|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08025 |
PRK08025 |
kdo(2)-lipid IV(A) palmitoleoyltransferase; |
1-305 |
0e+00 |
|
kdo(2)-lipid IV(A) palmitoleoyltransferase;
Pssm-ID: 181200 Cd Length: 305 Bit Score: 643.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 1 MFPQCKFSREFLHPRYWLTWFGLGVLWLWVQLPYPVLCFLGTRIGAMARPFLKRRESIARKNLELCFPQHSAEEREKMIA 80
Cdd:PRK08025 1 MFPQQKFSREFLHPRYWLTWFGLGVLWLLVQLPYPVLCFLGTRIGRMSRPFLKRRESIARKNLELCFPQMSAEEREKMIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 81 ENFRSLGMALVETGMAWFWPDSRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLCQPMMATYRPHNNQL 160
Cdd:PRK08025 81 ENFRSLGMALLETGMAWFWPDSRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLCQPMMATYRPHNNKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 161 MEWVQTRGRMRSNKAMIGRNNLRGIVGALKKGEAVWFAPDQDYGRKGSSFAPFFAVENVATTNGTYVLSRLSGAAMLTVT 240
Cdd:PRK08025 161 MEWVQTRGRMRSNKAMIGRNNLRGIVGALKKGEAVWFAPDQDYGPKGSSFAPFFAVENVATTNGTYVLSRLSGAAMLTVT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111426 241 MVRKADYSGYRLFITPEMEGYPTDENQAAAYMNKIIEKEIMRAPEQYLWIHRRFKTRPVGESSLY 305
Cdd:PRK08025 241 MVRKADYSGYRLFITPEMEGYPTDENQAAAYMNKIIEKEIMRAPEQYLWIHRRFKTRPVGESSLY 305
|
|
| lipid_A_htrB |
TIGR02207 |
lipid A biosynthesis lauroyl (or palmitoleoyl) acyltransferase; This model represents a narrow ... |
5-305 |
0e+00 |
|
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: 535.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 5 CKFSREFLHPRYWLTWFGLGVLWLWVQLPYPVLCFLGTRIGAMARPFLKRRESIARKNLELCFPQHSAEEREKMIAENFR 84
Cdd:TIGR02207 1 PEFSASLLHPRYWPTWLGLGVLWLIVQLPYPVLLALGRGIGRLAMRLMKRRVHIARRNLELCFPHMSDAERERLLRENFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 85 SLGMALVETGMAWFWPDSRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLCQPMMATYRPHNNQLMEWV 164
Cdd:TIGR02207 81 STGMALFETGMAWFWSDARIKKWMQIEGLEHLQRAQKQGRGVLLVGVHFLTLELGARIFGQQQPGIGVYRPHNNPLFDWI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 165 QTRGRMRSNKAMIGRNNLRGIVGALKKGEAVWFAPDQDYGRKGSSFAPFFAVENVATTNGTYVLSRLSGAAMLTVTMVRK 244
Cdd:TIGR02207 161 QTRGRLRSNKAMIDRKDLRGMIKALKNGERIWYAPDHDYGRKSSVFVPFFAVPDAATTTGTSILARLSKCAVVPFTPRRN 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90111426 245 ADYSGYRLFITPEMEGYPT-DENQAAAYMNKIIEKEIMRAPEQYLWIHRRFKTRP-VGESSLY 305
Cdd:TIGR02207 241 EDGSGYRLKIDPPLDDFPGdDEIAAAARMNKIVEKMIMRAPEQYMWLHRRFKTRPdEGESSLY 303
|
|
| Lip_A_acyltrans |
pfam03279 |
Bacterial lipid A biosynthesis acyltransferase; |
5-296 |
9.18e-141 |
|
Bacterial lipid A biosynthesis acyltransferase;
Pssm-ID: 281296 [Multi-domain] Cd Length: 294 Bit Score: 399.03 E-value: 9.18e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 5 CKFSREFLHPRYWLTWFGLGVLWLWVQLPYPVLCFLGTRIGAMARPFLKRRESIARKNLELCFPQHSAEEREKMIAENFR 84
Cdd:pfam03279 1 PKFSPELLHPRYWLDWLGIAVLRLLALLPYSALRRIGKGLGRLAGRFLKRRRKIARRNLALCFPEMSEAEREQIIDKSFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 85 SLGMALVETGMAWFWPDSRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLCQPMMATYRP-HNNQLMEW 163
Cdd:pfam03279 81 SVGRAIVETGRVWFWPDSRIAKRFEVIGLEHIKEALAQGRGAILVGPHFGNWDLGGRVLGQQYPGMAVYRPnLKNPLLDW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 164 VQTRGRMRSNKAMIGRNN-LRGIVGALKKGEAVWFAPDQDYGRKGSSFAPFFAVENVATTNGTYVLSRlSGAAMLTVTMV 242
Cdd:pfam03279 161 LQTSGRERFGGRMLPRQNgIKGLIKALRKGEVVWYLPDQDLGRKDSVFVPFFGVPAATTTGPAKLALK-TKAAVIPVFPI 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 90111426 243 RKADYSGYRLFITPEMEGYPT-DENQAAAYMNKIIEKEIMRAPEQYLWIHRRFKT 296
Cdd:pfam03279 240 RNGDGSGYTVIVHPALDLTITdDVEQIAQAMNQIVEKFIMPAPEQYFWLHRRWKT 294
|
|
| LpxP |
COG1560 |
Palmitoleoyl-ACP: Kdo2-lipid-IV acyltransferase (lipid A biosynthesis) [Lipid transport and ... |
25-294 |
7.28e-109 |
|
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: 317.13 E-value: 7.28e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 25 VLWLWVQLPYPVLCFLGTRIGAMARPFLKRRESIARKNLELCFPQHSAEEREKMIAENFRSLGMALVETGMAWFWPDSRV 104
Cdd:COG1560 1 LLRLLRLLPLRLLYRLGDLLGRLLYRLAGRRRRVARRNLALAFPELSEAEREALARASFRNLGRTLLETLRLWRLSPERL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 105 RKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLC-QPMMATYRPHNNQLMEWVQTRGRMRSNKAMIGRNN-L 182
Cdd:COG1560 81 RKRVEVEGLEHLEAALAEGRGVILLTPHFGNWELAGAALALRgYPVTAVYRPLKNPLLDRLIRRGRERFGGELIPRKDgV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 183 RGIVGALKKGEAVWFAPDQDYGRKGSSFAPFFAVEnVATTNGTYVLSRLSGAAMLTVTMVRKADYSGYRLFITPEMEGYP 262
Cdd:COG1560 161 RALLRALRKGGIVGLLPDQDPGRKSGVFVPFFGVP-AATPTGPARLARRTGAPVVPVFARRLPDGRGYRLEIEPPLEDFS 239
|
250 260 270
....*....|....*....|....*....|..
gi 90111426 263 TDENQAAAYMNKIIEKEIMRAPEQYLWIHRRF 294
Cdd:COG1560 240 EDVEADTQRLNRALEAWIREHPEQWLWLHRRW 271
|
|
| LPLAT_LABLAT-like |
cd07984 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LABLAT-like; ... |
105-295 |
1.06e-64 |
|
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: 201.67 E-value: 1.06e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 105 RKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLC-QPMMATYRPHNNQLMEWVQTRGRMRSNKAMIGRNN-L 182
Cdd:cd07984 1 LKRVEREGLEHLEAALAKGKGVILLTAHFGNWELAGLALALLgYPVTVVYRPLKNPLLDRLITRGRERFGARLIPRGGgL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 183 RGIVGALKKGEAVWFAPDQDYGRKGSSFAPFFAVEnVATTNGTYVLSRLSGAAMLTVTMVRKaDYSGYRLFITPEMEGYP 262
Cdd:cd07984 81 RELIRALKKGEIVGILPDQDPGRKGGVFVPFFGRP-AATPTGPARLALKTGAPVVPAFAYRL-PGGGYRIEFEPPLENPP 158
|
170 180 190
....*....|....*....|....*....|....
gi 90111426 263 T-DENQAAAYMNKIIEKEIMRAPEQYLWIHRRFK 295
Cdd:cd07984 159 SeDVEEDTQRLNDALEAAIREHPEQWLWFHRRWK 192
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08025 |
PRK08025 |
kdo(2)-lipid IV(A) palmitoleoyltransferase; |
1-305 |
0e+00 |
|
kdo(2)-lipid IV(A) palmitoleoyltransferase;
Pssm-ID: 181200 Cd Length: 305 Bit Score: 643.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 1 MFPQCKFSREFLHPRYWLTWFGLGVLWLWVQLPYPVLCFLGTRIGAMARPFLKRRESIARKNLELCFPQHSAEEREKMIA 80
Cdd:PRK08025 1 MFPQQKFSREFLHPRYWLTWFGLGVLWLLVQLPYPVLCFLGTRIGRMSRPFLKRRESIARKNLELCFPQMSAEEREKMIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 81 ENFRSLGMALVETGMAWFWPDSRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLCQPMMATYRPHNNQL 160
Cdd:PRK08025 81 ENFRSLGMALLETGMAWFWPDSRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLCQPMMATYRPHNNKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 161 MEWVQTRGRMRSNKAMIGRNNLRGIVGALKKGEAVWFAPDQDYGRKGSSFAPFFAVENVATTNGTYVLSRLSGAAMLTVT 240
Cdd:PRK08025 161 MEWVQTRGRMRSNKAMIGRNNLRGIVGALKKGEAVWFAPDQDYGPKGSSFAPFFAVENVATTNGTYVLSRLSGAAMLTVT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111426 241 MVRKADYSGYRLFITPEMEGYPTDENQAAAYMNKIIEKEIMRAPEQYLWIHRRFKTRPVGESSLY 305
Cdd:PRK08025 241 MVRKADYSGYRLFITPEMEGYPTDENQAAAYMNKIIEKEIMRAPEQYLWIHRRFKTRPVGESSLY 305
|
|
| lipid_A_htrB |
TIGR02207 |
lipid A biosynthesis lauroyl (or palmitoleoyl) acyltransferase; This model represents a narrow ... |
5-305 |
0e+00 |
|
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: 535.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 5 CKFSREFLHPRYWLTWFGLGVLWLWVQLPYPVLCFLGTRIGAMARPFLKRRESIARKNLELCFPQHSAEEREKMIAENFR 84
Cdd:TIGR02207 1 PEFSASLLHPRYWPTWLGLGVLWLIVQLPYPVLLALGRGIGRLAMRLMKRRVHIARRNLELCFPHMSDAERERLLRENFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 85 SLGMALVETGMAWFWPDSRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLCQPMMATYRPHNNQLMEWV 164
Cdd:TIGR02207 81 STGMALFETGMAWFWSDARIKKWMQIEGLEHLQRAQKQGRGVLLVGVHFLTLELGARIFGQQQPGIGVYRPHNNPLFDWI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 165 QTRGRMRSNKAMIGRNNLRGIVGALKKGEAVWFAPDQDYGRKGSSFAPFFAVENVATTNGTYVLSRLSGAAMLTVTMVRK 244
Cdd:TIGR02207 161 QTRGRLRSNKAMIDRKDLRGMIKALKNGERIWYAPDHDYGRKSSVFVPFFAVPDAATTTGTSILARLSKCAVVPFTPRRN 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90111426 245 ADYSGYRLFITPEMEGYPT-DENQAAAYMNKIIEKEIMRAPEQYLWIHRRFKTRP-VGESSLY 305
Cdd:TIGR02207 241 EDGSGYRLKIDPPLDDFPGdDEIAAAARMNKIVEKMIMRAPEQYMWLHRRFKTRPdEGESSLY 303
|
|
| PRK06860 |
PRK06860 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
1-305 |
2.30e-165 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 235880 [Multi-domain] Cd Length: 309 Bit Score: 461.69 E-value: 2.30e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 1 MFPQCKFSREFLHPRYWLTWFGLGVLWLWVQLPYPVLCFLGTRIGAMARPFLKRRESIARKNLELCFPQHSAEEREKMIA 80
Cdd:PRK06860 3 MTNLPKFSRALLHPRYWLTWLGIGLLWLIVLLPYPVLYKLGRGLGKLALRFMKRRAKIARRNLELCFPEMSEQEREAIVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 81 ENFRSLGMALVETGMAWFWPDSRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLCQPMMATYRPHNNQL 160
Cdd:PRK06860 83 KNFESVGMALIETGMAWFWPDWRIKRWTEVEGLEHIREVQAQGRGVLLVGVHFLTLELGARIFGMHNPGIGVYRPNDNPL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 161 MEWVQTRGRMRSNKAMIGRNNLRGIVGALKKGEAVWFAPDQDYGRKGSSFAPFFAVENVATTNGTYVLSRLSGAAMLTVT 240
Cdd:PRK06860 163 YDWLQTWGRLRSNKSMLDRKDLKGMIKALKKGERIWYAPDHDYGPRSSVFVPFFAVEQAATTTGTWMLARMSKAAVIPFV 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90111426 241 MVRKADYSGYRLFITPEMEGYP-TDENQAAAYMNKIIEKEIMRAPEQYLWIHRRFKTRPVGESSLY 305
Cdd:PRK06860 243 PRRKPDGKGYELIILPPEDSPPlDDAEATAAWMNKVVEKCILMAPEQYMWLHRRFKTRPEGVPSRY 308
|
|
| Lip_A_acyltrans |
pfam03279 |
Bacterial lipid A biosynthesis acyltransferase; |
5-296 |
9.18e-141 |
|
Bacterial lipid A biosynthesis acyltransferase;
Pssm-ID: 281296 [Multi-domain] Cd Length: 294 Bit Score: 399.03 E-value: 9.18e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 5 CKFSREFLHPRYWLTWFGLGVLWLWVQLPYPVLCFLGTRIGAMARPFLKRRESIARKNLELCFPQHSAEEREKMIAENFR 84
Cdd:pfam03279 1 PKFSPELLHPRYWLDWLGIAVLRLLALLPYSALRRIGKGLGRLAGRFLKRRRKIARRNLALCFPEMSEAEREQIIDKSFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 85 SLGMALVETGMAWFWPDSRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLCQPMMATYRP-HNNQLMEW 163
Cdd:pfam03279 81 SVGRAIVETGRVWFWPDSRIAKRFEVIGLEHIKEALAQGRGAILVGPHFGNWDLGGRVLGQQYPGMAVYRPnLKNPLLDW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 164 VQTRGRMRSNKAMIGRNN-LRGIVGALKKGEAVWFAPDQDYGRKGSSFAPFFAVENVATTNGTYVLSRlSGAAMLTVTMV 242
Cdd:pfam03279 161 LQTSGRERFGGRMLPRQNgIKGLIKALRKGEVVWYLPDQDLGRKDSVFVPFFGVPAATTTGPAKLALK-TKAAVIPVFPI 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 90111426 243 RKADYSGYRLFITPEMEGYPT-DENQAAAYMNKIIEKEIMRAPEQYLWIHRRFKT 296
Cdd:pfam03279 240 RNGDGSGYTVIVHPALDLTITdDVEQIAQAMNQIVEKFIMPAPEQYFWLHRRWKT 294
|
|
| LpxP |
COG1560 |
Palmitoleoyl-ACP: Kdo2-lipid-IV acyltransferase (lipid A biosynthesis) [Lipid transport and ... |
25-294 |
7.28e-109 |
|
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: 317.13 E-value: 7.28e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 25 VLWLWVQLPYPVLCFLGTRIGAMARPFLKRRESIARKNLELCFPQHSAEEREKMIAENFRSLGMALVETGMAWFWPDSRV 104
Cdd:COG1560 1 LLRLLRLLPLRLLYRLGDLLGRLLYRLAGRRRRVARRNLALAFPELSEAEREALARASFRNLGRTLLETLRLWRLSPERL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 105 RKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLC-QPMMATYRPHNNQLMEWVQTRGRMRSNKAMIGRNN-L 182
Cdd:COG1560 81 RKRVEVEGLEHLEAALAEGRGVILLTPHFGNWELAGAALALRgYPVTAVYRPLKNPLLDRLIRRGRERFGGELIPRKDgV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 183 RGIVGALKKGEAVWFAPDQDYGRKGSSFAPFFAVEnVATTNGTYVLSRLSGAAMLTVTMVRKADYSGYRLFITPEMEGYP 262
Cdd:COG1560 161 RALLRALRKGGIVGLLPDQDPGRKSGVFVPFFGVP-AATPTGPARLARRTGAPVVPVFARRLPDGRGYRLEIEPPLEDFS 239
|
250 260 270
....*....|....*....|....*....|..
gi 90111426 263 TDENQAAAYMNKIIEKEIMRAPEQYLWIHRRF 294
Cdd:COG1560 240 EDVEADTQRLNRALEAWIREHPEQWLWLHRRW 271
|
|
| PRK05646 |
PRK05646 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
6-305 |
8.73e-109 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 235543 [Multi-domain] Cd Length: 310 Bit Score: 318.30 E-value: 8.73e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 6 KFSREFLHPRYWLTWFGLGVLWLWVQLPYPVLCFLGTRIGAMARPFLKRRESIARKNLELCFPQHSAEEREKMIAENFRS 85
Cdd:PRK05646 5 RFRAAFLHPRFWPLWLGLGLLWLVVQLPYRVLLWLGRALGALMYRLAGSRRRIAARNLELCFPEKSAAERERLLKENFAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 86 LGMALVETGMAWFWPDSRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLCQPMMATYRPHNNQLMEWVQ 165
Cdd:PRK05646 85 TGIAFFEMAMSWWWPKARLARLAHIEGLEHLQQAQQEGQGVILMALHFTTLEIGAALLGQQHTIDGMYREHKNPVFDFIQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 166 TRGRMRSNK--AMIGRNNLRGIVGALKKGEAVWFAPDQDYGRKGSSFAPFFAVEnVATTNGTYVLSRLSGAAMLTVTMVR 243
Cdd:PRK05646 165 RRGRERHNLdsTAIEREDVRGMLKLLRAGRAIWYAPDQDYGAKQSIFVPLFGIP-AATVTATTKFARLGRARVIPFTQKR 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90111426 244 KADYSGYRLFITPEMEGYPTDENQAAAY-MNKIIEKEIMRAPEQYLWIHRRFKTRPVGESSLY 305
Cdd:PRK05646 244 LADGSGYRLVIHPPLEDFPGESEEADCLrINQWVERVVRECPEQYLWAHRRFKSRPEGEPKLY 306
|
|
| PRK08733 |
PRK08733 |
LpxL/LpxP family Kdo(2)-lipid IV(A) lauroyl/palmitoleoyl acyltransferase; |
12-305 |
3.32e-72 |
|
LpxL/LpxP family Kdo(2)-lipid IV(A) lauroyl/palmitoleoyl acyltransferase;
Pssm-ID: 181542 [Multi-domain] Cd Length: 306 Bit Score: 225.17 E-value: 3.32e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 12 LHPRYWLTWFGLGVLWLWVQLPYPVLCFLGTRIGAMARPFLKRRESIARKNLELCFPQHSAEEREKMIAENFRSLGMALV 91
Cdd:PRK08733 14 RNPKHWPMYLGLAVMVLAARLPWTLQRALGRGVGWVAMRLAGTRRRAAEVNLKLCFPEQDDAWRARLLRDSFDALGVGLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 92 ETGMAWFWPDSRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVmgLCQ--PMMATYRPHNNQLMEWVQTRGR 169
Cdd:PRK08733 94 EFARAWWGSIDVIRPGVQIEGLEHLQQLQQQGRGVLLVSGHFMTLEMCGRL--LCDhvPLAGMYRRHRNPVFEWAVKRGR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 170 MRSNKAMIGRNNLRGIVGALKKGEAVWFAPDQDYGRKGSSFAPFFAVEnVATTNGTYVLSRLSGAAMltVTMVRKADYSG 249
Cdd:PRK08733 172 LRYATHMFANEDLRATIKHLKRGGFLWYAPDQDMRGKDTVFVPFFGHP-ASTITATHQLARLTGCAV--VPYFHRREGGR 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 90111426 250 YRLFITPEMEGYPTDENQA-AAYMNKIIEKEIMRAPEQYLWIHRRFKTRPVGESSLY 305
Cdd:PRK08733 249 YVLKIAPPLADFPSDDVIAdTTRVNAAIEDMVREAPDQYLWIHRRFKRQPGGRSDFY 305
|
|
| PRK06946 |
PRK06946 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
19-305 |
7.30e-65 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 180770 [Multi-domain] Cd Length: 293 Bit Score: 205.69 E-value: 7.30e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 19 TWFGLGVLWLWVQLPYPVLCFLGTRIGAMARPFLKRRESIARKNLELCFPQHSAEEREKMIAENFRSLGMALVETGMAWF 98
Cdd:PRK06946 6 TALAIGLLKLLAFLPYGLTARFGDGLGWLLYRIPSRRRRIVHTNLKLCFPDWSDARREELARRHFRHVIRSYVERSVQWF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 99 WPDSRVRKWFDVEGLDNLKRAQMQNRgvMVVGVHFMSLELGG--RVMGLCQPMMATYRPHNNQLMEWVQTRGRMRSNKAM 176
Cdd:PRK06946 86 GSEKKLEKLVQVDSAIDLTDPDGPPT--IFLGLHFVGIEAGSiwLNYSLRRRVGSLYTPMSNPLLDAIAKAARGRFGAEM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 177 IGRN-NLRGIVGALKKGEAVWFAPDQDYGRKGSSFAPFFAVEnVATTNGTYVLSRLSGAAMLTVTMVRKADYSGYRLFIT 255
Cdd:PRK06946 164 VSRAdSARQVLRWLRDGKPVMLGADMDFGLRDSTFVPFFGVP-ACTLTAVSRLARTGGAQVVPFITEVLPDYKGYRLRVF 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 90111426 256 PEMEGYPTDENQA-AAYMNKIIEKEIMRAPEQYLWIHRRFKTRPVGESSLY 305
Cdd:PRK06946 243 KPWENYPTGDDDLdARRMNAFLEEQIRLMPEQYYWVHKRFKTRPPGEPSVY 293
|
|
| LPLAT_LABLAT-like |
cd07984 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LABLAT-like; ... |
105-295 |
1.06e-64 |
|
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: 201.67 E-value: 1.06e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 105 RKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLC-QPMMATYRPHNNQLMEWVQTRGRMRSNKAMIGRNN-L 182
Cdd:cd07984 1 LKRVEREGLEHLEAALAKGKGVILLTAHFGNWELAGLALALLgYPVTVVYRPLKNPLLDRLITRGRERFGARLIPRGGgL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 183 RGIVGALKKGEAVWFAPDQDYGRKGSSFAPFFAVEnVATTNGTYVLSRLSGAAMLTVTMVRKaDYSGYRLFITPEMEGYP 262
Cdd:cd07984 81 RELIRALKKGEIVGILPDQDPGRKGGVFVPFFGRP-AATPTGPARLALKTGAPVVPAFAYRL-PGGGYRIEFEPPLENPP 158
|
170 180 190
....*....|....*....|....*....|....
gi 90111426 263 T-DENQAAAYMNKIIEKEIMRAPEQYLWIHRRFK 295
Cdd:cd07984 159 SeDVEEDTQRLNDALEAAIREHPEQWLWFHRRWK 192
|
|
| lipid_A_msbB |
TIGR02208 |
lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; This family consists of MsbB ... |
6-305 |
1.65e-56 |
|
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: 184.62 E-value: 1.65e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 6 KFSREFLHPRYWLTWFGLGVLWLWVQLPY----PVLCFLGTRIGAMArpflKRRESIARKNLELCFPQHSAEEREKMIAE 81
Cdd:TIGR02208 4 RFQKSFLHPKYWGTWLGVFALVLLAFMPAklrdPIAKVLAKFVGPIA----KKPRGRARINLSACFPEKSEAERETIIDN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 82 NFRSLGMALVETGMAWFWPDSRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGG-RVMGLCQPMMATYRPHNNQL 160
Cdd:TIGR02208 80 NFATFVQVMLSQAELAIRSKAHLRRRVNLMGLEHIEAAQAAGKPVIFLVPHGWAIDYAGlRLASQGLPMVTMFNNHKNPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 161 MEWVQTRGRMRSNKAMIGRNN-LRGIVGALKKGEAVWFAPDQDYGRKGSSFAPFFAVENvATTNGTYVLSRLSGAAMLTV 239
Cdd:TIGR02208 160 FDWLWNRVRSRFGGHVYAREAgIKALLASLKRGESGYYLPDEDHGPEQSVFVPFFATYK-ATLPVVGRLAKAGNAQVVPV 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90111426 240 TMVRKADYSGYRLFITPEMEGYPT-DENQAAAYMNKIIEKEIMRAPEQYLWIHRRFKTRPVGESSLY 305
Cdd:TIGR02208 239 FPGYNQVTGKFELTVRPAMATELSvDPEQEARAMNKEVEQFILPYPEQYMWILRLLKTRPDGEASIY 305
|
|
| PRK08943 |
PRK08943 |
lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; Validated |
6-301 |
3.43e-55 |
|
lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; Validated
Pssm-ID: 236355 Cd Length: 314 Bit Score: 181.61 E-value: 3.43e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 6 KFSREFLHPRYWLTWFGLGVLWLWVQLPY----PVLCFLGTRIGAMARPFLKRresiARKNLELCFPQHSAEEREKMIAE 81
Cdd:PRK08943 13 RFQKSFLHPRYWGTWLGIGALAGLALMPPrlrdPLAAKLGRLVGKLAKKARRR----ARINLSLCFPEKSEAEREAIIDE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 82 NFRSLGMALVETGMAWFWPDSRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGL-CQPMMATYRPHNNQL 160
Cdd:PRK08943 89 MFATAPQAMLMMAELALRSPKHLQRRVEWHGLEILEEARANGENVIFLVPHGWAIDIPAMLLASqGQPMAAMFHNQRNPL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 161 MEWVQTRGRMRSNKAMIGRNNlrGI---VGALKKGEAVWFAPDQDYGRKGSSFAPFFAVENvATTNGTYVLSRLSGAAML 237
Cdd:PRK08943 169 FDWLWNRVRRRFGGRLHARED--GIkpfISSVRQGYWGYYLPDEDHGPEHSVFVDFFATYK-ATLPGIGRLAKVCRARVV 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111426 238 TVTMVRKADYSGYRLFITPEMEGYPT-DENQAAAYMNKIIEKEIMRAPEQYLWIHRRFKTRPVGE 301
Cdd:PRK08943 246 PLFPVYNGKTHRLDIEIRPPMDDLLSaDDETIARRMNEEVEQFVGPHPEQYMWILKLLKTRKPGE 310
|
|
| PRK08706 |
PRK08706 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
21-305 |
1.98e-48 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 169557 [Multi-domain] Cd Length: 289 Bit Score: 163.11 E-value: 1.98e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 21 FGLGVLWLWVQLPYPVLCFLGTRIGAMARPFLKRRESIARKNLELCFPQHSAEEREKMIAENFRSLGMALVETGMAWFWP 100
Cdd:PRK08706 3 FIFFVLYVLQFLPFALLHKLADLTGLLAYLLVKPRRRIGEINLAKCFPEWDEEKRKTVLKQHFKHMAKLMLEYGLYWYAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 101 DSRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGgrVMGLCQ--PMMATYRPHNNQLMEWVQTRGRMR-SNKAMI 177
Cdd:PRK08706 83 AGRLKSLVRYRNKHYLDDALAAGEKVIILYPHFTAFEMA--VYALNQdvPLISMYSHQKNKILDEQILKGRNRyHNVFLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 178 GRNN-LRGIVGALKKGEAVW-FAPDQDYGRKGSSFAPFFAVEnVATTNGTYVLSRLSGAAMLTVTMVRKADYSgYRLFIT 255
Cdd:PRK08706 161 GRTEgLRALVKQFRKSSAPFlYLPDQDFGRNDSVFVDFFGIQ-TATITGLSRIAALANAKVIPAIPVREADNT-VTLHFY 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 90111426 256 PEMEGYPTDENQA-AAYMNKIIEKEIMRAPEQYLWIHRRFKTRPVGESSLY 305
Cdd:PRK08706 239 PAWDSFPSEDAQAdAQRMNRFIEERVREHPEQYFWLHKRFKTRPEGSPDFY 289
|
|
| PRK05645 |
PRK05645 |
lysophospholipid acyltransferase; |
23-305 |
3.84e-36 |
|
lysophospholipid acyltransferase;
Pssm-ID: 135493 [Multi-domain] Cd Length: 295 Bit Score: 131.57 E-value: 3.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 23 LGVLWLWVQLPYPVLCFLGTRIGAMARPFLKRRESIARKNLELCFPQHSAEEREKMIAENFRSLGMALVETGMAWFWPDS 102
Cdd:PRK05645 10 VGALRLFALLPWRAVQGVGAGIGWLMWKLPNRSREVVRINLSKCFPELSPAELEKLVGQSLMDIGKTLTESACAWIWPPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 103 RVRKWF-DVEGLDNLKRAQMQNRGVMVVGVHFMSLE-LGGRVMGLCQPMMaTYRPHN----NQLMEwvQTRGRMRSNKAM 176
Cdd:PRK05645 90 KSLELVrEVEGLEVLEQALASGKGVVGITSHLGNWEvLNHFYCSQCKPII-FYRPPKlkavDELLR--KQRVQLGNRVAP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 177 IGRNNLRGIVGALKKGEAVWFAPDQDYGRKGSSFAPFFAVENVATtngTYVLSRLSGAAMLTVTM--VRKADYSGYRLFI 254
Cdd:PRK05645 167 STKEGILSVIKEVRKGGQVGIPADPEPAESAGIFVPFLGTQALTS---KFVPNMLAGGKAVGVFLhaLRLPDGSGYKVIL 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 90111426 255 TPEMEG-YPTDENQAAAYMNKIIEKEIMRAPEQYLWIHRRFKTRPVGESSLY 305
Cdd:PRK05645 244 EAAPEDmYSTDVEVSAAAMSKVVERYVRAYPSQYMWSMKRFKKRPAGEARWY 295
|
|
| PRK08905 |
PRK08905 |
lysophospholipid acyltransferase family protein; |
25-300 |
2.00e-34 |
|
lysophospholipid acyltransferase family protein;
Pssm-ID: 236348 [Multi-domain] Cd Length: 289 Bit Score: 126.64 E-value: 2.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 25 VLWLWVQLPYPVLCFLGTRIGAMARPFLKRRESIARKNLELCFPQhsaeEREKMIAENFRSLGMALVEtgMAWFW---PD 101
Cdd:PRK08905 5 LFRLLSRLPLSWLHALGGWLGRLAYRLPGRYRRRLRANLRQAGGD----PDPAMVKAAAAETGRMILE--LPYVWfrkPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 102 SRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLCQPMMATYRPHNNQ----LMEWVQTRGRMRSNKAMI 177
Cdd:PRK08905 79 EIETMVKDDHGWEHVEAALAEGRGILFLTPHLGCFEVTARYIAQRFPLTAMFRPPRKAalrpLMEAGRARGNMRTAPATP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 178 grNNLRGIVGALKKGEAVWFAPDQDYGRKGSSFAPFFAveNVATTNgTYV--LSRLSGAAMLTVTMVRKADYSGYRLFIT 255
Cdd:PRK08905 159 --QGVRMLVKALRRGEAVGILPDQVPSGGEGVWAPFFG--RPAYTM-TLVarLAEVTGVPVIFVAGERLPRGRGYRLHLR 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 90111426 256 PEMEGYPTDENQAAAYMNKIIEKEIMRAPEQYLWIHRRFKtRPVG 300
Cdd:PRK08905 234 PVQEPLPGDKAADAAVINAEIERLIRRFPTQYLWGYNRYK-RPRG 277
|
|
| PRK08419 |
PRK08419 |
lipid A biosynthesis lauroyl acyltransferase; Reviewed |
32-295 |
1.23e-23 |
|
lipid A biosynthesis lauroyl acyltransferase; Reviewed
Pssm-ID: 181420 [Multi-domain] Cd Length: 298 Bit Score: 97.79 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 32 LPYPVLCFLGTRIGAMARPFLKRRESIARKNLELCFPQH-SAEEREKMIAENFRSLGMALVETGMAWFWPDSRVRKWFDV 110
Cdd:PRK08419 20 MPHCIFLRLAKALAFIMRYLDKKRRKIAKANLDFCFGESkSQEEKKRIIKKCYENFAFFGLDFIRNQNTTKEEILNKVTF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 111 EGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGL-CQPMMATYRPHNNQLM-EWVQTRgRMRSNKAMIGRNN-LRGIVG 187
Cdd:PRK08419 100 INEENLLDALKKKRPIIVTTAHYGYWELFSLALAAyYGAVSIVGRLLKSAPInEMISKR-REQFGIELIDKKGaMKELLK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 188 ALKKGEAVWFAPDQDYGRKGSSFAPFFAVEnVATTNGTYVLSRLSGAAMLTVtMVRKADYSGYRLFITPEMEGYPTDENQ 267
Cdd:PRK08419 179 ALKQGRALGILVDQNVVPKEGVEVKFFNKR-VTHTTIASILARRYNALIIPV-FIFNDDYSHFTITFFPPIRSKITDDAE 256
|
250 260 270
....*....|....*....|....*....|...
gi 90111426 268 AA-----AYMNKIIEKEIMRAPEQYLWIHRRFK 295
Cdd:PRK08419 257 ADileatQAQASACEEMIRKKPDEYFWFHRRFK 289
|
|
| PRK08734 |
PRK08734 |
lauroyl acyltransferase; |
31-300 |
3.10e-21 |
|
lauroyl acyltransferase;
Pssm-ID: 181543 [Multi-domain] Cd Length: 305 Bit Score: 91.48 E-value: 3.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 31 QLPYPVLCFLGTRIGAMARPFLKRRESIARKNLELCFPQHSAEEREKMIAENFRSLGMALVETGMAWFWPDSR-VRKWFD 109
Cdd:PRK08734 19 RLPWPLLKRLADLLAWSWRKLNARESRVTRRNLELAYPELSPQQRAQLHAQILRSTARQALEVLRTWTHPPAEnLARLRQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 110 VEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLCQPMMATYRPHNNQLMEWVQTRGRMRSNKAMIGRNN--LRGIVG 187
Cdd:PRK08734 99 RHGQELYDAALASGRGVIVAAPHFGNWELLNQWLSERGPIAIVYRPPESEAVDGFLQLVRGGDNVRQVRAEGpaVRQLFK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 188 ALKKGEAVWFAPDQDYGRKGSSFAPFFAVENVATTngtyVLSRL---SGAAMLTVTMVRKADYSGYRLFITPEMEGYP-T 263
Cdd:PRK08734 179 VLKDGGAVGILPDQQPKMGDGVFAPFFGIPALTMT----LVNRLaerTGATVLYGWCERIGPDLEFALHVQPADPAVAdP 254
|
250 260 270
....*....|....*....|....*....|....*..
gi 90111426 264 DENQAAAYMNKIIEKEIMRAPEQYLWIHRRFKTRPVG 300
Cdd:PRK08734 255 DPLRAATALNAGIERIARRDPAQYQWTYKRYTLRPPG 291
|
|
| PRK05906 |
PRK05906 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
13-295 |
3.66e-08 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 168292 [Multi-domain] Cd Length: 454 Bit Score: 54.40 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 13 HPRYWLtwfGLGVLWLWVQLPYPVLCFLGTRIGAMARPFLKRRESIARKNLELCFPQHSAEEREK---------MI---- 79
Cdd:PRK05906 15 HLVYYL---GLGVITILRLLPRSSLRLFGKGLGTLLFYFISDYRKTALTNLALAFPEKSFAERYQiarqsvqhvIItfle 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 80 -------AENFRSL-GMALVETGMAWFWPDSRVRKwfdvEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLCQPMMA 151
Cdd:PRK05906 92 llaveklAGHIDELiAIATSEDAPEGFFPEEVSSQ----QELEHTFSRLDEQEGAILFCGHQANWELPFLYITKRYPGLA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 152 TYRPHNNQlmewvqtrgrmRSNKAMIG-RNNLRG-IVG----------ALKKGEAVWFAPDQdyGRKGSSFA-PFFAVEN 218
Cdd:PRK05906 168 FAKPIKNR-----------RLNKKIFSlRESFKGkIVPpknginqalrALHQGEVVGIVGDQ--ALLSSSYSyPLFGSQA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 219 VATTNGTyVLSRLSGAAMLTVTMVRKADysGYRlfITPEMEGYPTDE----NQAAAYMNKI---IEKEIMRAPEQYLWIH 291
Cdd:PRK05906 235 FTTTSPA-LLAYKTGKPVIAVAIYRKPN--GYL--VVPSKKFYANKSlpikESTEQLMDRLmrfLEKGIACKPEQWMWLH 309
|
....
gi 90111426 292 RRFK 295
Cdd:PRK05906 310 KRWK 313
|
|
| PRK06628 |
PRK06628 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
58-295 |
9.55e-08 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 102471 Cd Length: 290 Bit Score: 52.24 E-value: 9.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 58 IARKNLELCFpqHSAEEREKMIAENFRSLGMALVETGMAWFWPDSRVRKWFDVEGLDNLKRaqMQNRGVMVVGVHFMSLE 137
Cdd:PRK06628 52 IARRNIKAVF--GDMCDVEKIIDQTWDNFGRFIGEFTYVNKMDEAELERRIEIIGIENIKK--LEGQPFLLFSGHFANWD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 138 LGGRVMGLCQPMMAT-YRPHNNQLMEWVQTRGRMRSNKAMI--GRNNLRGIVGALKKGEAVWFAPDQDYgrKGSSFAPFF 214
Cdd:PRK06628 128 ISLKILHKFYPKVAViYRKANNPYVNKLVNESRAGDKLRLIpkGPEGSRALVRAIKESESIVMLVDQKM--NDGIEVPFL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 215 AVENVaTTNGTYVLSRLSGAAMLTVTMVR-KADYsgYRLFITPEMEGYPTDENQAAAY-----MNKIIEKEIMRAPEQYL 288
Cdd:PRK06628 206 GHPAM-TASAIAKIALQYKYPIIPCQIIRtKGSY--FKVIVHPQLKFEQTGDNKADCYnimlnINQMLGEWVKQNPAQWF 282
|
....*..
gi 90111426 289 WIHRRFK 295
Cdd:PRK06628 283 WFHNRWK 289
|
|
| PRK06553 |
PRK06553 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
15-293 |
4.64e-06 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 235827 [Multi-domain] Cd Length: 308 Bit Score: 47.28 E-value: 4.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 15 RYWLT-WFGLGVLWLWVQLPYPVLCFLGTRIGAMARPFLkRRESIARKNLELCFPQHSAEEREKMIAENFRSLGMALVE- 92
Cdd:PRK06553 20 AGWLVaQLVFGLLGLLRLFPADKAINFFGRLARLIGPLL-PRHRVALDNLRAAFPEKSEAEIEAIALGMWDNLGRLGAEy 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 93 --TGMAW-FWPDSRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLEL---GGRVMGLcqPMMATYRPHNNQLM-EWVQ 165
Cdd:PRK06553 99 afLDAIFdYDPEAPEPGRVEVRGIEIFERLRDDGKPALIFTAHLGNWELlaiAAAAFGL--DVTVLFRPPNNPYAaRKVL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111426 166 trgRMRSNK--AMI--GRNNLRGIVGALKKGEAVWFAPDQDYGRKGSSfaPFFAVEnvATTNGTYV-LSRLSGAAMLTVT 240
Cdd:PRK06553 177 ---EARRTTmgGLVpsGAGAAFALAGVLERGGHVGMLVDQKFTRGVEV--TFFGRP--VKTNPLLAkLARQYDCPVHGAR 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 90111426 241 MVRKADYSgYRLFITPEMEgYPTDEN-----QAAAY-MNKIIEKEIMRAPEQYLWIHRR 293
Cdd:PRK06553 250 CIRLPGGR-FRLELTERVE-LPRDADgqidvQATMQaLTDVVEGWVREYPGQWLWLHRR 306
|
|
| |
