|
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: 634.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 1 MTKLPKFSVALLHPRYWLTWLGIGALWLVVQLPYPVIYKLGCALGHLARRVMKRRAKIAYRNLELCFPEMSAQERHTMVV 80
Cdd:PRK06860 3 MTNLPKFSRALLHPRYWLTWLGIGLLWLIVLLPYPVLYKLGRGLGKLALRFMKRRAKIARRNLELCFPEMSEQEREAIVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 81 KNFESVGMGVMETGMAWFWPDRRVNRWMEASGLEHIREVKAQGLGFILVGIHFLTLEFGARMFGMHNPGIGVYRPNDNPL 160
Cdd:PRK06860 83 KNFESVGMALIETGMAWFWPDWRIKRWTEVEGLEHIREVQAQGRGVLLVGVHFLTLELGARIFGMHNPGIGVYRPNDNPL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 161 LDWLQTWGRLRSNKSMLDRKDLKGMVKALKSGELIWYAPDHDYGPRASVFVPLFAVDQAATTSGTWMLARMSKACIIPFV 240
Cdd:PRK06860 163 YDWLQTWGRLRSNKSMLDRKDLKGMIKALKKGERIWYAPDHDYGPRSSVFVPFFAVEQAATTTGTWMLARMSKAAVIPFV 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446086118 241 PRRKPDGKGYELIILPAEYSPPLESAEATAAWMNKIVEQCIMMAPEQYMWLHRRFKTRPEGVPSRY 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: 530.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 5 PKFSVALLHPRYWLTWLGIGALWLVVQLPYPVIYKLGCALGHLARRVMKRRAKIAYRNLELCFPEMSAQERHTMVVKNFE 84
Cdd:TIGR02207 1 PEFSASLLHPRYWPTWLGLGVLWLIVQLPYPVLLALGRGIGRLAMRLMKRRVHIARRNLELCFPHMSDAERERLLRENFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 85 SVGMGVMETGMAWFWPDRRVNRWMEASGLEHIREVKAQGLGFILVGIHFLTLEFGARMFGMHNPGIGVYRPNDNPLLDWL 164
Cdd:TIGR02207 81 STGMALFETGMAWFWSDARIKKWMQIEGLEHLQRAQKQGRGVLLVGVHFLTLELGARIFGQQQPGIGVYRPHNNPLFDWI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 165 QTWGRLRSNKSMLDRKDLKGMVKALKSGELIWYAPDHDYGPRASVFVPLFAVDQAATTSGTWMLARMSKACIIPFVPRRK 244
Cdd:TIGR02207 161 QTRGRLRSNKAMIDRKDLRGMIKALKNGERIWYAPDHDYGRKSSVFVPFFAVPDAATTTGTSILARLSKCAVVPFTPRRN 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446086118 245 PDGKGYELIILPAEYSPPLESAEATAAWMNKIVEQCIMMAPEQYMWLHRRFKTRP-EGVPSRY 306
Cdd:TIGR02207 241 EDGSGYRLKIDPPLDDFPGDDEIAAAARMNKIVEKMIMRAPEQYMWLHRRFKTRPdEGESSLY 303
|
|
| Lip_A_acyltrans |
pfam03279 |
Bacterial lipid A biosynthesis acyltransferase; |
5-297 |
1.26e-135 |
|
Bacterial lipid A biosynthesis acyltransferase;
Pssm-ID: 281296 [Multi-domain] Cd Length: 294 Bit Score: 385.93 E-value: 1.26e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 5 PKFSVALLHPRYWLTWLGIGALWLVVQLPYPVIYKLGCALGHLARRVMKRRAKIAYRNLELCFPEMSAQERHTMVVKNFE 84
Cdd:pfam03279 1 PKFSPELLHPRYWLDWLGIAVLRLLALLPYSALRRIGKGLGRLAGRFLKRRRKIARRNLALCFPEMSEAEREQIIDKSFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 85 SVGMGVMETGMAWFWPDRRVNRWMEASGLEHIREVKAQGLGFILVGIHFLTLEFGARMFGMHNPGIGVYRPND-NPLLDW 163
Cdd:pfam03279 81 SVGRAIVETGRVWFWPDSRIAKRFEVIGLEHIKEALAQGRGAILVGPHFGNWDLGGRVLGQQYPGMAVYRPNLkNPLLDW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 164 LQTWGRLRSNKSMLDRKD-LKGMVKALKSGELIWYAPDHDYGPRASVFVPLFAVDQAATTSGTWMLARMsKACIIPFVPR 242
Cdd:pfam03279 161 LQTSGRERFGGRMLPRQNgIKGLIKALRKGEVVWYLPDQDLGRKDSVFVPFFGVPAATTTGPAKLALKT-KAAVIPVFPI 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446086118 243 RKPDGKGYELIILPAEYSPPLESAEATAAWMNKIVEQCIMMAPEQYMWLHRRFKT 297
Cdd:pfam03279 240 RNGDGSGYTVIVHPALDLTITDDVEQIAQAMNQIVEKFIMPAPEQYFWLHRRWKT 294
|
|
| LpxP |
COG1560 |
Palmitoleoyl-ACP: Kdo2-lipid-IV acyltransferase (lipid A biosynthesis) [Lipid transport and ... |
25-295 |
9.32e-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: 321.76 E-value: 9.32e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 25 ALWLVVQLPYPVIYKLGCALGHLARRVMKRRAKIAYRNLELCFPEMSAQERHTMVVKNFESVGMGVMETGMAWFWPDRRV 104
Cdd:COG1560 1 LLRLLRLLPLRLLYRLGDLLGRLLYRLAGRRRRVARRNLALAFPELSEAEREALARASFRNLGRTLLETLRLWRLSPERL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 105 NRWMEASGLEHIREVKAQGLGFILVGIHFLTLEFGARMFGMHN-PGIGVYRPNDNPLLDWLQTWGRLRSNKSMLDRKD-L 182
Cdd:COG1560 81 RKRVEVEGLEHLEAALAEGRGVILLTPHFGNWELAGAALALRGyPVTAVYRPLKNPLLDRLIRRGRERFGGELIPRKDgV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 183 KGMVKALKSGELIWYAPDHDYGPRASVFVPLFAVDqAATTSGTWMLARMSKACIIPFVPRRKPDGKGYELIILPAEYsPP 262
Cdd:COG1560 161 RALLRALRKGGIVGLLPDQDPGRKSGVFVPFFGVP-AATPTGPARLARRTGAPVVPVFARRLPDGRGYRLEIEPPLE-DF 238
|
250 260 270
....*....|....*....|....*....|...
gi 446086118 263 LESAEATAAWMNKIVEQCIMMAPEQYMWLHRRF 295
Cdd:COG1560 239 SEDVEADTQRLNRALEAWIREHPEQWLWLHRRW 271
|
|
| LPLAT_LABLAT-like |
cd07984 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LABLAT-like; ... |
106-296 |
1.95e-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: 203.60 E-value: 1.95e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 106 RWMEASGLEHIREVKAQGLGFILVGIHFLTLEFGARMFGMHN-PGIGVYRPNDNPLLDWLQTWGRLRSNKSMLDRKD-LK 183
Cdd:cd07984 2 KRVEREGLEHLEAALAKGKGVILLTAHFGNWELAGLALALLGyPVTVVYRPLKNPLLDRLITRGRERFGARLIPRGGgLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 184 GMVKALKSGELIWYAPDHDYGPRASVFVPLFAVdQAATTSGTWMLARMSKACIIPFVPRRKPDGkGYELIILPAEYSPPL 263
Cdd:cd07984 82 ELIRALKKGEIVGILPDQDPGRKGGVFVPFFGR-PAATPTGPARLALKTGAPVVPAFAYRLPGG-GYRIEFEPPLENPPS 159
|
170 180 190
....*....|....*....|....*....|...
gi 446086118 264 ESAEATAAWMNKIVEQCIMMAPEQYMWLHRRFK 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: 634.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 1 MTKLPKFSVALLHPRYWLTWLGIGALWLVVQLPYPVIYKLGCALGHLARRVMKRRAKIAYRNLELCFPEMSAQERHTMVV 80
Cdd:PRK06860 3 MTNLPKFSRALLHPRYWLTWLGIGLLWLIVLLPYPVLYKLGRGLGKLALRFMKRRAKIARRNLELCFPEMSEQEREAIVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 81 KNFESVGMGVMETGMAWFWPDRRVNRWMEASGLEHIREVKAQGLGFILVGIHFLTLEFGARMFGMHNPGIGVYRPNDNPL 160
Cdd:PRK06860 83 KNFESVGMALIETGMAWFWPDWRIKRWTEVEGLEHIREVQAQGRGVLLVGVHFLTLELGARIFGMHNPGIGVYRPNDNPL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 161 LDWLQTWGRLRSNKSMLDRKDLKGMVKALKSGELIWYAPDHDYGPRASVFVPLFAVDQAATTSGTWMLARMSKACIIPFV 240
Cdd:PRK06860 163 YDWLQTWGRLRSNKSMLDRKDLKGMIKALKKGERIWYAPDHDYGPRSSVFVPFFAVEQAATTTGTWMLARMSKAAVIPFV 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446086118 241 PRRKPDGKGYELIILPAEYSPPLESAEATAAWMNKIVEQCIMMAPEQYMWLHRRFKTRPEGVPSRY 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: 530.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 5 PKFSVALLHPRYWLTWLGIGALWLVVQLPYPVIYKLGCALGHLARRVMKRRAKIAYRNLELCFPEMSAQERHTMVVKNFE 84
Cdd:TIGR02207 1 PEFSASLLHPRYWPTWLGLGVLWLIVQLPYPVLLALGRGIGRLAMRLMKRRVHIARRNLELCFPHMSDAERERLLRENFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 85 SVGMGVMETGMAWFWPDRRVNRWMEASGLEHIREVKAQGLGFILVGIHFLTLEFGARMFGMHNPGIGVYRPNDNPLLDWL 164
Cdd:TIGR02207 81 STGMALFETGMAWFWSDARIKKWMQIEGLEHLQRAQKQGRGVLLVGVHFLTLELGARIFGQQQPGIGVYRPHNNPLFDWI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 165 QTWGRLRSNKSMLDRKDLKGMVKALKSGELIWYAPDHDYGPRASVFVPLFAVDQAATTSGTWMLARMSKACIIPFVPRRK 244
Cdd:TIGR02207 161 QTRGRLRSNKAMIDRKDLRGMIKALKNGERIWYAPDHDYGRKSSVFVPFFAVPDAATTTGTSILARLSKCAVVPFTPRRN 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446086118 245 PDGKGYELIILPAEYSPPLESAEATAAWMNKIVEQCIMMAPEQYMWLHRRFKTRP-EGVPSRY 306
Cdd:TIGR02207 241 EDGSGYRLKIDPPLDDFPGDDEIAAAARMNKIVEKMIMRAPEQYMWLHRRFKTRPdEGESSLY 303
|
|
| PRK08025 |
PRK08025 |
kdo(2)-lipid IV(A) palmitoleoyltransferase; |
1-306 |
9.67e-160 |
|
kdo(2)-lipid IV(A) palmitoleoyltransferase;
Pssm-ID: 181200 Cd Length: 305 Bit Score: 447.26 E-value: 9.67e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 1 MTKLPKFSVALLHPRYWLTWLGIGALWLVVQLPYPVIYKLGCALGHLARRVMKRRAKIAYRNLELCFPEMSAQERHTMVV 80
Cdd:PRK08025 1 MFPQQKFSREFLHPRYWLTWFGLGVLWLLVQLPYPVLCFLGTRIGRMSRPFLKRRESIARKNLELCFPQMSAEEREKMIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 81 KNFESVGMGVMETGMAWFWPDRRVNRWMEASGLEHIREVKAQGLGFILVGIHFLTLEFGARMFGMHNPGIGVYRPNDNPL 160
Cdd:PRK08025 81 ENFRSLGMALLETGMAWFWPDSRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLCQPMMATYRPHNNKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 161 LDWLQTWGRLRSNKSMLDRKDLKGMVKALKSGELIWYAPDHDYGPRASVFVPLFAVDQAATTSGTWMLARMSKACIIPFV 240
Cdd:PRK08025 161 MEWVQTRGRMRSNKAMIGRNNLRGIVGALKKGEAVWFAPDQDYGPKGSSFAPFFAVENVATTNGTYVLSRLSGAAMLTVT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446086118 241 PRRKPDGKGYELIILPAEYSPPLESAEAtAAWMNKIVEQCIMMAPEQYMWLHRRFKTRPEGVPSRY 306
Cdd:PRK08025 241 MVRKADYSGYRLFITPEMEGYPTDENQA-AAYMNKIIEKEIMRAPEQYLWIHRRFKTRPVGESSLY 305
|
|
| Lip_A_acyltrans |
pfam03279 |
Bacterial lipid A biosynthesis acyltransferase; |
5-297 |
1.26e-135 |
|
Bacterial lipid A biosynthesis acyltransferase;
Pssm-ID: 281296 [Multi-domain] Cd Length: 294 Bit Score: 385.93 E-value: 1.26e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 5 PKFSVALLHPRYWLTWLGIGALWLVVQLPYPVIYKLGCALGHLARRVMKRRAKIAYRNLELCFPEMSAQERHTMVVKNFE 84
Cdd:pfam03279 1 PKFSPELLHPRYWLDWLGIAVLRLLALLPYSALRRIGKGLGRLAGRFLKRRRKIARRNLALCFPEMSEAEREQIIDKSFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 85 SVGMGVMETGMAWFWPDRRVNRWMEASGLEHIREVKAQGLGFILVGIHFLTLEFGARMFGMHNPGIGVYRPND-NPLLDW 163
Cdd:pfam03279 81 SVGRAIVETGRVWFWPDSRIAKRFEVIGLEHIKEALAQGRGAILVGPHFGNWDLGGRVLGQQYPGMAVYRPNLkNPLLDW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 164 LQTWGRLRSNKSMLDRKD-LKGMVKALKSGELIWYAPDHDYGPRASVFVPLFAVDQAATTSGTWMLARMsKACIIPFVPR 242
Cdd:pfam03279 161 LQTSGRERFGGRMLPRQNgIKGLIKALRKGEVVWYLPDQDLGRKDSVFVPFFGVPAATTTGPAKLALKT-KAAVIPVFPI 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446086118 243 RKPDGKGYELIILPAEYSPPLESAEATAAWMNKIVEQCIMMAPEQYMWLHRRFKT 297
Cdd:pfam03279 240 RNGDGSGYTVIVHPALDLTITDDVEQIAQAMNQIVEKFIMPAPEQYFWLHRRWKT 294
|
|
| PRK05646 |
PRK05646 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
5-306 |
1.50e-116 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 235543 [Multi-domain] Cd Length: 310 Bit Score: 337.94 E-value: 1.50e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 5 PKFSVALLHPRYWLTWLGIGALWLVVQLPYPVIYKLGCALGHLARRVMKRRAKIAYRNLELCFPEMSAQERHTMVVKNFE 84
Cdd:PRK05646 4 PRFRAAFLHPRFWPLWLGLGLLWLVVQLPYRVLLWLGRALGALMYRLAGSRRRIAARNLELCFPEKSAAERERLLKENFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 85 SVGMGVMETGMAWFWPDRRVNRWMEASGLEHIREVKAQGLGFILVGIHFLTLEFGARMFGMHNPGIGVYRPNDNPLLDWL 164
Cdd:PRK05646 84 STGIAFFEMAMSWWWPKARLARLAHIEGLEHLQQAQQEGQGVILMALHFTTLEIGAALLGQQHTIDGMYREHKNPVFDFI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 165 QTWGRLRSNKSML--DRKDLKGMVKALKSGELIWYAPDHDYGPRASVFVPLFAVdQAATTSGTWMLARMSKACIIPFVPR 242
Cdd:PRK05646 164 QRRGRERHNLDSTaiEREDVRGMLKLLRAGRAIWYAPDQDYGAKQSIFVPLFGI-PAATVTATTKFARLGRARVIPFTQK 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446086118 243 RKPDGKGYELIILPAEYSPPLESAEATAAWMNKIVEQCIMMAPEQYMWLHRRFKTRPEGVPSRY 306
Cdd:PRK05646 243 RLADGSGYRLVIHPPLEDFPGESEEADCLRINQWVERVVRECPEQYLWAHRRFKSRPEGEPKLY 306
|
|
| LpxP |
COG1560 |
Palmitoleoyl-ACP: Kdo2-lipid-IV acyltransferase (lipid A biosynthesis) [Lipid transport and ... |
25-295 |
9.32e-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: 321.76 E-value: 9.32e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 25 ALWLVVQLPYPVIYKLGCALGHLARRVMKRRAKIAYRNLELCFPEMSAQERHTMVVKNFESVGMGVMETGMAWFWPDRRV 104
Cdd:COG1560 1 LLRLLRLLPLRLLYRLGDLLGRLLYRLAGRRRRVARRNLALAFPELSEAEREALARASFRNLGRTLLETLRLWRLSPERL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 105 NRWMEASGLEHIREVKAQGLGFILVGIHFLTLEFGARMFGMHN-PGIGVYRPNDNPLLDWLQTWGRLRSNKSMLDRKD-L 182
Cdd:COG1560 81 RKRVEVEGLEHLEAALAEGRGVILLTPHFGNWELAGAALALRGyPVTAVYRPLKNPLLDRLIRRGRERFGGELIPRKDgV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 183 KGMVKALKSGELIWYAPDHDYGPRASVFVPLFAVDqAATTSGTWMLARMSKACIIPFVPRRKPDGKGYELIILPAEYsPP 262
Cdd:COG1560 161 RALLRALRKGGIVGLLPDQDPGRKSGVFVPFFGVP-AATPTGPARLARRTGAPVVPVFARRLPDGRGYRLEIEPPLE-DF 238
|
250 260 270
....*....|....*....|....*....|...
gi 446086118 263 LESAEATAAWMNKIVEQCIMMAPEQYMWLHRRF 295
Cdd:COG1560 239 SEDVEADTQRLNRALEAWIREHPEQWLWLHRRW 271
|
|
| PRK08733 |
PRK08733 |
LpxL/LpxP family Kdo(2)-lipid IV(A) lauroyl/palmitoleoyl acyltransferase; |
10-306 |
1.28e-69 |
|
LpxL/LpxP family Kdo(2)-lipid IV(A) lauroyl/palmitoleoyl acyltransferase;
Pssm-ID: 181542 [Multi-domain] Cd Length: 306 Bit Score: 218.23 E-value: 1.28e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 10 ALLHPRYWLTWLGIGALWLVVQLPYPVIYKLGCALGHLARRVMKRRAKIAYRNLELCFPEMSAQERHTMVVKNFESVGMG 89
Cdd:PRK08733 12 SLRNPKHWPMYLGLAVMVLAARLPWTLQRALGRGVGWVAMRLAGTRRRAAEVNLKLCFPEQDDAWRARLLRDSFDALGVG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 90 VMETGMAWFWPDRRVNRWMEASGLEHIREVKAQGLGFILVGIHFLTLEFGARMFGMHNPGIGVYRPNDNPLLDWLQTWGR 169
Cdd:PRK08733 92 LFEFARAWWGSIDVIRPGVQIEGLEHLQQLQQQGRGVLLVSGHFMTLEMCGRLLCDHVPLAGMYRRHRNPVFEWAVKRGR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 170 LRSNKSMLDRKDLKGMVKALKSGELIWYAPDHDYGPRASVFVPLFAVdQAATTSGTWMLARMSKACIIPFVPRRkpDGKG 249
Cdd:PRK08733 172 LRYATHMFANEDLRATIKHLKRGGFLWYAPDQDMRGKDTVFVPFFGH-PASTITATHQLARLTGCAVVPYFHRR--EGGR 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 446086118 250 YELIILPAEYSPPLESAEATAAWMNKIVEQCIMMAPEQYMWLHRRFKTRPEGVPSRY 306
Cdd:PRK08733 249 YVLKIAPPLADFPSDDVIADTTRVNAAIEDMVREAPDQYLWIHRRFKRQPGGRSDFY 305
|
|
| lipid_A_msbB |
TIGR02208 |
lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; This family consists of MsbB ... |
5-306 |
8.32e-66 |
|
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: 208.51 E-value: 8.32e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 5 PKFSVALLHPRYWLTWLGIGALWLVVQLPYPVIYKLGCALGHLARRVMKRRAKIAYRNLELCFPEMSAQERHTMVVKNFE 84
Cdd:TIGR02208 3 RRFQKSFLHPKYWGTWLGVFALVLLAFMPAKLRDPIAKVLAKFVGPIAKKPRGRARINLSACFPEKSEAERETIIDNNFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 85 SVGMGVMETGMAWFWPDRRVNRWMEASGLEHIREVKAQGLGFILVGIHFLTLEF-GARMFGMHNPGIGVYRPNDNPLLDW 163
Cdd:TIGR02208 83 TFVQVMLSQAELAIRSKAHLRRRVNLMGLEHIEAAQAAGKPVIFLVPHGWAIDYaGLRLASQGLPMVTMFNNHKNPLFDW 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 164 LQTWGRLRSNKSMLDRKD-LKGMVKALKSGELIWYAPDHDYGPRASVFVPLFAVdQAATTSGTWMLARMSKACIIPFVPR 242
Cdd:TIGR02208 163 LWNRVRSRFGGHVYAREAgIKALLASLKRGESGYYLPDEDHGPEQSVFVPFFAT-YKATLPVVGRLAKAGNAQVVPVFPG 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446086118 243 RKPDGKGYELIILPAEYSPPLESAEATAAWMNKIVEQCIMMAPEQYMWLHRRFKTRPEGVPSRY 306
Cdd:TIGR02208 242 YNQVTGKFELTVRPAMATELSVDPEQEARAMNKEVEQFILPYPEQYMWILRLLKTRPDGEASIY 305
|
|
| LPLAT_LABLAT-like |
cd07984 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LABLAT-like; ... |
106-296 |
1.95e-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: 203.60 E-value: 1.95e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 106 RWMEASGLEHIREVKAQGLGFILVGIHFLTLEFGARMFGMHN-PGIGVYRPNDNPLLDWLQTWGRLRSNKSMLDRKD-LK 183
Cdd:cd07984 2 KRVEREGLEHLEAALAKGKGVILLTAHFGNWELAGLALALLGyPVTVVYRPLKNPLLDRLITRGRERFGARLIPRGGgLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 184 GMVKALKSGELIWYAPDHDYGPRASVFVPLFAVdQAATTSGTWMLARMSKACIIPFVPRRKPDGkGYELIILPAEYSPPL 263
Cdd:cd07984 82 ELIRALKKGEIVGILPDQDPGRKGGVFVPFFGR-PAATPTGPARLALKTGAPVVPAFAYRLPGG-GYRIEFEPPLENPPS 159
|
170 180 190
....*....|....*....|....*....|...
gi 446086118 264 ESAEATAAWMNKIVEQCIMMAPEQYMWLHRRFK 296
Cdd:cd07984 160 EDVEEDTQRLNDALEAAIREHPEQWLWFHRRWK 192
|
|
| PRK06946 |
PRK06946 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
19-306 |
6.90e-64 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 180770 [Multi-domain] Cd Length: 293 Bit Score: 203.38 E-value: 6.90e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 19 TWLGIGALWLVVQLPYPVIYKLGCALGHLARRVMKRRAKIAYRNLELCFPEMSAQERHTMVVKNFESVGMGVMETGMAWF 98
Cdd:PRK06946 6 TALAIGLLKLLAFLPYGLTARFGDGLGWLLYRIPSRRRRIVHTNLKLCFPDWSDARREELARRHFRHVIRSYVERSVQWF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 99 WPDRRVNRWMEASglEHIREVKAQGLGFILVGIHFLTLEFGARMFGMH--NPGIGVYRPNDNPLLDWLQTWGRLRSNKSM 176
Cdd:PRK06946 86 GSEKKLEKLVQVD--SAIDLTDPDGPPTIFLGLHFVGIEAGSIWLNYSlrRRVGSLYTPMSNPLLDAIAKAARGRFGAEM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 177 LDRKD-LKGMVKALKSGELIWYAPDHDYGPRASVFVPLFAVdQAATTSGTWMLARMSKACIIPFVPRRKPDGKGYELIIL 255
Cdd:PRK06946 164 VSRADsARQVLRWLRDGKPVMLGADMDFGLRDSTFVPFFGV-PACTLTAVSRLARTGGAQVVPFITEVLPDYKGYRLRVF 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446086118 256 PAEYSPPLESAEATAAWMNKIVEQCIMMAPEQYMWLHRRFKTRPEGVPSRY 306
Cdd:PRK06946 243 KPWENYPTGDDDLDARRMNAFLEEQIRLMPEQYYWVHKRFKTRPPGEPSVY 293
|
|
| PRK08943 |
PRK08943 |
lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; Validated |
5-301 |
7.16e-59 |
|
lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; Validated
Pssm-ID: 236355 Cd Length: 314 Bit Score: 190.85 E-value: 7.16e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 5 PKFSVALLHPRYWLTWLGIGALWLVVQLPY----PVIYKLGCALGHLARRVmKRRAKIayrNLELCFPEMSAQERHTMVV 80
Cdd:PRK08943 12 PRFQKSFLHPRYWGTWLGIGALAGLALMPPrlrdPLAAKLGRLVGKLAKKA-RRRARI---NLSLCFPEKSEAEREAIID 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 81 KNFESVGMGVMETGMAWFWPDRRVNRWMEASGLEHIREVKAQGLGFILVGIHFLTLEFGARMFGMHN-PGIGVYRPNDNP 159
Cdd:PRK08943 88 EMFATAPQAMLMMAELALRSPKHLQRRVEWHGLEILEEARANGENVIFLVPHGWAIDIPAMLLASQGqPMAAMFHNQRNP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 160 LLDWLQTWGRLRSNKSMLDRKD-LKGMVKALKSGELIWYAPDHDYGPRASVFVPLFAVdQAATTSGTWMLARMSKACIIP 238
Cdd:PRK08943 168 LFDWLWNRVRRRFGGRLHAREDgIKPFISSVRQGYWGYYLPDEDHGPEHSVFVDFFAT-YKATLPGIGRLAKVCRARVVP 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446086118 239 FVPRRKPDGKGYELIILPAEYSPPLESAEATAAWMNKIVEQCIMMAPEQYMWLHRRFKTRPEG 301
Cdd:PRK08943 247 LFPVYNGKTHRLDIEIRPPMDDLLSADDETIARRMNEEVEQFVGPHPEQYMWILKLLKTRKPG 309
|
|
| PRK08706 |
PRK08706 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
26-306 |
2.80e-56 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 169557 [Multi-domain] Cd Length: 289 Bit Score: 183.53 E-value: 2.80e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 26 LWLVVQLPYPVIYKLGCALGHLARRVMKRRAKIAYRNLELCFPEMSAQERHTMVVKNFESVGMGVMETGMAWFWPDRRVN 105
Cdd:PRK08706 8 LYVLQFLPFALLHKLADLTGLLAYLLVKPRRRIGEINLAKCFPEWDEEKRKTVLKQHFKHMAKLMLEYGLYWYAPAGRLK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 106 RWMEASGLEHIREVKAQGLGFILVGIHFLTLEFGARMFGMHNPGIGVYRPNDNPLLDWLQTWGRLR-SNKSMLDRKD-LK 183
Cdd:PRK08706 88 SLVRYRNKHYLDDALAAGEKVIILYPHFTAFEMAVYALNQDVPLISMYSHQKNKILDEQILKGRNRyHNVFLIGRTEgLR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 184 GMVKAL-KSGELIWYAPDHDYGPRASVFVPLFAVdQAATTSGTWMLARMSKACIIPFVPRRKPDGKgYELIILPAEYSPP 262
Cdd:PRK08706 168 ALVKQFrKSSAPFLYLPDQDFGRNDSVFVDFFGI-QTATITGLSRIAALANAKVIPAIPVREADNT-VTLHFYPAWDSFP 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 446086118 263 LESAEATAAWMNKIVEQCIMMAPEQYMWLHRRFKTRPEGVPSRY 306
Cdd:PRK08706 246 SEDAQADAQRMNRFIEERVREHPEQYFWLHKRFKTRPEGSPDFY 289
|
|
| PRK08905 |
PRK08905 |
lysophospholipid acyltransferase family protein; |
26-303 |
1.09e-31 |
|
lysophospholipid acyltransferase family protein;
Pssm-ID: 236348 [Multi-domain] Cd Length: 289 Bit Score: 119.32 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 26 LWLVVQLPYPVIYKLGCALGHLARRVMKRRAKIAYRNLELCFPEMSAQerhtMVVKNFESVGMGVMEtgMAWFW---PDR 102
Cdd:PRK08905 6 FRLLSRLPLSWLHALGGWLGRLAYRLPGRYRRRLRANLRQAGGDPDPA----MVKAAAAETGRMILE--LPYVWfrkPEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 103 RVNRWMEASGLEHIREVKAQGLGFILVGIHFLTLEFGARMFGMHNPGIGVYRPndnPLLDWLQTW---GRLRSNKSML-- 177
Cdd:PRK08905 80 IETMVKDDHGWEHVEAALAEGRGILFLTPHLGCFEVTARYIAQRFPLTAMFRP---PRKAALRPLmeaGRARGNMRTApa 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 178 DRKDLKGMVKALKSGELIWYAPDHDYGPRASVFVPLFAvDQAATTSGTWMLARMSKACIIPFVPRRKPDGKGYELIILPA 257
Cdd:PRK08905 157 TPQGVRMLVKALRRGEAVGILPDQVPSGGEGVWAPFFG-RPAYTMTLVARLAEVTGVPVIFVAGERLPRGRGYRLHLRPV 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 446086118 258 eySPPL-ESAEATAAWMNKIVEQCIMMAPEQYMWLHRRFKtRPEGVP 303
Cdd:PRK08905 236 --QEPLpGDKAADAAVINAEIERLIRRFPTQYLWGYNRYK-RPRGAP 279
|
|
| PRK05645 |
PRK05645 |
lysophospholipid acyltransferase; |
21-306 |
2.78e-31 |
|
lysophospholipid acyltransferase;
Pssm-ID: 135493 [Multi-domain] Cd Length: 295 Bit Score: 118.47 E-value: 2.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 21 LGIGALWLVVQLPYPVIYKLGCALGHLARRVMKRRAKIAYRNLELCFPEMSAQERHTMVVKNFESVGMGVMETGMAWFWP 100
Cdd:PRK05645 8 LMVGALRLFALLPWRAVQGVGAGIGWLMWKLPNRSREVVRINLSKCFPELSPAELEKLVGQSLMDIGKTLTESACAWIWP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 101 -DRRVNRWMEASGLEHIREVKAQGLGFILVGIHFLTLEFGARMFGMHNPGIGVYRPNDNPLLDWLQTWGRLR-SNKSMLD 178
Cdd:PRK05645 88 pQKSLELVREVEGLEVLEQALASGKGVVGITSHLGNWEVLNHFYCSQCKPIIFYRPPKLKAVDELLRKQRVQlGNRVAPS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 179 RKD-LKGMVKALKSGELIWYAPDHDYGPRASVFVPLFAVDQAATTSGTWMLARmSKACIIPFVPRRKPDGKGYELIILPA 257
Cdd:PRK05645 168 TKEgILSVIKEVRKGGQVGIPADPEPAESAGIFVPFLGTQALTSKFVPNMLAG-GKAVGVFLHALRLPDGSGYKVILEAA 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 446086118 258 EYSPPLESAEATAAWMNKIVEQCIMMAPEQYMWLHRRFKTRPEGVPSRY 306
Cdd:PRK05645 247 PEDMYSTDVEVSAAAMSKVVERYVRAYPSQYMWSMKRFKKRPAGEARWY 295
|
|
| PRK08419 |
PRK08419 |
lipid A biosynthesis lauroyl acyltransferase; Reviewed |
28-296 |
2.06e-21 |
|
lipid A biosynthesis lauroyl acyltransferase; Reviewed
Pssm-ID: 181420 [Multi-domain] Cd Length: 298 Bit Score: 92.01 E-value: 2.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 28 LVVQLPYPVIYKLGCALGHLARRVMKRRAKIAYRNLELCFPE-MSAQERHTMVVKNFESVGMGVMETGMAWFWPDRRVNR 106
Cdd:PRK08419 16 FLAKMPHCIFLRLAKALAFIMRYLDKKRRKIAKANLDFCFGEsKSQEEKKRIIKKCYENFAFFGLDFIRNQNTTKEEILN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 107 WMEASGLEHIREVKAQGLGFILVGIHFLTLEFGARMFGMHNPGIG-VYRPNDNPLLDWLQTWGRLRSNKSMLDRKD-LKG 184
Cdd:PRK08419 96 KVTFINEENLLDALKKKRPIIVTTAHYGYWELFSLALAAYYGAVSiVGRLLKSAPINEMISKRREQFGIELIDKKGaMKE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 185 MVKALKSGELIWYAPDHDYGPRASVFVPLFAVDQAATTSGTwMLARMSKACIIPFVPRRKpDGKGYELIILPAEYSPPLE 264
Cdd:PRK08419 176 LLKALKQGRALGILVDQNVVPKEGVEVKFFNKRVTHTTIAS-ILARRYNALIIPVFIFND-DYSHFTITFFPPIRSKITD 253
|
250 260 270
....*....|....*....|....*....|....*..
gi 446086118 265 SA-----EATAAwMNKIVEQCIMMAPEQYMWLHRRFK 296
Cdd:PRK08419 254 DAeadilEATQA-QASACEEMIRKKPDEYFWFHRRFK 289
|
|
| PRK08734 |
PRK08734 |
lauroyl acyltransferase; |
28-301 |
8.19e-18 |
|
lauroyl acyltransferase;
Pssm-ID: 181543 [Multi-domain] Cd Length: 305 Bit Score: 81.85 E-value: 8.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 28 LVVQLPYPVIYKLGCALGHLARRVMKRRAKIAYRNLELCFPEMSAQERHTMVVKNFESVGMGVMETGMAWFWPD-RRVNR 106
Cdd:PRK08734 16 LVGRLPWPLLKRLADLLAWSWRKLNARESRVTRRNLELAYPELSPQQRAQLHAQILRSTARQALEVLRTWTHPPaENLAR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 107 WMEASGLEHIREVKAQGLGFILVGIHFLTLEFGARMFGMHNPGIGVYRPNDNPLLD-WLQtwgRLRSNKSMLDRK----D 181
Cdd:PRK08734 96 LRQRHGQELYDAALASGRGVIVAAPHFGNWELLNQWLSERGPIAIVYRPPESEAVDgFLQ---LVRGGDNVRQVRaegpA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 182 LKGMVKALKSGELIWYAPDHDYGPRASVFVPLFAVdQAATTSGTWMLARMSKACIIPFVPRRKPDGKGYELIILPAEYS- 260
Cdd:PRK08734 173 VRQLFKVLKDGGAVGILPDQQPKMGDGVFAPFFGI-PALTMTLVNRLAERTGATVLYGWCERIGPDLEFALHVQPADPAv 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 446086118 261 ---PPLESAEAtaawMNKIVEQCIMMAPEQYMWLHRRFKTRPEG 301
Cdd:PRK08734 252 adpDPLRAATA----LNAGIERIARRDPAQYQWTYKRYTLRPPG 291
|
|
| PRK05906 |
PRK05906 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
13-296 |
4.63e-11 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 168292 [Multi-domain] Cd Length: 454 Bit Score: 63.26 E-value: 4.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 13 HPRYWLtwlGIGALWLVVQLPYPVIYKLGCALGHLARRVMKRRAKIAYRNLELCFPEMSAQER---------HTMV---- 79
Cdd:PRK05906 15 HLVYYL---GLGVITILRLLPRSSLRLFGKGLGTLLFYFISDYRKTALTNLALAFPEKSFAERyqiarqsvqHVIItfle 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 80 -------VKNFES-VGMGVMETGMAWFWPDRRVNRwmeaSGLEHIREVKAQGLGFILVGIHFLTLEFGARMFGMHNPGIG 151
Cdd:PRK05906 92 llaveklAGHIDElIAIATSEDAPEGFFPEEVSSQ----QELEHTFSRLDEQEGAILFCGHQANWELPFLYITKRYPGLA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 152 VYRPNDNPlldwlqtwgrlRSNKSMLD-RKDLKGMV-----------KALKSGELIWYAPDHDYgPRASVFVPLFAvDQA 219
Cdd:PRK05906 168 FAKPIKNR-----------RLNKKIFSlRESFKGKIvppknginqalRALHQGEVVGIVGDQAL-LSSSYSYPLFG-SQA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 220 ATTSGTWMLARMSKACIIPFVPRRKPdgKGYELIILPAEYS-PPLESAEATAAWMNKI---VEQCIMMAPEQYMWLHRRF 295
Cdd:PRK05906 235 FTTTSPALLAYKTGKPVIAVAIYRKP--NGYLVVPSKKFYAnKSLPIKESTEQLMDRLmrfLEKGIACKPEQWMWLHKRW 312
|
.
gi 446086118 296 K 296
Cdd:PRK05906 313 K 313
|
|
| LPLAT |
cd06551 |
Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; ... |
101-282 |
1.53e-10 |
|
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: 59.35 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 101 DRRVNRWMeaSGLEHIREVKAQ----GLGFILVGIHFLTLEFGARMFGMHN----PGIGVYRPNDN---PLLDWLQTWgR 169
Cdd:cd06551 1 FRYLLLNF--FGFVRLEVKGPPpppgGGPVLFVSNHSSWWDGLILFLLLERglrrDVYGLMDEELLeryPFFTRLGAF-S 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 170 LRSNKSMLDRKDLKGMVKALKS-GELIWYAPDHDYGPRaSVFVPLFAVDQAAttsgtwmLARMSKACIIPFVPRRKPDG- 247
Cdd:cd06551 78 VDRDSPRSAAKSLKYVARLLSKpGSVVWIFPEGTRTRR-DKRPLQFKPGVAH-------LAEKAGVPIVPVALRYTFELf 149
|
170 180 190
....*....|....*....|....*....|....*...
gi 446086118 248 -KGYELIILPAEYSPPLESA--EATAAWMNKIVEQCIM 282
Cdd:cd06551 150 eQFPEIFVRIGPPIPYAETAlgEELAAELANRLTRLLD 187
|
|
| PRK06628 |
PRK06628 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
57-296 |
6.77e-07 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 102471 Cd Length: 290 Bit Score: 49.93 E-value: 6.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 57 KIAYRNLELCFPEMSAQERhtMVVKNFESVGMGVMETGMAWFWPDRRVNRWMEASGLEHIREVKAQGlgFILVGIHFLTL 136
Cdd:PRK06628 51 KIARRNIKAVFGDMCDVEK--IIDQTWDNFGRFIGEFTYVNKMDEAELERRIEIIGIENIKKLEGQP--FLLFSGHFANW 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 137 EFGARMFGMHNPGIGV-YRPNDNPLLDWLQTWGRLRSNKSMLDR--KDLKGMVKALKSGELIWYAPDHDYGPraSVFVPl 213
Cdd:PRK06628 127 DISLKILHKFYPKVAViYRKANNPYVNKLVNESRAGDKLRLIPKgpEGSRALVRAIKESESIVMLVDQKMND--GIEVP- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 214 FAVDQAATTSGTWMLARMSKACIIPF-VPRRKpdGKGYELIILPA-EYSPPLESAEATAAWM---NKIVEQCIMMAPEQY 288
Cdd:PRK06628 204 FLGHPAMTASAIAKIALQYKYPIIPCqIIRTK--GSYFKVIVHPQlKFEQTGDNKADCYNIMlniNQMLGEWVKQNPAQW 281
|
....*...
gi 446086118 289 MWLHRRFK 296
Cdd:PRK06628 282 FWFHNRWK 289
|
|
| PRK06553 |
PRK06553 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
15-294 |
1.13e-06 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 235827 [Multi-domain] Cd Length: 308 Bit Score: 49.20 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 15 RYWLT-WLGIGALWLVVQLPypvIYKLGCALGHLARRV--MKRRAKIAYRNLELCFPEMSAQERHTMVVKNFESVGMGVM 91
Cdd:PRK06553 20 AGWLVaQLVFGLLGLLRLFP---ADKAINFFGRLARLIgpLLPRHRVALDNLRAAFPEKSEAEIEAIALGMWDNLGRLGA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 92 E---TGMAW-FWPDRRVNRWMEASGLEHIREVKAQGLGFILVGIH---FLTLEFGARMFGMhnPGIGVYRPNDNPLLDWL 164
Cdd:PRK06553 97 EyafLDAIFdYDPEAPEPGRVEVRGIEIFERLRDDGKPALIFTAHlgnWELLAIAAAAFGL--DVTVLFRPPNNPYAARK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446086118 165 ------QTWGRLRSNKSMLDRKdlkgMVKALKSGELIWYAPDHDYgpRASVFVPLFAVDQAATTsgtwMLARMSKACIIP 238
Cdd:PRK06553 175 vlearrTTMGGLVPSGAGAAFA----LAGVLERGGHVGMLVDQKF--TRGVEVTFFGRPVKTNP----LLAKLARQYDCP 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446086118 239 FVPR---RKPDGKgYELIILPaEYSPPLESA-----EATAAWMNKIVEQCIMMAPEQYMWLHRR 294
Cdd:PRK06553 245 VHGArciRLPGGR-FRLELTE-RVELPRDADgqidvQATMQALTDVVEGWVREYPGQWLWLHRR 306
|
|
| |
