|
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: 642.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 1 MFPQCKFSRAFLHPRYWLTWFGVGVLWLLVQLPYPVLCFLGTRTGTLARPFLKRRESIAHKNLELCFPNLSQEERDKLVD 80
Cdd:PRK08025 1 MFPQQKFSREFLHPRYWLTWFGLGVLWLLVQLPYPVLCFLGTRIGRMSRPFLKRRESIARKNLELCFPQMSAEEREKMIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 81 ENFRSLGMALLETGMAWFWPDRRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLCQPMMATYRPHNNKL 160
Cdd:PRK08025 81 ENFRSLGMALLETGMAWFWPDSRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLCQPMMATYRPHNNKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 161 MEWIQTRGRMRSNKAMIGRNNLRGIVGALKKGEAVWFAPDQDYGRKGSSFAPFFAVKNVATTNGTYVLSRLSGAAMLTVT 240
Cdd:PRK08025 161 MEWVQTRGRMRSNKAMIGRNNLRGIVGALKKGEAVWFAPDQDYGPKGSSFAPFFAVENVATTNGTYVLSRLSGAAMLTVT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507086329 241 MVRKADNSGYRLFITPEMEGYPTDESQAAAYMNKIIEKEIMRAPEQYLWIHRRFKTRPMGEASLY 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: 517.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 5 CKFSRAFLHPRYWLTWFGVGVLWLLVQLPYPVLCFLGTRTGTLARPFLKRRESIAHKNLELCFPNLSQEERDKLVDENFR 84
Cdd:TIGR02207 1 PEFSASLLHPRYWPTWLGLGVLWLIVQLPYPVLLALGRGIGRLAMRLMKRRVHIARRNLELCFPHMSDAERERLLRENFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 85 SLGMALLETGMAWFWPDRRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLCQPMMATYRPHNNKLMEWI 164
Cdd:TIGR02207 81 STGMALFETGMAWFWSDARIKKWMQIEGLEHLQRAQKQGRGVLLVGVHFLTLELGARIFGQQQPGIGVYRPHNNPLFDWI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 165 QTRGRMRSNKAMIGRNNLRGIVGALKKGEAVWFAPDQDYGRKGSSFAPFFAVKNVATTNGTYVLSRLSGAAMLTVTMVRK 244
Cdd:TIGR02207 161 QTRGRLRSNKAMIDRKDLRGMIKALKNGERIWYAPDHDYGRKSSVFVPFFAVPDAATTTGTSILARLSKCAVVPFTPRRN 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507086329 245 ADNSGYRLFITPEMEGYPT-DESQAAAYMNKIIEKEIMRAPEQYLWIHRRFKTRPM-GEASLY 305
Cdd:TIGR02207 241 EDGSGYRLKIDPPLDDFPGdDEIAAAARMNKIVEKMIMRAPEQYMWLHRRFKTRPDeGESSLY 303
|
|
| Lip_A_acyltrans |
pfam03279 |
Bacterial lipid A biosynthesis acyltransferase; |
5-296 |
2.98e-135 |
|
Bacterial lipid A biosynthesis acyltransferase;
Pssm-ID: 281296 [Multi-domain] Cd Length: 294 Bit Score: 384.77 E-value: 2.98e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 5 CKFSRAFLHPRYWLTWFGVGVLWLLVQLPYPVLCFLGTRTGTLARPFLKRRESIAHKNLELCFPNLSQEERDKLVDENFR 84
Cdd:pfam03279 1 PKFSPELLHPRYWLDWLGIAVLRLLALLPYSALRRIGKGLGRLAGRFLKRRRKIARRNLALCFPEMSEAEREQIIDKSFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 85 SLGMALLETGMAWFWPDRRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLCQPMMATYRP-HNNKLMEW 163
Cdd:pfam03279 81 SVGRAIVETGRVWFWPDSRIAKRFEVIGLEHIKEALAQGRGAILVGPHFGNWDLGGRVLGQQYPGMAVYRPnLKNPLLDW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 164 IQTRGRMRSNKAMIGRNN-LRGIVGALKKGEAVWFAPDQDYGRKGSSFAPFFAVKNVATTNGTYVLSRlSGAAMLTVTMV 242
Cdd:pfam03279 161 LQTSGRERFGGRMLPRQNgIKGLIKALRKGEVVWYLPDQDLGRKDSVFVPFFGVPAATTTGPAKLALK-TKAAVIPVFPI 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 507086329 243 RKADNSGYRLFITPEMEGYPT-DESQAAAYMNKIIEKEIMRAPEQYLWIHRRFKT 296
Cdd:pfam03279 240 RNGDGSGYTVIVHPALDLTITdDVEQIAQAMNQIVEKFIMPAPEQYFWLHRRWKT 294
|
|
| LpxP |
COG1560 |
Palmitoleoyl-ACP: Kdo2-lipid-IV acyltransferase (lipid A biosynthesis) [Lipid transport and ... |
25-294 |
1.00e-111 |
|
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: 324.45 E-value: 1.00e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 25 VLWLLVQLPYPVLCFLGTRTGTLARPFLKRRESIAHKNLELCFPNLSQEERDKLVDENFRSLGMALLETGMAWFWPDRRV 104
Cdd:COG1560 1 LLRLLRLLPLRLLYRLGDLLGRLLYRLAGRRRRVARRNLALAFPELSEAEREALARASFRNLGRTLLETLRLWRLSPERL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 105 RKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLC-QPMMATYRPHNNKLMEWIQTRGRMRSNKAMIGRNN-L 182
Cdd:COG1560 81 RKRVEVEGLEHLEAALAEGRGVILLTPHFGNWELAGAALALRgYPVTAVYRPLKNPLLDRLIRRGRERFGGELIPRKDgV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 183 RGIVGALKKGEAVWFAPDQDYGRKGSSFAPFFAVKnVATTNGTYVLSRLSGAAMLTVTMVRKADNSGYRLFITPEMEGYP 262
Cdd:COG1560 161 RALLRALRKGGIVGLLPDQDPGRKSGVFVPFFGVP-AATPTGPARLARRTGAPVVPVFARRLPDGRGYRLEIEPPLEDFS 239
|
250 260 270
....*....|....*....|....*....|..
gi 507086329 263 TDESQAAAYMNKIIEKEIMRAPEQYLWIHRRF 294
Cdd:COG1560 240 EDVEADTQRLNRALEAWIREHPEQWLWLHRRW 271
|
|
| LPLAT_LABLAT-like |
cd07984 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LABLAT-like; ... |
105-295 |
1.69e-65 |
|
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: 203.99 E-value: 1.69e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 105 RKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLC-QPMMATYRPHNNKLMEWIQTRGRMRSNKAMIGRNN-L 182
Cdd:cd07984 1 LKRVEREGLEHLEAALAKGKGVILLTAHFGNWELAGLALALLgYPVTVVYRPLKNPLLDRLITRGRERFGARLIPRGGgL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 183 RGIVGALKKGEAVWFAPDQDYGRKGSSFAPFFAVKnVATTNGTYVLSRLSGAAMLTVTMVRKADNsGYRLFITPEMEGYP 262
Cdd:cd07984 81 RELIRALKKGEIVGILPDQDPGRKGGVFVPFFGRP-AATPTGPARLALKTGAPVVPAFAYRLPGG-GYRIEFEPPLENPP 158
|
170 180 190
....*....|....*....|....*....|....
gi 507086329 263 T-DESQAAAYMNKIIEKEIMRAPEQYLWIHRRFK 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: 642.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 1 MFPQCKFSRAFLHPRYWLTWFGVGVLWLLVQLPYPVLCFLGTRTGTLARPFLKRRESIAHKNLELCFPNLSQEERDKLVD 80
Cdd:PRK08025 1 MFPQQKFSREFLHPRYWLTWFGLGVLWLLVQLPYPVLCFLGTRIGRMSRPFLKRRESIARKNLELCFPQMSAEEREKMIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 81 ENFRSLGMALLETGMAWFWPDRRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLCQPMMATYRPHNNKL 160
Cdd:PRK08025 81 ENFRSLGMALLETGMAWFWPDSRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLCQPMMATYRPHNNKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 161 MEWIQTRGRMRSNKAMIGRNNLRGIVGALKKGEAVWFAPDQDYGRKGSSFAPFFAVKNVATTNGTYVLSRLSGAAMLTVT 240
Cdd:PRK08025 161 MEWVQTRGRMRSNKAMIGRNNLRGIVGALKKGEAVWFAPDQDYGPKGSSFAPFFAVENVATTNGTYVLSRLSGAAMLTVT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507086329 241 MVRKADNSGYRLFITPEMEGYPTDESQAAAYMNKIIEKEIMRAPEQYLWIHRRFKTRPMGEASLY 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: 517.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 5 CKFSRAFLHPRYWLTWFGVGVLWLLVQLPYPVLCFLGTRTGTLARPFLKRRESIAHKNLELCFPNLSQEERDKLVDENFR 84
Cdd:TIGR02207 1 PEFSASLLHPRYWPTWLGLGVLWLIVQLPYPVLLALGRGIGRLAMRLMKRRVHIARRNLELCFPHMSDAERERLLRENFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 85 SLGMALLETGMAWFWPDRRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLCQPMMATYRPHNNKLMEWI 164
Cdd:TIGR02207 81 STGMALFETGMAWFWSDARIKKWMQIEGLEHLQRAQKQGRGVLLVGVHFLTLELGARIFGQQQPGIGVYRPHNNPLFDWI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 165 QTRGRMRSNKAMIGRNNLRGIVGALKKGEAVWFAPDQDYGRKGSSFAPFFAVKNVATTNGTYVLSRLSGAAMLTVTMVRK 244
Cdd:TIGR02207 161 QTRGRLRSNKAMIDRKDLRGMIKALKNGERIWYAPDHDYGRKSSVFVPFFAVPDAATTTGTSILARLSKCAVVPFTPRRN 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507086329 245 ADNSGYRLFITPEMEGYPT-DESQAAAYMNKIIEKEIMRAPEQYLWIHRRFKTRPM-GEASLY 305
Cdd:TIGR02207 241 EDGSGYRLKIDPPLDDFPGdDEIAAAARMNKIVEKMIMRAPEQYMWLHRRFKTRPDeGESSLY 303
|
|
| PRK06860 |
PRK06860 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
1-305 |
2.67e-169 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 235880 [Multi-domain] Cd Length: 309 Bit Score: 471.70 E-value: 2.67e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 1 MFPQCKFSRAFLHPRYWLTWFGVGVLWLLVQLPYPVLCFLGTRTGTLARPFLKRRESIAHKNLELCFPNLSQEERDKLVD 80
Cdd:PRK06860 3 MTNLPKFSRALLHPRYWLTWLGIGLLWLIVLLPYPVLYKLGRGLGKLALRFMKRRAKIARRNLELCFPEMSEQEREAIVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 81 ENFRSLGMALLETGMAWFWPDRRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLCQPMMATYRPHNNKL 160
Cdd:PRK06860 83 KNFESVGMALIETGMAWFWPDWRIKRWTEVEGLEHIREVQAQGRGVLLVGVHFLTLELGARIFGMHNPGIGVYRPNDNPL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 161 MEWIQTRGRMRSNKAMIGRNNLRGIVGALKKGEAVWFAPDQDYGRKGSSFAPFFAVKNVATTNGTYVLSRLSGAAMLTVT 240
Cdd:PRK06860 163 YDWLQTWGRLRSNKSMLDRKDLKGMIKALKKGERIWYAPDHDYGPRSSVFVPFFAVEQAATTTGTWMLARMSKAAVIPFV 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507086329 241 MVRKADNSGYRLFITPEMEGYP-TDESQAAAYMNKIIEKEIMRAPEQYLWIHRRFKTRPMGEASLY 305
Cdd:PRK06860 243 PRRKPDGKGYELIILPPEDSPPlDDAEATAAWMNKVVEKCILMAPEQYMWLHRRFKTRPEGVPSRY 308
|
|
| Lip_A_acyltrans |
pfam03279 |
Bacterial lipid A biosynthesis acyltransferase; |
5-296 |
2.98e-135 |
|
Bacterial lipid A biosynthesis acyltransferase;
Pssm-ID: 281296 [Multi-domain] Cd Length: 294 Bit Score: 384.77 E-value: 2.98e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 5 CKFSRAFLHPRYWLTWFGVGVLWLLVQLPYPVLCFLGTRTGTLARPFLKRRESIAHKNLELCFPNLSQEERDKLVDENFR 84
Cdd:pfam03279 1 PKFSPELLHPRYWLDWLGIAVLRLLALLPYSALRRIGKGLGRLAGRFLKRRRKIARRNLALCFPEMSEAEREQIIDKSFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 85 SLGMALLETGMAWFWPDRRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLCQPMMATYRP-HNNKLMEW 163
Cdd:pfam03279 81 SVGRAIVETGRVWFWPDSRIAKRFEVIGLEHIKEALAQGRGAILVGPHFGNWDLGGRVLGQQYPGMAVYRPnLKNPLLDW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 164 IQTRGRMRSNKAMIGRNN-LRGIVGALKKGEAVWFAPDQDYGRKGSSFAPFFAVKNVATTNGTYVLSRlSGAAMLTVTMV 242
Cdd:pfam03279 161 LQTSGRERFGGRMLPRQNgIKGLIKALRKGEVVWYLPDQDLGRKDSVFVPFFGVPAATTTGPAKLALK-TKAAVIPVFPI 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 507086329 243 RKADNSGYRLFITPEMEGYPT-DESQAAAYMNKIIEKEIMRAPEQYLWIHRRFKT 296
Cdd:pfam03279 240 RNGDGSGYTVIVHPALDLTITdDVEQIAQAMNQIVEKFIMPAPEQYFWLHRRWKT 294
|
|
| LpxP |
COG1560 |
Palmitoleoyl-ACP: Kdo2-lipid-IV acyltransferase (lipid A biosynthesis) [Lipid transport and ... |
25-294 |
1.00e-111 |
|
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: 324.45 E-value: 1.00e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 25 VLWLLVQLPYPVLCFLGTRTGTLARPFLKRRESIAHKNLELCFPNLSQEERDKLVDENFRSLGMALLETGMAWFWPDRRV 104
Cdd:COG1560 1 LLRLLRLLPLRLLYRLGDLLGRLLYRLAGRRRRVARRNLALAFPELSEAEREALARASFRNLGRTLLETLRLWRLSPERL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 105 RKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLC-QPMMATYRPHNNKLMEWIQTRGRMRSNKAMIGRNN-L 182
Cdd:COG1560 81 RKRVEVEGLEHLEAALAEGRGVILLTPHFGNWELAGAALALRgYPVTAVYRPLKNPLLDRLIRRGRERFGGELIPRKDgV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 183 RGIVGALKKGEAVWFAPDQDYGRKGSSFAPFFAVKnVATTNGTYVLSRLSGAAMLTVTMVRKADNSGYRLFITPEMEGYP 262
Cdd:COG1560 161 RALLRALRKGGIVGLLPDQDPGRKSGVFVPFFGVP-AATPTGPARLARRTGAPVVPVFARRLPDGRGYRLEIEPPLEDFS 239
|
250 260 270
....*....|....*....|....*....|..
gi 507086329 263 TDESQAAAYMNKIIEKEIMRAPEQYLWIHRRF 294
Cdd:COG1560 240 EDVEADTQRLNRALEAWIREHPEQWLWLHRRW 271
|
|
| PRK05646 |
PRK05646 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
6-305 |
2.69e-109 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 235543 [Multi-domain] Cd Length: 310 Bit Score: 319.84 E-value: 2.69e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 6 KFSRAFLHPRYWLTWFGVGVLWLLVQLPYPVLCFLGTRTGTLARPFLKRRESIAHKNLELCFPNLSQEERDKLVDENFRS 85
Cdd:PRK05646 5 RFRAAFLHPRFWPLWLGLGLLWLVVQLPYRVLLWLGRALGALMYRLAGSRRRIAARNLELCFPEKSAAERERLLKENFAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 86 LGMALLETGMAWFWPDRRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLCQPMMATYRPHNNKLMEWIQ 165
Cdd:PRK05646 85 TGIAFFEMAMSWWWPKARLARLAHIEGLEHLQQAQQEGQGVILMALHFTTLEIGAALLGQQHTIDGMYREHKNPVFDFIQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 166 TRGRMRSNK--AMIGRNNLRGIVGALKKGEAVWFAPDQDYGRKGSSFAPFFAVKnVATTNGTYVLSRLSGAAMLTVTMVR 243
Cdd:PRK05646 165 RRGRERHNLdsTAIEREDVRGMLKLLRAGRAIWYAPDQDYGAKQSIFVPLFGIP-AATVTATTKFARLGRARVIPFTQKR 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507086329 244 KADNSGYRLFITPEMEGYPTDESQAAAY-MNKIIEKEIMRAPEQYLWIHRRFKTRPMGEASLY 305
Cdd:PRK05646 244 LADGSGYRLVIHPPLEDFPGESEEADCLrINQWVERVVRECPEQYLWAHRRFKSRPEGEPKLY 306
|
|
| PRK08733 |
PRK08733 |
LpxL/LpxP family Kdo(2)-lipid IV(A) lauroyl/palmitoleoyl acyltransferase; |
12-305 |
3.80e-70 |
|
LpxL/LpxP family Kdo(2)-lipid IV(A) lauroyl/palmitoleoyl acyltransferase;
Pssm-ID: 181542 [Multi-domain] Cd Length: 306 Bit Score: 219.77 E-value: 3.80e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 12 LHPRYWLTWFGVGVLWLLVQLPYPVLCFLGTRTGTLARPFLKRRESIAHKNLELCFPNLSQEERDKLVDENFRSLGMALL 91
Cdd:PRK08733 14 RNPKHWPMYLGLAVMVLAARLPWTLQRALGRGVGWVAMRLAGTRRRAAEVNLKLCFPEQDDAWRARLLRDSFDALGVGLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 92 ETGMAWFWPDRRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVmgLCQ--PMMATYRPHNNKLMEWIQTRGR 169
Cdd:PRK08733 94 EFARAWWGSIDVIRPGVQIEGLEHLQQLQQQGRGVLLVSGHFMTLEMCGRL--LCDhvPLAGMYRRHRNPVFEWAVKRGR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 170 MRSNKAMIGRNNLRGIVGALKKGEAVWFAPDQDYGRKGSSFAPFFAVKnVATTNGTYVLSRLSGAAMLTVTMVRKADNsg 249
Cdd:PRK08733 172 LRYATHMFANEDLRATIKHLKRGGFLWYAPDQDMRGKDTVFVPFFGHP-ASTITATHQLARLTGCAVVPYFHRREGGR-- 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 507086329 250 YRLFITPEMEGYPTDESQA-AAYMNKIIEKEIMRAPEQYLWIHRRFKTRPMGEASLY 305
Cdd:PRK08733 249 YVLKIAPPLADFPSDDVIAdTTRVNAAIEDMVREAPDQYLWIHRRFKRQPGGRSDFY 305
|
|
| LPLAT_LABLAT-like |
cd07984 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LABLAT-like; ... |
105-295 |
1.69e-65 |
|
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: 203.99 E-value: 1.69e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 105 RKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLC-QPMMATYRPHNNKLMEWIQTRGRMRSNKAMIGRNN-L 182
Cdd:cd07984 1 LKRVEREGLEHLEAALAKGKGVILLTAHFGNWELAGLALALLgYPVTVVYRPLKNPLLDRLITRGRERFGARLIPRGGgL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 183 RGIVGALKKGEAVWFAPDQDYGRKGSSFAPFFAVKnVATTNGTYVLSRLSGAAMLTVTMVRKADNsGYRLFITPEMEGYP 262
Cdd:cd07984 81 RELIRALKKGEIVGILPDQDPGRKGGVFVPFFGRP-AATPTGPARLALKTGAPVVPAFAYRLPGG-GYRIEFEPPLENPP 158
|
170 180 190
....*....|....*....|....*....|....
gi 507086329 263 T-DESQAAAYMNKIIEKEIMRAPEQYLWIHRRFK 295
Cdd:cd07984 159 SeDVEEDTQRLNDALEAAIREHPEQWLWFHRRWK 192
|
|
| PRK06946 |
PRK06946 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
19-305 |
1.91e-64 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 180770 [Multi-domain] Cd Length: 293 Bit Score: 204.53 E-value: 1.91e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 19 TWFGVGVLWLLVQLPYPVLCFLGTRTGTLARPFLKRRESIAHKNLELCFPNLSQEERDKLVDENFRSLGMALLETGMAWF 98
Cdd:PRK06946 6 TALAIGLLKLLAFLPYGLTARFGDGLGWLLYRIPSRRRRIVHTNLKLCFPDWSDARREELARRHFRHVIRSYVERSVQWF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 99 WPDRRVRKWFDVEGLDNLKRAQMQNRgvMVVGVHFMSLELGG--RVMGLCQPMMATYRPHNNKLMEWIQTRGRMRSNKAM 176
Cdd:PRK06946 86 GSEKKLEKLVQVDSAIDLTDPDGPPT--IFLGLHFVGIEAGSiwLNYSLRRRVGSLYTPMSNPLLDAIAKAARGRFGAEM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 177 IGRN-NLRGIVGALKKGEAVWFAPDQDYGRKGSSFAPFFAVKnVATTNGTYVLSRLSGAAMLTVTMVRKADNSGYRLFIT 255
Cdd:PRK06946 164 VSRAdSARQVLRWLRDGKPVMLGADMDFGLRDSTFVPFFGVP-ACTLTAVSRLARTGGAQVVPFITEVLPDYKGYRLRVF 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 507086329 256 PEMEGYPTDESQA-AAYMNKIIEKEIMRAPEQYLWIHRRFKTRPMGEASLY 305
Cdd:PRK06946 243 KPWENYPTGDDDLdARRMNAFLEEQIRLMPEQYYWVHKRFKTRPPGEPSVY 293
|
|
| lipid_A_msbB |
TIGR02208 |
lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; This family consists of MsbB ... |
6-305 |
2.10e-58 |
|
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: 189.63 E-value: 2.10e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 6 KFSRAFLHPRYWLTWFGVGVLWLLVQLPYPVLCFLGTRTGTLARPFLKRRESIAHKNLELCFPNLSQEERDKLVDENFRS 85
Cdd:TIGR02208 4 RFQKSFLHPKYWGTWLGVFALVLLAFMPAKLRDPIAKVLAKFVGPIAKKPRGRARINLSACFPEKSEAERETIIDNNFAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 86 LGMALLETGMAWFWPDRRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGG-RVMGLCQPMMATYRPHNNKLMEWI 164
Cdd:TIGR02208 84 FVQVMLSQAELAIRSKAHLRRRVNLMGLEHIEAAQAAGKPVIFLVPHGWAIDYAGlRLASQGLPMVTMFNNHKNPLFDWL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 165 QTRGRMRSNKAMIGRNN-LRGIVGALKKGEAVWFAPDQDYGRKGSSFAPFFAVKNvATTNGTYVLSRLSGAAMLTVTMVR 243
Cdd:TIGR02208 164 WNRVRSRFGGHVYAREAgIKALLASLKRGESGYYLPDEDHGPEQSVFVPFFATYK-ATLPVVGRLAKAGNAQVVPVFPGY 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507086329 244 KADNSGYRLFITPEMEGYPT-DESQAAAYMNKIIEKEIMRAPEQYLWIHRRFKTRPMGEASLY 305
Cdd:TIGR02208 243 NQVTGKFELTVRPAMATELSvDPEQEARAMNKEVEQFILPYPEQYMWILRLLKTRPDGEASIY 305
|
|
| PRK08943 |
PRK08943 |
lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; Validated |
6-301 |
7.05e-57 |
|
lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; Validated
Pssm-ID: 236355 Cd Length: 314 Bit Score: 185.84 E-value: 7.05e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 6 KFSRAFLHPRYWLTWFGVGVLWLLVQLPY----PVLCFLGTRTGTLARPFLKRresiAHKNLELCFPNLSQEERDKLVDE 81
Cdd:PRK08943 13 RFQKSFLHPRYWGTWLGIGALAGLALMPPrlrdPLAAKLGRLVGKLAKKARRR----ARINLSLCFPEKSEAEREAIIDE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 82 NFRSLGMALLETGMAWFWPDRRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGL-CQPMMATYRPHNNKL 160
Cdd:PRK08943 89 MFATAPQAMLMMAELALRSPKHLQRRVEWHGLEILEEARANGENVIFLVPHGWAIDIPAMLLASqGQPMAAMFHNQRNPL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 161 MEWIQTRGRMRSNKAMIGRNNlrGI---VGALKKGEAVWFAPDQDYGRKGSSFAPFFA-VKnvATTNGTYVLSRLSGAAM 236
Cdd:PRK08943 169 FDWLWNRVRRRFGGRLHARED--GIkpfISSVRQGYWGYYLPDEDHGPEHSVFVDFFAtYK--ATLPGIGRLAKVCRARV 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507086329 237 LTVTMVRKADNSGYRLFITPEMEGYPT-DESQAAAYMNKIIEKEIMRAPEQYLWIHRRFKTRPMGE 301
Cdd:PRK08943 245 VPLFPVYNGKTHRLDIEIRPPMDDLLSaDDETIARRMNEEVEQFVGPHPEQYMWILKLLKTRKPGE 310
|
|
| PRK08706 |
PRK08706 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
21-305 |
2.20e-52 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 169557 [Multi-domain] Cd Length: 289 Bit Score: 173.51 E-value: 2.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 21 FGVGVLWLLVQLPYPVLCFLGTRTGTLARPFLKRRESIAHKNLELCFPNLSQEERDKLVDENFRSLGMALLETGMAWFWP 100
Cdd:PRK08706 3 FIFFVLYVLQFLPFALLHKLADLTGLLAYLLVKPRRRIGEINLAKCFPEWDEEKRKTVLKQHFKHMAKLMLEYGLYWYAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 101 DRRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGgrVMGLCQ--PMMATYRPHNNKLMEWIQTRGRMR-SNKAMI 177
Cdd:PRK08706 83 AGRLKSLVRYRNKHYLDDALAAGEKVIILYPHFTAFEMA--VYALNQdvPLISMYSHQKNKILDEQILKGRNRyHNVFLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 178 GRNN-LRGIVGALKKGEAVW-FAPDQDYGRKGSSFAPFFAVKnVATTNGTYVLSRLSGAAMLTVTMVRKADNSgYRLFIT 255
Cdd:PRK08706 161 GRTEgLRALVKQFRKSSAPFlYLPDQDFGRNDSVFVDFFGIQ-TATITGLSRIAALANAKVIPAIPVREADNT-VTLHFY 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 507086329 256 PEMEGYPTDESQA-AAYMNKIIEKEIMRAPEQYLWIHRRFKTRPMGEASLY 305
Cdd:PRK08706 239 PAWDSFPSEDAQAdAQRMNRFIEERVREHPEQYFWLHKRFKTRPEGSPDFY 289
|
|
| PRK05645 |
PRK05645 |
lysophospholipid acyltransferase; |
23-305 |
1.91e-37 |
|
lysophospholipid acyltransferase;
Pssm-ID: 135493 [Multi-domain] Cd Length: 295 Bit Score: 134.65 E-value: 1.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 23 VGVLWLLVQLPYPVLCFLGTRTGTLARPFLKRRESIAHKNLELCFPNLSQEERDKLVDENFRSLGMALLETGMAWFWPDR 102
Cdd:PRK05645 10 VGALRLFALLPWRAVQGVGAGIGWLMWKLPNRSREVVRINLSKCFPELSPAELEKLVGQSLMDIGKTLTESACAWIWPPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 103 RVRKWF-DVEGLDNLKRAQMQNRGVMVVGVHFMSLE-LGGRVMGLCQPMMaTYRPHNNKLMEWI--QTRGRMRSNKAMIG 178
Cdd:PRK05645 90 KSLELVrEVEGLEVLEQALASGKGVVGITSHLGNWEvLNHFYCSQCKPII-FYRPPKLKAVDELlrKQRVQLGNRVAPST 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 179 RNNLRGIVGALKKGEAVWFAPDQDYGRKGSSFAPFFAVKNVATtngTYVLSRLSGAAMLTVTM--VRKADNSGYRLFITP 256
Cdd:PRK05645 169 KEGILSVIKEVRKGGQVGIPADPEPAESAGIFVPFLGTQALTS---KFVPNMLAGGKAVGVFLhaLRLPDGSGYKVILEA 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 507086329 257 EMEG-YPTDESQAAAYMNKIIEKEIMRAPEQYLWIHRRFKTRPMGEASLY 305
Cdd:PRK05645 246 APEDmYSTDVEVSAAAMSKVVERYVRAYPSQYMWSMKRFKKRPAGEARWY 295
|
|
| PRK08905 |
PRK08905 |
lysophospholipid acyltransferase family protein; |
25-300 |
1.13e-35 |
|
lysophospholipid acyltransferase family protein;
Pssm-ID: 236348 [Multi-domain] Cd Length: 289 Bit Score: 130.11 E-value: 1.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 25 VLWLLVQLPYPVLCFLGTRTGTLARPFLKRRESIAHKNLELCFPNLSqeerDKLVDENFRSLGMALLEtgMAWFW---PD 101
Cdd:PRK08905 5 LFRLLSRLPLSWLHALGGWLGRLAYRLPGRYRRRLRANLRQAGGDPD----PAMVKAAAAETGRMILE--LPYVWfrkPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 102 RRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLCQPMMATYRPHNNK-LMEWIQtRGRMRSNKAMI--G 178
Cdd:PRK08905 79 EIETMVKDDHGWEHVEAALAEGRGILFLTPHLGCFEVTARYIAQRFPLTAMFRPPRKAaLRPLME-AGRARGNMRTApaT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 179 RNNLRGIVGALKKGEAVWFAPDQDYGRKGSSFAPFFAvKNVATTNGTYVLSRLSGAAMLTVTMVRKADNSGYRLFITPEM 258
Cdd:PRK08905 158 PQGVRMLVKALRRGEAVGILPDQVPSGGEGVWAPFFG-RPAYTMTLVARLAEVTGVPVIFVAGERLPRGRGYRLHLRPVQ 236
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 507086329 259 EGYPTDESQAAAYMNKIIEKEIMRAPEQYLWIHRRFKtRPMG 300
Cdd:PRK08905 237 EPLPGDKAADAAVINAEIERLIRRFPTQYLWGYNRYK-RPRG 277
|
|
| PRK08419 |
PRK08419 |
lipid A biosynthesis lauroyl acyltransferase; Reviewed |
28-295 |
2.32e-24 |
|
lipid A biosynthesis lauroyl acyltransferase; Reviewed
Pssm-ID: 181420 [Multi-domain] Cd Length: 298 Bit Score: 100.10 E-value: 2.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 28 LLVQLPYPVLCFLGTRTGTLARPFLKRRESIAHKNLELCFP-NLSQEERDKLVDENFRSLGMALLETGMAWFWPDRRVRK 106
Cdd:PRK08419 16 FLAKMPHCIFLRLAKALAFIMRYLDKKRRKIAKANLDFCFGeSKSQEEKKRIIKKCYENFAFFGLDFIRNQNTTKEEILN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 107 WFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGL-CQPMMATYRPHNNKLM-EWIQTRgRMRSNKAMIGRNN-LR 183
Cdd:PRK08419 96 KVTFINEENLLDALKKKRPIIVTTAHYGYWELFSLALAAyYGAVSIVGRLLKSAPInEMISKR-REQFGIELIDKKGaMK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 184 GIVGALKKGEAVWFAPDQDYGRKGSSFAPFFAvKNVATTNGTYVLSRLSGAAMLTVtMVRKADNSGYRLFITPEMEGYPT 263
Cdd:PRK08419 175 ELLKALKQGRALGILVDQNVVPKEGVEVKFFN-KRVTHTTIASILARRYNALIIPV-FIFNDDYSHFTITFFPPIRSKIT 252
|
250 260 270
....*....|....*....|....*....|....*..
gi 507086329 264 DESQAA-----AYMNKIIEKEIMRAPEQYLWIHRRFK 295
Cdd:PRK08419 253 DDAEADileatQAQASACEEMIRKKPDEYFWFHRRFK 289
|
|
| PRK08734 |
PRK08734 |
lauroyl acyltransferase; |
28-300 |
2.23e-21 |
|
lauroyl acyltransferase;
Pssm-ID: 181543 [Multi-domain] Cd Length: 305 Bit Score: 91.87 E-value: 2.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 28 LLVQLPYPVLCFLGTRTGTLARPFLKRRESIAHKNLELCFPNLSQEERDKLVDENFRSLGMALLETGMAWFWPD----RR 103
Cdd:PRK08734 16 LVGRLPWPLLKRLADLLAWSWRKLNARESRVTRRNLELAYPELSPQQRAQLHAQILRSTARQALEVLRTWTHPPaenlAR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 104 VRKWFDVEGLDnlkRAQMQNRGVMVVGVHFMSLELGGRVMGLCQPMMATYRPHNNKLMEWIQTRGRMRSNKAMIGRNN-- 181
Cdd:PRK08734 96 LRQRHGQELYD---AALASGRGVIVAAPHFGNWELLNQWLSERGPIAIVYRPPESEAVDGFLQLVRGGDNVRQVRAEGpa 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 182 LRGIVGALKKGEAVWFAPDQDYGRKGSSFAPFFAVKNVATTngtyVLSRL---SGAAMLTVTMVRKADNSGYRLFITPEM 258
Cdd:PRK08734 173 VRQLFKVLKDGGAVGILPDQQPKMGDGVFAPFFGIPALTMT----LVNRLaerTGATVLYGWCERIGPDLEFALHVQPAD 248
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 507086329 259 EGYP-TDESQAAAYMNKIIEKEIMRAPEQYLWIHRRFKTRPMG 300
Cdd:PRK08734 249 PAVAdPDPLRAATALNAGIERIARRDPAQYQWTYKRYTLRPPG 291
|
|
| PRK05906 |
PRK05906 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
13-295 |
9.10e-09 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 168292 [Multi-domain] Cd Length: 454 Bit Score: 55.94 E-value: 9.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 13 HPRYWLtwfGVGVLWLLVQLPYPVLCFLGTRTGTLARPFLKRRESIAHKNLELCFPNLSQEERDKLVDENFRSLGMALLE 92
Cdd:PRK05906 15 HLVYYL---GLGVITILRLLPRSSLRLFGKGLGTLLFYFISDYRKTALTNLALAFPEKSFAERYQIARQSVQHVIITFLE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 93 ---------------------TGMAWFWPDRRVRKwfdvEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLCQPMMA 151
Cdd:PRK05906 92 llaveklaghideliaiatseDAPEGFFPEEVSSQ----QELEHTFSRLDEQEGAILFCGHQANWELPFLYITKRYPGLA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 152 TYRP-HNNKLMEWIQTRGRMRSNKAMIGRNNLRGIVGALKKGEAVWFAPDQdyGRKGSSFA-PFFAVKNVATTNGTyVLS 229
Cdd:PRK05906 168 FAKPiKNRRLNKKIFSLRESFKGKIVPPKNGINQALRALHQGEVVGIVGDQ--ALLSSSYSyPLFGSQAFTTTSPA-LLA 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507086329 230 RLSGAAMLTVTMVRKadNSGYRlfITPEMEGY-----PTDESqAAAYMNKI---IEKEIMRAPEQYLWIHRRFK 295
Cdd:PRK05906 245 YKTGKPVIAVAIYRK--PNGYL--VVPSKKFYankslPIKES-TEQLMDRLmrfLEKGIACKPEQWMWLHKRWK 313
|
|
| PRK06628 |
PRK06628 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
58-295 |
3.00e-07 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 102471 Cd Length: 290 Bit Score: 51.08 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 58 IAHKNLELCFPNLSQEErdKLVDENFRSLGMALLETGMAWFWPDRRVRKWFDVEGLDNLKRaqMQNRGVMVVGVHFMSLE 137
Cdd:PRK06628 52 IARRNIKAVFGDMCDVE--KIIDQTWDNFGRFIGEFTYVNKMDEAELERRIEIIGIENIKK--LEGQPFLLFSGHFANWD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 138 LGGRVMGLCQPMMAT-YRPHNNKLMEWIQTRGRMRSNKAMI--GRNNLRGIVGALKKGEAVWFAPDQDYgrKGSSFAPFF 214
Cdd:PRK06628 128 ISLKILHKFYPKVAViYRKANNPYVNKLVNESRAGDKLRLIpkGPEGSRALVRAIKESESIVMLVDQKM--NDGIEVPFL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 215 AVKNVaTTNGTYVLSRLSGAAMLTVTMVRkADNSGYRLFITPEMEGYPTDESQAAAY-----MNKIIEKEIMRAPEQYLW 289
Cdd:PRK06628 206 GHPAM-TASAIAKIALQYKYPIIPCQIIR-TKGSYFKVIVHPQLKFEQTGDNKADCYnimlnINQMLGEWVKQNPAQWFW 283
|
....*.
gi 507086329 290 IHRRFK 295
Cdd:PRK06628 284 FHNRWK 289
|
|
| PRK06553 |
PRK06553 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
6-293 |
2.55e-06 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 235827 [Multi-domain] Cd Length: 308 Bit Score: 48.05 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 6 KFSRAFLHPRYWLT-WFGVGVLWLLVQLPYPVLCFLGTRTGTLARPFLkRRESIAHKNLELCFPNLSQEERDKLVDENFR 84
Cdd:PRK06553 11 RLRRALKRFAGWLVaQLVFGLLGLLRLFPADKAINFFGRLARLIGPLL-PRHRVALDNLRAAFPEKSEAEIEAIALGMWD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 85 SLGMALLE---TGMAW-FWPDRRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLEL---GGRVMGLcqPMMATYRPHN 157
Cdd:PRK06553 90 NLGRLGAEyafLDAIFdYDPEAPEPGRVEVRGIEIFERLRDDGKPALIFTAHLGNWELlaiAAAAFGL--DVTVLFRPPN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507086329 158 NKLMEWIQTRGRMRSNKAMI--GRNNLRGIVGALKKGEAVWFAPDQDYGRKGSSfaPFFAVKnvATTNGTYV-LSRLSGA 234
Cdd:PRK06553 168 NPYAARKVLEARRTTMGGLVpsGAGAAFALAGVLERGGHVGMLVDQKFTRGVEV--TFFGRP--VKTNPLLAkLARQYDC 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507086329 235 AMLTVTMVRKADNSgYRLFITPEMEgYPTDES-----QAAAY-MNKIIEKEIMRAPEQYLWIHRR 293
Cdd:PRK06553 244 PVHGARCIRLPGGR-FRLELTERVE-LPRDADgqidvQATMQaLTDVVEGWVREYPGQWLWLHRR 306
|
|
|