|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08025 |
PRK08025 |
kdo(2)-lipid IV(A) palmitoleoyltransferase; |
1-306 |
7.97e-159 |
|
kdo(2)-lipid IV(A) palmitoleoyltransferase;
Pssm-ID: 181200 Cd Length: 305 Bit Score: 444.95 E-value: 7.97e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 1 MYAKNPFSLKLVHPKYVVTWVGVFILFLLVQLPYKWQMWLGAFLGSNSRYFIKRRVSIIKRNLELCFPNKNKNEIDTLVN 80
Cdd:PRK08025 1 MFPQQKFSREFLHPRYWLTWFGLGVLWLLVQLPYPVLCFLGTRIGRMSRPFLKRRESIARKNLELCFPQMSAEEREKMIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 81 DNLKSLGIALFETGIAWFWSDKKVKKLFQVKGMSNYLDAIAKNKGVIIVGVHFMSLELGGRIMGLCFPVNAMYRPHNNKA 160
Cdd:PRK08025 81 ENFRSLGMALLETGMAWFWPDSRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLCQPMMATYRPHNNKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 161 MEYIQTKGRCRSGKGMIDRKNLKFMVQELKSGKSIWFAPDQDFGRKGTIFAPFFSVKNSSTSKGTSILAQLSKSPTLTVT 240
Cdd:PRK08025 161 MEWVQTRGRMRSNKAMIGRNNLRGIVGALKKGEAVWFAPDQDYGPKGSSFAPFFAVENVATTNGTYVLSRLSGAAMLTVT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490380420 241 LLRNKSGANYDLVLGKEILEYPsSDALQDATIINSILEVEIMKAPEQYLWAHRRFKTRPEGEVSLY 306
Cdd:PRK08025 241 MVRKADYSGYRLFITPEMEGYP-TDENQAAAYMNKIIEKEIMRAPEQYLWIHRRFKTRPVGESSLY 305
|
|
| lipid_A_htrB |
TIGR02207 |
lipid A biosynthesis lauroyl (or palmitoleoyl) acyltransferase; This model represents a narrow ... |
7-306 |
1.99e-147 |
|
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: 415.97 E-value: 1.99e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 7 FSLKLVHPKYVVTWVGVFILFLLVQLPYKWQMWLGAFLGSNSRYFIKRRVSIIKRNLELCFPNKNKNEIDTLVNDNLKSL 86
Cdd:TIGR02207 3 FSASLLHPRYWPTWLGLGVLWLIVQLPYPVLLALGRGIGRLAMRLMKRRVHIARRNLELCFPHMSDAERERLLRENFEST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 87 GIALFETGIAWFWSDKKVKKLFQVKGMSNYLDAIAKNKGVIIVGVHFMSLELGGRIMGLCFPVNAMYRPHNNKAMEYIQT 166
Cdd:TIGR02207 83 GMALFETGMAWFWSDARIKKWMQIEGLEHLQRAQKQGRGVLLVGVHFLTLELGARIFGQQQPGIGVYRPHNNPLFDWIQT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 167 KGRCRSGKGMIDRKNLKFMVQELKSGKSIWFAPDQDFGRKGTIFAPFFSVKNSSTSKGTSILAQLSKSPTLTVTLLRNKS 246
Cdd:TIGR02207 163 RGRLRSNKAMIDRKDLRGMIKALKNGERIWYAPDHDYGRKSSVFVPFFAVPDAATTTGTSILARLSKCAVVPFTPRRNED 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490380420 247 GANYDLVLGKEILEYPSSDALQDATIINSILEVEIMKAPEQYLWAHRRFKTRP-EGEVSLY 306
Cdd:TIGR02207 243 GSGYRLKIDPPLDDFPGDDEIAAAARMNKIVEKMIMRAPEQYMWLHRRFKTRPdEGESSLY 303
|
|
| LpxP |
COG1560 |
Palmitoleoyl-ACP: Kdo2-lipid-IV acyltransferase (lipid A biosynthesis) [Lipid transport and ... |
25-295 |
1.64e-102 |
|
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: 300.95 E-value: 1.64e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 25 ILFLLVQLPYKWQMWLGAFLGSNSRYFIKRRVSIIKRNLELCFPNKNKNEIDTLVNDNLKSLGIALFETGIAWFWSDKKV 104
Cdd:COG1560 1 LLRLLRLLPLRLLYRLGDLLGRLLYRLAGRRRRVARRNLALAFPELSEAEREALARASFRNLGRTLLETLRLWRLSPERL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 105 KKLFQVKGMSNYLDAIAKNKGVIIVGVHFMSLELGGRIMGLC-FPVNAMYRPHNNKAMEYIQTKGRCRSGKGMIDRKN-L 182
Cdd:COG1560 81 RKRVEVEGLEHLEAALAEGRGVILLTPHFGNWELAGAALALRgYPVTAVYRPLKNPLLDRLIRRGRERFGGELIPRKDgV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 183 KFMVQELKSGKSIWFAPDQDFGRKGTIFAPFFSVKnSSTSKGTSILAQLSKSPTLTVTLLRNKSGANYDLVLGKEIlEYP 262
Cdd:COG1560 161 RALLRALRKGGIVGLLPDQDPGRKSGVFVPFFGVP-AATPTGPARLARRTGAPVVPVFARRLPDGRGYRLEIEPPL-EDF 238
|
250 260 270
....*....|....*....|....*....|...
gi 490380420 263 SSDALQDATIINSILEVEIMKAPEQYLWAHRRF 295
Cdd:COG1560 239 SEDVEADTQRLNRALEAWIREHPEQWLWLHRRW 271
|
|
| Lip_A_acyltrans |
pfam03279 |
Bacterial lipid A biosynthesis acyltransferase; |
6-297 |
7.25e-88 |
|
Bacterial lipid A biosynthesis acyltransferase;
Pssm-ID: 281296 [Multi-domain] Cd Length: 294 Bit Score: 264.59 E-value: 7.25e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 6 PFSLKLVHPKYVVTWVGVFILFLLVQLPYKWQMWLGAFLGSNSRYFIKRRVSIIKRNLELCFPNKNKNEIDTLVNDNLKS 85
Cdd:pfam03279 2 KFSPELLHPRYWLDWLGIAVLRLLALLPYSALRRIGKGLGRLAGRFLKRRRKIARRNLALCFPEMSEAEREQIIDKSFAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 86 LGIALFETGIAWFWSDKKVKKLFQVKGMSNYLDAIAKNKGVIIVGVHFMSLELGGRIMGLCFP-VNAMYRPHNNKAMEYI 164
Cdd:pfam03279 82 VGRAIVETGRVWFWPDSRIAKRFEVIGLEHIKEALAQGRGAILVGPHFGNWDLGGRVLGQQYPgMAVYRPNLKNPLLDWL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 165 QTKGRCRSGKGMIDRKN-LKFMVQELKSGKSIWFAPDQDFGRKGTIFAPFFSVKNSSTSkGTSILAQLSKSPTLTVTLLR 243
Cdd:pfam03279 162 QTSGRERFGGRMLPRQNgIKGLIKALRKGEVVWYLPDQDLGRKDSVFVPFFGVPAATTT-GPAKLALKTKAAVIPVFPIR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 490380420 244 NKSGANYDLVLGKEILEYPSSDALQDATIINSILEVEIMKAPEQYLWAHRRFKT 297
Cdd:pfam03279 241 NGDGSGYTVIVHPALDLTITDDVEQIAQAMNQIVEKFIMPAPEQYFWLHRRWKT 294
|
|
| LPLAT_LABLAT-like |
cd07984 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LABLAT-like; ... |
105-296 |
1.04e-62 |
|
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: 196.67 E-value: 1.04e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 105 KKLFQVKGMSNYLDAIAKNKGVIIVGVHFMSLELGGRIMGLC-FPVNAMYRPHNNKAMEYIQTKGRCRSGKGMIDRKN-L 182
Cdd:cd07984 1 LKRVEREGLEHLEAALAKGKGVILLTAHFGNWELAGLALALLgYPVTVVYRPLKNPLLDRLITRGRERFGARLIPRGGgL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 183 KFMVQELKSGKSIWFAPDQDFGRKGTIFAPFFSVKnSSTSKGTSILAQLSKSPTLTVTLLRNKsGANYDLVLGKEILEYP 262
Cdd:cd07984 81 RELIRALKKGEIVGILPDQDPGRKGGVFVPFFGRP-AATPTGPARLALKTGAPVVPAFAYRLP-GGGYRIEFEPPLENPP 158
|
170 180 190
....*....|....*....|....*....|....
gi 490380420 263 SSDALQDATIINSILEVEIMKAPEQYLWAHRRFK 296
Cdd:cd07984 159 SEDVEEDTQRLNDALEAAIREHPEQWLWFHRRWK 192
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08025 |
PRK08025 |
kdo(2)-lipid IV(A) palmitoleoyltransferase; |
1-306 |
7.97e-159 |
|
kdo(2)-lipid IV(A) palmitoleoyltransferase;
Pssm-ID: 181200 Cd Length: 305 Bit Score: 444.95 E-value: 7.97e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 1 MYAKNPFSLKLVHPKYVVTWVGVFILFLLVQLPYKWQMWLGAFLGSNSRYFIKRRVSIIKRNLELCFPNKNKNEIDTLVN 80
Cdd:PRK08025 1 MFPQQKFSREFLHPRYWLTWFGLGVLWLLVQLPYPVLCFLGTRIGRMSRPFLKRRESIARKNLELCFPQMSAEEREKMIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 81 DNLKSLGIALFETGIAWFWSDKKVKKLFQVKGMSNYLDAIAKNKGVIIVGVHFMSLELGGRIMGLCFPVNAMYRPHNNKA 160
Cdd:PRK08025 81 ENFRSLGMALLETGMAWFWPDSRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLCQPMMATYRPHNNKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 161 MEYIQTKGRCRSGKGMIDRKNLKFMVQELKSGKSIWFAPDQDFGRKGTIFAPFFSVKNSSTSKGTSILAQLSKSPTLTVT 240
Cdd:PRK08025 161 MEWVQTRGRMRSNKAMIGRNNLRGIVGALKKGEAVWFAPDQDYGPKGSSFAPFFAVENVATTNGTYVLSRLSGAAMLTVT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490380420 241 LLRNKSGANYDLVLGKEILEYPsSDALQDATIINSILEVEIMKAPEQYLWAHRRFKTRPEGEVSLY 306
Cdd:PRK08025 241 MVRKADYSGYRLFITPEMEGYP-TDENQAAAYMNKIIEKEIMRAPEQYLWIHRRFKTRPVGESSLY 305
|
|
| lipid_A_htrB |
TIGR02207 |
lipid A biosynthesis lauroyl (or palmitoleoyl) acyltransferase; This model represents a narrow ... |
7-306 |
1.99e-147 |
|
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: 415.97 E-value: 1.99e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 7 FSLKLVHPKYVVTWVGVFILFLLVQLPYKWQMWLGAFLGSNSRYFIKRRVSIIKRNLELCFPNKNKNEIDTLVNDNLKSL 86
Cdd:TIGR02207 3 FSASLLHPRYWPTWLGLGVLWLIVQLPYPVLLALGRGIGRLAMRLMKRRVHIARRNLELCFPHMSDAERERLLRENFEST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 87 GIALFETGIAWFWSDKKVKKLFQVKGMSNYLDAIAKNKGVIIVGVHFMSLELGGRIMGLCFPVNAMYRPHNNKAMEYIQT 166
Cdd:TIGR02207 83 GMALFETGMAWFWSDARIKKWMQIEGLEHLQRAQKQGRGVLLVGVHFLTLELGARIFGQQQPGIGVYRPHNNPLFDWIQT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 167 KGRCRSGKGMIDRKNLKFMVQELKSGKSIWFAPDQDFGRKGTIFAPFFSVKNSSTSKGTSILAQLSKSPTLTVTLLRNKS 246
Cdd:TIGR02207 163 RGRLRSNKAMIDRKDLRGMIKALKNGERIWYAPDHDYGRKSSVFVPFFAVPDAATTTGTSILARLSKCAVVPFTPRRNED 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490380420 247 GANYDLVLGKEILEYPSSDALQDATIINSILEVEIMKAPEQYLWAHRRFKTRP-EGEVSLY 306
Cdd:TIGR02207 243 GSGYRLKIDPPLDDFPGDDEIAAAARMNKIVEKMIMRAPEQYMWLHRRFKTRPdEGESSLY 303
|
|
| PRK06860 |
PRK06860 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
1-306 |
4.82e-136 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 235880 [Multi-domain] Cd Length: 309 Bit Score: 387.34 E-value: 4.82e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 1 MYAKNPFSLKLVHPKYVVTWVGVFILFLLVQLPYKWQMWLGAFLGSNSRYFIKRRVSIIKRNLELCFPNKNKNEIDTLVN 80
Cdd:PRK06860 3 MTNLPKFSRALLHPRYWLTWLGIGLLWLIVLLPYPVLYKLGRGLGKLALRFMKRRAKIARRNLELCFPEMSEQEREAIVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 81 DNLKSLGIALFETGIAWFWSDKKVKKLFQVKGMSNYLDAIAKNKGVIIVGVHFMSLELGGRIMGLCFPVNAMYRPHNNKA 160
Cdd:PRK06860 83 KNFESVGMALIETGMAWFWPDWRIKRWTEVEGLEHIREVQAQGRGVLLVGVHFLTLELGARIFGMHNPGIGVYRPNDNPL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 161 MEYIQTKGRCRSGKGMIDRKNLKFMVQELKSGKSIWFAPDQDFGRKGTIFAPFFSVKNSSTSKGTSILAQLSKSPTLTVT 240
Cdd:PRK06860 163 YDWLQTWGRLRSNKSMLDRKDLKGMIKALKKGERIWYAPDHDYGPRSSVFVPFFAVEQAATTTGTWMLARMSKAAVIPFV 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490380420 241 LLRNKSGANYDLVLGKEILEYPSSDALQDATIINSILEVEIMKAPEQYLWAHRRFKTRPEGEVSLY 306
Cdd:PRK06860 243 PRRKPDGKGYELIILPPEDSPPLDDAEATAAWMNKVVEKCILMAPEQYMWLHRRFKTRPEGVPSRY 308
|
|
| LpxP |
COG1560 |
Palmitoleoyl-ACP: Kdo2-lipid-IV acyltransferase (lipid A biosynthesis) [Lipid transport and ... |
25-295 |
1.64e-102 |
|
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: 300.95 E-value: 1.64e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 25 ILFLLVQLPYKWQMWLGAFLGSNSRYFIKRRVSIIKRNLELCFPNKNKNEIDTLVNDNLKSLGIALFETGIAWFWSDKKV 104
Cdd:COG1560 1 LLRLLRLLPLRLLYRLGDLLGRLLYRLAGRRRRVARRNLALAFPELSEAEREALARASFRNLGRTLLETLRLWRLSPERL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 105 KKLFQVKGMSNYLDAIAKNKGVIIVGVHFMSLELGGRIMGLC-FPVNAMYRPHNNKAMEYIQTKGRCRSGKGMIDRKN-L 182
Cdd:COG1560 81 RKRVEVEGLEHLEAALAEGRGVILLTPHFGNWELAGAALALRgYPVTAVYRPLKNPLLDRLIRRGRERFGGELIPRKDgV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 183 KFMVQELKSGKSIWFAPDQDFGRKGTIFAPFFSVKnSSTSKGTSILAQLSKSPTLTVTLLRNKSGANYDLVLGKEIlEYP 262
Cdd:COG1560 161 RALLRALRKGGIVGLLPDQDPGRKSGVFVPFFGVP-AATPTGPARLARRTGAPVVPVFARRLPDGRGYRLEIEPPL-EDF 238
|
250 260 270
....*....|....*....|....*....|...
gi 490380420 263 SSDALQDATIINSILEVEIMKAPEQYLWAHRRF 295
Cdd:COG1560 239 SEDVEADTQRLNRALEAWIREHPEQWLWLHRRW 271
|
|
| PRK05646 |
PRK05646 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
7-306 |
2.00e-98 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 235543 [Multi-domain] Cd Length: 310 Bit Score: 292.10 E-value: 2.00e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 7 FSLKLVHPKYVVTWVGVFILFLLVQLPYKWQMWLGAFLGSNSRYFIKRRVSIIKRNLELCFPNKNKNEIDTLVNDNLKSL 86
Cdd:PRK05646 6 FRAAFLHPRFWPLWLGLGLLWLVVQLPYRVLLWLGRALGALMYRLAGSRRRIAARNLELCFPEKSAAERERLLKENFAST 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 87 GIALFETGIAWFWSDKKVKKLFQVKGMSNYLDAIAKNKGVIIVGVHFMSLELGGRIMGLCFPVNAMYRPHNNKAMEYIQT 166
Cdd:PRK05646 86 GIAFFEMAMSWWWPKARLARLAHIEGLEHLQQAQQEGQGVILMALHFTTLEIGAALLGQQHTIDGMYREHKNPVFDFIQR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 167 KGRCRSGKG--MIDRKNLKFMVQELKSGKSIWFAPDQDFGRKGTIFAPFFSVKnSSTSKGTSILAQLSKSPTLTVTLLRN 244
Cdd:PRK05646 166 RGRERHNLDstAIEREDVRGMLKLLRAGRAIWYAPDQDYGAKQSIFVPLFGIP-AATVTATTKFARLGRARVIPFTQKRL 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490380420 245 KSGANYDLVLGKEILEYPSSDALQDATIINSILEVEIMKAPEQYLWAHRRFKTRPEGEVSLY 306
Cdd:PRK05646 245 ADGSGYRLVIHPPLEDFPGESEEADCLRINQWVERVVRECPEQYLWAHRRFKSRPEGEPKLY 306
|
|
| Lip_A_acyltrans |
pfam03279 |
Bacterial lipid A biosynthesis acyltransferase; |
6-297 |
7.25e-88 |
|
Bacterial lipid A biosynthesis acyltransferase;
Pssm-ID: 281296 [Multi-domain] Cd Length: 294 Bit Score: 264.59 E-value: 7.25e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 6 PFSLKLVHPKYVVTWVGVFILFLLVQLPYKWQMWLGAFLGSNSRYFIKRRVSIIKRNLELCFPNKNKNEIDTLVNDNLKS 85
Cdd:pfam03279 2 KFSPELLHPRYWLDWLGIAVLRLLALLPYSALRRIGKGLGRLAGRFLKRRRKIARRNLALCFPEMSEAEREQIIDKSFAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 86 LGIALFETGIAWFWSDKKVKKLFQVKGMSNYLDAIAKNKGVIIVGVHFMSLELGGRIMGLCFP-VNAMYRPHNNKAMEYI 164
Cdd:pfam03279 82 VGRAIVETGRVWFWPDSRIAKRFEVIGLEHIKEALAQGRGAILVGPHFGNWDLGGRVLGQQYPgMAVYRPNLKNPLLDWL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 165 QTKGRCRSGKGMIDRKN-LKFMVQELKSGKSIWFAPDQDFGRKGTIFAPFFSVKNSSTSkGTSILAQLSKSPTLTVTLLR 243
Cdd:pfam03279 162 QTSGRERFGGRMLPRQNgIKGLIKALRKGEVVWYLPDQDLGRKDSVFVPFFGVPAATTT-GPAKLALKTKAAVIPVFPIR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 490380420 244 NKSGANYDLVLGKEILEYPSSDALQDATIINSILEVEIMKAPEQYLWAHRRFKT 297
Cdd:pfam03279 241 NGDGSGYTVIVHPALDLTITDDVEQIAQAMNQIVEKFIMPAPEQYFWLHRRWKT 294
|
|
| PRK08733 |
PRK08733 |
LpxL/LpxP family Kdo(2)-lipid IV(A) lauroyl/palmitoleoyl acyltransferase; |
11-306 |
3.44e-63 |
|
LpxL/LpxP family Kdo(2)-lipid IV(A) lauroyl/palmitoleoyl acyltransferase;
Pssm-ID: 181542 [Multi-domain] Cd Length: 306 Bit Score: 202.06 E-value: 3.44e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 11 LVHPKYVVTWVGVFILFLLVQLPYKWQMWLGAFLGSNSRYFIKRRVSIIKRNLELCFPNKNKNEIDTLVNDNLKSLGIAL 90
Cdd:PRK08733 13 LRNPKHWPMYLGLAVMVLAARLPWTLQRALGRGVGWVAMRLAGTRRRAAEVNLKLCFPEQDDAWRARLLRDSFDALGVGL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 91 FETGIAWFWSDKKVKKLFQVKGMSNYLDAIAKNKGVIIVGVHFMSLELGGRIMGLCFPVNAMYRPHNNKAMEYIQTKGRC 170
Cdd:PRK08733 93 FEFARAWWGSIDVIRPGVQIEGLEHLQQLQQQGRGVLLVSGHFMTLEMCGRLLCDHVPLAGMYRRHRNPVFEWAVKRGRL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 171 RSGKGMIDRKNLKFMVQELKSGKSIWFAPDQDFGRKGTIFAPFFSVKnSSTSKGTSILAQLSKSPtlTVTLLRNKSGANY 250
Cdd:PRK08733 173 RYATHMFANEDLRATIKHLKRGGFLWYAPDQDMRGKDTVFVPFFGHP-ASTITATHQLARLTGCA--VVPYFHRREGGRY 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 490380420 251 DLVLGKEILEYPSSDALQDATIINSILEVEIMKAPEQYLWAHRRFKTRPEGEVSLY 306
Cdd:PRK08733 250 VLKIAPPLADFPSDDVIADTTRVNAAIEDMVREAPDQYLWIHRRFKRQPGGRSDFY 305
|
|
| LPLAT_LABLAT-like |
cd07984 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LABLAT-like; ... |
105-296 |
1.04e-62 |
|
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: 196.67 E-value: 1.04e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 105 KKLFQVKGMSNYLDAIAKNKGVIIVGVHFMSLELGGRIMGLC-FPVNAMYRPHNNKAMEYIQTKGRCRSGKGMIDRKN-L 182
Cdd:cd07984 1 LKRVEREGLEHLEAALAKGKGVILLTAHFGNWELAGLALALLgYPVTVVYRPLKNPLLDRLITRGRERFGARLIPRGGgL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 183 KFMVQELKSGKSIWFAPDQDFGRKGTIFAPFFSVKnSSTSKGTSILAQLSKSPTLTVTLLRNKsGANYDLVLGKEILEYP 262
Cdd:cd07984 81 RELIRALKKGEIVGILPDQDPGRKGGVFVPFFGRP-AATPTGPARLALKTGAPVVPAFAYRLP-GGGYRIEFEPPLENPP 158
|
170 180 190
....*....|....*....|....*....|....
gi 490380420 263 SSDALQDATIINSILEVEIMKAPEQYLWAHRRFK 296
Cdd:cd07984 159 SEDVEEDTQRLNDALEAAIREHPEQWLWFHRRWK 192
|
|
| lipid_A_msbB |
TIGR02208 |
lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; This family consists of MsbB ... |
7-306 |
1.13e-52 |
|
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: 174.61 E-value: 1.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 7 FSLKLVHPKYVVTWVGVFILFLLVQLPYKWQMWLGAFLGSNSRYFIKRRVSIIKRNLELCFPNKNKNEIDTLVNDNLKSL 86
Cdd:TIGR02208 5 FQKSFLHPKYWGTWLGVFALVLLAFMPAKLRDPIAKVLAKFVGPIAKKPRGRARINLSACFPEKSEAERETIIDNNFATF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 87 GIALFETGIAWFWSDKKVKKLFQVKGMSNYLDAIAKNKGVIIVGVHFMSLELGGRIM-GLCFPVNAMYRPHNNKAMEYIQ 165
Cdd:TIGR02208 85 VQVMLSQAELAIRSKAHLRRRVNLMGLEHIEAAQAAGKPVIFLVPHGWAIDYAGLRLaSQGLPMVTMFNNHKNPLFDWLW 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 166 TKGRCRSGKGMIDRKN-LKFMVQELKSGKSIWFAPDQDFGRKGTIFAPFFSVKNSsTSKGTSILAQLSKSPTLTVTLLRN 244
Cdd:TIGR02208 165 NRVRSRFGGHVYAREAgIKALLASLKRGESGYYLPDEDHGPEQSVFVPFFATYKA-TLPVVGRLAKAGNAQVVPVFPGYN 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490380420 245 KSGANYDLVLGKEILEYPSSDALQDATIINSILEVEIMKAPEQYLWAHRRFKTRPEGEVSLY 306
Cdd:TIGR02208 244 QVTGKFELTVRPAMATELSVDPEQEARAMNKEVEQFILPYPEQYMWILRLLKTRPDGEASIY 305
|
|
| PRK06946 |
PRK06946 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
19-306 |
1.49e-48 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 180770 [Multi-domain] Cd Length: 293 Bit Score: 163.70 E-value: 1.49e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 19 TWVGVFILFLLVQLPYKWQMWLGAFLGSNSRYFIKRRVSIIKRNLELCFPNKNKNEIDTLVNDNLKSLGIALFETGIAWF 98
Cdd:PRK06946 6 TALAIGLLKLLAFLPYGLTARFGDGLGWLLYRIPSRRRRIVHTNLKLCFPDWSDARREELARRHFRHVIRSYVERSVQWF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 99 WSDKKVKKLFQVKGMSNyLDAIAKnKGVIIVGVHFMSLELGG--RIMGLCFPVNAMYRPHNNKAMEYIQTKGRCRSGKGM 176
Cdd:PRK06946 86 GSEKKLEKLVQVDSAID-LTDPDG-PPTIFLGLHFVGIEAGSiwLNYSLRRRVGSLYTPMSNPLLDAIAKAARGRFGAEM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 177 IDR-KNLKFMVQELKSGKSIWFAPDQDFGRKGTIFAPFFSVKnSSTSKGTSILAQLSKSPTLTVT--LLRNKSGanYDLV 253
Cdd:PRK06946 164 VSRaDSARQVLRWLRDGKPVMLGADMDFGLRDSTFVPFFGVP-ACTLTAVSRLARTGGAQVVPFIteVLPDYKG--YRLR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 490380420 254 LGKEILEYPSSDALQDATIINSILEVEIMKAPEQYLWAHRRFKTRPEGEVSLY 306
Cdd:PRK06946 241 VFKPWENYPTGDDDLDARRMNAFLEEQIRLMPEQYYWVHKRFKTRPPGEPSVY 293
|
|
| PRK08706 |
PRK08706 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
24-306 |
2.55e-48 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 169557 [Multi-domain] Cd Length: 289 Bit Score: 163.11 E-value: 2.55e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 24 FILFLLVQLPYKWQMWLGAFLGSNSRYFIKRRVSIIKRNLELCFPNKNKNEIDTLVNDNLKSLGIALFETGIAWFWSDKK 103
Cdd:PRK08706 6 FVLYVLQFLPFALLHKLADLTGLLAYLLVKPRRRIGEINLAKCFPEWDEEKRKTVLKQHFKHMAKLMLEYGLYWYAPAGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 104 VKKLFQVKGMSNYLDAIAKNKGVIIVGVHFMSLELGGRIMGLCFPVNAMYRPHNNKAMEYIQTKGRCRSGKGMI--DRKN 181
Cdd:PRK08706 86 LKSLVRYRNKHYLDDALAAGEKVIILYPHFTAFEMAVYALNQDVPLISMYSHQKNKILDEQILKGRNRYHNVFLigRTEG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 182 LKFMVQEL-KSGKSIWFAPDQDFGRKGTIFAPFFSVKnSSTSKGTSILAQLSKSPTLTVtLLRNKSGANYDLVLGKEILE 260
Cdd:PRK08706 166 LRALVKQFrKSSAPFLYLPDQDFGRNDSVFVDFFGIQ-TATITGLSRIAALANAKVIPA-IPVREADNTVTLHFYPAWDS 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 490380420 261 YPSSDALQDATIINSILEVEIMKAPEQYLWAHRRFKTRPEGEVSLY 306
Cdd:PRK08706 244 FPSEDAQADAQRMNRFIEERVREHPEQYFWLHKRFKTRPEGSPDFY 289
|
|
| PRK08943 |
PRK08943 |
lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; Validated |
7-302 |
2.10e-42 |
|
lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; Validated
Pssm-ID: 236355 Cd Length: 314 Bit Score: 148.09 E-value: 2.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 7 FSLKLVHPKYVVTWVGVFILFLLVQLPYKWQMWLGAFLGsnsRYFIKRRVSIIKR---NLELCFPNKNKNEIDTLVNDNL 83
Cdd:PRK08943 14 FQKSFLHPRYWGTWLGIGALAGLALMPPRLRDPLAAKLG---RLVGKLAKKARRRariNLSLCFPEKSEAEREAIIDEMF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 84 KSLGIALFETGIAWFWSDKKVKKLFQVKGMSNYLDAIAKNKGVIIVGVHFMSLELGGRIM---GLcfPVNAMYRPHNNKA 160
Cdd:PRK08943 91 ATAPQAMLMMAELALRSPKHLQRRVEWHGLEILEEARANGENVIFLVPHGWAIDIPAMLLasqGQ--PMAAMFHNQRNPL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 161 MEYIQTKGRCRSGKGMIDRKN-LKFMVQELKSGKSIWFAPDQDFGRKGTIFAPFF-SVKnsSTSKGTSILAQLSKSPTLT 238
Cdd:PRK08943 169 FDWLWNRVRRRFGGRLHAREDgIKPFISSVRQGYWGYYLPDEDHGPEHSVFVDFFaTYK--ATLPGIGRLAKVCRARVVP 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490380420 239 VTLLRNKSGANYDLVLGKEILEYPSSDALQDATIINSILEVEIMKAPEQYLWAHRRFKTRPEGE 302
Cdd:PRK08943 247 LFPVYNGKTHRLDIEIRPPMDDLLSADDETIARRMNEEVEQFVGPHPEQYMWILKLLKTRKPGE 310
|
|
| PRK05645 |
PRK05645 |
lysophospholipid acyltransferase; |
21-306 |
5.85e-28 |
|
lysophospholipid acyltransferase;
Pssm-ID: 135493 [Multi-domain] Cd Length: 295 Bit Score: 109.61 E-value: 5.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 21 VGVFILFLLvqLPYKWQMWLGAFLGSNSRYFIKRRVSIIKRNLELCFPNKNKNEIDTLVNDNLKSLGIALFETGIAWFWS 100
Cdd:PRK05645 10 VGALRLFAL--LPWRAVQGVGAGIGWLMWKLPNRSREVVRINLSKCFPELSPAELEKLVGQSLMDIGKTLTESACAWIWP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 101 DKKVKKLF-QVKGMSNYLDAIAKNKGVIIVGVHFMSLE-LGGRIMGLCFPVnAMYRPHNNKAMEYIQTKGRCRSGKGMI- 177
Cdd:PRK05645 88 PQKSLELVrEVEGLEVLEQALASGKGVVGITSHLGNWEvLNHFYCSQCKPI-IFYRPPKLKAVDELLRKQRVQLGNRVAp 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 178 -DRKNLKFMVQELKSGKSIWFAPDQDFGRKGTIFAPFFSVKnSSTSKGTSILAQLSKSPTLTVTLLRNKSGANYDLVLGK 256
Cdd:PRK05645 167 sTKEGILSVIKEVRKGGQVGIPADPEPAESAGIFVPFLGTQ-ALTSKFVPNMLAGGKAVGVFLHALRLPDGSGYKVILEA 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 490380420 257 EILEYPSSDALQDATIINSILEVEIMKAPEQYLWAHRRFKTRPEGEVSLY 306
Cdd:PRK05645 246 APEDMYSTDVEVSAAAMSKVVERYVRAYPSQYMWSMKRFKKRPAGEARWY 295
|
|
| PRK08905 |
PRK08905 |
lysophospholipid acyltransferase family protein; |
23-301 |
1.36e-27 |
|
lysophospholipid acyltransferase family protein;
Pssm-ID: 236348 [Multi-domain] Cd Length: 289 Bit Score: 108.54 E-value: 1.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 23 VFILFLLVQLPYKWQMWLGAFLGSNSRYFIKRRVSIIKRNLELCFPNknknEIDTLVNDNLKSLGIALFETGIAWFWS-D 101
Cdd:PRK08905 3 TFLFRLLSRLPLSWLHALGGWLGRLAYRLPGRYRRRLRANLRQAGGD----PDPAMVKAAAAETGRMILELPYVWFRKpE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 102 KKVKKLFQVKGMSNYLDAIAKNKGVIIVGVHFMSLELGGRIMGLCFPVNAMYRPHNNKAMEYIQTKGRCRSGKGMI--DR 179
Cdd:PRK08905 79 EIETMVKDDHGWEHVEAALAEGRGILFLTPHLGCFEVTARYIAQRFPLTAMFRPPRKAALRPLMEAGRARGNMRTApaTP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 180 KNLKFMVQELKSGKSIWFAPDQDFGRKGTIFAPFFSvKNSSTSKGTSILAQLSKSPTLTVTLLRNKSGANYDLVLgKEIL 259
Cdd:PRK08905 159 QGVRMLVKALRRGEAVGILPDQVPSGGEGVWAPFFG-RPAYTMTLVARLAEVTGVPVIFVAGERLPRGRGYRLHL-RPVQ 236
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 490380420 260 EYPSSDALQDATIINSILEVEIMKAPEQYLWAHRRFKtRPEG 301
Cdd:PRK08905 237 EPLPGDKAADAAVINAEIERLIRRFPTQYLWGYNRYK-RPRG 277
|
|
| PRK08419 |
PRK08419 |
lipid A biosynthesis lauroyl acyltransferase; Reviewed |
22-296 |
1.11e-22 |
|
lipid A biosynthesis lauroyl acyltransferase; Reviewed
Pssm-ID: 181420 [Multi-domain] Cd Length: 298 Bit Score: 95.48 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 22 GVFIL-FLLVQLPYKWQMWLGAFLGSNSRYFIKRRVSIIKRNLELCFP-NKNKNEIDTLVNDNLKSLGIALFETGIAWFW 99
Cdd:PRK08419 9 LFYILkFFLAKMPHCIFLRLAKALAFIMRYLDKKRRKIAKANLDFCFGeSKSQEEKKRIIKKCYENFAFFGLDFIRNQNT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 100 SDKKVKKLFQVKGMSNYLDAIAKNKGVIIVGVHFMSLELGGRIMGLCF-PVNAMYRPHNNKAMEYIQTKGRCRSGKGMID 178
Cdd:PRK08419 89 TKEEILNKVTFINEENLLDALKKKRPIIVTTAHYGYWELFSLALAAYYgAVSIVGRLLKSAPINEMISKRREQFGIELID 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 179 RKN-LKFMVQELKSGKSIWFAPDQDFGRKGTIFAPFFSvKNSSTSKGTSILAQLSKSPTLTVTlLRNKSGANYDLVLGKE 257
Cdd:PRK08419 169 KKGaMKELLKALKQGRALGILVDQNVVPKEGVEVKFFN-KRVTHTTIASILARRYNALIIPVF-IFNDDYSHFTITFFPP 246
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 490380420 258 ILEYPSSDALQD---ATIIN-SILEVEIMKAPEQYLWAHRRFK 296
Cdd:PRK08419 247 IRSKITDDAEADileATQAQaSACEEMIRKKPDEYFWFHRRFK 289
|
|
| PRK08734 |
PRK08734 |
lauroyl acyltransferase; |
28-301 |
6.41e-19 |
|
lauroyl acyltransferase;
Pssm-ID: 181543 [Multi-domain] Cd Length: 305 Bit Score: 84.93 E-value: 6.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 28 LLVQLPYKWQMWLGAFLGSNSRYFIKRRVSIIKRNLELCFPNKNKNEIDTLVNDNLKSLGIALFETGIAWFWSD-KKVKK 106
Cdd:PRK08734 16 LVGRLPWPLLKRLADLLAWSWRKLNARESRVTRRNLELAYPELSPQQRAQLHAQILRSTARQALEVLRTWTHPPaENLAR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 107 LFQVKGMSNYLDAIAKNKGVIIVGVHFMSLELGGRIMGLCFPVNAMYRPHNNKAME-YIQtkgRCRSG--------KGMI 177
Cdd:PRK08734 96 LRQRHGQELYDAALASGRGVIVAAPHFGNWELLNQWLSERGPIAIVYRPPESEAVDgFLQ---LVRGGdnvrqvraEGPA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 178 DRKNLKFmvqeLKSGKSIWFAPDQDFGRKGTIFAPFFSVknsstskgtsilaqlsksPTLTVTL---LRNKSGANY---- 250
Cdd:PRK08734 173 VRQLFKV----LKDGGAVGILPDQQPKMGDGVFAPFFGI------------------PALTMTLvnrLAERTGATVlygw 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490380420 251 ------DLVLGKEILEYPSS----DALQDATIINSILEVEIMKAPEQYLWAHRRFKTRPEG 301
Cdd:PRK08734 231 cerigpDLEFALHVQPADPAvadpDPLRAATALNAGIERIARRDPAQYQWTYKRYTLRPPG 291
|
|
| PRK06628 |
PRK06628 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
51-296 |
8.22e-04 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 102471 Cd Length: 290 Bit Score: 40.30 E-value: 8.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 51 FIKRRVSII-------KRNLELCFpnKNKNEIDTLVNDNLKSLGIALFETGIAWFWSDKKVKKLFQVKGMSNyldaIAKN 123
Cdd:PRK06628 38 FIARKVGILfavnkiaRRNIKAVF--GDMCDVEKIIDQTWDNFGRFIGEFTYVNKMDEAELERRIEIIGIEN----IKKL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 124 KG--VIIVGVHFMSLELGGRIMGLCFP-VNAMYRPHNNKAMEYIQTKGRCRSGKGMIDR--KNLKFMVQELKSGKSIWFA 198
Cdd:PRK06628 112 EGqpFLLFSGHFANWDISLKILHKFYPkVAVIYRKANNPYVNKLVNESRAGDKLRLIPKgpEGSRALVRAIKESESIVML 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490380420 199 PDQDFgrKGTIFAPFFSvKNSSTSKGTSILAQLSKSPTLTVTLLRNKsGANYDLVLGKEILEYPSSDALQDA----TIIN 274
Cdd:PRK06628 192 VDQKM--NDGIEVPFLG-HPAMTASAIAKIALQYKYPIIPCQIIRTK-GSYFKVIVHPQLKFEQTGDNKADCynimLNIN 267
|
250 260
....*....|....*....|..
gi 490380420 275 SILEVEIMKAPEQYLWAHRRFK 296
Cdd:PRK06628 268 QMLGEWVKQNPAQWFWFHNRWK 289
|
|
|