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Conserved domains on  [gi|1797005300|gb|QHH08052|]
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lauroyl-Kdo(2)-lipid IV(A) myristoyltransferase [Vibrio parahaemolyticus]

Protein Classification

lauroyl-Kdo(2)-lipid IV(A) myristoyltransferase( domain architecture ID 10793125)

lauroyl-Kdo(2)-lipid IV(A) myristoyltransferase catalyzes the transfer of myristate from myristoyl-acyl carrier protein (ACP) to Kdo(2)-(lauroyl)-lipid IV(A) to form Kdo(2)-lipid A; can probably also catalyze the transfer of myristate to Kdo(2)-(palmitoleoyl)-lipid IV(A) to form the cold-adapted Kdo(2)-lipid A

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK08943 PRK08943
lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; Validated
 4-315 0e+00

lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; Validated


:

Pssm-ID: 236355  Cd Length: 314  Bit Score: 532.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300   4 KRDDYDSKAYNPEFERHFLSPKYWGTWLGVILFLPLALMPLSAQKWLAKTIAKKLSKSHKGPAHRARVNFELCFPGKTFQ 83
Cdd:PRK08943    1 MEMKKDNKEYIPRFQKSFLHPRYWGTWLGIGALAGLALMPPRLRDPLAAKLGRLVGKLAKKARRRARINLSLCFPEKSEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300  84 EREALIEKTLYTAAMFFFRFGLLSLRSPQWLQSRCQIRGLDVLRQHIDNNENVILMVPHSWAIDVPAILLASMGMPVSAM 163
Cdd:PRK08943   81 EREAIIDEMFATAPQAMLMMAELALRSPKHLQRRVEWHGLEILEEARANGENVIFLVPHGWAIDIPAMLLASQGQPMAAM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300 164 AKKQKNDVADWLMHKQRVQYGGRVYERSGGIKPFLKSIRDGYIGYYLPDQDHGPEHSVFVDFFATRKATLPGLGKIAKLS 243
Cdd:PRK08943  161 FHNQRNPLFDWLWNRVRRRFGGRLHAREDGIKPFISSVRQGYWGYYLPDEDHGPEHSVFVDFFATYKATLPGIGRLAKVC 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1797005300 244 RSKVLPLFASMNTEDGTFDIEILPAFD--LDKGEEQDARTCNEAIEYFVGDKPEQYMWVLQLLHSQEDGNNYYN 315
Cdd:PRK08943  241 RARVVPLFPVYNGKTHRLDIEIRPPMDdlLSADDETIARRMNEEVEQFVGPHPEQYMWILKLLKTRKPGEDLYP 314
 
Name Accession Description Interval E-value
PRK08943 PRK08943
lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; Validated
 4-315 0e+00

lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; Validated


Pssm-ID: 236355  Cd Length: 314  Bit Score: 532.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300   4 KRDDYDSKAYNPEFERHFLSPKYWGTWLGVILFLPLALMPLSAQKWLAKTIAKKLSKSHKGPAHRARVNFELCFPGKTFQ 83
Cdd:PRK08943    1 MEMKKDNKEYIPRFQKSFLHPRYWGTWLGIGALAGLALMPPRLRDPLAAKLGRLVGKLAKKARRRARINLSLCFPEKSEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300  84 EREALIEKTLYTAAMFFFRFGLLSLRSPQWLQSRCQIRGLDVLRQHIDNNENVILMVPHSWAIDVPAILLASMGMPVSAM 163
Cdd:PRK08943   81 EREAIIDEMFATAPQAMLMMAELALRSPKHLQRRVEWHGLEILEEARANGENVIFLVPHGWAIDIPAMLLASQGQPMAAM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300 164 AKKQKNDVADWLMHKQRVQYGGRVYERSGGIKPFLKSIRDGYIGYYLPDQDHGPEHSVFVDFFATRKATLPGLGKIAKLS 243
Cdd:PRK08943  161 FHNQRNPLFDWLWNRVRRRFGGRLHAREDGIKPFISSVRQGYWGYYLPDEDHGPEHSVFVDFFATYKATLPGIGRLAKVC 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1797005300 244 RSKVLPLFASMNTEDGTFDIEILPAFD--LDKGEEQDARTCNEAIEYFVGDKPEQYMWVLQLLHSQEDGNNYYN 315
Cdd:PRK08943  241 RARVVPLFPVYNGKTHRLDIEIRPPMDdlLSADDETIARRMNEEVEQFVGPHPEQYMWILKLLKTRKPGEDLYP 314
lipid_A_msbB TIGR02208
lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; This family consists of MsbB ...
 13-310 1.23e-120

lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; This family consists of MsbB in E. coli and closely related proteins in other species. MsbB is homologous to HtrB (TIGR02207) and acts immediately after it in the biosynthesis of KDO-2 lipid A (also called Re LPS and Re endotoxin). These two enzymes act after creation of KDO-2 lipid IV-A by addition of the KDO sugars. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 274032  Cd Length: 305  Bit Score: 349.10  E-value: 1.23e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300  13 YNPEFERHFLSPKYWGTWLGVILFLPLALMPLSAQKWLAKTIAKKLSKSHKGPAHRARVNFELCFPGKTFQEREALIEKT 92
Cdd:TIGR02208   1 YDRRFQKSFLHPKYWGTWLGVFALVLLAFMPAKLRDPIAKVLAKFVGPIAKKPRGRARINLSACFPEKSEAERETIIDNN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300  93 LYTAAMFFFRFGLLSLRSPQWLQSRCQIRGLDVLRQHIDNNENVILMVPHSWAIDVPAILLASMGMPVSAMAKKQKNDVA 172
Cdd:TIGR02208  81 FATFVQVMLSQAELAIRSKAHLRRRVNLMGLEHIEAAQAAGKPVIFLVPHGWAIDYAGLRLASQGLPMVTMFNNHKNPLF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300 173 DWLMHKQRVQYGGRVYERSGGIKPFLKSIRDGYIGYYLPDQDHGPEHSVFVDFFATRKATLPGLGKIAKLSRSKVLPLFA 252
Cdd:TIGR02208 161 DWLWNRVRSRFGGHVYAREAGIKALLASLKRGESGYYLPDEDHGPEQSVFVPFFATYKATLPVVGRLAKAGNAQVVPVFP 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300 253 SMNTEDGTFDIEILPAFD--LDKGEEQDARTCNEAIEYFVGDKPEQYMWVLQLLHSQEDG 310
Cdd:TIGR02208 241 GYNQVTGKFELTVRPAMAteLSVDPEQEARAMNKEVEQFILPYPEQYMWILRLLKTRPDG 300
Lip_A_acyltrans pfam03279
Bacterial lipid A biosynthesis acyltransferase;
15-304 1.38e-85

Bacterial lipid A biosynthesis acyltransferase;


Pssm-ID: 281296 [Multi-domain]  Cd Length: 294  Bit Score: 259.58  E-value: 1.38e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300  15 PEFERHFLSPKYWGTWLGVILFLPLALMPLSAQKWLAKTIAKKLSKSHKGPAHRARVNFELCFPGKTFQEREALIEKTLY 94
Cdd:pfam03279   1 PKFSPELLHPRYWLDWLGIAVLRLLALLPYSALRRIGKGLGRLAGRFLKRRRKIARRNLALCFPEMSEAEREQIIDKSFA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300  95 TAAMFFFRFGLLSLRSPQWLQSRCQIRGLDVLRQHIDNNENVILMVPHSWAIDVPAILLASMGMPVSAMAKKQKNDVADW 174
Cdd:pfam03279  81 SVGRAIVETGRVWFWPDSRIAKRFEVIGLEHIKEALAQGRGAILVGPHFGNWDLGGRVLGQQYPGMAVYRPNLKNPLLDW 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300 175 LMHKQRVQYGGRVYERSGGIKPFLKSIRDGYIGYYLPDQDHGPEHSVFVDFFATRKATLPGLGKIAKLSRSKVLPLFASM 254
Cdd:pfam03279 161 LQTSGRERFGGRMLPRQNGIKGLIKALRKGEVVWYLPDQDLGRKDSVFVPFFGVPAATTTGPAKLALKTKAAVIPVFPIR 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1797005300 255 NTEDGTFDIEILPAFDL--DKGEEQDARTCNEAIEYFVGDKPEQYMWVLQLL 304
Cdd:pfam03279 241 NGDGSGYTVIVHPALDLtiTDDVEQIAQAMNQIVEKFIMPAPEQYFWLHRRW 292
LpxP COG1560
Palmitoleoyl-ACP: Kdo2-lipid-IV acyltransferase (lipid A biosynthesis) [Lipid transport and ...
 35-300 8.46e-85

Palmitoleoyl-ACP: Kdo2-lipid-IV acyltransferase (lipid A biosynthesis) [Lipid transport and metabolism]; Palmitoleoyl-ACP: Kdo2-lipid-IV acyltransferase (lipid A biosynthesis) is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 441168 [Multi-domain]  Cd Length: 271  Bit Score: 256.66  E-value: 8.46e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300  35 LFLPLALMPLSAQKWLAKTIAKKLSKSHKGPAHRARVNFELCFPGKTFQEREALIEKTLYTAAMFFFRFGLLSLRSPQWL 114
Cdd:COG1560     1 LLRLLRLLPLRLLYRLGDLLGRLLYRLAGRRRRVARRNLALAFPELSEAEREALARASFRNLGRTLLETLRLWRLSPERL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300 115 QSRCQIRGLDVLRQHIDNNENVILMVPHSWAIDVPAILLASMGMPVSAMAKKQKNDVADWLMHKQRVQYGGRVYERSGGI 194
Cdd:COG1560    81 RKRVEVEGLEHLEAALAEGRGVILLTPHFGNWELAGAALALRGYPVTAVYRPLKNPLLDRLIRRGRERFGGELIPRKDGV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300 195 KPFLKSIRDGYIGYYLPDQDHGPEHSVFVDFFATRKATLPGLGKIAKLSRSKVLPLFASMNTEDGTFDIEILPAF-DLDK 273
Cdd:COG1560   161 RALLRALRKGGIVGLLPDQDPGRKSGVFVPFFGVPAATPTGPARLARRTGAPVVPVFARRLPDGRGYRLEIEPPLeDFSE 240

                         250       260
                  ....*....|....*....|....*..
gi 1797005300 274 GEEQDARTCNEAIEYFVGDKPEQYMWV 300
Cdd:COG1560   241 DVEADTQRLNRALEAWIREHPEQWLWL 267
LPLAT_LABLAT-like cd07984
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LABLAT-like; ...
 115-300 1.14e-52

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LABLAT-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as lipid A biosynthesis lauroyl/myristoyl (LABLAT, HtrB) acyltransferases and similar proteins.


Pssm-ID: 153246 [Multi-domain]  Cd Length: 192  Bit Score: 171.63  E-value: 1.14e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300 115 QSRCQIRGLDVLRQHIDNNENVILMVPHSWAIDVPAILLASMGMPVSAMAKKQKNDVADWLMHKQRVQYGGRVYERSGGI 194
Cdd:cd07984     1 LKRVEREGLEHLEAALAKGKGVILLTAHFGNWELAGLALALLGYPVTVVYRPLKNPLLDRLITRGRERFGARLIPRGGGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300 195 KPFLKSIRDGYIGYYLPDQDHGPEHSVFVDFFATRKATLPGLGKIAKLSRSKVLPLFASMNtEDGTFDIEILPAFDLDKG 274
Cdd:cd07984    81 RELIRALKKGEIVGILPDQDPGRKGGVFVPFFGRPAATPTGPARLALKTGAPVVPAFAYRL-PGGGYRIEFEPPLENPPS 159

                         170       180
                  ....*....|....*....|....*...
gi 1797005300 275 E--EQDARTCNEAIEYFVGDKPEQYMWV 300
Cdd:cd07984   160 EdvEEDTQRLNDALEAAIREHPEQWLWF 187
 
Name Accession Description Interval E-value
PRK08943 PRK08943
lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; Validated
 4-315 0e+00

lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; Validated


Pssm-ID: 236355  Cd Length: 314  Bit Score: 532.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300   4 KRDDYDSKAYNPEFERHFLSPKYWGTWLGVILFLPLALMPLSAQKWLAKTIAKKLSKSHKGPAHRARVNFELCFPGKTFQ 83
Cdd:PRK08943    1 MEMKKDNKEYIPRFQKSFLHPRYWGTWLGIGALAGLALMPPRLRDPLAAKLGRLVGKLAKKARRRARINLSLCFPEKSEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300  84 EREALIEKTLYTAAMFFFRFGLLSLRSPQWLQSRCQIRGLDVLRQHIDNNENVILMVPHSWAIDVPAILLASMGMPVSAM 163
Cdd:PRK08943   81 EREAIIDEMFATAPQAMLMMAELALRSPKHLQRRVEWHGLEILEEARANGENVIFLVPHGWAIDIPAMLLASQGQPMAAM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300 164 AKKQKNDVADWLMHKQRVQYGGRVYERSGGIKPFLKSIRDGYIGYYLPDQDHGPEHSVFVDFFATRKATLPGLGKIAKLS 243
Cdd:PRK08943  161 FHNQRNPLFDWLWNRVRRRFGGRLHAREDGIKPFISSVRQGYWGYYLPDEDHGPEHSVFVDFFATYKATLPGIGRLAKVC 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1797005300 244 RSKVLPLFASMNTEDGTFDIEILPAFD--LDKGEEQDARTCNEAIEYFVGDKPEQYMWVLQLLHSQEDGNNYYN 315
Cdd:PRK08943  241 RARVVPLFPVYNGKTHRLDIEIRPPMDdlLSADDETIARRMNEEVEQFVGPHPEQYMWILKLLKTRKPGEDLYP 314
lipid_A_msbB TIGR02208
lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; This family consists of MsbB ...
 13-310 1.23e-120

lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; This family consists of MsbB in E. coli and closely related proteins in other species. MsbB is homologous to HtrB (TIGR02207) and acts immediately after it in the biosynthesis of KDO-2 lipid A (also called Re LPS and Re endotoxin). These two enzymes act after creation of KDO-2 lipid IV-A by addition of the KDO sugars. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 274032  Cd Length: 305  Bit Score: 349.10  E-value: 1.23e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300  13 YNPEFERHFLSPKYWGTWLGVILFLPLALMPLSAQKWLAKTIAKKLSKSHKGPAHRARVNFELCFPGKTFQEREALIEKT 92
Cdd:TIGR02208   1 YDRRFQKSFLHPKYWGTWLGVFALVLLAFMPAKLRDPIAKVLAKFVGPIAKKPRGRARINLSACFPEKSEAERETIIDNN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300  93 LYTAAMFFFRFGLLSLRSPQWLQSRCQIRGLDVLRQHIDNNENVILMVPHSWAIDVPAILLASMGMPVSAMAKKQKNDVA 172
Cdd:TIGR02208  81 FATFVQVMLSQAELAIRSKAHLRRRVNLMGLEHIEAAQAAGKPVIFLVPHGWAIDYAGLRLASQGLPMVTMFNNHKNPLF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300 173 DWLMHKQRVQYGGRVYERSGGIKPFLKSIRDGYIGYYLPDQDHGPEHSVFVDFFATRKATLPGLGKIAKLSRSKVLPLFA 252
Cdd:TIGR02208 161 DWLWNRVRSRFGGHVYAREAGIKALLASLKRGESGYYLPDEDHGPEQSVFVPFFATYKATLPVVGRLAKAGNAQVVPVFP 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300 253 SMNTEDGTFDIEILPAFD--LDKGEEQDARTCNEAIEYFVGDKPEQYMWVLQLLHSQEDG 310
Cdd:TIGR02208 241 GYNQVTGKFELTVRPAMAteLSVDPEQEARAMNKEVEQFILPYPEQYMWILRLLKTRPDG 300
Lip_A_acyltrans pfam03279
Bacterial lipid A biosynthesis acyltransferase;
15-304 1.38e-85

Bacterial lipid A biosynthesis acyltransferase;


Pssm-ID: 281296 [Multi-domain]  Cd Length: 294  Bit Score: 259.58  E-value: 1.38e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300  15 PEFERHFLSPKYWGTWLGVILFLPLALMPLSAQKWLAKTIAKKLSKSHKGPAHRARVNFELCFPGKTFQEREALIEKTLY 94
Cdd:pfam03279   1 PKFSPELLHPRYWLDWLGIAVLRLLALLPYSALRRIGKGLGRLAGRFLKRRRKIARRNLALCFPEMSEAEREQIIDKSFA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300  95 TAAMFFFRFGLLSLRSPQWLQSRCQIRGLDVLRQHIDNNENVILMVPHSWAIDVPAILLASMGMPVSAMAKKQKNDVADW 174
Cdd:pfam03279  81 SVGRAIVETGRVWFWPDSRIAKRFEVIGLEHIKEALAQGRGAILVGPHFGNWDLGGRVLGQQYPGMAVYRPNLKNPLLDW 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300 175 LMHKQRVQYGGRVYERSGGIKPFLKSIRDGYIGYYLPDQDHGPEHSVFVDFFATRKATLPGLGKIAKLSRSKVLPLFASM 254
Cdd:pfam03279 161 LQTSGRERFGGRMLPRQNGIKGLIKALRKGEVVWYLPDQDLGRKDSVFVPFFGVPAATTTGPAKLALKTKAAVIPVFPIR 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1797005300 255 NTEDGTFDIEILPAFDL--DKGEEQDARTCNEAIEYFVGDKPEQYMWVLQLL 304
Cdd:pfam03279 241 NGDGSGYTVIVHPALDLtiTDDVEQIAQAMNQIVEKFIMPAPEQYFWLHRRW 292
LpxP COG1560
Palmitoleoyl-ACP: Kdo2-lipid-IV acyltransferase (lipid A biosynthesis) [Lipid transport and ...
 35-300 8.46e-85

Palmitoleoyl-ACP: Kdo2-lipid-IV acyltransferase (lipid A biosynthesis) [Lipid transport and metabolism]; Palmitoleoyl-ACP: Kdo2-lipid-IV acyltransferase (lipid A biosynthesis) is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 441168 [Multi-domain]  Cd Length: 271  Bit Score: 256.66  E-value: 8.46e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300  35 LFLPLALMPLSAQKWLAKTIAKKLSKSHKGPAHRARVNFELCFPGKTFQEREALIEKTLYTAAMFFFRFGLLSLRSPQWL 114
Cdd:COG1560     1 LLRLLRLLPLRLLYRLGDLLGRLLYRLAGRRRRVARRNLALAFPELSEAEREALARASFRNLGRTLLETLRLWRLSPERL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300 115 QSRCQIRGLDVLRQHIDNNENVILMVPHSWAIDVPAILLASMGMPVSAMAKKQKNDVADWLMHKQRVQYGGRVYERSGGI 194
Cdd:COG1560    81 RKRVEVEGLEHLEAALAEGRGVILLTPHFGNWELAGAALALRGYPVTAVYRPLKNPLLDRLIRRGRERFGGELIPRKDGV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300 195 KPFLKSIRDGYIGYYLPDQDHGPEHSVFVDFFATRKATLPGLGKIAKLSRSKVLPLFASMNTEDGTFDIEILPAF-DLDK 273
Cdd:COG1560   161 RALLRALRKGGIVGLLPDQDPGRKSGVFVPFFGVPAATPTGPARLARRTGAPVVPVFARRLPDGRGYRLEIEPPLeDFSE 240

                         250       260
                  ....*....|....*....|....*..
gi 1797005300 274 GEEQDARTCNEAIEYFVGDKPEQYMWV 300
Cdd:COG1560   241 DVEADTQRLNRALEAWIREHPEQWLWL 267
LPLAT_LABLAT-like cd07984
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LABLAT-like; ...
 115-300 1.14e-52

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LABLAT-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as lipid A biosynthesis lauroyl/myristoyl (LABLAT, HtrB) acyltransferases and similar proteins.


Pssm-ID: 153246 [Multi-domain]  Cd Length: 192  Bit Score: 171.63  E-value: 1.14e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300 115 QSRCQIRGLDVLRQHIDNNENVILMVPHSWAIDVPAILLASMGMPVSAMAKKQKNDVADWLMHKQRVQYGGRVYERSGGI 194
Cdd:cd07984     1 LKRVEREGLEHLEAALAKGKGVILLTAHFGNWELAGLALALLGYPVTVVYRPLKNPLLDRLITRGRERFGARLIPRGGGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300 195 KPFLKSIRDGYIGYYLPDQDHGPEHSVFVDFFATRKATLPGLGKIAKLSRSKVLPLFASMNtEDGTFDIEILPAFDLDKG 274
Cdd:cd07984    81 RELIRALKKGEIVGILPDQDPGRKGGVFVPFFGRPAATPTGPARLALKTGAPVVPAFAYRL-PGGGYRIEFEPPLENPPS 159

                         170       180
                  ....*....|....*....|....*...
gi 1797005300 275 E--EQDARTCNEAIEYFVGDKPEQYMWV 300
Cdd:cd07984   160 EdvEEDTQRLNDALEAAIREHPEQWLWF 187
lipid_A_htrB TIGR02207
lipid A biosynthesis lauroyl (or palmitoleoyl) acyltransferase; This model represents a narrow ...
 15-299 1.09e-50

lipid A biosynthesis lauroyl (or palmitoleoyl) acyltransferase; This model represents a narrow clade of acyltransferases, nearly all of which transfer a lauroyl group to KDO2-lipid IV-A, a lipid A precursor; these proteins are termed lipid A biosynthesis lauroyl acyltransferase, HtrB. An exception is a closely related paralog of E. coli HtrB, LpxP, which acts in cold shock conditions by transferring a palmitoleoyl rather than lauroyl group to the lipid A precursor. Members of this family are homologous to the family of acyltransferases responsible for the next step in lipid A biosynthesis. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 274031 [Multi-domain]  Cd Length: 303  Bit Score: 170.21  E-value: 1.09e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300  15 PEFERHFLSPKYWGTWLGVILFLPLALMPLSAQKWLAKTIAKKLSKSHKGPAHRARVNFELCFPGKTFQEREALIEKTLY 94
Cdd:TIGR02207   1 PEFSASLLHPRYWPTWLGLGVLWLIVQLPYPVLLALGRGIGRLAMRLMKRRVHIARRNLELCFPHMSDAERERLLRENFE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300  95 TAAMFFFRFGLLSLRSPQWLQSRCQIRGLDVLRQHIDNNENVILMVPHSWAIDVPAILLASMGmPVSAMAKKQKNDVADW 174
Cdd:TIGR02207  81 STGMALFETGMAWFWSDARIKKWMQIEGLEHLQRAQKQGRGVLLVGVHFLTLELGARIFGQQQ-PGIGVYRPHNNPLFDW 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300 175 LMHKQRVQYGGRVYERSgGIKPFLKSIRDGYIGYYLPDQDHGPEHSVFVDFFATRKA-TLPGLGKIAKLSRSKVLPLFAS 253
Cdd:TIGR02207 160 IQTRGRLRSNKAMIDRK-DLRGMIKALKNGERIWYAPDHDYGRKSSVFVPFFAVPDAaTTTGTSILARLSKCAVVPFTPR 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1797005300 254 MNTEDGTFDIEILP---AFDLDKgEEQDARTCNEAIEYFVGDKPEQYMW 299
Cdd:TIGR02207 239 RNEDGSGYRLKIDPpldDFPGDD-EIAAAARMNKIVEKMIMRAPEQYMW 286
PRK05646 PRK05646
lipid A biosynthesis lauroyl acyltransferase; Provisional
 15-310 4.73e-48

lipid A biosynthesis lauroyl acyltransferase; Provisional


Pssm-ID: 235543 [Multi-domain]  Cd Length: 310  Bit Score: 163.83  E-value: 4.73e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300  15 PEFERHFLSPKYWGTWLGVILFLPLALMPLSAQKWLAKTIAKKLSKSHKGPAHRARVNFELCFPGKTFQEREALIEKTLY 94
Cdd:PRK05646    4 PRFRAAFLHPRFWPLWLGLGLLWLVVQLPYRVLLWLGRALGALMYRLAGSRRRIAARNLELCFPEKSAAERERLLKENFA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300  95 TAAMFFFRFGLLSLRSPQWLQSRCQIRGLDVLRQHIDNNENVILMVPHSWAIDVPAILLASMgMPVSAMAKKQKNDVADW 174
Cdd:PRK05646   84 STGIAFFEMAMSWWWPKARLARLAHIEGLEHLQQAQQEGQGVILMALHFTTLEIGAALLGQQ-HTIDGMYREHKNPVFDF 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300 175 LMHKQRVQY--GGRVYERSgGIKPFLKSIRDGYIGYYLPDQDHGPEHSVFVDFFATRKATLPGLGKIAKLSRSKVLPlFA 252
Cdd:PRK05646  163 IQRRGRERHnlDSTAIERE-DVRGMLKLLRAGRAIWYAPDQDYGAKQSIFVPLFGIPAATVTATTKFARLGRARVIP-FT 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1797005300 253 SMNTEDGT-FDIEILPAFDLDKGE--EQDARTCNEAIEYFVGDKPEQYMWVLQLLHSQEDG 310
Cdd:PRK05646  241 QKRLADGSgYRLVIHPPLEDFPGEseEADCLRINQWVERVVRECPEQYLWAHRRFKSRPEG 301
PRK06860 PRK06860
lipid A biosynthesis lauroyl acyltransferase; Provisional
 15-305 3.99e-42

lipid A biosynthesis lauroyl acyltransferase; Provisional


Pssm-ID: 235880 [Multi-domain]  Cd Length: 309  Bit Score: 148.14  E-value: 3.99e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300  15 PEFERHFLSPKYWGTWLGVILFLPLALMPLSAQKWLAKTIAKKLSKSHKGPAHRARVNFELCFPGKTFQEREALIEKTLY 94
Cdd:PRK06860    7 PKFSRALLHPRYWLTWLGIGLLWLIVLLPYPVLYKLGRGLGKLALRFMKRRAKIARRNLELCFPEMSEQEREAIVVKNFE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300  95 TAAMFFFRFGlLSLRSPQWLQSR-CQIRGLDVLRQHIDNNENVILMVPHSWAIDVPAILLaSMGMPVSAMAKKQKNDVAD 173
Cdd:PRK06860   87 SVGMALIETG-MAWFWPDWRIKRwTEVEGLEHIREVQAQGRGVLLVGVHFLTLELGARIF-GMHNPGIGVYRPNDNPLYD 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300 174 WLMHKQRVQYGGRVYERSgGIKPFLKSIRDGYIGYYLPDQDHGPEHSVFVDFFATRKA-TLPGLGKIAKLSRSKVLPlFA 252
Cdd:PRK06860  165 WLQTWGRLRSNKSMLDRK-DLKGMIKALKKGERIWYAPDHDYGPRSSVFVPFFAVEQAaTTTGTWMLARMSKAAVIP-FV 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1797005300 253 SMNTEDGT-FDIEILPA--FDLDKGEEQDARTCNEAIEYFVGDKPEQYMWvlqlLH 305
Cdd:PRK06860  243 PRRKPDGKgYELIILPPedSPPLDDAEATAAWMNKVVEKCILMAPEQYMW----LH 294
PRK08706 PRK08706
lipid A biosynthesis lauroyl acyltransferase; Provisional
 31-310 3.57e-39

lipid A biosynthesis lauroyl acyltransferase; Provisional


Pssm-ID: 169557 [Multi-domain]  Cd Length: 289  Bit Score: 140.00  E-value: 3.57e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300  31 LGVILFLPLALMPLSAQ--KWLAKTIAKklskshkgPAHR-ARVNFELCFPGKTFQEREALIEKTLYTAAMFFFRFGLLS 107
Cdd:PRK08706    8 LYVLQFLPFALLHKLADltGLLAYLLVK--------PRRRiGEINLAKCFPEWDEEKRKTVLKQHFKHMAKLMLEYGLYW 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300 108 LRSPQWLQSRCQIRGLDVLRQHIDNNENVILMVPHSWAIDVpAILLASMGMPVSAMAKKQKNDVADWLMHKQRVQYGG-R 186
Cdd:PRK08706   80 YAPAGRLKSLVRYRNKHYLDDALAAGEKVIILYPHFTAFEM-AVYALNQDVPLISMYSHQKNKILDEQILKGRNRYHNvF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300 187 VYERSGGIKPFLKSIRDGYIGY-YLPDQDHGPEHSVFVDFFATRKATLPGLGKIAKLSRSKVLPLFAsMNTEDGTFDIEI 265
Cdd:PRK08706  159 LIGRTEGLRALVKQFRKSSAPFlYLPDQDFGRNDSVFVDFFGIQTATITGLSRIAALANAKVIPAIP-VREADNTVTLHF 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1797005300 266 LPAFD--LDKGEEQDARTCNEAIEYFVGDKPEQYMWVLQLLHSQEDG 310
Cdd:PRK08706  238 YPAWDsfPSEDAQADAQRMNRFIEERVREHPEQYFWLHKRFKTRPEG 284
PRK08733 PRK08733
LpxL/LpxP family Kdo(2)-lipid IV(A) lauroyl/palmitoleoyl acyltransferase;
22-315 3.64e-30

LpxL/LpxP family Kdo(2)-lipid IV(A) lauroyl/palmitoleoyl acyltransferase;


Pssm-ID: 181542 [Multi-domain]  Cd Length: 306  Bit Score: 116.54  E-value: 3.64e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300  22 LSPKYWGTWLGVILFLPLALMPLSAQKWLAKTI---AKKLSKSHKgpaHRARVNFELCFPGKTFQEREALIEKTLYTAAM 98
Cdd:PRK08733   14 RNPKHWPMYLGLAVMVLAARLPWTLQRALGRGVgwvAMRLAGTRR---RAAEVNLKLCFPEQDDAWRARLLRDSFDALGV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300  99 FFFRFGLLSLRSPQWLQSRCQIRGLDVLRQHIDNNENVILMVPHSWAIDVPAILLASMgMPVSAMAKKQKNDVADWLMHK 178
Cdd:PRK08733   91 GLFEFARAWWGSIDVIRPGVQIEGLEHLQQLQQQGRGVLLVSGHFMTLEMCGRLLCDH-VPLAGMYRRHRNPVFEWAVKR 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300 179 QRVQYGGRVYERSGgIKPFLKSIRDGYIGYYLPDQDHGPEHSVFVDFFATRKATLPGLGKIAKLSRSKVLPLFasMNTED 258
Cdd:PRK08733  170 GRLRYATHMFANED-LRATIKHLKRGGFLWYAPDQDMRGKDTVFVPFFGHPASTITATHQLARLTGCAVVPYF--HRREG 246

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300 259 GTFDIEILPAFDLDKGEEQDARTC--NEAIEYFVGDKPEQYMWVLQLLHSQEDG-NNYYN 315
Cdd:PRK08733  247 GRYVLKIAPPLADFPSDDVIADTTrvNAAIEDMVREAPDQYLWIHRRFKRQPGGrSDFYR 306
PRK06946 PRK06946
lipid A biosynthesis lauroyl acyltransferase; Provisional
 28-300 1.61e-26

lipid A biosynthesis lauroyl acyltransferase; Provisional


Pssm-ID: 180770 [Multi-domain]  Cd Length: 293  Bit Score: 106.31  E-value: 1.61e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300  28 GTWLGVILFLPLALMPLSAQKWLAKTIAKKLsksHKGPAHRARV---NFELCFPGKTFQEREALIEKTlytaamffFRFG 104
Cdd:PRK06946    5 GTALAIGLLKLLAFLPYGLTARFGDGLGWLL---YRIPSRRRRIvhtNLKLCFPDWSDARREELARRH--------FRHV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300 105 LLSL--RSPQWLQSRCQIRGLDVLRQHID----NNENVILMVPHSWAIDVPAILLA-SMGMPVSAMAKKQKNDVADWLMH 177
Cdd:PRK06946   74 IRSYveRSVQWFGSEKKLEKLVQVDSAIDltdpDGPPTIFLGLHFVGIEAGSIWLNySLRRRVGSLYTPMSNPLLDAIAK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300 178 KQRVQYGGRVYERSGGIKPFLKSIRDGYIGYYLPDQDHGPEHSVFVDFFATRKATLPGLGKIAKLSRSKVLPLFASMNTE 257
Cdd:PRK06946  154 AARGRFGAEMVSRADSARQVLRWLRDGKPVMLGADMDFGLRDSTFVPFFGVPACTLTAVSRLARTGGAQVVPFITEVLPD 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1797005300 258 DGTFDIEILPAFDLDKGE--EQDARTCNEAIEYFVGDKPEQYMWV 300
Cdd:PRK06946  234 YKGYRLRVFKPWENYPTGddDLDARRMNAFLEEQIRLMPEQYYWV 278
PRK08025 PRK08025
kdo(2)-lipid IV(A) palmitoleoyltransferase;
15-300 1.10e-25

kdo(2)-lipid IV(A) palmitoleoyltransferase;


Pssm-ID: 181200  Cd Length: 305  Bit Score: 104.05  E-value: 1.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300  15 PEFERHFLSPKYWGTWLGV-ILFLpLALMPLSAQKWLAKTIAKKLSKSHKGPAHRARVNFELCFPGKTFQEREALIEKTL 93
Cdd:PRK08025    5 QKFSREFLHPRYWLTWFGLgVLWL-LVQLPYPVLCFLGTRIGRMSRPFLKRRESIARKNLELCFPQMSAEEREKMIAENF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300  94 YTAAMFFFRFGLLSLRSPQWLQSRCQIRGLDVLRQHIDNNENVILMVPHSWAIDVPAillASMGM--PVSAMAKKQKNDV 171
Cdd:PRK08025   84 RSLGMALLETGMAWFWPDSRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGG---RVMGLcqPMMATYRPHNNKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300 172 ADWLMHKQRVQYGGRVYERSGgIKPFLKSIRDGYIGYYLPDQDHGPEHSVFVDFFATRK-ATLPGLGKIAKLSRSKVLPL 250
Cdd:PRK08025  161 MEWVQTRGRMRSNKAMIGRNN-LRGIVGALKKGEAVWFAPDQDYGPKGSSFAPFFAVENvATTNGTYVLSRLSGAAMLTV 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1797005300 251 FASMNTEDGTFDIEILPAF-DLDKGEEQDARTCNEAIEYFVGDKPEQYMWV 300
Cdd:PRK08025  240 TMVRKADYSGYRLFITPEMeGYPTDENQAAAYMNKIIEKEIMRAPEQYLWI 290
PRK08419 PRK08419
lipid A biosynthesis lauroyl acyltransferase; Reviewed
 39-299 8.28e-21

lipid A biosynthesis lauroyl acyltransferase; Reviewed


Pssm-ID: 181420 [Multi-domain]  Cd Length: 298  Bit Score: 90.47  E-value: 8.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300  39 LALMPLSAQKWLAKTIA---KKLSKSHKgpaHRARVNFELCFP-GKTFQEREALIEKTLYTAAMFFFRFGLLSLRSPQWL 114
Cdd:PRK08419   17 LAKMPHCIFLRLAKALAfimRYLDKKRR---KIAKANLDFCFGeSKSQEEKKRIIKKCYENFAFFGLDFIRNQNTTKEEI 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300 115 QSRCQIRGLDVLRQHIDNNENVILMVPHSWAIDVPAILLASMGMPVSAMAKKQKNDVADWLMHKQRVQYGGRVYERSGGI 194
Cdd:PRK08419   94 LNKVTFINEENLLDALKKKRPIIVTTAHYGYWELFSLALAAYYGAVSIVGRLLKSAPINEMISKRREQFGIELIDKKGAM 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300 195 KPFLKSIRDGYIGYYLPDQDHGPEHSVFVDFFATRKATLPGLGKIAKLSRSKVLPLFASmNTEDGTFDIEILPAFDLDK- 273
Cdd:PRK08419  174 KELLKALKQGRALGILVDQNVVPKEGVEVKFFNKRVTHTTIASILARRYNALIIPVFIF-NDDYSHFTITFFPPIRSKIt 252

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1797005300 274 -GEEQDARTCNEA----IEYFVGDKPEQYMW 299
Cdd:PRK08419  253 dDAEADILEATQAqasaCEEMIRKKPDEYFW 283
PRK05645 PRK05645
lysophospholipid acyltransferase;
39-310 7.90e-15

lysophospholipid acyltransferase;


Pssm-ID: 135493 [Multi-domain]  Cd Length: 295  Bit Score: 73.79  E-value: 7.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300  39 LALMPLSAQKWLAKTIAKKLSKSHKGPAHRARVNFELCFPGKTFQEREALIEKTLYTAAMFFFRFGLLSLRSPQ-WLQSR 117
Cdd:PRK05645   16 FALLPWRAVQGVGAGIGWLMWKLPNRSREVVRINLSKCFPELSPAELEKLVGQSLMDIGKTLTESACAWIWPPQkSLELV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300 118 CQIRGLDVLRQHIDNNENVILMVPHSWAIDVPAILLASMGMPVsAMAKKQKNDVADWLMHKQRVQYGGRVYERSG-GIKP 196
Cdd:PRK05645   96 REVEGLEVLEQALASGKGVVGITSHLGNWEVLNHFYCSQCKPI-IFYRPPKLKAVDELLRKQRVQLGNRVAPSTKeGILS 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300 197 FLKSIRDGYIGYYLPDQDHGPEHSVFVDFFATRKAT---LPGLgkiakLSRSKVLPLFA-SMNTEDGT---FDIEILPAF 269
Cdd:PRK05645  175 VIKEVRKGGQVGIPADPEPAESAGIFVPFLGTQALTskfVPNM-----LAGGKAVGVFLhALRLPDGSgykVILEAAPED 249

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1797005300 270 DLDKGEEQDARTCNEAIEYFVGDKPEQYMWVLQLLHSQEDG 310
Cdd:PRK05645  250 MYSTDVEVSAAAMSKVVERYVRAYPSQYMWSMKRFKKRPAG 290
PRK08905 PRK08905
lysophospholipid acyltransferase family protein;
35-299 3.16e-11

lysophospholipid acyltransferase family protein;


Pssm-ID: 236348 [Multi-domain]  Cd Length: 289  Bit Score: 63.09  E-value: 3.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300  35 LFLPLALMPLSaqkWLAKT------IAKKLSKSHkgpAHRARVNFELCFPGKTfqerEALIEKTLYTAAMFFFRFGLLSL 108
Cdd:PRK08905    5 LFRLLSRLPLS---WLHALggwlgrLAYRLPGRY---RRRLRANLRQAGGDPD----PAMVKAAAAETGRMILELPYVWF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300 109 RSPQWLQSR-CQIRGLDVLRQHIDNNENVILMVPHSWAIDVPAILLASMgMPVSAMAKKQKNDVADWLMHKQRVQYGGR- 186
Cdd:PRK08905   75 RKPEEIETMvKDDHGWEHVEAALAEGRGILFLTPHLGCFEVTARYIAQR-FPLTAMFRPPRKAALRPLMEAGRARGNMRt 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300 187 VYERSGGIKPFLKSIRDGYIGYYLPDQDHGPEHSVFVDFFAtRKA---TLPGlgKIAKLSRSKVLpLFASMNTEDGT-FD 262
Cdd:PRK08905  154 APATPQGVRMLVKALRRGEAVGILPDQVPSGGEGVWAPFFG-RPAytmTLVA--RLAEVTGVPVI-FVAGERLPRGRgYR 229

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1797005300 263 IEILPAFD-LDKGEEQDARTCNEAIEYFVGDKPEQYMW 299
Cdd:PRK08905  230 LHLRPVQEpLPGDKAADAAVINAEIERLIRRFPTQYLW 267
PRK08734 PRK08734
lauroyl acyltransferase;
39-299 2.41e-09

lauroyl acyltransferase;


Pssm-ID: 181543 [Multi-domain]  Cd Length: 305  Bit Score: 57.58  E-value: 2.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300  39 LALMPLSAQKWLAKTIAKKLSKSHKGPAHRARVNFELCFPGKTFQEREALIEKTLYTAAMFFFRFGLLSLRSP-QWLQSR 117
Cdd:PRK08734   17 VGRLPWPLLKRLADLLAWSWRKLNARESRVTRRNLELAYPELSPQQRAQLHAQILRSTARQALEVLRTWTHPPaENLARL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300 118 CQIRGLDVLRQHIDNNENVILMVPHSWAIDVPAILLASMGmPVSAMAKKQKNDVADWLMhkQRVQYGGRVYE-RSGG--I 194
Cdd:PRK08734   97 RQRHGQELYDAALASGRGVIVAAPHFGNWELLNQWLSERG-PIAIVYRPPESEAVDGFL--QLVRGGDNVRQvRAEGpaV 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300 195 KPFLKSIRDGYIGYYLPDQDHGPEHSVFVDFFATRKATLPGLGKIAKLSRSKVLPLFASMNTEDGTFDIEILPAFD--LD 272
Cdd:PRK08734  174 RQLFKVLKDGGAVGILPDQQPKMGDGVFAPFFGIPALTMTLVNRLAERTGATVLYGWCERIGPDLEFALHVQPADPavAD 253

                         250       260
                  ....*....|....*....|....*..
gi 1797005300 273 KGEEQDARTCNEAIEYFVGDKPEQYMW 299
Cdd:PRK08734  254 PDPLRAATALNAGIERIARRDPAQYQW 280
PRK06553 PRK06553
lipid A biosynthesis lauroyl acyltransferase; Provisional
 49-299 9.82e-05

lipid A biosynthesis lauroyl acyltransferase; Provisional


Pssm-ID: 235827 [Multi-domain]  Cd Length: 308  Bit Score: 43.42  E-value: 9.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300  49 WLAKTIAKKLskshkgPAHR-ARVNFELCFPGKTFQEREALI----EKTLYTAAMFFFRFGLLSLrSPQWLQ-SRCQIRG 122
Cdd:PRK06553   49 RLARLIGPLL------PRHRvALDNLRAAFPEKSEAEIEAIAlgmwDNLGRLGAEYAFLDAIFDY-DPEAPEpGRVEVRG 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300 123 LDVLRQHIDNNENVILMVPHSWAIDVPAILLASMGMPVSAMAKKQKNDVADWLMHKQR-VQYGGRVyeRSGGIKPF---- 197
Cdd:PRK06553  122 IEIFERLRDDGKPALIFTAHLGNWELLAIAAAAFGLDVTVLFRPPNNPYAARKVLEARrTTMGGLV--PSGAGAAFalag 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1797005300 198 -LKsiRDGYIGYyLPDQDHGpeHSVFVDFFATRKATLPGLGKIAKL-------SRSKVLPlfasmnteDGTFDIEILPAF 269
Cdd:PRK06553  200 vLE--RGGHVGM-LVDQKFT--RGVEVTFFGRPVKTNPLLAKLARQydcpvhgARCIRLP--------GGRFRLELTERV 266

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1797005300 270 DLDKGEEQD------ARTCNEAIEYFVGDKPEQYMW 299
Cdd:PRK06553  267 ELPRDADGQidvqatMQALTDVVEGWVREYPGQWLW 302
 
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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