  Bit Score: 515.10  E-value: 1.24e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524  12 LKASSFTFWVSIVMTFAYNLVLLEYVNQNTNvwstsGLGIFLSTVVIVFIFSYTIFSLLALISPTVLKIFLVIITVLNAS 91
Cdd:PRK09598   13 LSCLQAGLLYSLLNGVLYHFPLFAYVYKESN-----QVSFIAMLVVLLFCVNGLLFLLLGLLSRRLMRLSAIVFSLLNSI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524  92 AIYYMSNYQVVLDRTMMGNIFNTRYSESIELLTVSLVFPIIMLGLMPACFVALIKIKQVDRVKILGNASIALVVSGAFLY 171
Cdd:PRK09598   88 AFYFINTYKVFLNKSMMGNVLNTNTAESSGFLSVKLFIYIVVLGVLPGYIIYKIPLKNSSKKAPFAAILALVLIFLASAF 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 172 TNSTSWLWIDKHASVLGGKILPWSYIINSGRYYSSINRTTDGQKALPDGHFLDNNKTVFVLVIGETARAANFSLYGYSKL 251
Cdd:PRK09598  168 ANSKNWLWFDKHAKFLGGLILPWSYSVNTFRVSAHKFFAPTIKPLLPPLFSPNHSKSVVVLVIGESARKHNYALYGYEKP 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 252 TNPKLA--EQPNLLVLNNTKSCTTYTTGSLACILAPS--DQYLDFEALPTYLARHGVDVQWRTNNWGEPPIKVTSYTEAG 327
Cdd:PRK09598  248 TNPRLSkrLATHELTLFNATSCATYTTASLECILDSSfkNTSNAYENLPTYLTRAGIKVFWRSANDGEPNVKVTSYLKNY 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 328 ELRADCVGEGCKLDEVLLTNLINAIDSSDKQKIFVVLHTKGSHGPSYYSRYTKEFNQFTPVCRDEEISKCSPEELINAYD 407
Cdd:PRK09598  328 ELIQKCPNCEAPYDESLLYNLPELIKASSNENVLLILHLAGSHGPNYDNKYPLNFRVFKPVCSSVELSSCSKESLINAYD 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 408 NTLLYTDHFLTTLIMELQTLaKTSSAMMYISDHGESLGEHGLYLHGTPYSFAPDYQKDIPFLFWASDTFldarnLKLKNL 487
Cdd:PRK09598  408 NTIFYNDYLLDKIISMLKNL-KQPALMIYLSDHGESLGEGAFYLHGIPKSIAPKEQYEIPFIVWASDSF-----KKQHSI 481
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 1394421524 488 NQANSH-NQFNVFHTVLGALSLE--SSIYDSTLDVL 520
Cdd:PRK09598  482 IQTQTPiNQNVIFHSVLGVFDFKnpSAVYRPSLDLF 517
 
Name Accession Description Interval E-value
PRK09598 PRK09598
phosphoethanolamine--lipid A transferase EptA;
12-520 1.24e-179

phosphoethanolamine--lipid A transferase EptA;


Pssm-ID: 236581 [Multi-domain]  Cd Length: 522  Bit Score: 515.10  E-value: 1.24e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524  12 LKASSFTFWVSIVMTFAYNLVLLEYVNQNTNvwstsGLGIFLSTVVIVFIFSYTIFSLLALISPTVLKIFLVIITVLNAS 91
Cdd:PRK09598   13 LSCLQAGLLYSLLNGVLYHFPLFAYVYKESN-----QVSFIAMLVVLLFCVNGLLFLLLGLLSRRLMRLSAIVFSLLNSI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524  92 AIYYMSNYQVVLDRTMMGNIFNTRYSESIELLTVSLVFPIIMLGLMPACFVALIKIKQVDRVKILGNASIALVVSGAFLY 171
Cdd:PRK09598   88 AFYFINTYKVFLNKSMMGNVLNTNTAESSGFLSVKLFIYIVVLGVLPGYIIYKIPLKNSSKKAPFAAILALVLIFLASAF 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 172 TNSTSWLWIDKHASVLGGKILPWSYIINSGRYYSSINRTTDGQKALPDGHFLDNNKTVFVLVIGETARAANFSLYGYSKL 251
Cdd:PRK09598  168 ANSKNWLWFDKHAKFLGGLILPWSYSVNTFRVSAHKFFAPTIKPLLPPLFSPNHSKSVVVLVIGESARKHNYALYGYEKP 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 252 TNPKLA--EQPNLLVLNNTKSCTTYTTGSLACILAPS--DQYLDFEALPTYLARHGVDVQWRTNNWGEPPIKVTSYTEAG 327
Cdd:PRK09598  248 TNPRLSkrLATHELTLFNATSCATYTTASLECILDSSfkNTSNAYENLPTYLTRAGIKVFWRSANDGEPNVKVTSYLKNY 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 328 ELRADCVGEGCKLDEVLLTNLINAIDSSDKQKIFVVLHTKGSHGPSYYSRYTKEFNQFTPVCRDEEISKCSPEELINAYD 407
Cdd:PRK09598  328 ELIQKCPNCEAPYDESLLYNLPELIKASSNENVLLILHLAGSHGPNYDNKYPLNFRVFKPVCSSVELSSCSKESLINAYD 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 408 NTLLYTDHFLTTLIMELQTLaKTSSAMMYISDHGESLGEHGLYLHGTPYSFAPDYQKDIPFLFWASDTFldarnLKLKNL 487
Cdd:PRK09598  408 NTIFYNDYLLDKIISMLKNL-KQPALMIYLSDHGESLGEGAFYLHGIPKSIAPKEQYEIPFIVWASDSF-----KKQHSI 481
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 1394421524 488 NQANSH-NQFNVFHTVLGALSLE--SSIYDSTLDVL 520
Cdd:PRK09598  482 IQTQTPiNQNVIFHSVLGVFDFKnpSAVYRPSLDLF 517
OpgE COG2194
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall ...
12-522 4.13e-154

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


Pssm-ID: 441797 [Multi-domain]  Cd Length: 537  Bit Score: 450.85  E-value: 4.13e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524  12 LKASSFTFWVSIVMTFAYNLVLLEYVnQNTNVWSTSGLGIFLSTVVIVFIFSYTIFSLLALisPTVLKIFLVIITVLNAS 91
Cdd:COG2194     7 LSPLKLILLLALYFALFLNLPFWGRL-LAILPLDGVNLLFLLSLPLLLLAALNLLLSLLAW--RYLFKPLLILLLLISAA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524  92 AIYYMSNYQVVLDRTMMGNIFNTRYSESIELLTVSLVFPIIMLGLMPACFVALIKIKQVDRVKILG----NASIALVVSG 167
Cdd:COG2194    84 ASYFMDFYGVVIDYGMIQNVLETDPAEASELLSPKLILWLLLLGVLPALLLWRVRIRYRPLLRELGqrlaLLLLALLVIV 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 168 AFLYTNSTSWLWIDKHASVLGGKILPWSYIINSGRYYSSINRTTDGQ-KALPDGHFL---DNNKTVFVLVIGETARAANF 243
Cdd:COG2194   164 LLALLFYKDYASFFRNHKELRYLINPSNFIYALGKYAKARYFAAPLPlQPLGADAKLaaaGAKPTLVVLVVGETARADNF 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 244 SLYGYSKLTNPKLAEQPNLLVLNNTKSCTTYTTGSLACILAPS--DQYLDFEALPT-----YLARHGVDVQWRTNNWGep 316
Cdd:COG2194   244 SLNGYARDTTPELAKEKNLVSFRDVTSCGTATAVSVPCMFSRLgrADYDPQRALNQenlldVLQRAGVKVLWRDNQSG-- 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 317 pIK-----VTSYT-EAGELRADCVGEGCkLDEVLLTNLINAIDSsDKQKIFVVLHTKGSHGPSYYSRYTKEFNQFTPVCR 390
Cdd:COG2194   322 -CKgvcdrVPTIDlTADNLPPLCDGGEC-LDEVLLDGLDEALAD-LAGDKLIVLHQMGSHGPAYYKRYPPEFRKFTPTCD 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 391 DEEISKCSPEELINAYDNTLLYTDHFLTTLIMELQTLAKTS-SAMMYISDHGESLGEHGLYLHGTPYSFAPDYQKDIPFL 469
Cdd:COG2194   399 TNDLQNCSREELVNAYDNTILYTDYVLSQVIDLLKAKQDRYdTAMLYVSDHGESLGENGLYLHGTPYAIAPDEQTHVPMI 478
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1394421524 470 FWASDTFLDARNLKLKNLNQ--ANSHNQFNVFHTVLGALSLESSIYDSTLDVLHN 522
Cdd:COG2194   479 MWLSDGYAQRYGIDFACLKAraDKPYSHDNLFHTLLGLLDVRTSVYDPELDILAP 533
LptA cd16017
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ...
226-509 5.39e-91

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: 279.89  E-value: 5.39e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 226 NKTVFVLVIGETARAANFSLYGYSKLTNPKLAEQP-NLLVLNNTKSCTTYTTGSLACILAPSDQY-----LDFEALPTYL 299
Cdd:cd16017     1 KPKNVVLVIGESARRDHMSLYGYPRDTTPFLSKLKkNLIVFDNVISCGTSTAVSLPCMLSFANREnydraYYQENLIDLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 300 ARHGVDVQWRTNNWGEP----PIKVTSYTEAGELRADCVGEGCKLDEVLLTNLINAIDsSDKQKIFVVLHTKGSHGPsYY 375
Cdd:cd16017    81 KKAGYKTYWISNQGGCGgydtRISAIAKIETVFTNKGSCNSSNCYDEALLPLLDEALA-DSSKKKLIVLHLMGSHGP-YY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 376 SRYTKEFNQFTPVCrDEEISKCSPEELINAYDNTLLYTDHFLTTLIMELQTlAKTSSAMMYISDHGESLGEHGLYLHGTP 455
Cdd:cd16017   159 DRYPEEFAKFTPDC-DNELQSCSKEELINAYDNSILYTDYVLSQIIERLKK-KDKDAALIYFSDHGESLGENGLYLHGAP 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1394421524 456 YsfAPDYQKDIPFLFWASDTFLDARNLKLKNLNQANSHNQFNVFHTVLGALSLE 509
Cdd:cd16017   237 Y--APKEQYHVPFIIWSSDSYKQRYPVERLRANKDRPFSHDNLFHTLLGLLGIK 288
Sulfatase pfam00884
Sulfatase;
230-506 2.47e-46

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 163.75  E-value: 2.47e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 230 FVLVIGETARAANFSLYGYSKLTNPKLAE-QPNLLVLNNTKSCTTYTTGSLACILA-------------PSDQYLDFEAL 295
Cdd:pfam00884   3 VVLVLGESLRAPDLGLYGYPRPTTPFLDRlAEEGLLFSNFYSGGTLTAPSRFALLTglpphnfgsyvstPVGLPRTEPSL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 296 PTYLARHGVDVQ----WRTNNWGE--PPI----KVTSYTEAGELRAD-------CVGEGCkLDEVLLTNLINAIDSSDKq 358
Cdd:pfam00884  83 PDLLKRAGYNTGaigkWHLGWYNNqsPCNlgfdKFFGRNTGSDLYADppdvpynCSGGGV-SDEALLDEALEFLDNNDK- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 359 KIFVVLHTKGSHGPSYYS-RYTKEFNQFTPvcrdeeiSKCSPEELINAYDNTLLYTDHFLTTLIMELQTLAK-TSSAMMY 436
Cdd:pfam00884 161 PFFLVLHTLGSHGPPYYPdRYPEKYATFKP-------SSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLlDNTLVVY 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 437 ISDHGESLGEHGLYLHGTPYSFAPDYQKDIPFLFWASDTFldarnLKLKNLNQANSHNqfNVFHTVLGAL 506
Cdd:pfam00884 234 TSDHGESLGEGGGYLHGGKYDNAPEGGYRVPLLIWSPGGK-----AKGQKSEALVSHV--DLFPTILDLA 296
 
Name Accession Description Interval E-value
PRK09598 PRK09598
phosphoethanolamine--lipid A transferase EptA;
12-520 1.24e-179

phosphoethanolamine--lipid A transferase EptA;


Pssm-ID: 236581 [Multi-domain]  Cd Length: 522  Bit Score: 515.10  E-value: 1.24e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524  12 LKASSFTFWVSIVMTFAYNLVLLEYVNQNTNvwstsGLGIFLSTVVIVFIFSYTIFSLLALISPTVLKIFLVIITVLNAS 91
Cdd:PRK09598   13 LSCLQAGLLYSLLNGVLYHFPLFAYVYKESN-----QVSFIAMLVVLLFCVNGLLFLLLGLLSRRLMRLSAIVFSLLNSI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524  92 AIYYMSNYQVVLDRTMMGNIFNTRYSESIELLTVSLVFPIIMLGLMPACFVALIKIKQVDRVKILGNASIALVVSGAFLY 171
Cdd:PRK09598   88 AFYFINTYKVFLNKSMMGNVLNTNTAESSGFLSVKLFIYIVVLGVLPGYIIYKIPLKNSSKKAPFAAILALVLIFLASAF 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 172 TNSTSWLWIDKHASVLGGKILPWSYIINSGRYYSSINRTTDGQKALPDGHFLDNNKTVFVLVIGETARAANFSLYGYSKL 251
Cdd:PRK09598  168 ANSKNWLWFDKHAKFLGGLILPWSYSVNTFRVSAHKFFAPTIKPLLPPLFSPNHSKSVVVLVIGESARKHNYALYGYEKP 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 252 TNPKLA--EQPNLLVLNNTKSCTTYTTGSLACILAPS--DQYLDFEALPTYLARHGVDVQWRTNNWGEPPIKVTSYTEAG 327
Cdd:PRK09598  248 TNPRLSkrLATHELTLFNATSCATYTTASLECILDSSfkNTSNAYENLPTYLTRAGIKVFWRSANDGEPNVKVTSYLKNY 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 328 ELRADCVGEGCKLDEVLLTNLINAIDSSDKQKIFVVLHTKGSHGPSYYSRYTKEFNQFTPVCRDEEISKCSPEELINAYD 407
Cdd:PRK09598  328 ELIQKCPNCEAPYDESLLYNLPELIKASSNENVLLILHLAGSHGPNYDNKYPLNFRVFKPVCSSVELSSCSKESLINAYD 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 408 NTLLYTDHFLTTLIMELQTLaKTSSAMMYISDHGESLGEHGLYLHGTPYSFAPDYQKDIPFLFWASDTFldarnLKLKNL 487
Cdd:PRK09598  408 NTIFYNDYLLDKIISMLKNL-KQPALMIYLSDHGESLGEGAFYLHGIPKSIAPKEQYEIPFIVWASDSF-----KKQHSI 481
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 1394421524 488 NQANSH-NQFNVFHTVLGALSLE--SSIYDSTLDVL 520
Cdd:PRK09598  482 IQTQTPiNQNVIFHSVLGVFDFKnpSAVYRPSLDLF 517
OpgE COG2194
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall ...
12-522 4.13e-154

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


Pssm-ID: 441797 [Multi-domain]  Cd Length: 537  Bit Score: 450.85  E-value: 4.13e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524  12 LKASSFTFWVSIVMTFAYNLVLLEYVnQNTNVWSTSGLGIFLSTVVIVFIFSYTIFSLLALisPTVLKIFLVIITVLNAS 91
Cdd:COG2194     7 LSPLKLILLLALYFALFLNLPFWGRL-LAILPLDGVNLLFLLSLPLLLLAALNLLLSLLAW--RYLFKPLLILLLLISAA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524  92 AIYYMSNYQVVLDRTMMGNIFNTRYSESIELLTVSLVFPIIMLGLMPACFVALIKIKQVDRVKILG----NASIALVVSG 167
Cdd:COG2194    84 ASYFMDFYGVVIDYGMIQNVLETDPAEASELLSPKLILWLLLLGVLPALLLWRVRIRYRPLLRELGqrlaLLLLALLVIV 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 168 AFLYTNSTSWLWIDKHASVLGGKILPWSYIINSGRYYSSINRTTDGQ-KALPDGHFL---DNNKTVFVLVIGETARAANF 243
Cdd:COG2194   164 LLALLFYKDYASFFRNHKELRYLINPSNFIYALGKYAKARYFAAPLPlQPLGADAKLaaaGAKPTLVVLVVGETARADNF 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 244 SLYGYSKLTNPKLAEQPNLLVLNNTKSCTTYTTGSLACILAPS--DQYLDFEALPT-----YLARHGVDVQWRTNNWGep 316
Cdd:COG2194   244 SLNGYARDTTPELAKEKNLVSFRDVTSCGTATAVSVPCMFSRLgrADYDPQRALNQenlldVLQRAGVKVLWRDNQSG-- 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 317 pIK-----VTSYT-EAGELRADCVGEGCkLDEVLLTNLINAIDSsDKQKIFVVLHTKGSHGPSYYSRYTKEFNQFTPVCR 390
Cdd:COG2194   322 -CKgvcdrVPTIDlTADNLPPLCDGGEC-LDEVLLDGLDEALAD-LAGDKLIVLHQMGSHGPAYYKRYPPEFRKFTPTCD 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 391 DEEISKCSPEELINAYDNTLLYTDHFLTTLIMELQTLAKTS-SAMMYISDHGESLGEHGLYLHGTPYSFAPDYQKDIPFL 469
Cdd:COG2194   399 TNDLQNCSREELVNAYDNTILYTDYVLSQVIDLLKAKQDRYdTAMLYVSDHGESLGENGLYLHGTPYAIAPDEQTHVPMI 478
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1394421524 470 FWASDTFLDARNLKLKNLNQ--ANSHNQFNVFHTVLGALSLESSIYDSTLDVLHN 522
Cdd:COG2194   479 MWLSDGYAQRYGIDFACLKAraDKPYSHDNLFHTLLGLLDVRTSVYDPELDILAP 533
PRK11598 PRK11598
putative metal dependent hydrolase; Provisional
16-520 1.37e-110

putative metal dependent hydrolase; Provisional


Pssm-ID: 183224 [Multi-domain]  Cd Length: 545  Bit Score: 339.34  E-value: 1.37e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524  16 SFTFWVSIVMTFAYNLVLLEYVNQNTNVWSTSGLGIFLSTVVIVFIFSYTIFSLLALisPTVLKIFLVIITVLNASAIYY 95
Cdd:PRK11598   14 TFLLLAAFYITLCLNIAFYKQVLQLLPLDSLHNVLVFASMPVVAFSVINIVFTLLSF--PWLRRPLACLFILVGAAAQYF 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524  96 MSNYQVVLDRTMMGNIFNTRYSESIELLTVSLVFPIIMLGLMPACFVALIKIKQ--------VDRV-KILGNASIALVVS 166
Cdd:PRK11598   92 MMTYGIVIDRSMIQNIFETTPAESFALMTPQMLLWLGLSGVLPALIACWIKIRPatprwrsvLFRLaNILVSVLLILLVA 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 167 gAFLYTNSTSWLWIDKHasvLGGKILPWSYIINSGRYYSSiNRTTD------GQKALPDGHFL-DNNKTVFVLVIGETAR 239
Cdd:PRK11598  172 -ALFYKDYASLFRNNKE---LVKSLTPSNSIVASWSWYSH-QRLANlplvriGEDAHKNPLMQnQKRKNLTILVVGETSR 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 240 AANFSLYGYSKLTNPKLAEQpNLLVLNNTKSCTTYTTGSLACILA--PSDQYLDF-----EALPTYLARHGVDVQWRTNN 312
Cdd:PRK11598  247 AENFSLGGYPRETNPRLAKD-NVIYFPHTTSCGTATAVSVPCMFSnmPRKHYDEElahhqEGLLDIIQRAGINVLWNDND 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 313 WG-------EPPIKVTSYteagELRADCVGEGCkLDEVLLTNLINAIDSSdKQKIFVVLHTKGSHGPSYYSRYTKEFNQF 385
Cdd:PRK11598  326 GGckgacdrVPHQDVTAL----NLPGQCIDGEC-YDEVLFHGLENYINNL-QGDGVIVLHTIGSHGPTYYNRYPPQFRKF 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 386 TPVCRDEEISKCSPEELINAYDNTLLYTDHFLTTLIMELQTL-AKTSSAMMYISDHGESLGEHGLYLHGTPYSFAPDYQK 464
Cdd:PRK11598  400 TPTCDTNEIQTCTQQQLVNTYDNTILYVDYIVDKAINLLKQHqDKFNTSLVYLSDHGESLGENGIYLHGLPYAIAPDQQT 479
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1394421524 465 DIPFLFWASDTFldARNLK-----LKNLNQANSHNQFNVFHTVLGALSLESSIYDSTLDVL 520
Cdd:PRK11598  480 HVPMLLWLSPDY--QKRYGvdqqcLQKQAQTQDYSQDNLFSTLLGLTGVQTKEYQAADDIL 538
LptA cd16017
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ...
226-509 5.39e-91

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: 279.89  E-value: 5.39e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 226 NKTVFVLVIGETARAANFSLYGYSKLTNPKLAEQP-NLLVLNNTKSCTTYTTGSLACILAPSDQY-----LDFEALPTYL 299
Cdd:cd16017     1 KPKNVVLVIGESARRDHMSLYGYPRDTTPFLSKLKkNLIVFDNVISCGTSTAVSLPCMLSFANREnydraYYQENLIDLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 300 ARHGVDVQWRTNNWGEP----PIKVTSYTEAGELRADCVGEGCKLDEVLLTNLINAIDsSDKQKIFVVLHTKGSHGPsYY 375
Cdd:cd16017    81 KKAGYKTYWISNQGGCGgydtRISAIAKIETVFTNKGSCNSSNCYDEALLPLLDEALA-DSSKKKLIVLHLMGSHGP-YY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 376 SRYTKEFNQFTPVCrDEEISKCSPEELINAYDNTLLYTDHFLTTLIMELQTlAKTSSAMMYISDHGESLGEHGLYLHGTP 455
Cdd:cd16017   159 DRYPEEFAKFTPDC-DNELQSCSKEELINAYDNSILYTDYVLSQIIERLKK-KDKDAALIYFSDHGESLGENGLYLHGAP 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1394421524 456 YsfAPDYQKDIPFLFWASDTFLDARNLKLKNLNQANSHNQFNVFHTVLGALSLE 509
Cdd:cd16017   237 Y--APKEQYHVPFIIWSSDSYKQRYPVERLRANKDRPFSHDNLFHTLLGLLGIK 288
PRK11560 PRK11560
kdo(2)-lipid A phosphoethanolamine 7''-transferase;
7-510 1.33e-52

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


Pssm-ID: 183198 [Multi-domain]  Cd Length: 558  Bit Score: 187.56  E-value: 1.33e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524   7 SKISILKAssftFWVSIVMTFAYNLVLLEYVNQNTNVWStsGLGIFLSTVVIVFiFSYTIFSLLALISPTVLKIFLVIIT 86
Cdd:PRK11560   10 QKLSFLLA----VYIGLFLNIAVFYRRFDSYAQDFTVWK--GLSAVVELAATVL-VTFFLLRLLSLFGRRFWRVLASLLV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524  87 VLNASAIYYMSNYQVVLDRTMMGNIFNTRYSESIELLTVSLVFPIIMLGLMPACFVALIK-----IKQVDRVKILGNASI 161
Cdd:PRK11560   83 LFSAAASYYMTFFNVVIGYGIIASVMTTDIDLSKEVVGLHFILWLVAVSALPLILIWNNRcrytlLRQLRTPGQRIRSLA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 162 ALVVSGAFLytnstsWL---WIDKHAS---------------VLGGKILPWSYIINSGRY-YSSINRTTDGQKAL-PDGH 221
Cdd:PRK11560  163 VVVLAGLLV------WApirLLDIQQKkveratgvdlpsyggVVANSYLPSNWLSALGLYaWAQVDESSDNNSLLnPAKK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 222 FL-----DNNKTVFVLVIGETARAANFSLYGYSKLTNPKLAEQPNLLVLNNTkSCTTYTTGSLACIL----APSD---QY 289
Cdd:PRK11560  237 FTyqapkGVDDTYVVFIIGETTRWDHMGILGYERNTTPKLAQEKNLAAFRGY-SCDTATKLSLRCMFvregGAEDnpqRT 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 290 LDFEALPTYLARHGVDVQ--------WRTNNwgeppIKVTSYTEAGELRADCVGEGCKLDEVLLTN-LINAIDSSDKQKI 360
Cdd:PRK11560  316 LKEQNVFAVLKQLGFSSElfamqsemWFYNN-----TMADNYAYREQIGAEPRNRGKPVDDMLLVDeMKQSLGRNPDGKH 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 361 FVVLHTKGSHGpSYYSRYTKEFNQFTPVCRDEEiSKCSPEELINAYDNTLLYTDHFLTTLImelQTLAKTSSAMMYISDH 440
Cdd:PRK11560  391 LIILHTKGSHY-NYTQRYPRSFARYQPECIGVD-SGCSKAQLINSYDNSVLYVDHFISSVI---DQLRDKKAIVFYAADH 465
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1394421524 441 GESLGEhGLYLHGTPYSFAPDYQKDIPFLFWASDTFL-DARNLK----LKNLNQAN-SHNQFNVFHTVLGALSLES 510
Cdd:PRK11560  466 GESINE-REHLHGTPREMAPPEQFRVPMMVWMSDKYLaNPDNAQafaqLKKQADMKvPRRHVELFDTILGCLGYTS 540
Sulfatase pfam00884
Sulfatase;
230-506 2.47e-46

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 163.75  E-value: 2.47e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 230 FVLVIGETARAANFSLYGYSKLTNPKLAE-QPNLLVLNNTKSCTTYTTGSLACILA-------------PSDQYLDFEAL 295
Cdd:pfam00884   3 VVLVLGESLRAPDLGLYGYPRPTTPFLDRlAEEGLLFSNFYSGGTLTAPSRFALLTglpphnfgsyvstPVGLPRTEPSL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 296 PTYLARHGVDVQ----WRTNNWGE--PPI----KVTSYTEAGELRAD-------CVGEGCkLDEVLLTNLINAIDSSDKq 358
Cdd:pfam00884  83 PDLLKRAGYNTGaigkWHLGWYNNqsPCNlgfdKFFGRNTGSDLYADppdvpynCSGGGV-SDEALLDEALEFLDNNDK- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 359 KIFVVLHTKGSHGPSYYS-RYTKEFNQFTPvcrdeeiSKCSPEELINAYDNTLLYTDHFLTTLIMELQTLAK-TSSAMMY 436
Cdd:pfam00884 161 PFFLVLHTLGSHGPPYYPdRYPEKYATFKP-------SSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLlDNTLVVY 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 437 ISDHGESLGEHGLYLHGTPYSFAPDYQKDIPFLFWASDTFldarnLKLKNLNQANSHNqfNVFHTVLGAL 506
Cdd:pfam00884 234 TSDHGESLGEGGGYLHGGKYDNAPEGGYRVPLLIWSPGGK-----AKGQKSEALVSHV--DLFPTILDLA 296
EptA_B_N pfam08019
Phosphoethanolamine transferase EptA/EptB; This entry represents a domain found in a group of ...
61-205 3.32e-30

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: 115.31  E-value: 3.32e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524  61 IFSYTIFSLLALISPTVLKIFLVIITVLNASAIYYMSNYQVVLDRTMMGNIFNTRYSESIELLTVSLVFPIIMLGLMPAC 140
Cdd:pfam08019   1 LFAALNLLLSLLSWRYLLKPLLILLLLLSAAASYFMDTYGVVIDRDMIQNVLETDVAEASDLLSPKLLLYLLLLGVLPAL 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1394421524 141 FVALIKIKQVDRVKIL----GNASIALVVSGAFLYTNSTSWLWIDKHASVLGGKILPWSYIINSGRYYS 205
Cdd:pfam08019  81 LLWRVRIRYRPWLRELlsrlALILVSLLVIGLVAFLFYKDYASFFRNHKELRYLINPTNYIYSTVKYAK 149
PRK10649 PRK10649
phosphoethanolamine transferase CptA;
193-474 9.78e-22

phosphoethanolamine transferase CptA;


Pssm-ID: 182617 [Multi-domain]  Cd Length: 577  Bit Score: 98.62  E-value: 9.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 193 PWSYIINSGRY---YSSINRTTDGQKALPD-GHFLDNNKT---VFVLVIGETARAANFSLYGYSKLTNPKL----AEQPN 261
Cdd:PRK10649  195 PWQFLTGYYQYrqqLNSLQKLLNENAALPPlANLKDESGNaprTLVLVIGESTQRGRMSLYGYPRETTPELdalhKTDPG 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 262 LLVLNNTKSCTTYTTGSLACILAPSDQ-----YLDFEALPTYLARHGVDVQWRTNNwgeppikvTSYTEAGELRADCVGE 336
Cdd:PRK10649  275 LTVFNNVVTSRPYTIEILQQALTFADEknpdlYLTQPSLMNMMKQAGYKTFWITNQ--------QTMTARNTMLTVFSRQ 346
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 337 GCK--------------LDEVLLTNLINAIDSSDKQKiFVVLHTKGSHgPSYYSRYTKEFNQFT-------PVCRDEEIs 395
Cdd:PRK10649  347 TDKqyymnqqrtqnareYDTNVLKPFSEVLADPAPKK-FIIVHLLGTH-IKYKYRYPENQGKFDdrtghvpPGLNADEL- 423
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 396 kcspeELINAYDNTLLYTDHFLTTLIMELQTLAkTSSAMMYISDHGE---------SLGEHglylHGTPYsfAPDYQkdI 466
Cdd:PRK10649  424 -----ESYNDYDNANLYNDHVVASLIKDFKATD-PNGFLVYFSDHGEevydtpphkTQGRN----EDNPT--RHMYT--I 489

                  ....*...
gi 1394421524 467 PFLFWASD 474
Cdd:PRK10649  490 PFLLWTSE 497
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
229-471 9.56e-08

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


Pssm-ID: 293767 [Multi-domain]  Cd Length: 271  Bit Score: 53.32  E-value: 9.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 229 VFVLVIgETARAANFSLYGYSKLTNP---KLAEQPnlLVLNNTKSCTTYTTGSLACIL------------APSDQylDFE 293
Cdd:cd16148     3 VILIVI-DSLRADHLGCYGYDRVTTPnldRLAAEG--VVFDNHYSGSNPTLPSRFSLFtglypfyhgvwgGPLEP--DDP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 294 ALPTYLARHGVDVQWRTNN---WGEPPIK--VTSYTEAGELRADCVGEGCKLDEVLLTNLINAIDS-SDKQKIFVVLHTK 367
Cdd:cd16148    78 TLAEILRKAGYYTAAVSSNphlFGGPGFDrgFDTFEDFRGQEGDPGEEGDERAERVTDRALEWLDRnADDDPFFLFLHYF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 368 GSHGPsyysrYtkefnqftpvcrdeeiskcspeelinAYDNTLLYTDHFLTTLimeLQTLAKTS----SAMMYISDHGES 443
Cdd:cd16148   158 DPHEP-----Y--------------------------LYDAEVRYVDEQIGRL---LDKLKELGlledTLVIVTSDHGEE 203
                         250       260
                  ....*....|....*....|....*....
gi 1394421524 444 LGEHGLYL-HGTPYSfapDYQKDIPFLFW 471
Cdd:cd16148   204 FGEHGLYWgHGSNLY---DEQLHVPLIIR 229
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
17-513 8.44e-06

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 48.50  E-value: 8.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524  17 FTFWVSIVMTFAYNLVLLEYVNQNTNVWSTSGLGIFLSTVVIVFIFSYTIFSLLALISPTVLK-----IFLVIITVLNAS 91
Cdd:COG1368     1 FFLLFLLLLSLRLVFLLFNFDLSLGEILQAFLYGLRFILYLLLLLLLLLLLLLPLLFRRPKLRwiyllLVLLLLLLLLVA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524  92 AIYYMSNYQVVLDRTMMGNIFNTRysESIE-LLTVSLVFPIIMLGLMPACFVALIKIKQVDRVKILGNASIALVVSGAFL 170
Cdd:COG1368    81 DILYYRFFGDRLNFSDLDYLGDTG--EVLGsLLSSYDLLLLLDLLLLLLLLLLLYRLLKKLRKSLPWRKRLALLLLLLAL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 171 ------YTNSTSWLWID--------KHASVLGGKILPWSYIINSGR-YYSS-----INRTTDGQKALPDGHFLDNNKTVf 230
Cdd:COG1368   159 lllgirLGEDRPLNLSDafsrnnfvNELGLNGPYSFYDALRNNKAPaTYSEeealeIKKYLKSNRPTPNPFGPAKKPNV- 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 231 VLVIGETARAANFSLYGYSK-LTnP---KLAEQpnLLVLNNTKSCTTYTTGSLACIL---------APSDQYL--DFEAL 295
Cdd:COG1368   238 VVILLESFSDFFIGALGNGKdVT-PfldSLAKE--SLYFGNFYSQGGRTSRGEFAVLtglpplpggSPYKRPGqnNFPSL 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 296 PTYLAR--------HGVDVQWR-----TNNWGeppikVTSYTEAGELRADCVGE-GCKlDEVLLTNLINAIDSSdKQKIF 361
Cdd:COG1368   315 PSILKKqgyetsffHGGDGSFWnrdsfYKNLG-----FDEFYDREDFDDPFDGGwGVS-DEDLFDKALEELEKL-KKPFF 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 362 VVLHTKGSHGPSYYSRYTKEFNQFtpvcrdeeiskcsPEELINAYDNTLLYTDHFLTTLImelqTLAKTSSAM-----MY 436
Cdd:COG1368   388 AFLITLSNHGPYTLPEEDKKIPDY-------------GKTTLNNYLNAVRYADQALGEFI----EKLKKSGWYdntifVI 450
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1394421524 437 ISDHGESLGEHglylhgTPYSFAPDYQKdIPFLFWASDtfldarNLKLKNLNQANShnQFNVFHTVLGALSLESSIY 513
Cdd:COG1368   451 YGDHGPRSPGK------TDYENPLERYR-VPLLIYSPG------LKKPKVIDTVGS--QIDIAPTLLDLLGIDYPSY 512
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
230-471 9.82e-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: 9.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 230 FVLVIGETARAANFSLYGYSKLTNPKLAEQPNLLVLNNTKSCTTYTTG--SLACILAPSDqyldfealPTYlarHGVdvq 307
Cdd:cd00016     3 VVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFNFRSVSPPTSSapNHAALLTGAY--------PTL---HGY--- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 308 wRTNNWGEPPIKVTSYTEA-------GELRAdcvgegcKLDEVLLTNLINAIDSSDKQKIFVV-LHTKGSHGPSYYSRYT 379
Cdd:cd00016    69 -TGNGSADPELPSRAAGKDedgptipELLKQ-------AGYRTGVIGLLKAIDETSKEKPFVLfLHFDGPDGPGHAYGPN 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 380 kefnqftpvcrdeeiskcSPEelinaYDNTLLYTDHFLTTLIMELQTLAKT-SSAMMYISDHGESLGEHGLYLHGTPYSF 458
Cdd:cd00016   141 ------------------TPE-----YYDAVEEIDERIGKVLDALKKAGDAdDTVIIVTADHGGIDKGHGGDPKADGKAD 197
                         250
                  ....*....|...
gi 1394421524 459 APDYQKDIPFLFW 471
Cdd:cd00016   198 KSHTGMRVPFIAY 210
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
341-474 2.08e-04

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: 43.44  E-value: 2.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 341 DEVLLTNLINAIDSSDKQKIFVVLHTKGSHGPsyysrYTKEFNQFtpvcrDEEISKCSPEELINAYDNTLLYTDHFLTTL 420
Cdd:cd16015   139 DESLFDQALEELEELKKKPFFIFLVTMSNHGP-----YDLPEEKK-----DEPLKVEEDKTELENYLNAIHYTDKALGEF 208
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1394421524 421 ImelqTLAKTSSAM-----MYISDHGESLGEHGLYlhgTPYSFAPDYQkdIPFLFWASD 474
Cdd:cd16015   209 I----EKLKKSGLYentiiVIYGDHLPSLGSDYDE---TDEDPLDLYR--TPLLIYSPG 258
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
361-456 3.05e-03

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 39.86  E-value: 3.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394421524 361 FVVLHTKGSHGP-----SYYSRYTKEFNQFTPVCRDEEISKCSPEELINAYDNTLLYTDHFLTTLIMELQ-------TLa 428
Cdd:COG3119   152 FLYLAFNAPHAPyqapeEYLDKYDGKDIPLPPNLAPRDLTEEELRRARAAYAAMIEEVDDQVGRLLDALEelgladnTI- 230
                          90       100
                  ....*....|....*....|....*....
gi 1394421524 429 ktssaMMYISDHGESLGEHGLYLH-GTPY 456
Cdd:COG3119   231 -----VVFTSDNGPSLGEHGLRGGkGTLY 254
 
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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