|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06860 |
PRK06860 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
1-306 |
0e+00 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 235880 [Multi-domain] Cd Length: 309 Bit Score: 648.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 1 MTNLPKFSTALLHPRYWLTWLGIGVLWLVVQLPYPVIYRLGCGLGKLALRFMKRRAKIVHRNLELCFPEMSEQERRKMVV 80
Cdd:PRK06860 3 MTNLPKFSRALLHPRYWLTWLGIGLLWLIVLLPYPVLYKLGRGLGKLALRFMKRRAKIARRNLELCFPEMSEQEREAIVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 81 KNFESVGMGLMETGMAWFWPDRRIARWTEVIGMEHIRDVQAQKRGILLVGIHFLTLELGARQFGMQEPGIGVYRPNDNPL 160
Cdd:PRK06860 83 KNFESVGMALIETGMAWFWPDWRIKRWTEVEGLEHIREVQAQGRGVLLVGVHFLTLELGARIFGMHNPGIGVYRPNDNPL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 161 IDWLQTWGRLRSNKSMLDRKDLKGMIKALKKGEVVWYAPDHDYGPRSSVFVPLFAVEQAATTTGTWMLARMSGACLVPFV 240
Cdd:PRK06860 163 YDWLQTWGRLRSNKSMLDRKDLKGMIKALKKGERIWYAPDHDYGPRSSVFVPFFAVEQAATTTGTWMLARMSKAAVIPFV 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129017 241 PRRKPDGKGYQLIMLPPECSPPLDDAETTAAWMNKVVEKCIMMAPEQYMWLHRRFKTRPEGVPSRY 306
Cdd:PRK06860 243 PRRKPDGKGYELIILPPEDSPPLDDAEATAAWMNKVVEKCILMAPEQYMWLHRRFKTRPEGVPSRY 308
|
|
| lipid_A_htrB |
TIGR02207 |
lipid A biosynthesis lauroyl (or palmitoleoyl) acyltransferase; This model represents a narrow ... |
5-306 |
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: 561.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 5 PKFSTALLHPRYWLTWLGIGVLWLVVQLPYPVIYRLGCGLGKLALRFMKRRAKIVHRNLELCFPEMSEQERRKMVVKNFE 84
Cdd:TIGR02207 1 PEFSASLLHPRYWPTWLGLGVLWLIVQLPYPVLLALGRGIGRLAMRLMKRRVHIARRNLELCFPHMSDAERERLLRENFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 85 SVGMGLMETGMAWFWPDRRIARWTEVIGMEHIRDVQAQKRGILLVGIHFLTLELGARQFGMQEPGIGVYRPNDNPLIDWL 164
Cdd:TIGR02207 81 STGMALFETGMAWFWSDARIKKWMQIEGLEHLQRAQKQGRGVLLVGVHFLTLELGARIFGQQQPGIGVYRPHNNPLFDWI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 165 QTWGRLRSNKSMLDRKDLKGMIKALKKGEVVWYAPDHDYGPRSSVFVPLFAVEQAATTTGTWMLARMSGACLVPFVPRRK 244
Cdd:TIGR02207 161 QTRGRLRSNKAMIDRKDLRGMIKALKNGERIWYAPDHDYGRKSSVFVPFFAVPDAATTTGTSILARLSKCAVVPFTPRRN 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129017 245 PDGKGYQLIMLPPECSPPLDDAETTAAWMNKVVEKCIMMAPEQYMWLHRRFKTRP-EGVPSRY 306
Cdd:TIGR02207 241 EDGSGYRLKIDPPLDDFPGDDEIAAAARMNKIVEKMIMRAPEQYMWLHRRFKTRPdEGESSLY 303
|
|
| Lip_A_acyltrans |
pfam03279 |
Bacterial lipid A biosynthesis acyltransferase; |
5-297 |
1.85e-148 |
|
Bacterial lipid A biosynthesis acyltransferase;
Pssm-ID: 281296 [Multi-domain] Cd Length: 294 Bit Score: 418.29 E-value: 1.85e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 5 PKFSTALLHPRYWLTWLGIGVLWLVVQLPYPVIYRLGCGLGKLALRFMKRRAKIVHRNLELCFPEMSEQERRKMVVKNFE 84
Cdd:pfam03279 1 PKFSPELLHPRYWLDWLGIAVLRLLALLPYSALRRIGKGLGRLAGRFLKRRRKIARRNLALCFPEMSEAEREQIIDKSFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 85 SVGMGLMETGMAWFWPDRRIARWTEVIGMEHIRDVQAQKRGILLVGIHFLTLELGARQFGMQEPGIGVYRPND-NPLIDW 163
Cdd:pfam03279 81 SVGRAIVETGRVWFWPDSRIAKRFEVIGLEHIKEALAQGRGAILVGPHFGNWDLGGRVLGQQYPGMAVYRPNLkNPLLDW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 164 LQTWGRLRSNKSMLDRKD-LKGMIKALKKGEVVWYAPDHDYGPRSSVFVPLFAVEQAATTTGTWMLARMSgACLVPFVPR 242
Cdd:pfam03279 161 LQTSGRERFGGRMLPRQNgIKGLIKALRKGEVVWYLPDQDLGRKDSVFVPFFGVPAATTTGPAKLALKTK-AAVIPVFPI 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 16129017 243 RKPDGKGYQLIMLPPECSPPLDDAETTAAWMNKVVEKCIMMAPEQYMWLHRRFKT 297
Cdd:pfam03279 240 RNGDGSGYTVIVHPALDLTITDDVEQIAQAMNQIVEKFIMPAPEQYFWLHRRWKT 294
|
|
| LpxP |
COG1560 |
Palmitoleoyl-ACP: Kdo2-lipid-IV acyltransferase (lipid A biosynthesis) [Lipid transport and ... |
25-295 |
2.06e-116 |
|
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: 336.01 E-value: 2.06e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 25 VLWLVVQLPYPVIYRLGCGLGKLALRFMKRRAKIVHRNLELCFPEMSEQERRKMVVKNFESVGMGLMETGMAWFWPDRRI 104
Cdd:COG1560 1 LLRLLRLLPLRLLYRLGDLLGRLLYRLAGRRRRVARRNLALAFPELSEAEREALARASFRNLGRTLLETLRLWRLSPERL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 105 ARWTEVIGMEHIRDVQAQKRGILLVGIHFLTLELGARQFGMQE-PGIGVYRPNDNPLIDWLQTWGRLRSNKSMLDRKD-L 182
Cdd:COG1560 81 RKRVEVEGLEHLEAALAEGRGVILLTPHFGNWELAGAALALRGyPVTAVYRPLKNPLLDRLIRRGRERFGGELIPRKDgV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 183 KGMIKALKKGEVVWYAPDHDYGPRSSVFVPLFAVEqAATTTGTWMLARMSGACLVPFVPRRKPDGKGYQLIMLPPEcSPP 262
Cdd:COG1560 161 RALLRALRKGGIVGLLPDQDPGRKSGVFVPFFGVP-AATPTGPARLARRTGAPVVPVFARRLPDGRGYRLEIEPPL-EDF 238
|
250 260 270
....*....|....*....|....*....|...
gi 16129017 263 LDDAETTAAWMNKVVEKCIMMAPEQYMWLHRRF 295
Cdd:COG1560 239 SEDVEADTQRLNRALEAWIREHPEQWLWLHRRW 271
|
|
| LPLAT_LABLAT-like |
cd07984 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LABLAT-like; ... |
106-296 |
3.04e-69 |
|
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: 213.23 E-value: 3.04e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 106 RWTEVIGMEHIRDVQAQKRGILLVGIHFLTLELGARQFGMQE-PGIGVYRPNDNPLIDWLQTWGRLRSNKSMLDRKD-LK 183
Cdd:cd07984 2 KRVEREGLEHLEAALAKGKGVILLTAHFGNWELAGLALALLGyPVTVVYRPLKNPLLDRLITRGRERFGARLIPRGGgLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 184 GMIKALKKGEVVWYAPDHDYGPRSSVFVPlFAVEQAATTTGTWMLARMSGACLVPFVPRRKPDGkGYQLIMLPPECSPPL 263
Cdd:cd07984 82 ELIRALKKGEIVGILPDQDPGRKGGVFVP-FFGRPAATPTGPARLALKTGAPVVPAFAYRLPGG-GYRIEFEPPLENPPS 159
|
170 180 190
....*....|....*....|....*....|...
gi 16129017 264 DDAETTAAWMNKVVEKCIMMAPEQYMWLHRRFK 296
Cdd:cd07984 160 EDVEEDTQRLNDALEAAIREHPEQWLWFHRRWK 192
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06860 |
PRK06860 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
1-306 |
0e+00 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 235880 [Multi-domain] Cd Length: 309 Bit Score: 648.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 1 MTNLPKFSTALLHPRYWLTWLGIGVLWLVVQLPYPVIYRLGCGLGKLALRFMKRRAKIVHRNLELCFPEMSEQERRKMVV 80
Cdd:PRK06860 3 MTNLPKFSRALLHPRYWLTWLGIGLLWLIVLLPYPVLYKLGRGLGKLALRFMKRRAKIARRNLELCFPEMSEQEREAIVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 81 KNFESVGMGLMETGMAWFWPDRRIARWTEVIGMEHIRDVQAQKRGILLVGIHFLTLELGARQFGMQEPGIGVYRPNDNPL 160
Cdd:PRK06860 83 KNFESVGMALIETGMAWFWPDWRIKRWTEVEGLEHIREVQAQGRGVLLVGVHFLTLELGARIFGMHNPGIGVYRPNDNPL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 161 IDWLQTWGRLRSNKSMLDRKDLKGMIKALKKGEVVWYAPDHDYGPRSSVFVPLFAVEQAATTTGTWMLARMSGACLVPFV 240
Cdd:PRK06860 163 YDWLQTWGRLRSNKSMLDRKDLKGMIKALKKGERIWYAPDHDYGPRSSVFVPFFAVEQAATTTGTWMLARMSKAAVIPFV 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129017 241 PRRKPDGKGYQLIMLPPECSPPLDDAETTAAWMNKVVEKCIMMAPEQYMWLHRRFKTRPEGVPSRY 306
Cdd:PRK06860 243 PRRKPDGKGYELIILPPEDSPPLDDAEATAAWMNKVVEKCILMAPEQYMWLHRRFKTRPEGVPSRY 308
|
|
| lipid_A_htrB |
TIGR02207 |
lipid A biosynthesis lauroyl (or palmitoleoyl) acyltransferase; This model represents a narrow ... |
5-306 |
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: 561.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 5 PKFSTALLHPRYWLTWLGIGVLWLVVQLPYPVIYRLGCGLGKLALRFMKRRAKIVHRNLELCFPEMSEQERRKMVVKNFE 84
Cdd:TIGR02207 1 PEFSASLLHPRYWPTWLGLGVLWLIVQLPYPVLLALGRGIGRLAMRLMKRRVHIARRNLELCFPHMSDAERERLLRENFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 85 SVGMGLMETGMAWFWPDRRIARWTEVIGMEHIRDVQAQKRGILLVGIHFLTLELGARQFGMQEPGIGVYRPNDNPLIDWL 164
Cdd:TIGR02207 81 STGMALFETGMAWFWSDARIKKWMQIEGLEHLQRAQKQGRGVLLVGVHFLTLELGARIFGQQQPGIGVYRPHNNPLFDWI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 165 QTWGRLRSNKSMLDRKDLKGMIKALKKGEVVWYAPDHDYGPRSSVFVPLFAVEQAATTTGTWMLARMSGACLVPFVPRRK 244
Cdd:TIGR02207 161 QTRGRLRSNKAMIDRKDLRGMIKALKNGERIWYAPDHDYGRKSSVFVPFFAVPDAATTTGTSILARLSKCAVVPFTPRRN 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129017 245 PDGKGYQLIMLPPECSPPLDDAETTAAWMNKVVEKCIMMAPEQYMWLHRRFKTRP-EGVPSRY 306
Cdd:TIGR02207 241 EDGSGYRLKIDPPLDDFPGDDEIAAAARMNKIVEKMIMRAPEQYMWLHRRFKTRPdEGESSLY 303
|
|
| PRK08025 |
PRK08025 |
kdo(2)-lipid IV(A) palmitoleoyltransferase; |
1-306 |
7.34e-163 |
|
kdo(2)-lipid IV(A) palmitoleoyltransferase;
Pssm-ID: 181200 Cd Length: 305 Bit Score: 455.35 E-value: 7.34e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 1 MTNLPKFSTALLHPRYWLTWLGIGVLWLVVQLPYPVIYRLGCGLGKLALRFMKRRAKIVHRNLELCFPEMSEQERRKMVV 80
Cdd:PRK08025 1 MFPQQKFSREFLHPRYWLTWFGLGVLWLLVQLPYPVLCFLGTRIGRMSRPFLKRRESIARKNLELCFPQMSAEEREKMIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 81 KNFESVGMGLMETGMAWFWPDRRIARWTEVIGMEHIRDVQAQKRGILLVGIHFLTLELGARQFGMQEPGIGVYRPNDNPL 160
Cdd:PRK08025 81 ENFRSLGMALLETGMAWFWPDSRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLCQPMMATYRPHNNKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 161 IDWLQTWGRLRSNKSMLDRKDLKGMIKALKKGEVVWYAPDHDYGPRSSVFVPLFAVEQAATTTGTWMLARMSGACLVPFV 240
Cdd:PRK08025 161 MEWVQTRGRMRSNKAMIGRNNLRGIVGALKKGEAVWFAPDQDYGPKGSSFAPFFAVENVATTNGTYVLSRLSGAAMLTVT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129017 241 PRRKPDGKGYQLIMLPPECSPPlDDAETTAAWMNKVVEKCIMMAPEQYMWLHRRFKTRPEGVPSRY 306
Cdd:PRK08025 241 MVRKADYSGYRLFITPEMEGYP-TDENQAAAYMNKIIEKEIMRAPEQYLWIHRRFKTRPVGESSLY 305
|
|
| Lip_A_acyltrans |
pfam03279 |
Bacterial lipid A biosynthesis acyltransferase; |
5-297 |
1.85e-148 |
|
Bacterial lipid A biosynthesis acyltransferase;
Pssm-ID: 281296 [Multi-domain] Cd Length: 294 Bit Score: 418.29 E-value: 1.85e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 5 PKFSTALLHPRYWLTWLGIGVLWLVVQLPYPVIYRLGCGLGKLALRFMKRRAKIVHRNLELCFPEMSEQERRKMVVKNFE 84
Cdd:pfam03279 1 PKFSPELLHPRYWLDWLGIAVLRLLALLPYSALRRIGKGLGRLAGRFLKRRRKIARRNLALCFPEMSEAEREQIIDKSFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 85 SVGMGLMETGMAWFWPDRRIARWTEVIGMEHIRDVQAQKRGILLVGIHFLTLELGARQFGMQEPGIGVYRPND-NPLIDW 163
Cdd:pfam03279 81 SVGRAIVETGRVWFWPDSRIAKRFEVIGLEHIKEALAQGRGAILVGPHFGNWDLGGRVLGQQYPGMAVYRPNLkNPLLDW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 164 LQTWGRLRSNKSMLDRKD-LKGMIKALKKGEVVWYAPDHDYGPRSSVFVPLFAVEQAATTTGTWMLARMSgACLVPFVPR 242
Cdd:pfam03279 161 LQTSGRERFGGRMLPRQNgIKGLIKALRKGEVVWYLPDQDLGRKDSVFVPFFGVPAATTTGPAKLALKTK-AAVIPVFPI 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 16129017 243 RKPDGKGYQLIMLPPECSPPLDDAETTAAWMNKVVEKCIMMAPEQYMWLHRRFKT 297
Cdd:pfam03279 240 RNGDGSGYTVIVHPALDLTITDDVEQIAQAMNQIVEKFIMPAPEQYFWLHRRWKT 294
|
|
| LpxP |
COG1560 |
Palmitoleoyl-ACP: Kdo2-lipid-IV acyltransferase (lipid A biosynthesis) [Lipid transport and ... |
25-295 |
2.06e-116 |
|
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: 336.01 E-value: 2.06e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 25 VLWLVVQLPYPVIYRLGCGLGKLALRFMKRRAKIVHRNLELCFPEMSEQERRKMVVKNFESVGMGLMETGMAWFWPDRRI 104
Cdd:COG1560 1 LLRLLRLLPLRLLYRLGDLLGRLLYRLAGRRRRVARRNLALAFPELSEAEREALARASFRNLGRTLLETLRLWRLSPERL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 105 ARWTEVIGMEHIRDVQAQKRGILLVGIHFLTLELGARQFGMQE-PGIGVYRPNDNPLIDWLQTWGRLRSNKSMLDRKD-L 182
Cdd:COG1560 81 RKRVEVEGLEHLEAALAEGRGVILLTPHFGNWELAGAALALRGyPVTAVYRPLKNPLLDRLIRRGRERFGGELIPRKDgV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 183 KGMIKALKKGEVVWYAPDHDYGPRSSVFVPLFAVEqAATTTGTWMLARMSGACLVPFVPRRKPDGKGYQLIMLPPEcSPP 262
Cdd:COG1560 161 RALLRALRKGGIVGLLPDQDPGRKSGVFVPFFGVP-AATPTGPARLARRTGAPVVPVFARRLPDGRGYRLEIEPPL-EDF 238
|
250 260 270
....*....|....*....|....*....|...
gi 16129017 263 LDDAETTAAWMNKVVEKCIMMAPEQYMWLHRRF 295
Cdd:COG1560 239 SEDVEADTQRLNRALEAWIREHPEQWLWLHRRW 271
|
|
| PRK05646 |
PRK05646 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
5-306 |
1.32e-113 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 235543 [Multi-domain] Cd Length: 310 Bit Score: 330.62 E-value: 1.32e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 5 PKFSTALLHPRYWLTWLGIGVLWLVVQLPYPVIYRLGCGLGKLALRFMKRRAKIVHRNLELCFPEMSEQERRKMVVKNFE 84
Cdd:PRK05646 4 PRFRAAFLHPRFWPLWLGLGLLWLVVQLPYRVLLWLGRALGALMYRLAGSRRRIAARNLELCFPEKSAAERERLLKENFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 85 SVGMGLMETGMAWFWPDRRIARWTEVIGMEHIRDVQAQKRGILLVGIHFLTLELGARQFGMQEPGIGVYRPNDNPLIDWL 164
Cdd:PRK05646 84 STGIAFFEMAMSWWWPKARLARLAHIEGLEHLQQAQQEGQGVILMALHFTTLEIGAALLGQQHTIDGMYREHKNPVFDFI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 165 QTWGRLRSNKSML--DRKDLKGMIKALKKGEVVWYAPDHDYGPRSSVFVPLFAVeQAATTTGTWMLARMSGACLVPFVPR 242
Cdd:PRK05646 164 QRRGRERHNLDSTaiEREDVRGMLKLLRAGRAIWYAPDQDYGAKQSIFVPLFGI-PAATVTATTKFARLGRARVIPFTQK 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129017 243 RKPDGKGYQLIMLPPECSPPLDDAETTAAWMNKVVEKCIMMAPEQYMWLHRRFKTRPEGVPSRY 306
Cdd:PRK05646 243 RLADGSGYRLVIHPPLEDFPGESEEADCLRINQWVERVVRECPEQYLWAHRRFKSRPEGEPKLY 306
|
|
| PRK08733 |
PRK08733 |
LpxL/LpxP family Kdo(2)-lipid IV(A) lauroyl/palmitoleoyl acyltransferase; |
10-306 |
6.22e-78 |
|
LpxL/LpxP family Kdo(2)-lipid IV(A) lauroyl/palmitoleoyl acyltransferase;
Pssm-ID: 181542 [Multi-domain] Cd Length: 306 Bit Score: 239.81 E-value: 6.22e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 10 ALLHPRYWLTWLGIGVLWLVVQLPYPVIYRLGCGLGKLALRFMKRRAKIVHRNLELCFPEMSEQERRKMVVKNFESVGMG 89
Cdd:PRK08733 12 SLRNPKHWPMYLGLAVMVLAARLPWTLQRALGRGVGWVAMRLAGTRRRAAEVNLKLCFPEQDDAWRARLLRDSFDALGVG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 90 LMETGMAWFWPDRRIARWTEVIGMEHIRDVQAQKRGILLVGIHFLTLELGARQFGMQEPGIGVYRPNDNPLIDWLQTWGR 169
Cdd:PRK08733 92 LFEFARAWWGSIDVIRPGVQIEGLEHLQQLQQQGRGVLLVSGHFMTLEMCGRLLCDHVPLAGMYRRHRNPVFEWAVKRGR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 170 LRSNKSMLDRKDLKGMIKALKKGEVVWYAPDHDYGPRSSVFVPLFAVEqAATTTGTWMLARMSGACLVPFVPRRkpDGKG 249
Cdd:PRK08733 172 LRYATHMFANEDLRATIKHLKRGGFLWYAPDQDMRGKDTVFVPFFGHP-ASTITATHQLARLTGCAVVPYFHRR--EGGR 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 16129017 250 YQLIMLPPECSPPLDDAETTAAWMNKVVEKCIMMAPEQYMWLHRRFKTRPEGVPSRY 306
Cdd:PRK08733 249 YVLKIAPPLADFPSDDVIADTTRVNAAIEDMVREAPDQYLWIHRRFKRQPGGRSDFY 305
|
|
| PRK06946 |
PRK06946 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
19-306 |
9.32e-73 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 180770 [Multi-domain] Cd Length: 293 Bit Score: 226.10 E-value: 9.32e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 19 TWLGIGVLWLVVQLPYPVIYRLGCGLGKLALRFMKRRAKIVHRNLELCFPEMSEQERRKMVVKNFESVGMGLMETGMAWF 98
Cdd:PRK06946 6 TALAIGLLKLLAFLPYGLTARFGDGLGWLLYRIPSRRRRIVHTNLKLCFPDWSDARREELARRHFRHVIRSYVERSVQWF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 99 WPDRRIARWTEVIGMEHIRDVQAQKRgiLLVGIHFLTLELGARQ--FGMQEPGIGVYRPNDNPLIDWLQTWGRLRSNKSM 176
Cdd:PRK06946 86 GSEKKLEKLVQVDSAIDLTDPDGPPT--IFLGLHFVGIEAGSIWlnYSLRRRVGSLYTPMSNPLLDAIAKAARGRFGAEM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 177 LDRKD-LKGMIKALKKGEVVWYAPDHDYGPRSSVFVPLFAVeQAATTTGTWMLARMSGACLVPFVPRRKPDGKGYQLIML 255
Cdd:PRK06946 164 VSRADsARQVLRWLRDGKPVMLGADMDFGLRDSTFVPFFGV-PACTLTAVSRLARTGGAQVVPFITEVLPDYKGYRLRVF 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 16129017 256 PPECSPPLDDAETTAAWMNKVVEKCIMMAPEQYMWLHRRFKTRPEGVPSRY 306
Cdd:PRK06946 243 KPWENYPTGDDDLDARRMNAFLEEQIRLMPEQYYWVHKRFKTRPPGEPSVY 293
|
|
| LPLAT_LABLAT-like |
cd07984 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LABLAT-like; ... |
106-296 |
3.04e-69 |
|
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: 213.23 E-value: 3.04e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 106 RWTEVIGMEHIRDVQAQKRGILLVGIHFLTLELGARQFGMQE-PGIGVYRPNDNPLIDWLQTWGRLRSNKSMLDRKD-LK 183
Cdd:cd07984 2 KRVEREGLEHLEAALAKGKGVILLTAHFGNWELAGLALALLGyPVTVVYRPLKNPLLDRLITRGRERFGARLIPRGGgLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 184 GMIKALKKGEVVWYAPDHDYGPRSSVFVPlFAVEQAATTTGTWMLARMSGACLVPFVPRRKPDGkGYQLIMLPPECSPPL 263
Cdd:cd07984 82 ELIRALKKGEIVGILPDQDPGRKGGVFVP-FFGRPAATPTGPARLALKTGAPVVPAFAYRLPGG-GYRIEFEPPLENPPS 159
|
170 180 190
....*....|....*....|....*....|...
gi 16129017 264 DDAETTAAWMNKVVEKCIMMAPEQYMWLHRRFK 296
Cdd:cd07984 160 EDVEEDTQRLNDALEAAIREHPEQWLWFHRRWK 192
|
|
| PRK08943 |
PRK08943 |
lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; Validated |
5-301 |
3.57e-63 |
|
lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; Validated
Pssm-ID: 236355 Cd Length: 314 Bit Score: 202.02 E-value: 3.57e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 5 PKFSTALLHPRYWLTWLGIGVLWLVVQLPYPVIYRLGCGLGKLALRFMK---RRAKIvhrNLELCFPEMSEQERRKMVVK 81
Cdd:PRK08943 12 PRFQKSFLHPRYWGTWLGIGALAGLALMPPRLRDPLAAKLGRLVGKLAKkarRRARI---NLSLCFPEKSEAEREAIIDE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 82 NFESVGMGLMETGMAWFWPDRRIARWTEVIGMEHIRDVQAQKRG-ILLV----GIHFLTLELGARqfGMqePGIGVYRPN 156
Cdd:PRK08943 89 MFATAPQAMLMMAELALRSPKHLQRRVEWHGLEILEEARANGENvIFLVphgwAIDIPAMLLASQ--GQ--PMAAMFHNQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 157 DNPLIDWLQTWGRLRSNKSMLDRKD-LKGMIKALKKGEVVWYAPDHDYGPRSSVFVPLFAVEQAaTTTGTWMLARMSGAC 235
Cdd:PRK08943 165 RNPLFDWLWNRVRRRFGGRLHAREDgIKPFISSVRQGYWGYYLPDEDHGPEHSVFVDFFATYKA-TLPGIGRLAKVCRAR 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129017 236 LVPFVPRRKPDGKGYQLIMLPPECSPPLDDAETTAAWMNKVVEKCIMMAPEQYMWLHRRFKTRPEG 301
Cdd:PRK08943 244 VVPLFPVYNGKTHRLDIEIRPPMDDLLSADDETIARRMNEEVEQFVGPHPEQYMWILKLLKTRKPG 309
|
|
| lipid_A_msbB |
TIGR02208 |
lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; This family consists of MsbB ... |
5-306 |
1.16e-62 |
|
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: 200.42 E-value: 1.16e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 5 PKFSTALLHPRYWLTWLGIGVLWLVVQLPYPVIYRLGCGLGKLALRFMKRRAKIVHRNLELCFPEMSEQERRKMVVKNFE 84
Cdd:TIGR02208 3 RRFQKSFLHPKYWGTWLGVFALVLLAFMPAKLRDPIAKVLAKFVGPIAKKPRGRARINLSACFPEKSEAERETIIDNNFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 85 SVGMGLMETGMAWFWPDRRIARWTEVIGMEHIRDVQAQKRGILLVGIHFLTLELGARQFGMQE-PGIGVYRPNDNPLIDW 163
Cdd:TIGR02208 83 TFVQVMLSQAELAIRSKAHLRRRVNLMGLEHIEAAQAAGKPVIFLVPHGWAIDYAGLRLASQGlPMVTMFNNHKNPLFDW 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 164 LQTWGRLRSNKSMLDRKD-LKGMIKALKKGEVVWYAPDHDYGPRSSVFVPLFAVeQAATTTGTWMLARMSGACLVPFVPR 242
Cdd:TIGR02208 163 LWNRVRSRFGGHVYAREAgIKALLASLKRGESGYYLPDEDHGPEQSVFVPFFAT-YKATLPVVGRLAKAGNAQVVPVFPG 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129017 243 RKPDGKGYQLIMLPPECSPPLDDAETTAAWMNKVVEKCIMMAPEQYMWLHRRFKTRPEGVPSRY 306
Cdd:TIGR02208 242 YNQVTGKFELTVRPAMATELSVDPEQEARAMNKEVEQFILPYPEQYMWILRLLKTRPDGEASIY 305
|
|
| PRK08706 |
PRK08706 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
25-306 |
2.05e-57 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 169557 [Multi-domain] Cd Length: 289 Bit Score: 186.61 E-value: 2.05e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 25 VLWLVVQLPYPVIYRLGCGLGKLALRFMKRRAKIVHRNLELCFPEMSEQERRKMVVKNFESVGMGLMETGMAWFWPDRRI 104
Cdd:PRK08706 7 VLYVLQFLPFALLHKLADLTGLLAYLLVKPRRRIGEINLAKCFPEWDEEKRKTVLKQHFKHMAKLMLEYGLYWYAPAGRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 105 ARWTEVIGMEHIRDVQAQKRGILLVGIHFLTLELGARQFGMQEPGIGVYRPNDNPLIDWLQTWGRLR-SNKSMLDRKD-L 182
Cdd:PRK08706 87 KSLVRYRNKHYLDDALAAGEKVIILYPHFTAFEMAVYALNQDVPLISMYSHQKNKILDEQILKGRNRyHNVFLIGRTEgL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 183 KGMIKALKKGEVVW-YAPDHDYGPRSSVFVPLFAVeQAATTTGTWMLARMSGACLVPFVPRRKPDGKgYQLIMLPPECSP 261
Cdd:PRK08706 167 RALVKQFRKSSAPFlYLPDQDFGRNDSVFVDFFGI-QTATITGLSRIAALANAKVIPAIPVREADNT-VTLHFYPAWDSF 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 16129017 262 PLDDAETTAAWMNKVVEKCIMMAPEQYMWLHRRFKTRPEGVPSRY 306
Cdd:PRK08706 245 PSEDAQADAQRMNRFIEERVREHPEQYFWLHKRFKTRPEGSPDFY 289
|
|
| PRK08905 |
PRK08905 |
lysophospholipid acyltransferase family protein; |
25-303 |
2.40e-37 |
|
lysophospholipid acyltransferase family protein;
Pssm-ID: 236348 [Multi-domain] Cd Length: 289 Bit Score: 134.35 E-value: 2.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 25 VLWLVVQLPYPVIYRLGCGLGKLALRFMKRRAKIVHRNLELCFPEMSEQERRKMVVknfeSVGMGLMEtgMAWFW---PD 101
Cdd:PRK08905 5 LFRLLSRLPLSWLHALGGWLGRLAYRLPGRYRRRLRANLRQAGGDPDPAMVKAAAA----ETGRMILE--LPYVWfrkPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 102 RRIARWTEVIGMEHIRDVQAQKRGILLVGIHFLTLELGARQFGMQEPGIGVYRPndnPLIDWLQTW---GRLRSNKSML- 177
Cdd:PRK08905 79 EIETMVKDDHGWEHVEAALAEGRGILFLTPHLGCFEVTARYIAQRFPLTAMFRP---PRKAALRPLmeaGRARGNMRTAp 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 178 -DRKDLKGMIKALKKGEVVWYAPDHDYGPRSSVFVPLFAvEQAATTTGTWMLARMSGACLVPFVPRRKPDGKGYQL-IML 255
Cdd:PRK08905 156 aTPQGVRMLVKALRRGEAVGILPDQVPSGGEGVWAPFFG-RPAYTMTLVARLAEVTGVPVIFVAGERLPRGRGYRLhLRP 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 16129017 256 PPECSPplDDAETTAAWMNKVVEKCIMMAPEQYMWLHRRFKtRPEGVP 303
Cdd:PRK08905 235 VQEPLP--GDKAADAAVINAEIERLIRRFPTQYLWGYNRYK-RPRGAP 279
|
|
| PRK05645 |
PRK05645 |
lysophospholipid acyltransferase; |
21-306 |
6.50e-36 |
|
lysophospholipid acyltransferase;
Pssm-ID: 135493 [Multi-domain] Cd Length: 295 Bit Score: 130.80 E-value: 6.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 21 LGIGVLWLVVQLPYPVIYRLGCGLGKLALRFMKRRAKIVHRNLELCFPEMSEQERRKMVVKNFESVGMGLMETGMAWFWP 100
Cdd:PRK05645 8 LMVGALRLFALLPWRAVQGVGAGIGWLMWKLPNRSREVVRINLSKCFPELSPAELEKLVGQSLMDIGKTLTESACAWIWP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 101 DRRIARWT-EVIGMEHIRDVQAQKRGILLVGIHFLTLELGARQFGMQEPGIGVYRPNDNPLIDWLQTWGRLR-SNKSMLD 178
Cdd:PRK05645 88 PQKSLELVrEVEGLEVLEQALASGKGVVGITSHLGNWEVLNHFYCSQCKPIIFYRPPKLKAVDELLRKQRVQlGNRVAPS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 179 RKD-LKGMIKALKKGEVVWYAPDHDYGPRSSVFVPLFAVEQAATTTGTWMLARmSGACLVPFVPRRKPDGKGYQLIMlpp 257
Cdd:PRK05645 168 TKEgILSVIKEVRKGGQVGIPADPEPAESAGIFVPFLGTQALTSKFVPNMLAG-GKAVGVFLHALRLPDGSGYKVIL--- 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 16129017 258 ECSPP---LDDAETTAAWMNKVVEKCIMMAPEQYMWLHRRFKTRPEGVPSRY 306
Cdd:PRK05645 244 EAAPEdmySTDVEVSAAAMSKVVERYVRAYPSQYMWSMKRFKKRPAGEARWY 295
|
|
| PRK08419 |
PRK08419 |
lipid A biosynthesis lauroyl acyltransferase; Reviewed |
28-296 |
2.24e-27 |
|
lipid A biosynthesis lauroyl acyltransferase; Reviewed
Pssm-ID: 181420 [Multi-domain] Cd Length: 298 Bit Score: 108.19 E-value: 2.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 28 LVVQLPYPVIYRLGCGLGKLALRFMKRRAKIVHRNLELCFPE-MSEQERRKMVVKNFESVGMGLMETGMAWFWPDRRIAR 106
Cdd:PRK08419 16 FLAKMPHCIFLRLAKALAFIMRYLDKKRRKIAKANLDFCFGEsKSQEEKKRIIKKCYENFAFFGLDFIRNQNTTKEEILN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 107 WTEVIGMEHIRDVQAQKRGILLVGIHFLTLELGARQFGMQEPGIG-VYRPNDNPLIDWLQTWGRLRSNKSMLDRKD-LKG 184
Cdd:PRK08419 96 KVTFINEENLLDALKKKRPIIVTTAHYGYWELFSLALAAYYGAVSiVGRLLKSAPINEMISKRREQFGIELIDKKGaMKE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 185 MIKALKKGEVVWYAPDHDYGPRSSVFVPLFAvEQAATTTGTWMLARMSGACLVPFVPRRKpDGKGYQLIMLPPECSPPLD 264
Cdd:PRK08419 176 LLKALKQGRALGILVDQNVVPKEGVEVKFFN-KRVTHTTIASILARRYNALIIPVFIFND-DYSHFTITFFPPIRSKITD 253
|
250 260 270
....*....|....*....|....*....|....*..
gi 16129017 265 DA-----ETTAAwMNKVVEKCIMMAPEQYMWLHRRFK 296
Cdd:PRK08419 254 DAeadilEATQA-QASACEEMIRKKPDEYFWFHRRFK 289
|
|
| PRK08734 |
PRK08734 |
lauroyl acyltransferase; |
28-301 |
1.24e-20 |
|
lauroyl acyltransferase;
Pssm-ID: 181543 [Multi-domain] Cd Length: 305 Bit Score: 89.94 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 28 LVVQLPYPVIYRLGCGLGKLALRFMKRRAKIVHRNLELCFPEMSEQERRKMVVKNFESVGMGLMETGMAWFWPD-RRIAR 106
Cdd:PRK08734 16 LVGRLPWPLLKRLADLLAWSWRKLNARESRVTRRNLELAYPELSPQQRAQLHAQILRSTARQALEVLRTWTHPPaENLAR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 107 WTEVIGMEHIRDVQAQKRGILLVGIHFLTLELGARQFGMQEPGIGVYRPNDNPLID-WLQtwgRLRSNKSMLDRK----D 181
Cdd:PRK08734 96 LRQRHGQELYDAALASGRGVIVAAPHFGNWELLNQWLSERGPIAIVYRPPESEAVDgFLQ---LVRGGDNVRQVRaegpA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 182 LKGMIKALKKGEVVWYAPDHDYGPRSSVFVPLFAVeQAATTTGTWMLARMSGACLVPFVPRRKPDGKGYQLIMLPPECSP 261
Cdd:PRK08734 173 VRQLFKVLKDGGAVGILPDQQPKMGDGVFAPFFGI-PALTMTLVNRLAERTGATVLYGWCERIGPDLEFALHVQPADPAV 251
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 16129017 262 PLDDAETTAAWMNKVVEKCIMMAPEQYMWLHRRFKTRPEG 301
Cdd:PRK08734 252 ADPDPLRAATALNAGIERIARRDPAQYQWTYKRYTLRPPG 291
|
|
| LPLAT |
cd06551 |
Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; ... |
101-282 |
1.03e-16 |
|
Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; Lysophospholipid acyltransferase (LPLAT) superfamily members are acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis. These proteins 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 superfamily are LPLATs such as glycerol-3-phosphate 1-acyltransferase (GPAT, PlsB), 1-acyl-sn-glycerol-3-phosphate acyltransferase (AGPAT, PlsC), lysophosphatidylcholine acyltransferase 1 (LPCAT-1), lysophosphatidylethanolamine acyltransferase (LPEAT, also known as, MBOAT2, membrane-bound O-acyltransferase domain-containing protein 2), lipid A biosynthesis lauroyl/myristoyl acyltransferase, 2-acylglycerol O-acyltransferase (MGAT), dihydroxyacetone phosphate acyltransferase (DHAPAT, also known as 1 glycerol-3-phosphate O-acyltransferase 1) and Tafazzin (the protein product of the Barth syndrome (TAZ) gene).
Pssm-ID: 153244 [Multi-domain] Cd Length: 187 Bit Score: 76.68 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 101 DRRIARWTevIGMEHIRDVQAQK----RGILLVGIHFLTLELGARQFGMQ----EPGIGVYRPNDN---PLIDWLQTWgR 169
Cdd:cd06551 1 FRYLLLNF--FGFVRLEVKGPPPppggGPVLFVSNHSSWWDGLILFLLLErglrRDVYGLMDEELLeryPFFTRLGAF-S 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 170 LRSNKSMLDRKDLKGMIKALKK-GEVVWYAPDHDYGPRSsVFVPLFAVEQAAtttgtwmLARMSGACLVPFVPRRKPDG- 247
Cdd:cd06551 78 VDRDSPRSAAKSLKYVARLLSKpGSVVWIFPEGTRTRRD-KRPLQFKPGVAH-------LAEKAGVPIVPVALRYTFELf 149
|
170 180 190
....*....|....*....|....*....|....*...
gi 16129017 248 -KGYQLIMLPPECSPPLDDA--ETTAAWMNKVVEKCIM 282
Cdd:cd06551 150 eQFPEIFVRIGPPIPYAETAlgEELAAELANRLTRLLD 187
|
|
| PRK05906 |
PRK05906 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
13-296 |
1.59e-16 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 168292 [Multi-domain] Cd Length: 454 Bit Score: 79.44 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 13 HPRYWLtwlGIGVLWLVVQLPYPVIYRLGCGLGKLALRFMKRRAKIVHRNLELCFPEMSEQERRKMVVKNFESVGMGLME 92
Cdd:PRK05906 15 HLVYYL---GLGVITILRLLPRSSLRLFGKGLGTLLFYFISDYRKTALTNLALAFPEKSFAERYQIARQSVQHVIITFLE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 93 ---------------------TGMAWFWPDrriarwtEVIGMEHIRDVQA---QKRGILLVGIHFLTLELGARQFGMQEP 148
Cdd:PRK05906 92 llaveklaghideliaiatseDAPEGFFPE-------EVSSQQELEHTFSrldEQEGAILFCGHQANWELPFLYITKRYP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 149 GIGVYRPNDNPlidwlqtwgrlRSNKSMLD-RKDLKGMI-----------KALKKGEVVWYAPDHDYgPRSSVFVPLFAv 216
Cdd:PRK05906 165 GLAFAKPIKNR-----------RLNKKIFSlRESFKGKIvppknginqalRALHQGEVVGIVGDQAL-LSSSYSYPLFG- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 217 EQAATTTGTWMLARMSGACLVPFVPRRKPdgKGYQLI---MLPPECSPPLDDAetTAAWMNKV---VEKCIMMAPEQYMW 290
Cdd:PRK05906 232 SQAFTTTSPALLAYKTGKPVIAVAIYRKP--NGYLVVpskKFYANKSLPIKES--TEQLMDRLmrfLEKGIACKPEQWMW 307
|
....*.
gi 16129017 291 LHRRFK 296
Cdd:PRK05906 308 LHKRWK 313
|
|
| PRK06553 |
PRK06553 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
15-294 |
1.06e-07 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 235827 [Multi-domain] Cd Length: 308 Bit Score: 52.28 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 15 RYWLT-WLGIGVLWLVVQLPypvIYRLGCGLGKLALRF--MKRRAKIVHRNLELCFPEMSEQERRKMVVKNFESVGMGLM 91
Cdd:PRK06553 20 AGWLVaQLVFGLLGLLRLFP---ADKAINFFGRLARLIgpLLPRHRVALDNLRAAFPEKSEAEIEAIALGMWDNLGRLGA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 92 E---TGMAW-FWPDRRIARWTEVIGMEHIRDVQAQKRGILLVGIHFLTLEL---GARQFGMqePGIGVYRPNDNPLIDWL 164
Cdd:PRK06553 97 EyafLDAIFdYDPEAPEPGRVEVRGIEIFERLRDDGKPALIFTAHLGNWELlaiAAAAFGL--DVTVLFRPPNNPYAARK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 165 ------QTWGRLRSNKSMLDRKdlkgMIKALKKGEVVWYAPDHDYgpRSSVFVPLFAVEQAATTtgtwMLARMSGACLVP 238
Cdd:PRK06553 175 vlearrTTMGGLVPSGAGAAFA----LAGVLERGGHVGMLVDQKF--TRGVEVTFFGRPVKTNP----LLAKLARQYDCP 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129017 239 FVPR---RKPDGKgYQLiMLPPECSPPLD-----DAETTAAWMNKVVEKCIMMAPEQYMWLHRR 294
Cdd:PRK06553 245 VHGArciRLPGGR-FRL-ELTERVELPRDadgqiDVQATMQALTDVVEGWVREYPGQWLWLHRR 306
|
|
| PRK06628 |
PRK06628 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
57-296 |
4.98e-06 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 102471 Cd Length: 290 Bit Score: 47.23 E-value: 4.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 57 KIVHRNLELCFPEMSEQErrKMVVKNFESVGMGLMETGMAWFWPDRRIARWTEVIGMEHIRDVQAQKrgILLVGIHFLTL 136
Cdd:PRK06628 51 KIARRNIKAVFGDMCDVE--KIIDQTWDNFGRFIGEFTYVNKMDEAELERRIEIIGIENIKKLEGQP--FLLFSGHFANW 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 137 ELGARQFGMQEPGIGV-YRPNDNPLIDWLQTWGRLRSNKSMLDR--KDLKGMIKALKKGEVVWYAPDHDYGprSSVFVPl 213
Cdd:PRK06628 127 DISLKILHKFYPKVAViYRKANNPYVNKLVNESRAGDKLRLIPKgpEGSRALVRAIKESESIVMLVDQKMN--DGIEVP- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129017 214 FAVEQAATTTGTWMLARMSGACLVPF-VPRRKpdGKGYQLIMLP----PECSPPLDDAETTAAWMNKVVEKCIMMAPEQY 288
Cdd:PRK06628 204 FLGHPAMTASAIAKIALQYKYPIIPCqIIRTK--GSYFKVIVHPqlkfEQTGDNKADCYNIMLNINQMLGEWVKQNPAQW 281
|
....*...
gi 16129017 289 MWLHRRFK 296
Cdd:PRK06628 282 FWFHNRWK 289
|
|
| |
