|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08025 |
PRK08025 |
kdo(2)-lipid IV(A) palmitoleoyltransferase; |
1-306 |
0e+00 |
|
kdo(2)-lipid IV(A) palmitoleoyltransferase;
Pssm-ID: 181200 Cd Length: 305 Bit Score: 567.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 1 MKSAKAFQLALLHPRYWLTWFGLALLFLLVQLPYPLLYRLGVWMGRTSMRFLKRRVTITRRNLELCFPEMDEAQRERKVV 80
Cdd:PRK08025 1 MFPQQKFSREFLHPRYWLTWFGLGVLWLLVQLPYPVLCFLGTRIGRMSRPFLKRRESIARKNLELCFPQMSAEEREKMIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 81 GNFESLGMGLLETGMAWFWSDKRVKRWFNVSGINHLKMAQRDERGVLVIGVHFMSLELGGRAMGLCQPMMAMYRPHNNKA 160
Cdd:PRK08025 81 ENFRSLGMALLETGMAWFWPDSRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLCQPMMATYRPHNNKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 161 MEWAQTKGRMRSNKAMIDRKDLRGMVHALKRGEAVWFAPDQDYGPRGSVFAPLFAVDKAATTSGTFMLARMANPALVPVV 240
Cdd:PRK08025 161 MEWVQTRGRMRSNKAMIGRNNLRGIVGALKKGEAVWFAPDQDYGPKGSSFAPFFAVENVATTNGTYVLSRLSGAAMLTVT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727181982 241 LIRREGGRGYDLLIQPALEDYPlSDEQAAAAYMNKVIEKEIMRAPEQYMWLHRRFKTRPAGAPSLY 306
Cdd:PRK08025 241 MVRKADYSGYRLFITPEMEGYP-TDENQAAAYMNKIIEKEIMRAPEQYLWIHRRFKTRPVGESSLY 305
|
|
| lipid_A_htrB |
TIGR02207 |
lipid A biosynthesis lauroyl (or palmitoleoyl) acyltransferase; This model represents a narrow ... |
6-306 |
1.23e-168 |
|
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: 469.90 E-value: 1.23e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 6 AFQLALLHPRYWLTWFGLALLFLLVQLPYPLLYRLGVWMGRTSMRFLKRRVTITRRNLELCFPEMDEAQRERKVVGNFES 85
Cdd:TIGR02207 2 EFSASLLHPRYWPTWLGLGVLWLIVQLPYPVLLALGRGIGRLAMRLMKRRVHIARRNLELCFPHMSDAERERLLRENFES 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 86 LGMGLLETGMAWFWSDKRVKRWFNVSGINHLKMAQRDERGVLVIGVHFMSLELGGRAMGLCQPMMAMYRPHNNKAMEWAQ 165
Cdd:TIGR02207 82 TGMALFETGMAWFWSDARIKKWMQIEGLEHLQRAQKQGRGVLLVGVHFLTLELGARIFGQQQPGIGVYRPHNNPLFDWIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 166 TKGRMRSNKAMIDRKDLRGMVHALKRGEAVWFAPDQDYGPRGSVFAPLFAVDKAATTSGTFMLARMANPALVPVVLIRRE 245
Cdd:TIGR02207 162 TRGRLRSNKAMIDRKDLRGMIKALKNGERIWYAPDHDYGRKSSVFVPFFAVPDAATTTGTSILARLSKCAVVPFTPRRNE 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727181982 246 GGRGYDLLIQPALEDYPLSDEQAAAAYMNKVIEKEIMRAPEQYMWLHRRFKTRP-AGAPSLY 306
Cdd:TIGR02207 242 DGSGYRLKIDPPLDDFPGDDEIAAAARMNKIVEKMIMRAPEQYMWLHRRFKTRPdEGESSLY 303
|
|
| LpxP |
COG1560 |
Palmitoleoyl-ACP: Kdo2-lipid-IV acyltransferase (lipid A biosynthesis) [Lipid transport and ... |
33-295 |
1.45e-108 |
|
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: 316.36 E-value: 1.45e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 33 PYPLLYRLGVWMGRTSMRFLKRRVTITRRNLELCFPEMDEAQRERKVVGNFESLGMGLLETGMAWFWSDKRVKRWFNVSG 112
Cdd:COG1560 9 PLRLLYRLGDLLGRLLYRLAGRRRRVARRNLALAFPELSEAEREALARASFRNLGRTLLETLRLWRLSPERLRKRVEVEG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 113 INHLKMAQRDERGVLVIGVHFMSLELGGRAMGLC-QPMMAMYRPHNNKAMEWAQTKGRMRSNKAMIDRKD-LRGMVHALK 190
Cdd:COG1560 89 LEHLEAALAEGRGVILLTPHFGNWELAGAALALRgYPVTAVYRPLKNPLLDRLIRRGRERFGGELIPRKDgVRALLRALR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 191 RGEAVWFAPDQDYGPRGSVFAPLFAVDkAATTSGTFMLARMANPALVPVVLIRREGGRGYDLLIQPALEDyPLSDEQAAA 270
Cdd:COG1560 169 KGGIVGLLPDQDPGRKSGVFVPFFGVP-AATPTGPARLARRTGAPVVPVFARRLPDGRGYRLEIEPPLED-FSEDVEADT 246
|
250 260
....*....|....*....|....*
gi 727181982 271 AYMNKVIEKEIMRAPEQYMWLHRRF 295
Cdd:COG1560 247 QRLNRALEAWIREHPEQWLWLHRRW 271
|
|
| Lip_A_acyltrans |
pfam03279 |
Bacterial lipid A biosynthesis acyltransferase; |
5-297 |
8.27e-108 |
|
Bacterial lipid A biosynthesis acyltransferase;
Pssm-ID: 281296 [Multi-domain] Cd Length: 294 Bit Score: 315.44 E-value: 8.27e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 5 KAFQLALLHPRYWLTWFGLALLFLLVQLPYPLLYRLGVWMGRTSMRFLKRRVTITRRNLELCFPEMDEAQRERKVVGNFE 84
Cdd:pfam03279 1 PKFSPELLHPRYWLDWLGIAVLRLLALLPYSALRRIGKGLGRLAGRFLKRRRKIARRNLALCFPEMSEAEREQIIDKSFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 85 SLGMGLLETGMAWFWSDKRVKRWFNVSGINHLKMAQRDERGVLVIGVHFMSLELGGRAMGLCQPMMA-MYRPHNNKAMEW 163
Cdd:pfam03279 81 SVGRAIVETGRVWFWPDSRIAKRFEVIGLEHIKEALAQGRGAILVGPHFGNWDLGGRVLGQQYPGMAvYRPNLKNPLLDW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 164 AQTKGRMRSNKAMIDRKD-LRGMVHALKRGEAVWFAPDQDYGPRGSVFAPLFAVDKAATTSGTFMLARMaNPALVPVVLI 242
Cdd:pfam03279 161 LQTSGRERFGGRMLPRQNgIKGLIKALRKGEVVWYLPDQDLGRKDSVFVPFFGVPAATTTGPAKLALKT-KAAVIPVFPI 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 727181982 243 RREGGRGYDLLIQPALEDYPLSDEQAAAAYMNKVIEKEIMRAPEQYMWLHRRFKT 297
Cdd:pfam03279 240 RNGDGSGYTVIVHPALDLTITDDVEQIAQAMNQIVEKFIMPAPEQYFWLHRRWKT 294
|
|
| LPLAT_LABLAT-like |
cd07984 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LABLAT-like; ... |
105-296 |
3.83e-67 |
|
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: 208.22 E-value: 3.83e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 105 KRWFNVSGINHLKMAQRDERGVLVIGVHFMSLELGGRAMGLC-QPMMAMYRPHNNKAMEWAQTKGRMRSNKAMIDRKD-L 182
Cdd:cd07984 1 LKRVEREGLEHLEAALAKGKGVILLTAHFGNWELAGLALALLgYPVTVVYRPLKNPLLDRLITRGRERFGARLIPRGGgL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 183 RGMVHALKRGEAVWFAPDQDYGPRGSVFAPLFAVDkAATTSGTFMLARMANPALVPVvLIRREGGRGYDLLIQPALEDYP 262
Cdd:cd07984 81 RELIRALKKGEIVGILPDQDPGRKGGVFVPFFGRP-AATPTGPARLALKTGAPVVPA-FAYRLPGGGYRIEFEPPLENPP 158
|
170 180 190
....*....|....*....|....*....|....
gi 727181982 263 LSDEQAAAAYMNKVIEKEIMRAPEQYMWLHRRFK 296
Cdd:cd07984 159 SEDVEEDTQRLNDALEAAIREHPEQWLWFHRRWK 192
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08025 |
PRK08025 |
kdo(2)-lipid IV(A) palmitoleoyltransferase; |
1-306 |
0e+00 |
|
kdo(2)-lipid IV(A) palmitoleoyltransferase;
Pssm-ID: 181200 Cd Length: 305 Bit Score: 567.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 1 MKSAKAFQLALLHPRYWLTWFGLALLFLLVQLPYPLLYRLGVWMGRTSMRFLKRRVTITRRNLELCFPEMDEAQRERKVV 80
Cdd:PRK08025 1 MFPQQKFSREFLHPRYWLTWFGLGVLWLLVQLPYPVLCFLGTRIGRMSRPFLKRRESIARKNLELCFPQMSAEEREKMIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 81 GNFESLGMGLLETGMAWFWSDKRVKRWFNVSGINHLKMAQRDERGVLVIGVHFMSLELGGRAMGLCQPMMAMYRPHNNKA 160
Cdd:PRK08025 81 ENFRSLGMALLETGMAWFWPDSRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLCQPMMATYRPHNNKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 161 MEWAQTKGRMRSNKAMIDRKDLRGMVHALKRGEAVWFAPDQDYGPRGSVFAPLFAVDKAATTSGTFMLARMANPALVPVV 240
Cdd:PRK08025 161 MEWVQTRGRMRSNKAMIGRNNLRGIVGALKKGEAVWFAPDQDYGPKGSSFAPFFAVENVATTNGTYVLSRLSGAAMLTVT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727181982 241 LIRREGGRGYDLLIQPALEDYPlSDEQAAAAYMNKVIEKEIMRAPEQYMWLHRRFKTRPAGAPSLY 306
Cdd:PRK08025 241 MVRKADYSGYRLFITPEMEGYP-TDENQAAAYMNKIIEKEIMRAPEQYLWIHRRFKTRPVGESSLY 305
|
|
| PRK06860 |
PRK06860 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
1-306 |
1.56e-176 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 235880 [Multi-domain] Cd Length: 309 Bit Score: 489.81 E-value: 1.56e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 1 MKSAKAFQLALLHPRYWLTWFGLALLFLLVQLPYPLLYRLGVWMGRTSMRFLKRRVTITRRNLELCFPEMDEAQRERKVV 80
Cdd:PRK06860 3 MTNLPKFSRALLHPRYWLTWLGIGLLWLIVLLPYPVLYKLGRGLGKLALRFMKRRAKIARRNLELCFPEMSEQEREAIVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 81 GNFESLGMGLLETGMAWFWSDKRVKRWFNVSGINHLKMAQRDERGVLVIGVHFMSLELGGRAMGLCQPMMAMYRPHNNKA 160
Cdd:PRK06860 83 KNFESVGMALIETGMAWFWPDWRIKRWTEVEGLEHIREVQAQGRGVLLVGVHFLTLELGARIFGMHNPGIGVYRPNDNPL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 161 MEWAQTKGRMRSNKAMIDRKDLRGMVHALKRGEAVWFAPDQDYGPRGSVFAPLFAVDKAATTSGTFMLARMANPALVPVV 240
Cdd:PRK06860 163 YDWLQTWGRLRSNKSMLDRKDLKGMIKALKKGERIWYAPDHDYGPRSSVFVPFFAVEQAATTTGTWMLARMSKAAVIPFV 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727181982 241 LIRREGGRGYDLLIQPALEDYPLSDEQAAAAYMNKVIEKEIMRAPEQYMWLHRRFKTRPAGAPSLY 306
Cdd:PRK06860 243 PRRKPDGKGYELIILPPEDSPPLDDAEATAAWMNKVVEKCILMAPEQYMWLHRRFKTRPEGVPSRY 308
|
|
| lipid_A_htrB |
TIGR02207 |
lipid A biosynthesis lauroyl (or palmitoleoyl) acyltransferase; This model represents a narrow ... |
6-306 |
1.23e-168 |
|
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: 469.90 E-value: 1.23e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 6 AFQLALLHPRYWLTWFGLALLFLLVQLPYPLLYRLGVWMGRTSMRFLKRRVTITRRNLELCFPEMDEAQRERKVVGNFES 85
Cdd:TIGR02207 2 EFSASLLHPRYWPTWLGLGVLWLIVQLPYPVLLALGRGIGRLAMRLMKRRVHIARRNLELCFPHMSDAERERLLRENFES 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 86 LGMGLLETGMAWFWSDKRVKRWFNVSGINHLKMAQRDERGVLVIGVHFMSLELGGRAMGLCQPMMAMYRPHNNKAMEWAQ 165
Cdd:TIGR02207 82 TGMALFETGMAWFWSDARIKKWMQIEGLEHLQRAQKQGRGVLLVGVHFLTLELGARIFGQQQPGIGVYRPHNNPLFDWIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 166 TKGRMRSNKAMIDRKDLRGMVHALKRGEAVWFAPDQDYGPRGSVFAPLFAVDKAATTSGTFMLARMANPALVPVVLIRRE 245
Cdd:TIGR02207 162 TRGRLRSNKAMIDRKDLRGMIKALKNGERIWYAPDHDYGRKSSVFVPFFAVPDAATTTGTSILARLSKCAVVPFTPRRNE 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727181982 246 GGRGYDLLIQPALEDYPLSDEQAAAAYMNKVIEKEIMRAPEQYMWLHRRFKTRP-AGAPSLY 306
Cdd:TIGR02207 242 DGSGYRLKIDPPLDDFPGDDEIAAAARMNKIVEKMIMRAPEQYMWLHRRFKTRPdEGESSLY 303
|
|
| LpxP |
COG1560 |
Palmitoleoyl-ACP: Kdo2-lipid-IV acyltransferase (lipid A biosynthesis) [Lipid transport and ... |
33-295 |
1.45e-108 |
|
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: 316.36 E-value: 1.45e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 33 PYPLLYRLGVWMGRTSMRFLKRRVTITRRNLELCFPEMDEAQRERKVVGNFESLGMGLLETGMAWFWSDKRVKRWFNVSG 112
Cdd:COG1560 9 PLRLLYRLGDLLGRLLYRLAGRRRRVARRNLALAFPELSEAEREALARASFRNLGRTLLETLRLWRLSPERLRKRVEVEG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 113 INHLKMAQRDERGVLVIGVHFMSLELGGRAMGLC-QPMMAMYRPHNNKAMEWAQTKGRMRSNKAMIDRKD-LRGMVHALK 190
Cdd:COG1560 89 LEHLEAALAEGRGVILLTPHFGNWELAGAALALRgYPVTAVYRPLKNPLLDRLIRRGRERFGGELIPRKDgVRALLRALR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 191 RGEAVWFAPDQDYGPRGSVFAPLFAVDkAATTSGTFMLARMANPALVPVVLIRREGGRGYDLLIQPALEDyPLSDEQAAA 270
Cdd:COG1560 169 KGGIVGLLPDQDPGRKSGVFVPFFGVP-AATPTGPARLARRTGAPVVPVFARRLPDGRGYRLEIEPPLED-FSEDVEADT 246
|
250 260
....*....|....*....|....*
gi 727181982 271 AYMNKVIEKEIMRAPEQYMWLHRRF 295
Cdd:COG1560 247 QRLNRALEAWIREHPEQWLWLHRRW 271
|
|
| Lip_A_acyltrans |
pfam03279 |
Bacterial lipid A biosynthesis acyltransferase; |
5-297 |
8.27e-108 |
|
Bacterial lipid A biosynthesis acyltransferase;
Pssm-ID: 281296 [Multi-domain] Cd Length: 294 Bit Score: 315.44 E-value: 8.27e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 5 KAFQLALLHPRYWLTWFGLALLFLLVQLPYPLLYRLGVWMGRTSMRFLKRRVTITRRNLELCFPEMDEAQRERKVVGNFE 84
Cdd:pfam03279 1 PKFSPELLHPRYWLDWLGIAVLRLLALLPYSALRRIGKGLGRLAGRFLKRRRKIARRNLALCFPEMSEAEREQIIDKSFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 85 SLGMGLLETGMAWFWSDKRVKRWFNVSGINHLKMAQRDERGVLVIGVHFMSLELGGRAMGLCQPMMA-MYRPHNNKAMEW 163
Cdd:pfam03279 81 SVGRAIVETGRVWFWPDSRIAKRFEVIGLEHIKEALAQGRGAILVGPHFGNWDLGGRVLGQQYPGMAvYRPNLKNPLLDW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 164 AQTKGRMRSNKAMIDRKD-LRGMVHALKRGEAVWFAPDQDYGPRGSVFAPLFAVDKAATTSGTFMLARMaNPALVPVVLI 242
Cdd:pfam03279 161 LQTSGRERFGGRMLPRQNgIKGLIKALRKGEVVWYLPDQDLGRKDSVFVPFFGVPAATTTGPAKLALKT-KAAVIPVFPI 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 727181982 243 RREGGRGYDLLIQPALEDYPLSDEQAAAAYMNKVIEKEIMRAPEQYMWLHRRFKT 297
Cdd:pfam03279 240 RNGDGSGYTVIVHPALDLTITDDVEQIAQAMNQIVEKFIMPAPEQYFWLHRRWKT 294
|
|
| PRK05646 |
PRK05646 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
7-306 |
6.81e-100 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 235543 [Multi-domain] Cd Length: 310 Bit Score: 295.95 E-value: 6.81e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 7 FQLALLHPRYWLTWFGLALLFLLVQLPYPLLYRLGVWMGRTSMRFLKRRVTITRRNLELCFPEMDEAQRERKVVGNFESL 86
Cdd:PRK05646 6 FRAAFLHPRFWPLWLGLGLLWLVVQLPYRVLLWLGRALGALMYRLAGSRRRIAARNLELCFPEKSAAERERLLKENFAST 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 87 GMGLLETGMAWFWSDKRVKRWFNVSGINHLKMAQRDERGVLVIGVHFMSLELGGRAMGLCQPMMAMYRPHNNKAMEWAQT 166
Cdd:PRK05646 86 GIAFFEMAMSWWWPKARLARLAHIEGLEHLQQAQQEGQGVILMALHFTTLEIGAALLGQQHTIDGMYREHKNPVFDFIQR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 167 KGRMRSNK--AMIDRKDLRGMVHALKRGEAVWFAPDQDYGPRGSVFAPLFAVdKAATTSGTFMLARMANPALVPVVLIRR 244
Cdd:PRK05646 166 RGRERHNLdsTAIEREDVRGMLKLLRAGRAIWYAPDQDYGAKQSIFVPLFGI-PAATVTATTKFARLGRARVIPFTQKRL 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727181982 245 EGGRGYDLLIQPALEDYPLSDEQAAAAYMNKVIEKEIMRAPEQYMWLHRRFKTRPAGAPSLY 306
Cdd:PRK05646 245 ADGSGYRLVIHPPLEDFPGESEEADCLRINQWVERVVRECPEQYLWAHRRFKSRPEGEPKLY 306
|
|
| PRK08733 |
PRK08733 |
LpxL/LpxP family Kdo(2)-lipid IV(A) lauroyl/palmitoleoyl acyltransferase; |
3-306 |
4.94e-77 |
|
LpxL/LpxP family Kdo(2)-lipid IV(A) lauroyl/palmitoleoyl acyltransferase;
Pssm-ID: 181542 [Multi-domain] Cd Length: 306 Bit Score: 237.49 E-value: 4.94e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 3 SAKAFQLALLHPRYWLTWFGLALLFLLVQLPYPLLYRLGVWMGRTSMRFLKRRVTITRRNLELCFPEMDEAQRERKVVGN 82
Cdd:PRK08733 5 ANVAVRPSLRNPKHWPMYLGLAVMVLAARLPWTLQRALGRGVGWVAMRLAGTRRRAAEVNLKLCFPEQDDAWRARLLRDS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 83 FESLGMGLLETGMAWFWSDKRVKRWFNVSGINHLKMAQRDERGVLVIGVHFMSLELGGRAmgLCQ--PMMAMYRPHNNKA 160
Cdd:PRK08733 85 FDALGVGLFEFARAWWGSIDVIRPGVQIEGLEHLQQLQQQGRGVLLVSGHFMTLEMCGRL--LCDhvPLAGMYRRHRNPV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 161 MEWAQTKGRMRSNKAMIDRKDLRGMVHALKRGEAVWFAPDQDYGPRGSVFAPLFAVdKAATTSGTFMLARMANPALVPvV 240
Cdd:PRK08733 163 FEWAVKRGRLRYATHMFANEDLRATIKHLKRGGFLWYAPDQDMRGKDTVFVPFFGH-PASTITATHQLARLTGCAVVP-Y 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727181982 241 LIRREGGRgYDLLIQPALEDYPLSDEQAAAAYMNKVIEKEIMRAPEQYMWLHRRFKTRPAGAPSLY 306
Cdd:PRK08733 241 FHRREGGR-YVLKIAPPLADFPSDDVIADTTRVNAAIEDMVREAPDQYLWIHRRFKRQPGGRSDFY 305
|
|
| LPLAT_LABLAT-like |
cd07984 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LABLAT-like; ... |
105-296 |
3.83e-67 |
|
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: 208.22 E-value: 3.83e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 105 KRWFNVSGINHLKMAQRDERGVLVIGVHFMSLELGGRAMGLC-QPMMAMYRPHNNKAMEWAQTKGRMRSNKAMIDRKD-L 182
Cdd:cd07984 1 LKRVEREGLEHLEAALAKGKGVILLTAHFGNWELAGLALALLgYPVTVVYRPLKNPLLDRLITRGRERFGARLIPRGGgL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 183 RGMVHALKRGEAVWFAPDQDYGPRGSVFAPLFAVDkAATTSGTFMLARMANPALVPVvLIRREGGRGYDLLIQPALEDYP 262
Cdd:cd07984 81 RELIRALKKGEIVGILPDQDPGRKGGVFVPFFGRP-AATPTGPARLALKTGAPVVPA-FAYRLPGGGYRIEFEPPLENPP 158
|
170 180 190
....*....|....*....|....*....|....
gi 727181982 263 LSDEQAAAAYMNKVIEKEIMRAPEQYMWLHRRFK 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 |
1.06e-60 |
|
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: 195.41 E-value: 1.06e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 7 FQLALLHPRYWLTWFGLALLFLLVQLPY----PLLYRLGVWMGRTSmrflKRRVTITRRNLELCFPEMDEAQRERKVVGN 82
Cdd:TIGR02208 5 FQKSFLHPKYWGTWLGVFALVLLAFMPAklrdPIAKVLAKFVGPIA----KKPRGRARINLSACFPEKSEAERETIIDNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 83 FESLGMGLLETGMAWFWSDKRVKRWFNVSGINHLKMAQRDERGVLVIGVHFMSLELGGRAM-GLCQPMMAMYRPHNNKAM 161
Cdd:TIGR02208 81 FATFVQVMLSQAELAIRSKAHLRRRVNLMGLEHIEAAQAAGKPVIFLVPHGWAIDYAGLRLaSQGLPMVTMFNNHKNPLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 162 EWAQTKGRMRSNKAMIDRKD-LRGMVHALKRGEAVWFAPDQDYGPRGSVFAPLFAVDKaATTSGTFMLARMANPALVPVV 240
Cdd:TIGR02208 161 DWLWNRVRSRFGGHVYAREAgIKALLASLKRGESGYYLPDEDHGPEQSVFVPFFATYK-ATLPVVGRLAKAGNAQVVPVF 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727181982 241 LIRREGGRGYDLLIQPALEDYPLSDEQAAAAYMNKVIEKEIMRAPEQYMWLHRRFKTRPAGAPSLY 306
Cdd:TIGR02208 240 PGYNQVTGKFELTVRPAMATELSVDPEQEARAMNKEVEQFILPYPEQYMWILRLLKTRPDGEASIY 305
|
|
| PRK06946 |
PRK06946 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
19-306 |
2.72e-56 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 180770 [Multi-domain] Cd Length: 293 Bit Score: 183.73 E-value: 2.72e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 19 TWFGLALLFLLVQLPYPLLYRLGVWMGRTSMRFLKRRVTITRRNLELCFPEMDEAQRERKVVGNFESLGMGLLETGMAWF 98
Cdd:PRK06946 6 TALAIGLLKLLAFLPYGLTARFGDGLGWLLYRIPSRRRRIVHTNLKLCFPDWSDARREELARRHFRHVIRSYVERSVQWF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 99 WSDKRVKRWFNV-SGINhlkMAQRDERGVLVIGVHFMSLELGGRA--MGLCQPMMAMYRPHNNKAMEWAQTKGRMRSNKA 175
Cdd:PRK06946 86 GSEKKLEKLVQVdSAID---LTDPDGPPTIFLGLHFVGIEAGSIWlnYSLRRRVGSLYTPMSNPLLDAIAKAARGRFGAE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 176 MIDRKD-LRGMVHALKRGEAVWFAPDQDYGPRGSVFAPLFAVdKAATTSGTFMLARMANPALVPVVLIRREGGRGYDLLI 254
Cdd:PRK06946 163 MVSRADsARQVLRWLRDGKPVMLGADMDFGLRDSTFVPFFGV-PACTLTAVSRLARTGGAQVVPFITEVLPDYKGYRLRV 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 727181982 255 QPALEDYPLSDEQAAAAYMNKVIEKEIMRAPEQYMWLHRRFKTRPAGAPSLY 306
Cdd:PRK06946 242 FKPWENYPTGDDDLDARRMNAFLEEQIRLMPEQYYWVHKRFKTRPPGEPSVY 293
|
|
| PRK08706 |
PRK08706 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
33-306 |
2.35e-54 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 169557 [Multi-domain] Cd Length: 289 Bit Score: 178.52 E-value: 2.35e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 33 PYPLLYRLGVWMGRTSMRFLKRRVTITRRNLELCFPEMDEAQRERKVVGNFESLGMGLLETGMAWFWSDKRVKRWFNVSG 112
Cdd:PRK08706 15 PFALLHKLADLTGLLAYLLVKPRRRIGEINLAKCFPEWDEEKRKTVLKQHFKHMAKLMLEYGLYWYAPAGRLKSLVRYRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 113 INHLKMAQRDERGVLVIGVHFMSLELGGRAMGLCQPMMAMYRPHNNKAMEWAQTKGRMRSNKAMI--DRKDLRGMVHALK 190
Cdd:PRK08706 95 KHYLDDALAAGEKVIILYPHFTAFEMAVYALNQDVPLISMYSHQKNKILDEQILKGRNRYHNVFLigRTEGLRALVKQFR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 191 RGEAVW-FAPDQDYGPRGSVFAPLFAVdKAATTSGTFMLARMANPALVPVVlIRREGGRGYDLLIQPALEDYPLSDEQAA 269
Cdd:PRK08706 175 KSSAPFlYLPDQDFGRNDSVFVDFFGI-QTATITGLSRIAALANAKVIPAI-PVREADNTVTLHFYPAWDSFPSEDAQAD 252
|
250 260 270
....*....|....*....|....*....|....*..
gi 727181982 270 AAYMNKVIEKEIMRAPEQYMWLHRRFKTRPAGAPSLY 306
Cdd:PRK08706 253 AQRMNRFIEERVREHPEQYFWLHKRFKTRPEGSPDFY 289
|
|
| PRK08943 |
PRK08943 |
lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; Validated |
7-306 |
5.01e-54 |
|
lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; Validated
Pssm-ID: 236355 Cd Length: 314 Bit Score: 178.52 E-value: 5.01e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 7 FQLALLHPRYWLTWFGLALLFLLVQLPYPLLYRLGVWMGRTSMRFLKRRVTITRRNLELCFPEMDEAQRERKVVGNFESL 86
Cdd:PRK08943 14 FQKSFLHPRYWGTWLGIGALAGLALMPPRLRDPLAAKLGRLVGKLAKKARRRARINLSLCFPEKSEAEREAIIDEMFATA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 87 GMGLLETGMAWFWSDKRVKRWFNVSGINHLKMAQRDERGVLVIGVHFMSLELGGRAMGL-CQPMMAMYRPHNNKAMEWAQ 165
Cdd:PRK08943 94 PQAMLMMAELALRSPKHLQRRVEWHGLEILEEARANGENVIFLVPHGWAIDIPAMLLASqGQPMAAMFHNQRNPLFDWLW 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 166 TKGRMRSNKAMIDRKD-LRGMVHALKRGEAVWFAPDQDYGPRGSVFAPLFAVDKaATTSGTFMLARMANPALVPVVLIRR 244
Cdd:PRK08943 174 NRVRRRFGGRLHAREDgIKPFISSVRQGYWGYYLPDEDHGPEHSVFVDFFATYK-ATLPGIGRLAKVCRARVVPLFPVYN 252
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727181982 245 EGGRGYDLLIQPALEDYPLSDEQAAAAYMNKVIEKEIMRAPEQYMWLHRRFKTRPAGAPsLY 306
Cdd:PRK08943 253 GKTHRLDIEIRPPMDDLLSADDETIARRMNEEVEQFVGPHPEQYMWILKLLKTRKPGED-LY 313
|
|
| PRK08905 |
PRK08905 |
lysophospholipid acyltransferase family protein; |
33-303 |
2.66e-39 |
|
lysophospholipid acyltransferase family protein;
Pssm-ID: 236348 [Multi-domain] Cd Length: 289 Bit Score: 139.36 E-value: 2.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 33 PYPLLYRLGVWMGRTSMRFLKRRVTITRRNLELCFPEMDEAQRERKVVgnfeSLGMGLLEtgMAWFWS---DKRVKRWFN 109
Cdd:PRK08905 13 PLSWLHALGGWLGRLAYRLPGRYRRRLRANLRQAGGDPDPAMVKAAAA----ETGRMILE--LPYVWFrkpEEIETMVKD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 110 VSGINHLKMAQRDERGVLVIGVHFMSLELGGRAMGLCQPMMAMYRPHNNKAMEWAQTKGRMRSNKAMI--DRKDLRGMVH 187
Cdd:PRK08905 87 DHGWEHVEAALAEGRGILFLTPHLGCFEVTARYIAQRFPLTAMFRPPRKAALRPLMEAGRARGNMRTApaTPQGVRMLVK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 188 ALKRGEAVWFAPDQDYGPRGSVFAPLFAvdKAATTsgTFMLARMANPALVPVVLI---RREGGRGYDLLIQPALEDYPlS 264
Cdd:PRK08905 167 ALRRGEAVGILPDQVPSGGEGVWAPFFG--RPAYT--MTLVARLAEVTGVPVIFVageRLPRGRGYRLHLRPVQEPLP-G 241
|
250 260 270
....*....|....*....|....*....|....*....
gi 727181982 265 DEQAAAAYMNKVIEKEIMRAPEQYMWLHRRFKtRPAGAP 303
Cdd:PRK08905 242 DKAADAAVINAEIERLIRRFPTQYLWGYNRYK-RPRGAP 279
|
|
| PRK05645 |
PRK05645 |
lysophospholipid acyltransferase; |
33-306 |
4.38e-28 |
|
lysophospholipid acyltransferase;
Pssm-ID: 135493 [Multi-domain] Cd Length: 295 Bit Score: 110.00 E-value: 4.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 33 PYPLLYRLGVWMGRTSMRFLKRRVTITRRNLELCFPEMDEAQRERKVVGNFESLGMGLLETGMAWFW-SDKRVKRWFNVS 111
Cdd:PRK05645 20 PWRAVQGVGAGIGWLMWKLPNRSREVVRINLSKCFPELSPAELEKLVGQSLMDIGKTLTESACAWIWpPQKSLELVREVE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 112 GINHLKMAQRDERGVLVIGVHFMSLE-LGGRAMGLCQPMMaMYRPHNNKAMEWAQTKGR--MRSNKAMIDRKDLRGMVHA 188
Cdd:PRK05645 100 GLEVLEQALASGKGVVGITSHLGNWEvLNHFYCSQCKPII-FYRPPKLKAVDELLRKQRvqLGNRVAPSTKEGILSVIKE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 189 LKRGEAVWFAPDQDYGPRGSVFAPLFAVdkAATTSgTFMLARMANPALVPVVL--IRREGGRGYDLLIQPALEDYPLSDE 266
Cdd:PRK05645 179 VRKGGQVGIPADPEPAESAGIFVPFLGT--QALTS-KFVPNMLAGGKAVGVFLhaLRLPDGSGYKVILEAAPEDMYSTDV 255
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 727181982 267 QAAAAYMNKVIEKEIMRAPEQYMWLHRRFKTRPAGAPSLY 306
Cdd:PRK05645 256 EVSAAAMSKVVERYVRAYPSQYMWSMKRFKKRPAGEARWY 295
|
|
| PRK08419 |
PRK08419 |
lipid A biosynthesis lauroyl acyltransferase; Reviewed |
33-296 |
8.23e-21 |
|
lipid A biosynthesis lauroyl acyltransferase; Reviewed
Pssm-ID: 181420 [Multi-domain] Cd Length: 298 Bit Score: 90.09 E-value: 8.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 33 PYPLLYRLGVWMGRTSMRFLKRRVTITRRNLELCFPE-MDEAQRERKVVGNFESLGMGLLETGMAWFWSDKRVKRWFNVS 111
Cdd:PRK08419 21 PHCIFLRLAKALAFIMRYLDKKRRKIAKANLDFCFGEsKSQEEKKRIIKKCYENFAFFGLDFIRNQNTTKEEILNKVTFI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 112 GINHLKMAQRDERGVLVIGVHFMSLELGGRAMGL-CQPMMAMYRPHNNKAMEWAQTKGRMRSNKAMIDRKD-LRGMVHAL 189
Cdd:PRK08419 101 NEENLLDALKKKRPIIVTTAHYGYWELFSLALAAyYGAVSIVGRLLKSAPINEMISKRREQFGIELIDKKGaMKELLKAL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 190 KRGEAVWFAPDQDYGPRGSVFAPLFavDKAAT-TSGTFMLARMANPALVPvVLIRREGGRGYDLLIQPALEDYPLSDEQA 268
Cdd:PRK08419 181 KQGRALGILVDQNVVPKEGVEVKFF--NKRVThTTIASILARRYNALIIP-VFIFNDDYSHFTITFFPPIRSKITDDAEA 257
|
250 260 270
....*....|....*....|....*....|..
gi 727181982 269 ----AAAYMNKVIEKEIMRAPEQYMWLHRRFK 296
Cdd:PRK08419 258 dileATQAQASACEEMIRKKPDEYFWFHRRFK 289
|
|
| PRK08734 |
PRK08734 |
lauroyl acyltransferase; |
33-302 |
1.80e-18 |
|
lauroyl acyltransferase;
Pssm-ID: 181543 [Multi-domain] Cd Length: 305 Bit Score: 83.78 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 33 PYPLLYRLGVWMGRTSMRFLKRRVTITRRNLELCFPEMDEAQRERKVVGNFESLGMGLLETGMAWFWSD-KRVKRWFNVS 111
Cdd:PRK08734 21 PWPLLKRLADLLAWSWRKLNARESRVTRRNLELAYPELSPQQRAQLHAQILRSTARQALEVLRTWTHPPaENLARLRQRH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 112 GINHLKMAQRDERGVLVIGVHFMSLELGGRAMGLCQPMMAMYRPHNNKAMEWAQTKGRMRSNKAMIDRKD--LRGMVHAL 189
Cdd:PRK08734 101 GQELYDAALASGRGVIVAAPHFGNWELLNQWLSERGPIAIVYRPPESEAVDGFLQLVRGGDNVRQVRAEGpaVRQLFKVL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 190 KRGEAVWFAPDQDYGPRGSVFAPLFAVdKAATTSGTFMLARMANPALVPVVLIRREGGRGYDLLIQPALEDYPLSDEQAA 269
Cdd:PRK08734 181 KDGGAVGILPDQQPKMGDGVFAPFFGI-PALTMTLVNRLAERTGATVLYGWCERIGPDLEFALHVQPADPAVADPDPLRA 259
|
250 260 270
....*....|....*....|....*....|...
gi 727181982 270 AAYMNKVIEKEIMRAPEQYMWLHRRFKTRPAGA 302
Cdd:PRK08734 260 ATALNAGIERIARRDPAQYQWTYKRYTLRPPGS 292
|
|
| PRK06553 |
PRK06553 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
39-294 |
5.25e-10 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 235827 [Multi-domain] Cd Length: 308 Bit Score: 59.22 E-value: 5.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 39 RLGVWMGRTSMRFLkRRVTITRRNLELCFPEMDEAQRERKVVGNFESLGMGLLE---TGMAWFWSDKRVKRWF-NVSGIN 114
Cdd:PRK06553 45 NFFGRLARLIGPLL-PRHRVALDNLRAAFPEKSEAEIEAIALGMWDNLGRLGAEyafLDAIFDYDPEAPEPGRvEVRGIE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 115 HLKMAQRDERGVLVIGVHFMSLEL---GGRAMGLcqPMMAMYRPHNNKAMEWAQTKGRMRSNKAMI--DRKDLRGMVHAL 189
Cdd:PRK06553 124 IFERLRDDGKPALIFTAHLGNWELlaiAAAAFGL--DVTVLFRPPNNPYAARKVLEARRTTMGGLVpsGAGAAFALAGVL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 190 KRGEAVWFAPDQDY--GPRGSVFA------PLFAvdkaattsgtfMLARMANPALVPVVLIRREGGRgYDLLIQPALEdy 261
Cdd:PRK06553 202 ERGGHVGMLVDQKFtrGVEVTFFGrpvktnPLLA-----------KLARQYDCPVHGARCIRLPGGR-FRLELTERVE-- 267
|
250 260 270
....*....|....*....|....*....|....*....
gi 727181982 262 PLSDE------QAAAAYMNKVIEKEIMRAPEQYMWLHRR 294
Cdd:PRK06553 268 LPRDAdgqidvQATMQALTDVVEGWVREYPGQWLWLHRR 306
|
|
| PRK05906 |
PRK05906 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
186-296 |
1.58e-06 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 168292 [Multi-domain] Cd Length: 454 Bit Score: 49.01 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 186 VHALKRGEAVWFAPDQDYgPRGSVFAPLFAvDKAATTSGTFMLARMANPALVPVVLIRREggRGYDLLIQPAL-EDYPLS 264
Cdd:PRK05906 203 LRALHQGEVVGIVGDQAL-LSSSYSYPLFG-SQAFTTTSPALLAYKTGKPVIAVAIYRKP--NGYLVVPSKKFyANKSLP 278
|
90 100 110
....*....|....*....|....*....|....*
gi 727181982 265 DEQAAAAYMNKV---IEKEIMRAPEQYMWLHRRFK 296
Cdd:PRK05906 279 IKESTEQLMDRLmrfLEKGIACKPEQWMWLHKRWK 313
|
|
| PRK06628 |
PRK06628 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
51-296 |
2.10e-06 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 102471 Cd Length: 290 Bit Score: 48.39 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 51 FLKRRV-------TITRRNLELCFPEMDEAqrERKVVGNFESLGMGLLETGMAWFWSDKRVKRWFNVSGINHLKmaQRDE 123
Cdd:PRK06628 38 FIARKVgilfavnKIARRNIKAVFGDMCDV--EKIIDQTWDNFGRFIGEFTYVNKMDEAELERRIEIIGIENIK--KLEG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 124 RGVLVIGVHFMSLELGGRAMGLCQPMMA-MYRPHNNKAMEWAQTKGRMRSNKAMIDR--KDLRGMVHALKRGEAVWFAPD 200
Cdd:PRK06628 114 QPFLLFSGHFANWDISLKILHKFYPKVAvIYRKANNPYVNKLVNESRAGDKLRLIPKgpEGSRALVRAIKESESIVMLVD 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181982 201 QDYGprGSVFAPlFAVDKAATTSGTFMLARMANPALVPVVLIRREGGRgYDLLIQPALEdYPLSDEQAAAAY-----MNK 275
Cdd:PRK06628 194 QKMN--DGIEVP-FLGHPAMTASAIAKIALQYKYPIIPCQIIRTKGSY-FKVIVHPQLK-FEQTGDNKADCYnimlnINQ 268
|
250 260
....*....|....*....|.
gi 727181982 276 VIEKEIMRAPEQYMWLHRRFK 296
Cdd:PRK06628 269 MLGEWVKQNPAQWFWFHNRWK 289
|
|
| LPLAT |
cd06551 |
Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; ... |
169-241 |
7.30e-03 |
|
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: 37.01 E-value: 7.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727181982 169 RMRSNKAMIDRKDLRGMVHALKR-GEAVWFAPDQDYGPRgSVFAPLFAvdkaattSGTFMLARMANPALVPVVL 241
Cdd:cd06551 77 SVDRDSPRSAAKSLKYVARLLSKpGSVVWIFPEGTRTRR-DKRPLQFK-------PGVAHLAEKAGVPIVPVAL 142
|
|
| LPLAT_DUF374-like |
cd07983 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: DUF374; ... |
182-240 |
8.68e-03 |
|
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: DUF374; 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 the uncharacterized DUF374 phospholipid/glycerol acyltransferases and similar proteins.
Pssm-ID: 153245 [Multi-domain] Cd Length: 189 Bit Score: 36.42 E-value: 8.68e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 727181982 182 LRGMVHALKRGEAVWFAPDqdyGPRGsvfaPLFAVdkaatTSGTFMLARMANPALVPVV 240
Cdd:cd07983 87 LREMLRALKDGYNIAITPD---GPRG----PRYKV-----KPGVILLARKSGAPIVPVA 133
|
|
| |
