|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06860 |
PRK06860 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
1-307 |
0e+00 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 235880 [Multi-domain] Cd Length: 309 Bit Score: 558.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 1 MTKLPRFSLAFLHPRYWLSWAGIAALWLIMLLPYPLLFRIGHSLGRLAMRLLPRRVEIARRNLELCFPEMKKAERESLLQ 80
Cdd:PRK06860 3 MTNLPKFSRALLHPRYWLTWLGIGLLWLIVLLPYPVLYKLGRGLGKLALRFMKRRAKIARRNLELCFPEMSEQEREAIVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 81 RNFESVGMGVIETGMAWFWPAWRVKKCFTVTGYEHMEKARAKGNGVVLVGMHFLTLELGARLFGMLNPGIGVYRPNNNAL 160
Cdd:PRK06860 83 KNFESVGMALIETGMAWFWPDWRIKRWTEVEGLEHIREVQAQGRGVLLVGVHFLTLELGARIFGMHNPGIGVYRPNDNPL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 161 LDWLQTRGRLRSNKTMLDRHDLKGMIRSLKQNEILWYAPDHDYGKTNSVFVPFFAVADAATTAGSYMLVKSAKPAVIPFV 240
Cdd:PRK06860 163 YDWLQTWGRLRSNKSMLDRKDLKGMIKALKKGERIWYAPDHDYGPRSSVFVPFFAVEQAATTTGTWMLARMSKAAVIPFV 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2255845135 241 PRRRADGTGYELIILEDISEALQgGDKESVATQMNRAIEQAVRMAPEQYMWLHRRFKTRPEGQPDRY 307
Cdd:PRK06860 243 PRRKPDGKGYELIILPPEDSPPL-DDAEATAAWMNKVVEKCILMAPEQYMWLHRRFKTRPEGVPSRY 308
|
|
| lipid_A_htrB |
TIGR02207 |
lipid A biosynthesis lauroyl (or palmitoleoyl) acyltransferase; This model represents a narrow ... |
5-307 |
7.83e-174 |
|
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: 484.15 E-value: 7.83e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 5 PRFSLAFLHPRYWLSWAGIAALWLIMLLPYPLLFRIGHSLGRLAMRLLPRRVEIARRNLELCFPEMKKAERESLLQRNFE 84
Cdd:TIGR02207 1 PEFSASLLHPRYWPTWLGLGVLWLIVQLPYPVLLALGRGIGRLAMRLMKRRVHIARRNLELCFPHMSDAERERLLRENFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 85 SVGMGVIETGMAWFWPAWRVKKCFTVTGYEHMEKARAKGNGVVLVGMHFLTLELGARLFGMLNPGIGVYRPNNNALLDWL 164
Cdd:TIGR02207 81 STGMALFETGMAWFWSDARIKKWMQIEGLEHLQRAQKQGRGVLLVGVHFLTLELGARIFGQQQPGIGVYRPHNNPLFDWI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 165 QTRGRLRSNKTMLDRHDLKGMIRSLKQNEILWYAPDHDYGKTNSVFVPFFAVADAATTAGSYMLVKSAKPAVIPFVPRRR 244
Cdd:TIGR02207 161 QTRGRLRSNKAMIDRKDLRGMIKALKNGERIWYAPDHDYGRKSSVFVPFFAVPDAATTTGTSILARLSKCAVVPFTPRRN 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2255845135 245 ADGTGYELIILEDIsEALQGGDKESVATQMNRAIEQAVRMAPEQYMWLHRRFKTRP-EGQPDRY 307
Cdd:TIGR02207 241 EDGSGYRLKIDPPL-DDFPGDDEIAAAARMNKIVEKMIMRAPEQYMWLHRRFKTRPdEGESSLY 303
|
|
| Lip_A_acyltrans |
pfam03279 |
Bacterial lipid A biosynthesis acyltransferase; |
5-298 |
3.11e-114 |
|
Bacterial lipid A biosynthesis acyltransferase;
Pssm-ID: 281296 [Multi-domain] Cd Length: 294 Bit Score: 332.77 E-value: 3.11e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 5 PRFSLAFLHPRYWLSWAGIAALWLIMLLPYPLLFRIGHSLGRLAMRLLPRRVEIARRNLELCFPEMKKAERESLLQRNFE 84
Cdd:pfam03279 1 PKFSPELLHPRYWLDWLGIAVLRLLALLPYSALRRIGKGLGRLAGRFLKRRRKIARRNLALCFPEMSEAEREQIIDKSFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 85 SVGMGVIETGMAWFWPAWRVKKCFTVTGYEHMEKARAKGNGVVLVGMHFLTLELGARLFGMLNPGIGVYRPN-NNALLDW 163
Cdd:pfam03279 81 SVGRAIVETGRVWFWPDSRIAKRFEVIGLEHIKEALAQGRGAILVGPHFGNWDLGGRVLGQQYPGMAVYRPNlKNPLLDW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 164 LQTRGRLRSNKTMLDRHD-LKGMIRSLKQNEILWYAPDHDYGKTNSVFVPFFAVADAATTAGSYMLVKSaKPAVIPFVPR 242
Cdd:pfam03279 161 LQTSGRERFGGRMLPRQNgIKGLIKALRKGEVVWYLPDQDLGRKDSVFVPFFGVPAATTTGPAKLALKT-KAAVIPVFPI 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2255845135 243 RRADGTGYELIILEDIsEALQGGDKESVATQMNRAIEQAVRMAPEQYMWLHRRFKT 298
Cdd:pfam03279 240 RNGDGSGYTVIVHPAL-DLTITDDVEQIAQAMNQIVEKFIMPAPEQYFWLHRRWKT 294
|
|
| LpxP |
COG1560 |
Palmitoleoyl-ACP: Kdo2-lipid-IV acyltransferase (lipid A biosynthesis) [Lipid transport and ... |
25-296 |
1.08e-109 |
|
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: 320.21 E-value: 1.08e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 25 ALWLIMLLPYPLLFRIGHSLGRLAMRLLPRRVEIARRNLELCFPEMKKAERESLLQRNFESVGMGVIETGMAWFWPAWRV 104
Cdd:COG1560 1 LLRLLRLLPLRLLYRLGDLLGRLLYRLAGRRRRVARRNLALAFPELSEAEREALARASFRNLGRTLLETLRLWRLSPERL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 105 KKCFTVTGYEHMEKARAKGNGVVLVGMHFLTLELGARLFGMLN-PGIGVYRPNNNALLDWLQTRGRLRSNKTMLDRHD-L 182
Cdd:COG1560 81 RKRVEVEGLEHLEAALAEGRGVILLTPHFGNWELAGAALALRGyPVTAVYRPLKNPLLDRLIRRGRERFGGELIPRKDgV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 183 KGMIRSLKQNEILWYAPDHDYGKTNSVFVPFFAVaDAATTAGSYMLVKSAKPAVIPFVPRRRADGTGYELIILEDISEAl 262
Cdd:COG1560 161 RALLRALRKGGIVGLLPDQDPGRKSGVFVPFFGV-PAATPTGPARLARRTGAPVVPVFARRLPDGRGYRLEIEPPLEDF- 238
|
250 260 270
....*....|....*....|....*....|....
gi 2255845135 263 qGGDKESVATQMNRAIEQAVRMAPEQYMWLHRRF 296
Cdd:COG1560 239 -SEDVEADTQRLNRALEAWIREHPEQWLWLHRRW 271
|
|
| LPLAT_LABLAT-like |
cd07984 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LABLAT-like; ... |
105-297 |
2.22e-62 |
|
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LABLAT-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as lipid A biosynthesis lauroyl/myristoyl (LABLAT, HtrB) acyltransferases and similar proteins.
Pssm-ID: 153246 [Multi-domain] Cd Length: 192 Bit Score: 196.67 E-value: 2.22e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 105 KKCFTVTGYEHMEKARAKGNGVVLVGMHFLTLELGARLFGMLN-PGIGVYRPNNNALLDWLQTRGRLRSNKTMLDRHD-L 182
Cdd:cd07984 1 LKRVEREGLEHLEAALAKGKGVILLTAHFGNWELAGLALALLGyPVTVVYRPLKNPLLDRLITRGRERFGARLIPRGGgL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 183 KGMIRSLKQNEILWYAPDHDYGKTNSVFVPFFAVaDAATTAGSYMLVKSAKPAVIPFVPRRRADGtGYELIIlEDISEAL 262
Cdd:cd07984 81 RELIRALKKGEIVGILPDQDPGRKGGVFVPFFGR-PAATPTGPARLALKTGAPVVPAFAYRLPGG-GYRIEF-EPPLENP 157
|
170 180 190
....*....|....*....|....*....|....*
gi 2255845135 263 QGGDKESVATQMNRAIEQAVRMAPEQYMWLHRRFK 297
Cdd:cd07984 158 PSEDVEEDTQRLNDALEAAIREHPEQWLWFHRRWK 192
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06860 |
PRK06860 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
1-307 |
0e+00 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 235880 [Multi-domain] Cd Length: 309 Bit Score: 558.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 1 MTKLPRFSLAFLHPRYWLSWAGIAALWLIMLLPYPLLFRIGHSLGRLAMRLLPRRVEIARRNLELCFPEMKKAERESLLQ 80
Cdd:PRK06860 3 MTNLPKFSRALLHPRYWLTWLGIGLLWLIVLLPYPVLYKLGRGLGKLALRFMKRRAKIARRNLELCFPEMSEQEREAIVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 81 RNFESVGMGVIETGMAWFWPAWRVKKCFTVTGYEHMEKARAKGNGVVLVGMHFLTLELGARLFGMLNPGIGVYRPNNNAL 160
Cdd:PRK06860 83 KNFESVGMALIETGMAWFWPDWRIKRWTEVEGLEHIREVQAQGRGVLLVGVHFLTLELGARIFGMHNPGIGVYRPNDNPL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 161 LDWLQTRGRLRSNKTMLDRHDLKGMIRSLKQNEILWYAPDHDYGKTNSVFVPFFAVADAATTAGSYMLVKSAKPAVIPFV 240
Cdd:PRK06860 163 YDWLQTWGRLRSNKSMLDRKDLKGMIKALKKGERIWYAPDHDYGPRSSVFVPFFAVEQAATTTGTWMLARMSKAAVIPFV 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2255845135 241 PRRRADGTGYELIILEDISEALQgGDKESVATQMNRAIEQAVRMAPEQYMWLHRRFKTRPEGQPDRY 307
Cdd:PRK06860 243 PRRKPDGKGYELIILPPEDSPPL-DDAEATAAWMNKVVEKCILMAPEQYMWLHRRFKTRPEGVPSRY 308
|
|
| lipid_A_htrB |
TIGR02207 |
lipid A biosynthesis lauroyl (or palmitoleoyl) acyltransferase; This model represents a narrow ... |
5-307 |
7.83e-174 |
|
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: 484.15 E-value: 7.83e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 5 PRFSLAFLHPRYWLSWAGIAALWLIMLLPYPLLFRIGHSLGRLAMRLLPRRVEIARRNLELCFPEMKKAERESLLQRNFE 84
Cdd:TIGR02207 1 PEFSASLLHPRYWPTWLGLGVLWLIVQLPYPVLLALGRGIGRLAMRLMKRRVHIARRNLELCFPHMSDAERERLLRENFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 85 SVGMGVIETGMAWFWPAWRVKKCFTVTGYEHMEKARAKGNGVVLVGMHFLTLELGARLFGMLNPGIGVYRPNNNALLDWL 164
Cdd:TIGR02207 81 STGMALFETGMAWFWSDARIKKWMQIEGLEHLQRAQKQGRGVLLVGVHFLTLELGARIFGQQQPGIGVYRPHNNPLFDWI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 165 QTRGRLRSNKTMLDRHDLKGMIRSLKQNEILWYAPDHDYGKTNSVFVPFFAVADAATTAGSYMLVKSAKPAVIPFVPRRR 244
Cdd:TIGR02207 161 QTRGRLRSNKAMIDRKDLRGMIKALKNGERIWYAPDHDYGRKSSVFVPFFAVPDAATTTGTSILARLSKCAVVPFTPRRN 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2255845135 245 ADGTGYELIILEDIsEALQGGDKESVATQMNRAIEQAVRMAPEQYMWLHRRFKTRP-EGQPDRY 307
Cdd:TIGR02207 241 EDGSGYRLKIDPPL-DDFPGDDEIAAAARMNKIVEKMIMRAPEQYMWLHRRFKTRPdEGESSLY 303
|
|
| PRK08025 |
PRK08025 |
kdo(2)-lipid IV(A) palmitoleoyltransferase; |
1-307 |
3.39e-141 |
|
kdo(2)-lipid IV(A) palmitoleoyltransferase;
Pssm-ID: 181200 Cd Length: 305 Bit Score: 401.42 E-value: 3.39e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 1 MTKLPRFSLAFLHPRYWLSWAGIAALWLIMLLPYPLLFRIGHSLGRLAMRLLPRRVEIARRNLELCFPEMKKAERESLLQ 80
Cdd:PRK08025 1 MFPQQKFSREFLHPRYWLTWFGLGVLWLLVQLPYPVLCFLGTRIGRMSRPFLKRRESIARKNLELCFPQMSAEEREKMIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 81 RNFESVGMGVIETGMAWFWPAWRVKKCFTVTGYEHMEKARAKGNGVVLVGMHFLTLELGARLFGMLNPGIGVYRPNNNAL 160
Cdd:PRK08025 81 ENFRSLGMALLETGMAWFWPDSRVRKWFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGLCQPMMATYRPHNNKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 161 LDWLQTRGRLRSNKTMLDRHDLKGMIRSLKQNEILWYAPDHDYGKTNSVFVPFFAVADAATTAGSYMLVKSAKPAVIPFV 240
Cdd:PRK08025 161 MEWVQTRGRMRSNKAMIGRNNLRGIVGALKKGEAVWFAPDQDYGPKGSSFAPFFAVENVATTNGTYVLSRLSGAAMLTVT 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 241 PRRRADGTGYELII---LEDISEalqggDKESVATQMNRAIEQAVRMAPEQYMWLHRRFKTRPEGQPDRY 307
Cdd:PRK08025 241 MVRKADYSGYRLFItpeMEGYPT-----DENQAAAYMNKIIEKEIMRAPEQYLWIHRRFKTRPVGESSLY 305
|
|
| Lip_A_acyltrans |
pfam03279 |
Bacterial lipid A biosynthesis acyltransferase; |
5-298 |
3.11e-114 |
|
Bacterial lipid A biosynthesis acyltransferase;
Pssm-ID: 281296 [Multi-domain] Cd Length: 294 Bit Score: 332.77 E-value: 3.11e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 5 PRFSLAFLHPRYWLSWAGIAALWLIMLLPYPLLFRIGHSLGRLAMRLLPRRVEIARRNLELCFPEMKKAERESLLQRNFE 84
Cdd:pfam03279 1 PKFSPELLHPRYWLDWLGIAVLRLLALLPYSALRRIGKGLGRLAGRFLKRRRKIARRNLALCFPEMSEAEREQIIDKSFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 85 SVGMGVIETGMAWFWPAWRVKKCFTVTGYEHMEKARAKGNGVVLVGMHFLTLELGARLFGMLNPGIGVYRPN-NNALLDW 163
Cdd:pfam03279 81 SVGRAIVETGRVWFWPDSRIAKRFEVIGLEHIKEALAQGRGAILVGPHFGNWDLGGRVLGQQYPGMAVYRPNlKNPLLDW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 164 LQTRGRLRSNKTMLDRHD-LKGMIRSLKQNEILWYAPDHDYGKTNSVFVPFFAVADAATTAGSYMLVKSaKPAVIPFVPR 242
Cdd:pfam03279 161 LQTSGRERFGGRMLPRQNgIKGLIKALRKGEVVWYLPDQDLGRKDSVFVPFFGVPAATTTGPAKLALKT-KAAVIPVFPI 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2255845135 243 RRADGTGYELIILEDIsEALQGGDKESVATQMNRAIEQAVRMAPEQYMWLHRRFKT 298
Cdd:pfam03279 240 RNGDGSGYTVIVHPAL-DLTITDDVEQIAQAMNQIVEKFIMPAPEQYFWLHRRWKT 294
|
|
| PRK05646 |
PRK05646 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
5-311 |
1.23e-112 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 235543 [Multi-domain] Cd Length: 310 Bit Score: 329.08 E-value: 1.23e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 5 PRFSLAFLHPRYWLSWAGIAALWLIMLLPYPLLFRIGHSLGRLAMRLLPRRVEIARRNLELCFPEMKKAERESLLQRNFE 84
Cdd:PRK05646 4 PRFRAAFLHPRFWPLWLGLGLLWLVVQLPYRVLLWLGRALGALMYRLAGSRRRIAARNLELCFPEKSAAERERLLKENFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 85 SVGMGVIETGMAWFWPAWRVKKCFTVTGYEHMEKARAKGNGVVLVGMHFLTLELGARLFGMLNPGIGVYRPNNNALLDWL 164
Cdd:PRK05646 84 STGIAFFEMAMSWWWPKARLARLAHIEGLEHLQQAQQEGQGVILMALHFTTLEIGAALLGQQHTIDGMYREHKNPVFDFI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 165 QTRGRLRSNK--TMLDRHDLKGMIRSLKQNEILWYAPDHDYGKTNSVFVPFFAVADAATTAGSyMLVKSAKPAVIPFVPR 242
Cdd:PRK05646 164 QRRGRERHNLdsTAIEREDVRGMLKLLRAGRAIWYAPDQDYGAKQSIFVPLFGIPAATVTATT-KFARLGRARVIPFTQK 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2255845135 243 RRADGTGYELII---LEDiseaLQGGDKESVATQMNRAIEQAVRMAPEQYMWLHRRFKTRPEGQPDRYARRK 311
Cdd:PRK05646 243 RLADGSGYRLVIhppLED----FPGESEEADCLRINQWVERVVRECPEQYLWAHRRFKSRPEGEPKLYPKRR 310
|
|
| LpxP |
COG1560 |
Palmitoleoyl-ACP: Kdo2-lipid-IV acyltransferase (lipid A biosynthesis) [Lipid transport and ... |
25-296 |
1.08e-109 |
|
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: 320.21 E-value: 1.08e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 25 ALWLIMLLPYPLLFRIGHSLGRLAMRLLPRRVEIARRNLELCFPEMKKAERESLLQRNFESVGMGVIETGMAWFWPAWRV 104
Cdd:COG1560 1 LLRLLRLLPLRLLYRLGDLLGRLLYRLAGRRRRVARRNLALAFPELSEAEREALARASFRNLGRTLLETLRLWRLSPERL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 105 KKCFTVTGYEHMEKARAKGNGVVLVGMHFLTLELGARLFGMLN-PGIGVYRPNNNALLDWLQTRGRLRSNKTMLDRHD-L 182
Cdd:COG1560 81 RKRVEVEGLEHLEAALAEGRGVILLTPHFGNWELAGAALALRGyPVTAVYRPLKNPLLDRLIRRGRERFGGELIPRKDgV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 183 KGMIRSLKQNEILWYAPDHDYGKTNSVFVPFFAVaDAATTAGSYMLVKSAKPAVIPFVPRRRADGTGYELIILEDISEAl 262
Cdd:COG1560 161 RALLRALRKGGIVGLLPDQDPGRKSGVFVPFFGV-PAATPTGPARLARRTGAPVVPVFARRLPDGRGYRLEIEPPLEDF- 238
|
250 260 270
....*....|....*....|....*....|....
gi 2255845135 263 qGGDKESVATQMNRAIEQAVRMAPEQYMWLHRRF 296
Cdd:COG1560 239 -SEDVEADTQRLNRALEAWIREHPEQWLWLHRRW 271
|
|
| PRK08733 |
PRK08733 |
LpxL/LpxP family Kdo(2)-lipid IV(A) lauroyl/palmitoleoyl acyltransferase; |
5-307 |
5.90e-71 |
|
LpxL/LpxP family Kdo(2)-lipid IV(A) lauroyl/palmitoleoyl acyltransferase;
Pssm-ID: 181542 [Multi-domain] Cd Length: 306 Bit Score: 222.86 E-value: 5.90e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 5 PRFSLafLHPRYWLSWAGIAALWLIMLLPYPLLFRIGHSLGRLAMRLLPRRVEIARRNLELCFPEMKKAERESLLQRNFE 84
Cdd:PRK08733 9 VRPSL--RNPKHWPMYLGLAVMVLAARLPWTLQRALGRGVGWVAMRLAGTRRRAAEVNLKLCFPEQDDAWRARLLRDSFD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 85 SVGMGVIETGMAWFWPAWRVKKCFTVTGYEHMEKARAKGNGVVLVGMHFLTLELGARLFGMLNPGIGVYRPNNNALLDWL 164
Cdd:PRK08733 87 ALGVGLFEFARAWWGSIDVIRPGVQIEGLEHLQQLQQQGRGVLLVSGHFMTLEMCGRLLCDHVPLAGMYRRHRNPVFEWA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 165 QTRGRLRSNKTMLDRHDLKGMIRSLKQNEILWYAPDHDYGKTNSVFVPFFAVAdAATTAGSYMLVKSAKPAVIPFVPRRr 244
Cdd:PRK08733 167 VKRGRLRYATHMFANEDLRATIKHLKRGGFLWYAPDQDMRGKDTVFVPFFGHP-ASTITATHQLARLTGCAVVPYFHRR- 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2255845135 245 aDGTGYELII---LEDISEAlqggDKESVATQMNRAIEQAVRMAPEQYMWLHRRFKTRPEGQPDRY 307
Cdd:PRK08733 245 -EGGRYVLKIappLADFPSD----DVIADTTRVNAAIEDMVREAPDQYLWIHRRFKRQPGGRSDFY 305
|
|
| PRK08943 |
PRK08943 |
lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; Validated |
5-307 |
2.45e-65 |
|
lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; Validated
Pssm-ID: 236355 Cd Length: 314 Bit Score: 208.57 E-value: 2.45e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 5 PRFSLAFLHPRYWLSWAGIAALWLIMLLPYPLLFRIGHSLGRLAMRLLPRRVEIARRNLELCFPEMKKAERESLLQRNFE 84
Cdd:PRK08943 12 PRFQKSFLHPRYWGTWLGIGALAGLALMPPRLRDPLAAKLGRLVGKLAKKARRRARINLSLCFPEKSEAEREAIIDEMFA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 85 SVGMGVIETG-MAWFWPAWRVKKCFtVTGYEHMEKARAKGNGVVLVGMHFLTLELGA-RLFGMLNPGIGVYRPNNNALLD 162
Cdd:PRK08943 92 TAPQAMLMMAeLALRSPKHLQRRVE-WHGLEILEEARANGENVIFLVPHGWAIDIPAmLLASQGQPMAAMFHNQRNPLFD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 163 WLQTRGRLRSNKTMLDRHD-LKGMIRSLKQNEILWYAPDHDYGKTNSVFVPFFAvADAATTAGSYMLVKSAKPAVIPFVP 241
Cdd:PRK08943 171 WLWNRVRRRFGGRLHAREDgIKPFISSVRQGYWGYYLPDEDHGPEHSVFVDFFA-TYKATLPGIGRLAKVCRARVVPLFP 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2255845135 242 RRRADGTGYELIILEDISEALqGGDKESVATQMNRAIEQAVRMAPEQYMWLHRRFKTRPEGQpDRY 307
Cdd:PRK08943 250 VYNGKTHRLDIEIRPPMDDLL-SADDETIARRMNEEVEQFVGPHPEQYMWILKLLKTRKPGE-DLY 313
|
|
| LPLAT_LABLAT-like |
cd07984 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LABLAT-like; ... |
105-297 |
2.22e-62 |
|
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LABLAT-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as lipid A biosynthesis lauroyl/myristoyl (LABLAT, HtrB) acyltransferases and similar proteins.
Pssm-ID: 153246 [Multi-domain] Cd Length: 192 Bit Score: 196.67 E-value: 2.22e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 105 KKCFTVTGYEHMEKARAKGNGVVLVGMHFLTLELGARLFGMLN-PGIGVYRPNNNALLDWLQTRGRLRSNKTMLDRHD-L 182
Cdd:cd07984 1 LKRVEREGLEHLEAALAKGKGVILLTAHFGNWELAGLALALLGyPVTVVYRPLKNPLLDRLITRGRERFGARLIPRGGgL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 183 KGMIRSLKQNEILWYAPDHDYGKTNSVFVPFFAVaDAATTAGSYMLVKSAKPAVIPFVPRRRADGtGYELIIlEDISEAL 262
Cdd:cd07984 81 RELIRALKKGEIVGILPDQDPGRKGGVFVPFFGR-PAATPTGPARLALKTGAPVVPAFAYRLPGG-GYRIEF-EPPLENP 157
|
170 180 190
....*....|....*....|....*....|....*
gi 2255845135 263 QGGDKESVATQMNRAIEQAVRMAPEQYMWLHRRFK 297
Cdd:cd07984 158 PSEDVEEDTQRLNDALEAAIREHPEQWLWFHRRWK 192
|
|
| lipid_A_msbB |
TIGR02208 |
lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; This family consists of MsbB ... |
5-307 |
1.01e-61 |
|
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: 198.88 E-value: 1.01e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 5 PRFSLAFLHPRYWLSWAGIAALWLIMLLPYPLLFRIGHSLGRLAMRLLPRRVEIARRNLELCFPEMKKAERESLLQRNFE 84
Cdd:TIGR02208 3 RRFQKSFLHPKYWGTWLGVFALVLLAFMPAKLRDPIAKVLAKFVGPIAKKPRGRARINLSACFPEKSEAERETIIDNNFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 85 SVGMGVIETGMAWFWPAWRVKKCFTVTGYEHMEKARAKGNGVVLVGMHFLTLEL-GARLFGMLNPGIGVYRPNNNALLDW 163
Cdd:TIGR02208 83 TFVQVMLSQAELAIRSKAHLRRRVNLMGLEHIEAAQAAGKPVIFLVPHGWAIDYaGLRLASQGLPMVTMFNNHKNPLFDW 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 164 LQTRGRLRSNKTMLDRHD-LKGMIRSLKQNEILWYAPDHDYGKTNSVFVPFFAVADaATTAGSYMLVKSAKPAVIPFVPR 242
Cdd:TIGR02208 163 LWNRVRSRFGGHVYAREAgIKALLASLKRGESGYYLPDEDHGPEQSVFVPFFATYK-ATLPVVGRLAKAGNAQVVPVFPG 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2255845135 243 RRADGTGYELIILEDISEALQgGDKESVATQMNRAIEQAVRMAPEQYMWLHRRFKTRPEGQPDRY 307
Cdd:TIGR02208 242 YNQVTGKFELTVRPAMATELS-VDPEQEARAMNKEVEQFILPYPEQYMWILRLLKTRPDGEASIY 305
|
|
| PRK08706 |
PRK08706 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
23-307 |
8.61e-57 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 169557 [Multi-domain] Cd Length: 289 Bit Score: 185.84 E-value: 8.61e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 23 IAALWLIMLLPYPLLFRIGHSLGRLAMRLLPRRVEIARRNLELCFPEMKKAERESLLQRNFESVGMGVIETGMAWFWPAW 102
Cdd:PRK08706 5 FFVLYVLQFLPFALLHKLADLTGLLAYLLVKPRRRIGEINLAKCFPEWDEEKRKTVLKQHFKHMAKLMLEYGLYWYAPAG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 103 RVKKCFTVTGYEHMEKARAKGNGVVLVGMHFLTLELGARLFGMLNPGIGVYRPNNNALLDWLQTRGRLR-SNKTMLDRHD 181
Cdd:PRK08706 85 RLKSLVRYRNKHYLDDALAAGEKVIILYPHFTAFEMAVYALNQDVPLISMYSHQKNKILDEQILKGRNRyHNVFLIGRTE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 182 -LKGMIRSLKQNEI-LWYAPDHDYGKTNSVFVPFFAVaDAATTAGSYMLVKSAKPAVIPFVPRRRADGTgYELIILEDIs 259
Cdd:PRK08706 165 gLRALVKQFRKSSApFLYLPDQDFGRNDSVFVDFFGI-QTATITGLSRIAALANAKVIPAIPVREADNT-VTLHFYPAW- 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2255845135 260 EALQGGDKESVATQMNRAIEQAVRMAPEQYMWLHRRFKTRPEGQPDRY 307
Cdd:PRK08706 242 DSFPSEDAQADAQRMNRFIEERVREHPEQYFWLHKRFKTRPEGSPDFY 289
|
|
| PRK06946 |
PRK06946 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
20-307 |
1.49e-56 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 180770 [Multi-domain] Cd Length: 293 Bit Score: 185.27 E-value: 1.49e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 20 WAGIAALWLIMLLPYPLLFRIGHSLGRLAMRLLPRRVEIARRNLELCFPEMKKAERESLLQRNFESVGMGVIETGMAWFW 99
Cdd:PRK06946 7 ALAIGLLKLLAFLPYGLTARFGDGLGWLLYRIPSRRRRIVHTNLKLCFPDWSDARREELARRHFRHVIRSYVERSVQWFG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 100 PAWRVKKCFTVTgyEHMEKARAKGNGVVLVGMHFLTLELGA-RLFGMLNPGIG-VYRPNNNALLDWLQTRGRLRSNKTML 177
Cdd:PRK06946 87 SEKKLEKLVQVD--SAIDLTDPDGPPTIFLGLHFVGIEAGSiWLNYSLRRRVGsLYTPMSNPLLDAIAKAARGRFGAEMV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 178 DRHD-LKGMIRSLKQNEILWYAPDHDYGKTNSVFVPFFAVADAATTAGSYMlVKSAKPAVIPFVPRRRADGTGYELIILE 256
Cdd:PRK06946 165 SRADsARQVLRWLRDGKPVMLGADMDFGLRDSTFVPFFGVPACTLTAVSRL-ARTGGAQVVPFITEVLPDYKGYRLRVFK 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2255845135 257 DIsEALQGGDKESVATQMNRAIEQAVRMAPEQYMWLHRRFKTRPEGQPDRY 307
Cdd:PRK06946 244 PW-ENYPTGDDDLDARRMNAFLEEQIRLMPEQYYWVHKRFKTRPPGEPSVY 293
|
|
| PRK05645 |
PRK05645 |
lysophospholipid acyltransferase; |
23-307 |
2.93e-36 |
|
lysophospholipid acyltransferase;
Pssm-ID: 135493 [Multi-domain] Cd Length: 295 Bit Score: 132.34 E-value: 2.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 23 IAALWLIMLLPYPLLFRIGHSLGRLAMRLLPRRVEIARRNLELCFPEMKKAERESLLQRNFESVGMGVIETGMAWFWPAW 102
Cdd:PRK05645 10 VGALRLFALLPWRAVQGVGAGIGWLMWKLPNRSREVVRINLSKCFPELSPAELEKLVGQSLMDIGKTLTESACAWIWPPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 103 R-VKKCFTVTGYEHMEKARAKGNGVVLVGMHFLTLELGARLFGMLNPGIGVYRPNNNALLDWL--QTRGRLRSNKTMLDR 179
Cdd:PRK05645 90 KsLELVREVEGLEVLEQALASGKGVVGITSHLGNWEVLNHFYCSQCKPIIFYRPPKLKAVDELlrKQRVQLGNRVAPSTK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 180 HDLKGMIRSLKQNEILWYAPDHDYGKTNSVFVPFFAVAdAATTAGSYMLVKSAKPAVIPFVPRRRADGTGYElIILEDIS 259
Cdd:PRK05645 170 EGILSVIKEVRKGGQVGIPADPEPAESAGIFVPFLGTQ-ALTSKFVPNMLAGGKAVGVFLHALRLPDGSGYK-VILEAAP 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2255845135 260 EALQGGDKESVATQMNRAIEQAVRMAPEQYMWLHRRFKTRPEGQPDRY 307
Cdd:PRK05645 248 EDMYSTDVEVSAAAMSKVVERYVRAYPSQYMWSMKRFKKRPAGEARWY 295
|
|
| PRK08905 |
PRK08905 |
lysophospholipid acyltransferase family protein; |
23-304 |
8.78e-35 |
|
lysophospholipid acyltransferase family protein;
Pssm-ID: 236348 [Multi-domain] Cd Length: 289 Bit Score: 128.18 E-value: 8.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 23 IAALWLIMLLPYPLLFRIGHSLGRLAMRLLPRRVEIARRNLELCFPemkkAERESLLQRNFESVGMGVIEtgMAWFW--- 99
Cdd:PRK08905 3 TFLFRLLSRLPLSWLHALGGWLGRLAYRLPGRYRRRLRANLRQAGG----DPDPAMVKAAAAETGRMILE--LPYVWfrk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 100 PAWRVKKCFTVTGYEHMEKARAKGNGVVLVGMHFLTLELGARLFGMLNPGIGVYRPNNNALLDWLQTRGRLRSNKTML-- 177
Cdd:PRK08905 77 PEEIETMVKDDHGWEHVEAALAEGRGILFLTPHLGCFEVTARYIAQRFPLTAMFRPPRKAALRPLMEAGRARGNMRTApa 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 178 DRHDLKGMIRSLKQNEILWYAPDHDYGKTNSVFVPFFA-VADAATTAGSYMLVKSAKpaVIPFVPRRRADGTGYELIiLE 256
Cdd:PRK08905 157 TPQGVRMLVKALRRGEAVGILPDQVPSGGEGVWAPFFGrPAYTMTLVARLAEVTGVP--VIFVAGERLPRGRGYRLH-LR 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2255845135 257 DISEALQGgDKESVATQMNRAIEQAVRMAPEQYMWLHRRFKtRPEGQP 304
Cdd:PRK08905 234 PVQEPLPG-DKAADAAVINAEIERLIRRFPTQYLWGYNRYK-RPRGAP 279
|
|
| PRK08419 |
PRK08419 |
lipid A biosynthesis lauroyl acyltransferase; Reviewed |
28-297 |
8.46e-25 |
|
lipid A biosynthesis lauroyl acyltransferase; Reviewed
Pssm-ID: 181420 [Multi-domain] Cd Length: 298 Bit Score: 101.64 E-value: 8.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 28 LIMLLPYPLLFRIGHSLGRLAMRLLPRRVEIARRNLELCFPEMK-KAERESLLQRNFESVGMGVIETGMAWFWPAWRVKK 106
Cdd:PRK08419 16 FLAKMPHCIFLRLAKALAFIMRYLDKKRRKIAKANLDFCFGESKsQEEKKRIIKKCYENFAFFGLDFIRNQNTTKEEILN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 107 CFTVTGYEHMEKARAKGNGVVLVGMHFLTLELGARLFGMLNPGIG-VYRPNNNALLDWLQTRGRLRSNKTMLDRHD-LKG 184
Cdd:PRK08419 96 KVTFINEENLLDALKKKRPIIVTTAHYGYWELFSLALAAYYGAVSiVGRLLKSAPINEMISKRREQFGIELIDKKGaMKE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 185 MIRSLKQNEILWYAPDHDYGKTNSVFVPFFAvADAATTAGSYMLVKSAKPAVIP-FVprRRADGTGYELIILEDI-SEAL 262
Cdd:PRK08419 176 LLKALKQGRALGILVDQNVVPKEGVEVKFFN-KRVTHTTIASILARRYNALIIPvFI--FNDDYSHFTITFFPPIrSKIT 252
|
250 260 270
....*....|....*....|....*....|....*..
gi 2255845135 263 QGGDKE-SVATQMN-RAIEQAVRMAPEQYMWLHRRFK 297
Cdd:PRK08419 253 DDAEADiLEATQAQaSACEEMIRKKPDEYFWFHRRFK 289
|
|
| PRK08734 |
PRK08734 |
lauroyl acyltransferase; |
32-308 |
1.32e-22 |
|
lauroyl acyltransferase;
Pssm-ID: 181543 [Multi-domain] Cd Length: 305 Bit Score: 95.72 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 32 LPYPLLFRIGHSLGRLAMRLLPRRVEIARRNLELCFPEMKKAERESLLQRNFESVGMGVIETGMAWFWP-AWRVKKCFTV 110
Cdd:PRK08734 20 LPWPLLKRLADLLAWSWRKLNARESRVTRRNLELAYPELSPQQRAQLHAQILRSTARQALEVLRTWTHPpAENLARLRQR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 111 TGYEHMEKARAKGNGVVLVGMHFLTLELGARLFGMLNPGIGVYRPNNNALLD-WLQ-TRGRLRSNKTMLDRHDLKGMIRS 188
Cdd:PRK08734 100 HGQELYDAALASGRGVIVAAPHFGNWELLNQWLSERGPIAIVYRPPESEAVDgFLQlVRGGDNVRQVRAEGPAVRQLFKV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 189 LKQNEILWYAPDHDYGKTNSVFVPFFAVaDAATTAGSYMLVKSAKPAVIPFVPRRRADGTGYELIIlEDISEALQGGDKE 268
Cdd:PRK08734 180 LKDGGAVGILPDQQPKMGDGVFAPFFGI-PALTMTLVNRLAERTGATVLYGWCERIGPDLEFALHV-QPADPAVADPDPL 257
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2255845135 269 SVATQMNRAIEQAVRMAPEQYMWLHRRFKTRP--EGQPDRYA 308
Cdd:PRK08734 258 RAATALNAGIERIARRDPAQYQWTYKRYTLRPpgSGEHNPYA 299
|
|
| PRK05906 |
PRK05906 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
13-297 |
1.15e-08 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 168292 [Multi-domain] Cd Length: 454 Bit Score: 55.94 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 13 HPRYWLswaGIAALWLIMLLPYPLLFRIGHSLGRLAMRLLPRRVEIARRNLELCFPEMKKAERESLLQRNFESVGMGVIE 92
Cdd:PRK05906 15 HLVYYL---GLGVITILRLLPRSSLRLFGKGLGTLLFYFISDYRKTALTNLALAFPEKSFAERYQIARQSVQHVIITFLE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 93 -----------TGMAWFWPAWRVKKCFT---VTGYEHMEKARAKGN---GVVLVGMHFLTLELGARLFGMLNPGIGVYRP 155
Cdd:PRK05906 92 llaveklaghiDELIAIATSEDAPEGFFpeeVSSQQELEHTFSRLDeqeGAILFCGHQANWELPFLYITKRYPGLAFAKP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 156 NNNALLDwlQTRGRLRS---NKTMLDRHDLKGMIRSLKQNEILWYAPDHDYgKTNSVFVPFFAVADAATTAGSYMLVKSA 232
Cdd:PRK05906 172 IKNRRLN--KKIFSLREsfkGKIVPPKNGINQALRALHQGEVVGIVGDQAL-LSSSYSYPLFGSQAFTTTSPALLAYKTG 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2255845135 233 KPAVIPFVPRRradGTGYELIIlediSEALQGGD----KESVATQMN---RAIEQAVRMAPEQYMWLHRRFK 297
Cdd:PRK05906 249 KPVIAVAIYRK---PNGYLVVP----SKKFYANKslpiKESTEQLMDrlmRFLEKGIACKPEQWMWLHKRWK 313
|
|
| PRK06628 |
PRK06628 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
57-297 |
1.07e-06 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 102471 Cd Length: 290 Bit Score: 49.54 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 57 EIARRNLELCFPEMKKAEResLLQRNFESVGMGVIETGMAWFWPAWRVKKCFTVTGYEHMEKAraKGNGVVLVGMHFLTL 136
Cdd:PRK06628 51 KIARRNIKAVFGDMCDVEK--IIDQTWDNFGRFIGEFTYVNKMDEAELERRIEIIGIENIKKL--EGQPFLLFSGHFANW 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 137 ELGARLFGMLNPGIGV-YRPNNNALLDWLQTRGRLRSNKTMLDR--HDLKGMIRSLKQNEILWYAPDHDYgkTNSVFVPF 213
Cdd:PRK06628 127 DISLKILHKFYPKVAViYRKANNPYVNKLVNESRAGDKLRLIPKgpEGSRALVRAIKESESIVMLVDQKM--NDGIEVPF 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 214 faVADAATTAGSymLVKSAKPAVIPFVPRR--RADGTGYELIILEDISEALQGGDKE---SVATQMNRAIEQAVRMAPEQ 288
Cdd:PRK06628 205 --LGHPAMTASA--IAKIALQYKYPIIPCQiiRTKGSYFKVIVHPQLKFEQTGDNKAdcyNIMLNINQMLGEWVKQNPAQ 280
|
....*....
gi 2255845135 289 YMWLHRRFK 297
Cdd:PRK06628 281 WFWFHNRWK 289
|
|
| PRK06553 |
PRK06553 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
6-295 |
3.05e-06 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 235827 [Multi-domain] Cd Length: 308 Bit Score: 48.05 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 6 RFSLAFLHPRYWL-SWAGIAALWLIMLLPYPLLFRIGHSLGRLAMRLLPRRvEIARRNLELCFPEMKKAERESLLQRNFE 84
Cdd:PRK06553 11 RLRRALKRFAGWLvAQLVFGLLGLLRLFPADKAINFFGRLARLIGPLLPRH-RVALDNLRAAFPEKSEAEIEAIALGMWD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 85 SVGMGVIE---TGMAW-FWPAWRVKKCFTVTGYEHMEKARAKGNGVVLVGMHFLTLEL---GARLFGMlnPGIGVYRPNN 157
Cdd:PRK06553 90 NLGRLGAEyafLDAIFdYDPEAPEPGRVEVRGIEIFERLRDDGKPALIFTAHLGNWELlaiAAAAFGL--DVTVLFRPPN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255845135 158 NALLDWLQTRGRLRSNKTMLDRHDLKG--MIRSLKQNEILWYAPDHDYgkTNSVFVPFFAvadaATTAGSYMLVKSAKPA 235
Cdd:PRK06553 168 NPYAARKVLEARRTTMGGLVPSGAGAAfaLAGVLERGGHVGMLVDQKF--TRGVEVTFFG----RPVKTNPLLAKLARQY 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2255845135 236 VIPFVPRR--RADGTGYELIILEDISEALQGGDKESV--ATQ-MNRAIEQAVRMAPEQYMWLHRR 295
Cdd:PRK06553 242 DCPVHGARciRLPGGRFRLELTERVELPRDADGQIDVqaTMQaLTDVVEGWVREYPGQWLWLHRR 306
|
|
| |
