|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08943 |
PRK08943 |
lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; Validated |
1-321 |
0e+00 |
|
lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; Validated
Pssm-ID: 236355 Cd Length: 314 Bit Score: 615.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 1 MDTKKTKSEYIPEFERAFLHPRYWGAWLGIGACAALALTPPSFRDPLLGKLGRLAGKFGKSARRRARINLFYCFPELSEA 80
Cdd:PRK08943 1 MEMKKDNKEYIPRFQKSFLHPRYWGTWLGIGALAGLALMPPRLRDPLAAKLGRLVGKLAKKARRRARINLSLCFPEKSEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 81 QREAIIDNMFATAPQAMVFMAELALRGPEKVLNRVDWHGEAFLNELLANKENVILLVPHGWGVDIPAMLLASRGVRMAAM 160
Cdd:PRK08943 81 EREAIIDEMFATAPQAMLMMAELALRSPKHLQRRVEWHGLEILEEARANGENVIFLVPHGWAIDIPAMLLASQGQPMAAM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 161 FHHQGNRLLDYVWNTVRRRFGGRLHPRQDGIKPFIKSVREGYWGYYLPDEDHGPEQSEFVDFFATYKATLPAVGRLMKVC 240
Cdd:PRK08943 161 FHNQRNPLFDWLWNRVRRRFGGRLHAREDGIKPFISSVRQGYWGYYLPDEDHGPEHSVFVDFFATYKATLPGIGRLAKVC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 241 NARVIPLFPVYNAKTHRLDVLIRPPMDDLANADDVTLARRMNEEVEHFVGPHPEQYTWILKLLKTRKAGEtepyrrkDLY 320
Cdd:PRK08943 241 RARVVPLFPVYNGKTHRLDIEIRPPMDDLLSADDETIARRMNEEVEQFVGPHPEQYMWILKLLKTRKPGE-------DLY 313
|
.
gi 333956870 321 P 321
Cdd:PRK08943 314 P 314
|
|
| lipid_A_msbB |
TIGR02208 |
lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; This family consists of MsbB ... |
10-314 |
6.84e-171 |
|
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: 476.22 E-value: 6.84e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 10 YIPEFERAFLHPRYWGAWLGIGACAALALTPPSFRDPLLGKLGRLAGKFGKSARRRARINLFYCFPELSEAQREAIIDNM 89
Cdd:TIGR02208 1 YDRRFQKSFLHPKYWGTWLGVFALVLLAFMPAKLRDPIAKVLAKFVGPIAKKPRGRARINLSACFPEKSEAERETIIDNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 90 FATAPQAMVFMAELALRGPEKVLNRVDWHGEAFLNELLANKENVILLVPHGWGVDIPAMLLASRGVRMAAMFHHQGNRLL 169
Cdd:TIGR02208 81 FATFVQVMLSQAELAIRSKAHLRRRVNLMGLEHIEAAQAAGKPVIFLVPHGWAIDYAGLRLASQGLPMVTMFNNHKNPLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 170 DYVWNTVRRRFGGRLHPRQDGIKPFIKSVREGYWGYYLPDEDHGPEQSEFVDFFATYKATLPAVGRLMKVCNARVIPLFP 249
Cdd:TIGR02208 161 DWLWNRVRSRFGGHVYAREAGIKALLASLKRGESGYYLPDEDHGPEQSVFVPFFATYKATLPVVGRLAKAGNAQVVPVFP 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333956870 250 VYNAKTHRLDVLIRPPMDDLANADDVTLARRMNEEVEHFVGPHPEQYTWILKLLKTRKAGETEPY 314
Cdd:TIGR02208 241 GYNQVTGKFELTVRPAMATELSVDPEQEARAMNKEVEQFILPYPEQYMWILRLLKTRPDGEASIY 305
|
|
| Lip_A_acyltrans |
pfam03279 |
Bacterial lipid A biosynthesis acyltransferase; |
12-305 |
2.42e-122 |
|
Bacterial lipid A biosynthesis acyltransferase;
Pssm-ID: 281296 [Multi-domain] Cd Length: 294 Bit Score: 352.80 E-value: 2.42e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 12 PEFERAFLHPRYWGAWLGIGACAALALTPPSFRDPLLGKLGRLAGKFGKSARRRARINLFYCFPELSEAQREAIIDNMFA 91
Cdd:pfam03279 1 PKFSPELLHPRYWLDWLGIAVLRLLALLPYSALRRIGKGLGRLAGRFLKRRRKIARRNLALCFPEMSEAEREQIIDKSFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 92 TAPQAMVFMAELALRGPEKVLNRVDWHGEAFLNELLANKENVILLVPHGWGVDIPAMLLASRGVRMAAMFHHQGNRLLDY 171
Cdd:pfam03279 81 SVGRAIVETGRVWFWPDSRIAKRFEVIGLEHIKEALAQGRGAILVGPHFGNWDLGGRVLGQQYPGMAVYRPNLKNPLLDW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 172 VWNTVRRRFGGRLHPRQDGIKPFIKSVREGYWGYYLPDEDHGPEQSEFVDFFATYKATLPAVGRLMKVCNARVIPLFPVY 251
Cdd:pfam03279 161 LQTSGRERFGGRMLPRQNGIKGLIKALRKGEVVWYLPDQDLGRKDSVFVPFFGVPAATTTGPAKLALKTKAAVIPVFPIR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 333956870 252 NAKTHRLDVLIRPPMDDLANADDVTLARRMNEEVEHFVGPHPEQYTWILKLLKT 305
Cdd:pfam03279 241 NGDGSGYTVIVHPALDLTITDDVEQIAQAMNQIVEKFIMPAPEQYFWLHRRWKT 294
|
|
| LpxP |
COG1560 |
Palmitoleoyl-ACP: Kdo2-lipid-IV acyltransferase (lipid A biosynthesis) [Lipid transport and ... |
34-301 |
2.88e-88 |
|
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: 265.13 E-value: 2.88e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 34 AALALTPPSFRDPLLGKLGRLAGKFGKSARRRARINLFYCFPELSEAQREAIIDNMFATAPQAMVFMAELALRGPEKVLN 113
Cdd:COG1560 3 RLLRLLPLRLLYRLGDLLGRLLYRLAGRRRRVARRNLALAFPELSEAEREALARASFRNLGRTLLETLRLWRLSPERLRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 114 RVDWHGEAFLNELLANKENVILLVPHGWGVDIPAMLLASRGVRMAAMFHHQGNRLLDYVWNTVRRRFGGRLHPRQDGIKP 193
Cdd:COG1560 83 RVEVEGLEHLEAALAEGRGVILLTPHFGNWELAGAALALRGYPVTAVYRPLKNPLLDRLIRRGRERFGGELIPRKDGVRA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 194 FIKSVREGYWGYYLPDEDHGPEQSEFVDFFATYKATLPAVGRLMKVCNARVIPLFPVYNAKTHRLDVLIRPPMDDLAnAD 273
Cdd:COG1560 163 LLRALRKGGIVGLLPDQDPGRKSGVFVPFFGVPAATPTGPARLARRTGAPVVPVFARRLPDGRGYRLEIEPPLEDFS-ED 241
|
250 260
....*....|....*....|....*...
gi 333956870 274 DVTLARRMNEEVEHFVGPHPEQYTWILK 301
Cdd:COG1560 242 VEADTQRLNRALEAWIREHPEQWLWLHR 269
|
|
| LPLAT_LABLAT-like |
cd07984 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LABLAT-like; ... |
112-304 |
1.54e-47 |
|
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: 158.15 E-value: 1.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 112 LNRVDWHGEAFLNELLANKENVILLVPHGWGVDIPAMLLASRGVRMAAMFHHQGNRLLDYVWNTVRRRFGGRLHPRQDGI 191
Cdd:cd07984 1 LKRVEREGLEHLEAALAKGKGVILLTAHFGNWELAGLALALLGYPVTVVYRPLKNPLLDRLITRGRERFGARLIPRGGGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 192 KPFIKSVREGYWGYYLPDEDHGPEQSEFVDFFATYKATLPAVGRLMKVCNARVIPLFPVYNaKTHRLDVLIRPPMDDLAN 271
Cdd:cd07984 81 RELIRALKKGEIVGILPDQDPGRKGGVFVPFFGRPAATPTGPARLALKTGAPVVPAFAYRL-PGGGYRIEFEPPLENPPS 159
|
170 180 190
....*....|....*....|....*....|...
gi 333956870 272 ADDVTLARRMNEEVEHFVGPHPEQYTWILKLLK 304
Cdd:cd07984 160 EDVEEDTQRLNDALEAAIREHPEQWLWFHRRWK 192
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08943 |
PRK08943 |
lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; Validated |
1-321 |
0e+00 |
|
lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; Validated
Pssm-ID: 236355 Cd Length: 314 Bit Score: 615.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 1 MDTKKTKSEYIPEFERAFLHPRYWGAWLGIGACAALALTPPSFRDPLLGKLGRLAGKFGKSARRRARINLFYCFPELSEA 80
Cdd:PRK08943 1 MEMKKDNKEYIPRFQKSFLHPRYWGTWLGIGALAGLALMPPRLRDPLAAKLGRLVGKLAKKARRRARINLSLCFPEKSEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 81 QREAIIDNMFATAPQAMVFMAELALRGPEKVLNRVDWHGEAFLNELLANKENVILLVPHGWGVDIPAMLLASRGVRMAAM 160
Cdd:PRK08943 81 EREAIIDEMFATAPQAMLMMAELALRSPKHLQRRVEWHGLEILEEARANGENVIFLVPHGWAIDIPAMLLASQGQPMAAM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 161 FHHQGNRLLDYVWNTVRRRFGGRLHPRQDGIKPFIKSVREGYWGYYLPDEDHGPEQSEFVDFFATYKATLPAVGRLMKVC 240
Cdd:PRK08943 161 FHNQRNPLFDWLWNRVRRRFGGRLHAREDGIKPFISSVRQGYWGYYLPDEDHGPEHSVFVDFFATYKATLPGIGRLAKVC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 241 NARVIPLFPVYNAKTHRLDVLIRPPMDDLANADDVTLARRMNEEVEHFVGPHPEQYTWILKLLKTRKAGEtepyrrkDLY 320
Cdd:PRK08943 241 RARVVPLFPVYNGKTHRLDIEIRPPMDDLLSADDETIARRMNEEVEQFVGPHPEQYMWILKLLKTRKPGE-------DLY 313
|
.
gi 333956870 321 P 321
Cdd:PRK08943 314 P 314
|
|
| lipid_A_msbB |
TIGR02208 |
lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; This family consists of MsbB ... |
10-314 |
6.84e-171 |
|
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: 476.22 E-value: 6.84e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 10 YIPEFERAFLHPRYWGAWLGIGACAALALTPPSFRDPLLGKLGRLAGKFGKSARRRARINLFYCFPELSEAQREAIIDNM 89
Cdd:TIGR02208 1 YDRRFQKSFLHPKYWGTWLGVFALVLLAFMPAKLRDPIAKVLAKFVGPIAKKPRGRARINLSACFPEKSEAERETIIDNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 90 FATAPQAMVFMAELALRGPEKVLNRVDWHGEAFLNELLANKENVILLVPHGWGVDIPAMLLASRGVRMAAMFHHQGNRLL 169
Cdd:TIGR02208 81 FATFVQVMLSQAELAIRSKAHLRRRVNLMGLEHIEAAQAAGKPVIFLVPHGWAIDYAGLRLASQGLPMVTMFNNHKNPLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 170 DYVWNTVRRRFGGRLHPRQDGIKPFIKSVREGYWGYYLPDEDHGPEQSEFVDFFATYKATLPAVGRLMKVCNARVIPLFP 249
Cdd:TIGR02208 161 DWLWNRVRSRFGGHVYAREAGIKALLASLKRGESGYYLPDEDHGPEQSVFVPFFATYKATLPVVGRLAKAGNAQVVPVFP 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333956870 250 VYNAKTHRLDVLIRPPMDDLANADDVTLARRMNEEVEHFVGPHPEQYTWILKLLKTRKAGETEPY 314
Cdd:TIGR02208 241 GYNQVTGKFELTVRPAMATELSVDPEQEARAMNKEVEQFILPYPEQYMWILRLLKTRPDGEASIY 305
|
|
| Lip_A_acyltrans |
pfam03279 |
Bacterial lipid A biosynthesis acyltransferase; |
12-305 |
2.42e-122 |
|
Bacterial lipid A biosynthesis acyltransferase;
Pssm-ID: 281296 [Multi-domain] Cd Length: 294 Bit Score: 352.80 E-value: 2.42e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 12 PEFERAFLHPRYWGAWLGIGACAALALTPPSFRDPLLGKLGRLAGKFGKSARRRARINLFYCFPELSEAQREAIIDNMFA 91
Cdd:pfam03279 1 PKFSPELLHPRYWLDWLGIAVLRLLALLPYSALRRIGKGLGRLAGRFLKRRRKIARRNLALCFPEMSEAEREQIIDKSFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 92 TAPQAMVFMAELALRGPEKVLNRVDWHGEAFLNELLANKENVILLVPHGWGVDIPAMLLASRGVRMAAMFHHQGNRLLDY 171
Cdd:pfam03279 81 SVGRAIVETGRVWFWPDSRIAKRFEVIGLEHIKEALAQGRGAILVGPHFGNWDLGGRVLGQQYPGMAVYRPNLKNPLLDW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 172 VWNTVRRRFGGRLHPRQDGIKPFIKSVREGYWGYYLPDEDHGPEQSEFVDFFATYKATLPAVGRLMKVCNARVIPLFPVY 251
Cdd:pfam03279 161 LQTSGRERFGGRMLPRQNGIKGLIKALRKGEVVWYLPDQDLGRKDSVFVPFFGVPAATTTGPAKLALKTKAAVIPVFPIR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 333956870 252 NAKTHRLDVLIRPPMDDLANADDVTLARRMNEEVEHFVGPHPEQYTWILKLLKT 305
Cdd:pfam03279 241 NGDGSGYTVIVHPALDLTITDDVEQIAQAMNQIVEKFIMPAPEQYFWLHRRWKT 294
|
|
| LpxP |
COG1560 |
Palmitoleoyl-ACP: Kdo2-lipid-IV acyltransferase (lipid A biosynthesis) [Lipid transport and ... |
34-301 |
2.88e-88 |
|
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: 265.13 E-value: 2.88e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 34 AALALTPPSFRDPLLGKLGRLAGKFGKSARRRARINLFYCFPELSEAQREAIIDNMFATAPQAMVFMAELALRGPEKVLN 113
Cdd:COG1560 3 RLLRLLPLRLLYRLGDLLGRLLYRLAGRRRRVARRNLALAFPELSEAEREALARASFRNLGRTLLETLRLWRLSPERLRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 114 RVDWHGEAFLNELLANKENVILLVPHGWGVDIPAMLLASRGVRMAAMFHHQGNRLLDYVWNTVRRRFGGRLHPRQDGIKP 193
Cdd:COG1560 83 RVEVEGLEHLEAALAEGRGVILLTPHFGNWELAGAALALRGYPVTAVYRPLKNPLLDRLIRRGRERFGGELIPRKDGVRA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 194 FIKSVREGYWGYYLPDEDHGPEQSEFVDFFATYKATLPAVGRLMKVCNARVIPLFPVYNAKTHRLDVLIRPPMDDLAnAD 273
Cdd:COG1560 163 LLRALRKGGIVGLLPDQDPGRKSGVFVPFFGVPAATPTGPARLARRTGAPVVPVFARRLPDGRGYRLEIEPPLEDFS-ED 241
|
250 260
....*....|....*....|....*...
gi 333956870 274 DVTLARRMNEEVEHFVGPHPEQYTWILK 301
Cdd:COG1560 242 VEADTQRLNRALEAWIREHPEQWLWLHR 269
|
|
| lipid_A_htrB |
TIGR02207 |
lipid A biosynthesis lauroyl (or palmitoleoyl) acyltransferase; This model represents a narrow ... |
12-306 |
2.78e-49 |
|
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: 166.36 E-value: 2.78e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 12 PEFERAFLHPRYWGAWLGIGACAALALTPPSFRDPLLGKLGRLAGKFGKSARRRARINLFYCFPELSEAQREAIIDNMFA 91
Cdd:TIGR02207 1 PEFSASLLHPRYWPTWLGLGVLWLIVQLPYPVLLALGRGIGRLAMRLMKRRVHIARRNLELCFPHMSDAERERLLRENFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 92 TAPQAMVFMAeLALRGPEKVLNR-VDWHGEAFLNELLANKENVILLVPHGWGVDIPAMLLASRGVrMAAMFHHQGNRLLD 170
Cdd:TIGR02207 81 STGMALFETG-MAWFWSDARIKKwMQIEGLEHLQRAQKQGRGVLLVGVHFLTLELGARIFGQQQP-GIGVYRPHNNPLFD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 171 YVWNTVRRRFGGRLHPRQDgIKPFIKSVREGYWGYYLPDEDHGPEQSEFVDFFATYKA-TLPAVGRLMKVCNARVIPLFP 249
Cdd:TIGR02207 159 WIQTRGRLRSNKAMIDRKD-LRGMIKALKNGERIWYAPDHDYGRKSSVFVPFFAVPDAaTTTGTSILARLSKCAVVPFTP 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 333956870 250 VYNAKTHRLDVLIRPPMDDLANADDVTLARRMNEEVEHFVGPHPEQYTWILKLLKTR 306
Cdd:TIGR02207 238 RRNEDGSGYRLKIDPPLDDFPGDDEIAAAARMNKIVEKMIMRAPEQYMWLHRRFKTR 294
|
|
| LPLAT_LABLAT-like |
cd07984 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LABLAT-like; ... |
112-304 |
1.54e-47 |
|
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: 158.15 E-value: 1.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 112 LNRVDWHGEAFLNELLANKENVILLVPHGWGVDIPAMLLASRGVRMAAMFHHQGNRLLDYVWNTVRRRFGGRLHPRQDGI 191
Cdd:cd07984 1 LKRVEREGLEHLEAALAKGKGVILLTAHFGNWELAGLALALLGYPVTVVYRPLKNPLLDRLITRGRERFGARLIPRGGGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 192 KPFIKSVREGYWGYYLPDEDHGPEQSEFVDFFATYKATLPAVGRLMKVCNARVIPLFPVYNaKTHRLDVLIRPPMDDLAN 271
Cdd:cd07984 81 RELIRALKKGEIVGILPDQDPGRKGGVFVPFFGRPAATPTGPARLALKTGAPVVPAFAYRL-PGGGYRIEFEPPLENPPS 159
|
170 180 190
....*....|....*....|....*....|...
gi 333956870 272 ADDVTLARRMNEEVEHFVGPHPEQYTWILKLLK 304
Cdd:cd07984 160 EDVEEDTQRLNDALEAAIREHPEQWLWFHRRWK 192
|
|
| PRK05646 |
PRK05646 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
12-317 |
1.02e-46 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 235543 [Multi-domain] Cd Length: 310 Bit Score: 159.98 E-value: 1.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 12 PEFERAFLHPRYWGAWLGIGACAALALTPPsfrdPLLGKLGRLAG----KFGKSARRRARINLFYCFPELSEAQREAIID 87
Cdd:PRK05646 4 PRFRAAFLHPRFWPLWLGLGLLWLVVQLPY----RVLLWLGRALGalmyRLAGSRRRIAARNLELCFPEKSAAERERLLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 88 NMFATAPQAMVFMAeLALRGPEKVLNRV-DWHGEAFLNELLANKENVILLVPHGWGVDIPAMLLASRgVRMAAMFHHQGN 166
Cdd:PRK05646 80 ENFASTGIAFFEMA-MSWWWPKARLARLaHIEGLEHLQQAQQEGQGVILMALHFTTLEIGAALLGQQ-HTIDGMYREHKN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 167 RLLDYVWNTVRRRFG-GRLHPRQDGIKPFIKSVREGYWGYYLPDEDHGPEQSEFVDFFATYKATLPAVGRLMKVCNARVI 245
Cdd:PRK05646 158 PVFDFIQRRGRERHNlDSTAIEREDVRGMLKLLRAGRAIWYAPDQDYGAKQSIFVPLFGIPAATVTATTKFARLGRARVI 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333956870 246 PLFPVYNAKTHRLDVLIRPPMDDLANADDVTLARRMNEEVEHFVGPHPEQYTWILKLLKTRKAGETEPYRRK 317
Cdd:PRK05646 238 PFTQKRLADGSGYRLVIHPPLEDFPGESEEADCLRINQWVERVVRECPEQYLWAHRRFKSRPEGEPKLYPKR 309
|
|
| PRK06860 |
PRK06860 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
11-315 |
2.01e-43 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 235880 [Multi-domain] Cd Length: 309 Bit Score: 151.22 E-value: 2.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 11 IPEFERAFLHPRYWGAWLGIGACAALALTP-PSFRdpLLGK-LGRLAGKFGKSARRRARINLFYCFPELSEAQREAIIDN 88
Cdd:PRK06860 6 LPKFSRALLHPRYWLTWLGIGLLWLIVLLPyPVLY--KLGRgLGKLALRFMKRRAKIARRNLELCFPEMSEQEREAIVVK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 89 MFATAPQAMVFMAeLALRGPEKVLNR-VDWHGEAFLNELLANKENVILLVPHGWGVDIpamllasrGVRMAAMfHHQG-- 165
Cdd:PRK06860 84 NFESVGMALIETG-MAWFWPDWRIKRwTEVEGLEHIREVQAQGRGVLLVGVHFLTLEL--------GARIFGM-HNPGig 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 166 ------NRLLDYVWNTVRRRFGGRLHPRQDgIKPFIKSVREGYWGYYLPDEDHGPEQSEFVDFFATYKA-TLPAVGRLMK 238
Cdd:PRK06860 154 vyrpndNPLYDWLQTWGRLRSNKSMLDRKD-LKGMIKALKKGERIWYAPDHDYGPRSSVFVPFFAVEQAaTTTGTWMLAR 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 333956870 239 VCNARVIPLFPVYNAKTHRLDVLIRPPMDDLANADDVTLARRMNEEVEHFVGPHPEQYTWILKLLKTRKAGETEPYR 315
Cdd:PRK06860 233 MSKAAVIPFVPRRKPDGKGYELIILPPEDSPPLDDAEATAAWMNKVVEKCILMAPEQYMWLHRRFKTRPEGVPSRYD 309
|
|
| PRK08706 |
PRK08706 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
36-314 |
9.70e-42 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 169557 [Multi-domain] Cd Length: 289 Bit Score: 146.55 E-value: 9.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 36 LALTPPSFRDPLLGKLGRLAGKFGKSARRRARINLFYCFPELSEAQREAIIDNMFATAPQAMVFMAELALRGPEKVLNRV 115
Cdd:PRK08706 11 LQFLPFALLHKLADLTGLLAYLLVKPRRRIGEINLAKCFPEWDEEKRKTVLKQHFKHMAKLMLEYGLYWYAPAGRLKSLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 116 DWHGEAFLNELLANKENVILLVPHGWGVDIPAMLLaSRGVRMAAMFHHQGNRLLDYVWNTVRRRFGG-RLHPRQDGIKPF 194
Cdd:PRK08706 91 RYRNKHYLDDALAAGEKVIILYPHFTAFEMAVYAL-NQDVPLISMYSHQKNKILDEQILKGRNRYHNvFLIGRTEGLRAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 195 IKSVREGYWGY-YLPDEDHGPEQSEFVDFFATYKATLPAVGRLMKVCNARVIPLFPVYNAKThRLDVLIRPPMDDLANAD 273
Cdd:PRK08706 170 VKQFRKSSAPFlYLPDQDFGRNDSVFVDFFGIQTATITGLSRIAALANAKVIPAIPVREADN-TVTLHFYPAWDSFPSED 248
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 333956870 274 DVTLARRMNEEVEHFVGPHPEQYTWILKLLKTRKAGETEPY 314
Cdd:PRK08706 249 AQADAQRMNRFIEERVREHPEQYFWLHKRFKTRPEGSPDFY 289
|
|
| PRK06946 |
PRK06946 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
25-314 |
3.82e-39 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 180770 [Multi-domain] Cd Length: 293 Bit Score: 139.82 E-value: 3.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 25 GAWLGIGACAALALTPPSFRDPLLGKLGRLAGKFGKSARRRARINLFYCFPELSEAQREAIIDNMFATAPQAMV------ 98
Cdd:PRK06946 5 GTALAIGLLKLLAFLPYGLTARFGDGLGWLLYRIPSRRRRIVHTNLKLCFPDWSDARREELARRHFRHVIRSYVersvqw 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 99 FMAELALRGPEKVLNRVDwhgeafLNELlaNKENVILLVPHGWGVDIPAMLLA-SRGVRMAAMFHHQGNRLLDYVWNTVR 177
Cdd:PRK06946 85 FGSEKKLEKLVQVDSAID------LTDP--DGPPTIFLGLHFVGIEAGSIWLNySLRRRVGSLYTPMSNPLLDAIAKAAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 178 RRFGGRLHPRQDGIKPFIKSVREGYWGYYLPDEDHGPEQSEFVDFFATYKATLPAVGRLMKVCNARVIPLF----PVYna 253
Cdd:PRK06946 157 GRFGAEMVSRADSARQVLRWLRDGKPVMLGADMDFGLRDSTFVPFFGVPACTLTAVSRLARTGGAQVVPFItevlPDY-- 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 333956870 254 KTHRLDVLirPPMDDLANADDVTLARRMNEEVEHFVGPHPEQYTWILKLLKTRKAGETEPY 314
Cdd:PRK06946 235 KGYRLRVF--KPWENYPTGDDDLDARRMNAFLEEQIRLMPEQYYWVHKRFKTRPPGEPSVY 293
|
|
| PRK08025 |
PRK08025 |
kdo(2)-lipid IV(A) palmitoleoyltransferase; |
12-314 |
1.44e-30 |
|
kdo(2)-lipid IV(A) palmitoleoyltransferase;
Pssm-ID: 181200 Cd Length: 305 Bit Score: 117.15 E-value: 1.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 12 PEFERAFLHPRYWGAWLGIGACAALALTPPSFRDPLLGKLGRLAGKFGKSARRRARINLFYCFPELSEAQREAIIDNMFA 91
Cdd:PRK08025 5 QKFSREFLHPRYWLTWFGLGVLWLLVQLPYPVLCFLGTRIGRMSRPFLKRRESIARKNLELCFPQMSAEEREKMIAENFR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 92 TAPQAMVFMAELALRGPEKVLNRVDWHGEAFLNELLANKENVILLvphgwGVDIPAMLLASRGV----RMAAMFHHQGNR 167
Cdd:PRK08025 85 SLGMALLETGMAWFWPDSRVRKWFDVEGLDNLKRAQMQNRGVMVV-----GVHFMSLELGGRVMglcqPMMATYRPHNNK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 168 LLDYVWNTVRRRFGGRLHPRQDgIKPFIKSVREGYWGYYLPDEDHGPEQSEFVDFFATYK-ATLPAVGRLMKVCNARVIP 246
Cdd:PRK08025 160 LMEWVQTRGRMRSNKAMIGRNN-LRGIVGALKKGEAVWFAPDQDYGPKGSSFAPFFAVENvATTNGTYVLSRLSGAAMLT 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 333956870 247 LFPVYNAKTHRLDVLIRPPMDDLAnADDVTLARRMNEEVEHFVGPHPEQYTWILKLLKTRKAGETEPY 314
Cdd:PRK08025 239 VTMVRKADYSGYRLFITPEMEGYP-TDENQAAAYMNKIIEKEIMRAPEQYLWIHRRFKTRPVGESSLY 305
|
|
| PRK08733 |
PRK08733 |
LpxL/LpxP family Kdo(2)-lipid IV(A) lauroyl/palmitoleoyl acyltransferase; |
19-315 |
2.74e-26 |
|
LpxL/LpxP family Kdo(2)-lipid IV(A) lauroyl/palmitoleoyl acyltransferase;
Pssm-ID: 181542 [Multi-domain] Cd Length: 306 Bit Score: 105.76 E-value: 2.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 19 LHPRYWGAWLGIGACAALALTPPSFRDPLLGKLGRLAGKFGKSARRRARINLFYCFPELSEAQREAIIDNMFATAPQAMV 98
Cdd:PRK08733 14 RNPKHWPMYLGLAVMVLAARLPWTLQRALGRGVGWVAMRLAGTRRRAAEVNLKLCFPEQDDAWRARLLRDSFDALGVGLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 99 FMAELALRGPEKVLNRVDWHGEAFLNELLANKENVILLVPHGWGVDIPAMLLASRgVRMAAMFHHQGNRLLDYVWNTVRR 178
Cdd:PRK08733 94 EFARAWWGSIDVIRPGVQIEGLEHLQQLQQQGRGVLLVSGHFMTLEMCGRLLCDH-VPLAGMYRRHRNPVFEWAVKRGRL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 179 RFGGRLHPRQDgIKPFIKSVREGYWGYYLPDEDHGPEQSEFVDFFATYKATLPAVGRLMKVCNARVIPLFpvYNAKTHRL 258
Cdd:PRK08733 173 RYATHMFANED-LRATIKHLKRGGFLWYAPDQDMRGKDTVFVPFFGHPASTITATHQLARLTGCAVVPYF--HRREGGRY 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 333956870 259 DVLIRPPMDDLANADDVTLARRMNEEVEHFVGPHPEQYTWILKLLKTRKAGETEPYR 315
Cdd:PRK08733 250 VLKIAPPLADFPSDDVIADTTRVNAAIEDMVREAPDQYLWIHRRFKRQPGGRSDFYR 306
|
|
| PRK08905 |
PRK08905 |
lysophospholipid acyltransferase family protein; |
33-313 |
1.59e-17 |
|
lysophospholipid acyltransferase family protein;
Pssm-ID: 236348 [Multi-domain] Cd Length: 289 Bit Score: 81.19 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 33 CAALALTPPSFRDPLLGKLGRLAGKFGKSARRRARINLFYCFPELSEAQREAIidnmFATAPQAMVFMAELALRGPEKVL 112
Cdd:PRK08905 6 FRLLSRLPLSWLHALGGWLGRLAYRLPGRYRRRLRANLRQAGGDPDPAMVKAA----AAETGRMILELPYVWFRKPEEIE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 113 NRV-DWHGEAFLNELLANKENVILLVPHGWGVDIPAMLLASRGvRMAAMFHHQGNRLLDYVWNTVRRRFGGRLHPRQ-DG 190
Cdd:PRK08905 82 TMVkDDHGWEHVEAALAEGRGILFLTPHLGCFEVTARYIAQRF-PLTAMFRPPRKAALRPLMEAGRARGNMRTAPATpQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 191 IKPFIKSVREGYWGYYLPdeDHGPEQSE--FVDFFATYKATLPAVGRLMKVCNARVIPLFpvynakTHRL------DVLI 262
Cdd:PRK08905 161 VRMLVKALRRGEAVGILP--DQVPSGGEgvWAPFFGRPAYTMTLVARLAEVTGVPVIFVA------GERLprgrgyRLHL 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 333956870 263 RPPMDDLaNADDVTLARRMNEEVEHFVGPHPEQYTWILKLLKTRKAGETEP 313
Cdd:PRK08905 233 RPVQEPL-PGDKAADAAVINAEIERLIRRFPTQYLWGYNRYKRPRGAPAPP 282
|
|
| PRK08419 |
PRK08419 |
lipid A biosynthesis lauroyl acyltransferase; Reviewed |
36-304 |
2.31e-15 |
|
lipid A biosynthesis lauroyl acyltransferase; Reviewed
Pssm-ID: 181420 [Multi-domain] Cd Length: 298 Bit Score: 75.06 E-value: 2.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 36 LALTPPSFRDPLLGKLGRLAGKFGKSARRRARINLFYCFPE-LSEAQREAIIDNMFATAPQAMVFMAELALRGPEKVLNR 114
Cdd:PRK08419 17 LAKMPHCIFLRLAKALAFIMRYLDKKRRKIAKANLDFCFGEsKSQEEKKRIIKKCYENFAFFGLDFIRNQNTTKEEILNK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 115 VDWHGEAFLNELLANKENVILLVPHGWGVDIPAMLLASRGVRMAAMFHHQGNRLLDYVWNTVRRRFGGRLHPRQDGIKPF 194
Cdd:PRK08419 97 VTFINEENLLDALKKKRPIIVTTAHYGYWELFSLALAAYYGAVSIVGRLLKSAPINEMISKRREQFGIELIDKKGAMKEL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 195 IKSVREGYWGYYLPDEDHGPEQSEFVDFFATYKATLPAVGRLMKVCNARVIPLFpVYNAKTHRLDVLIRPPMD----DLA 270
Cdd:PRK08419 177 LKALKQGRALGILVDQNVVPKEGVEVKFFNKRVTHTTIASILARRYNALIIPVF-IFNDDYSHFTITFFPPIRskitDDA 255
|
250 260 270
....*....|....*....|....*....|....
gi 333956870 271 NADDVTLARRMNEEVEHFVGPHPEQYTWILKLLK 304
Cdd:PRK08419 256 EADILEATQAQASACEEMIRKKPDEYFWFHRRFK 289
|
|
| PRK05645 |
PRK05645 |
lysophospholipid acyltransferase; |
28-314 |
1.22e-13 |
|
lysophospholipid acyltransferase;
Pssm-ID: 135493 [Multi-domain] Cd Length: 295 Bit Score: 69.93 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 28 LGIGACAALALTPPSFRDPLLGKLGRLAGKFGKSARRRARINLFYCFPELSEAQREAIIDNMFATAPQAMVFMAELALRG 107
Cdd:PRK05645 8 LMVGALRLFALLPWRAVQGVGAGIGWLMWKLPNRSREVVRINLSKCFPELSPAELEKLVGQSLMDIGKTLTESACAWIWP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 108 PEKVLNRV-DWHGEAFLNELLANKENVILLVPHGWGVDIPAMLLASRgVRMAAMFHHQGNRLLDYVWNTVRRRFGGRLHP 186
Cdd:PRK05645 88 PQKSLELVrEVEGLEVLEQALASGKGVVGITSHLGNWEVLNHFYCSQ-CKPIIFYRPPKLKAVDELLRKQRVQLGNRVAP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 187 R-QDGIKPFIKSVREGywGYYLPDEDHGPEQSE--FVDFFATYKATLPAVGRLMKVCNARVIPLFPVYNAKTHRLDVLIR 263
Cdd:PRK05645 167 StKEGILSVIKEVRKG--GQVGIPADPEPAESAgiFVPFLGTQALTSKFVPNMLAGGKAVGVFLHALRLPDGSGYKVILE 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 333956870 264 PPMDDLANADDVTLARRMNEEVEHFVGPHPEQYTWILKLLKTRKAGETEPY 314
Cdd:PRK05645 245 AAPEDMYSTDVEVSAAAMSKVVERYVRAYPSQYMWSMKRFKKRPAGEARWY 295
|
|
| PRK08734 |
PRK08734 |
lauroyl acyltransferase; |
46-313 |
1.45e-10 |
|
lauroyl acyltransferase;
Pssm-ID: 181543 [Multi-domain] Cd Length: 305 Bit Score: 61.05 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 46 PLLGKLGRLAG----KFGKSARRRARINLFYCFPELSEAQREAI-IDNMFATAPQAMVfMAELALRGPEKVLNRV-DWHG 119
Cdd:PRK08734 23 PLLKRLADLLAwswrKLNARESRVTRRNLELAYPELSPQQRAQLhAQILRSTARQALE-VLRTWTHPPAENLARLrQRHG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 120 EAFLNELLANKENVILLVPHGWGVDIPAMLLASRGvRMAAMFHHQGNRLLDYVWNTVRRRFGGRlHPRQDG--IKPFIKS 197
Cdd:PRK08734 102 QELYDAALASGRGVIVAAPHFGNWELLNQWLSERG-PIAIVYRPPESEAVDGFLQLVRGGDNVR-QVRAEGpaVRQLFKV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 198 VREGYWGYYLPDEDHGPEQSEFVDFFATYKATLPAVGRLMKVCNARVIPLFPVYNAKTHRLDVLIRPPMDDLANADDVTL 277
Cdd:PRK08734 180 LKDGGAVGILPDQQPKMGDGVFAPFFGIPALTMTLVNRLAERTGATVLYGWCERIGPDLEFALHVQPADPAVADPDPLRA 259
|
250 260 270
....*....|....*....|....*....|....*.
gi 333956870 278 ARRMNEEVEHFVGPHPEQYTWILKLLKTRKAGETEP 313
Cdd:PRK08734 260 ATALNAGIERIARRDPAQYQWTYKRYTLRPPGSGEH 295
|
|
| PRK06553 |
PRK06553 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
26-298 |
1.96e-04 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 235827 [Multi-domain] Cd Length: 308 Bit Score: 42.65 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 26 AWLGIGACAALALTPPsfrDPLLGKLGRLAGKFGK--SARRRARINLFYCFPELSEAQREAII----DNMFATAPQaMVF 99
Cdd:PRK06553 25 AQLVFGLLGLLRLFPA---DKAINFFGRLARLIGPllPRHRVALDNLRAAFPEKSEAEIEAIAlgmwDNLGRLGAE-YAF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 100 MAELALRGPEKV-LNRVDWHGEAFLNELLANKENVILLVPHGWGVDIPAMLLASRGVRMAAMFHHQGNRLLDYVWNTVRR 178
Cdd:PRK06553 101 LDAIFDYDPEAPePGRVEVRGIEIFERLRDDGKPALIFTAHLGNWELLAIAAAAFGLDVTVLFRPPNNPYAARKVLEARR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956870 179 RFGGRLHPRQDGiKPF--IKSVREGYWGYYLPDE--DHGPEqsefVDFFATYKATLPAVGRLMK-----VCNARVIPLfp 249
Cdd:PRK06553 181 TTMGGLVPSGAG-AAFalAGVLERGGHVGMLVDQkfTRGVE----VTFFGRPVKTNPLLAKLARqydcpVHGARCIRL-- 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 333956870 250 vyNAKTHRLDVL--IRPPMDDLANADDVTLARRMNEEVEHFVGPHPEQYTW 298
Cdd:PRK06553 254 --PGGRFRLELTerVELPRDADGQIDVQATMQALTDVVEGWVREYPGQWLW 302
|
|
|