|
Name |
Accession |
Description |
Interval |
E-value |
| LpxP |
COG1560 |
Palmitoleoyl-ACP: Kdo2-lipid-IV acyltransferase (lipid A biosynthesis) [Lipid transport and ... |
24-296 |
3.58e-83 |
|
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: 251.65 E-value: 3.58e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 24 SKLPLFTHKYIVSTIGFIIKPFLKSRNDIARENLKIAFPEKSNKEIKKLVKKSYYSMVLSGAETTAAWFLSKKRFNK-IE 102
Cdd:COG1560 6 RLLPLRLLYRLGDLLGRLLYRLAGRRRRVARRNLALAFPELSEAEREALARASFRNLGRTLLETLRLWRLSPERLRKrVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 103 FEweegSRERFEKYHNDpEKKLIILGFHFHCIEIIGRYMGQEFSPFTVMYQKNGNDLIEELIKQYREKSLYKCLDSKNFV 182
Cdd:COG1560 86 VE----GLEHLEAALAE-GRGVILLTPHFGNWELAGAALALRGYPVTAVYRPLKNPLLDRLIRRGRERFGGELIPRKDGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 183 -SVIKSLKKGYTMWYAPDQDFglestGLENSIFAPFFGKLCSTLTVTPWLAQKTGAVVIPAYYVREKCLKKYKIVTGEPF 261
Cdd:COG1560 161 rALLRALRKGGIVGLLPDQDP-----GRKSGVFVPFFGVPAATPTGPARLARRTGAPVVPVFARRLPDGRGYRLEIEPPL 235
|
250 260 270
....*....|....*....|....*....|....*.
gi 1053731840 262 E-FTGDSYKDAEMTNKFLEDAVRKYPEQYLWQHRRY 296
Cdd:COG1560 236 EdFSEDVEADTQRLNRALEAWIREHPEQWLWLHRRW 271
|
|
| lipid_A_htrB |
TIGR02207 |
lipid A biosynthesis lauroyl (or palmitoleoyl) acyltransferase; This model represents a narrow ... |
8-307 |
6.41e-66 |
|
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: 208.73 E-value: 6.41e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 8 PKNWGIWIVVGIMNCGSKLPLFTHKYIVSTIGFIIKPFLKSRNDIARENLKIAFPEKSNKEIKKLVKKSYYSMVLSGAET 87
Cdd:TIGR02207 10 PRYWPTWLGLGVLWLIVQLPYPVLLALGRGIGRLAMRLMKRRVHIARRNLELCFPHMSDAERERLLRENFESTGMALFET 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 88 TAAWFLSKKRFNKIeFEwEEGsRERFEKYHNDpEKKLIILGFHFHCIEIIGRYMGQeFSPFTVMYQKNGNDLIEELIKQY 167
Cdd:TIGR02207 90 GMAWFWSDARIKKW-MQ-IEG-LEHLQRAQKQ-GRGVLLVGVHFLTLELGARIFGQ-QQPGIGVYRPHNNPLFDWIQTRG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 168 REKSLYKCLDSKNFVSVIKSLKKGYTMWYAPDQDFglestGLENSIFAPFFG-KLCSTLTVTPWLAQKTGAVVIPAYYVR 246
Cdd:TIGR02207 165 RLRSNKAMIDRKDLRGMIKALKNGERIWYAPDHDY-----GRKSSVFVPFFAvPDAATTTGTSILARLSKCAVVPFTPRR 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1053731840 247 EKCLKKYKIVTGEPFEF--TGDSYKDAEMTNKFLEDAVRKYPEQYLWQHRRYRTRPN-GEPQIY 307
Cdd:TIGR02207 240 NEDGSGYRLKIDPPLDDfpGDDEIAAAARMNKIVEKMIMRAPEQYMWLHRRFKTRPDeGESSLY 303
|
|
| Lip_A_acyltrans |
pfam03279 |
Bacterial lipid A biosynthesis acyltransferase; |
8-298 |
5.95e-58 |
|
Bacterial lipid A biosynthesis acyltransferase;
Pssm-ID: 281296 [Multi-domain] Cd Length: 294 Bit Score: 187.94 E-value: 5.95e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 8 PKNWGIWIVVGIMNCGSKLPLFTHKYIVSTIGFIIKPFLKSRNDIARENLKIAFPEKSNKEIKKLVKKSYYSMVLSGAET 87
Cdd:pfam03279 10 PRYWLDWLGIAVLRLLALLPYSALRRIGKGLGRLAGRFLKRRRKIARRNLALCFPEMSEAEREQIIDKSFASVGRAIVET 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 88 TAAWFLSKKRFNKiEFEWEEgsRERFEKYHNDpEKKLIILGFHFHCIEIIGRYMGQEFSPFTVMYQKNGNDLIEELIKQY 167
Cdd:pfam03279 90 GRVWFWPDSRIAK-RFEVIG--LEHIKEALAQ-GRGAILVGPHFGNWDLGGRVLGQQYPGMAVYRPNLKNPLLDWLQTSG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 168 REKSLYKCLDSKN-FVSVIKSLKKGYTMWYAPDQDFglestGLENSIFAPFFGKLCSTLTVTPWLAQKTGAVVIPAYYVR 246
Cdd:pfam03279 166 RERFGGRMLPRQNgIKGLIKALRKGEVVWYLPDQDL-----GRKDSVFVPFFGVPAATTTGPAKLALKTKAAVIPVFPIR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1053731840 247 EKCLKKYKIVTGEPFEF--TGDSYKDAEMTNKFLEDAVRKYPEQYLWQHRRYRT 298
Cdd:pfam03279 241 NGDGSGYTVIVHPALDLtiTDDVEQIAQAMNQIVEKFIMPAPEQYFWLHRRWKT 294
|
|
| LPLAT_LABLAT-like |
cd07984 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LABLAT-like; ... |
110-297 |
1.20e-56 |
|
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: 181.26 E-value: 1.20e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 110 RERFEKYHNDpEKKLIILGFHFHCIEIIGRYMGQEFSPFTVMYQKNGNDLIEELIKQYREKSLYKCLDSKN-FVSVIKSL 188
Cdd:cd07984 9 LEHLEAALAK-GKGVILLTAHFGNWELAGLALALLGYPVTVVYRPLKNPLLDRLITRGRERFGARLIPRGGgLRELIRAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 189 KKGYTMWYAPDQDFGLEstgleNSIFAPFFGKLCSTLTVTPWLAQKTGAVVIPAYYVREKClKKYKIVTGEPFEF--TGD 266
Cdd:cd07984 88 KKGEIVGILPDQDPGRK-----GGVFVPFFGRPAATPTGPARLALKTGAPVVPAFAYRLPG-GGYRIEFEPPLENppSED 161
|
170 180 190
....*....|....*....|....*....|.
gi 1053731840 267 SYKDAEMTNKFLEDAVRKYPEQYLWQHRRYR 297
Cdd:cd07984 162 VEEDTQRLNDALEAAIREHPEQWLWFHRRWK 192
|
|
| PRK05646 |
PRK05646 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
6-307 |
1.65e-54 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 235543 [Multi-domain] Cd Length: 310 Bit Score: 179.62 E-value: 1.65e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 6 FSPKNWGIWIVVGIMNCGSKLPLFTHKYIVSTIGFIIKPFLKSRNDIARENLKIAFPEKSNKEIKKLVKKSYYSMVLSGA 85
Cdd:PRK05646 11 LHPRFWPLWLGLGLLWLVVQLPYRVLLWLGRALGALMYRLAGSRRRIAARNLELCFPEKSAAERERLLKENFASTGIAFF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 86 ETTAAWFLSKKRFNKIEFEweEGSrERFEKYHNDPEKkLIILGFHFHCIEIIGRYMGQEFSpFTVMYQKNGNDLIEELIK 165
Cdd:PRK05646 91 EMAMSWWWPKARLARLAHI--EGL-EHLQQAQQEGQG-VILMALHFTTLEIGAALLGQQHT-IDGMYREHKNPVFDFIQR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 166 QYREKslyKCLDS-----KNFVSVIKSLKKGYTMWYAPDQDFGLEStglenSIFAPFFGKLCSTLTVTPWLAQKTGAVVI 240
Cdd:PRK05646 166 RGRER---HNLDStaierEDVRGMLKLLRAGRAIWYAPDQDYGAKQ-----SIFVPLFGIPAATVTATTKFARLGRARVI 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1053731840 241 PAYYVREKCLKKYKIVTGEPFE-FTGDS-YKDAEMTNKFLEDAVRKYPEQYLWQHRRYRTRPNGEPQIY 307
Cdd:PRK05646 238 PFTQKRLADGSGYRLVIHPPLEdFPGESeEADCLRINQWVERVVRECPEQYLWAHRRFKSRPEGEPKLY 306
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| LpxP |
COG1560 |
Palmitoleoyl-ACP: Kdo2-lipid-IV acyltransferase (lipid A biosynthesis) [Lipid transport and ... |
24-296 |
3.58e-83 |
|
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: 251.65 E-value: 3.58e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 24 SKLPLFTHKYIVSTIGFIIKPFLKSRNDIARENLKIAFPEKSNKEIKKLVKKSYYSMVLSGAETTAAWFLSKKRFNK-IE 102
Cdd:COG1560 6 RLLPLRLLYRLGDLLGRLLYRLAGRRRRVARRNLALAFPELSEAEREALARASFRNLGRTLLETLRLWRLSPERLRKrVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 103 FEweegSRERFEKYHNDpEKKLIILGFHFHCIEIIGRYMGQEFSPFTVMYQKNGNDLIEELIKQYREKSLYKCLDSKNFV 182
Cdd:COG1560 86 VE----GLEHLEAALAE-GRGVILLTPHFGNWELAGAALALRGYPVTAVYRPLKNPLLDRLIRRGRERFGGELIPRKDGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 183 -SVIKSLKKGYTMWYAPDQDFglestGLENSIFAPFFGKLCSTLTVTPWLAQKTGAVVIPAYYVREKCLKKYKIVTGEPF 261
Cdd:COG1560 161 rALLRALRKGGIVGLLPDQDP-----GRKSGVFVPFFGVPAATPTGPARLARRTGAPVVPVFARRLPDGRGYRLEIEPPL 235
|
250 260 270
....*....|....*....|....*....|....*.
gi 1053731840 262 E-FTGDSYKDAEMTNKFLEDAVRKYPEQYLWQHRRY 296
Cdd:COG1560 236 EdFSEDVEADTQRLNRALEAWIREHPEQWLWLHRRW 271
|
|
| lipid_A_htrB |
TIGR02207 |
lipid A biosynthesis lauroyl (or palmitoleoyl) acyltransferase; This model represents a narrow ... |
8-307 |
6.41e-66 |
|
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: 208.73 E-value: 6.41e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 8 PKNWGIWIVVGIMNCGSKLPLFTHKYIVSTIGFIIKPFLKSRNDIARENLKIAFPEKSNKEIKKLVKKSYYSMVLSGAET 87
Cdd:TIGR02207 10 PRYWPTWLGLGVLWLIVQLPYPVLLALGRGIGRLAMRLMKRRVHIARRNLELCFPHMSDAERERLLRENFESTGMALFET 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 88 TAAWFLSKKRFNKIeFEwEEGsRERFEKYHNDpEKKLIILGFHFHCIEIIGRYMGQeFSPFTVMYQKNGNDLIEELIKQY 167
Cdd:TIGR02207 90 GMAWFWSDARIKKW-MQ-IEG-LEHLQRAQKQ-GRGVLLVGVHFLTLELGARIFGQ-QQPGIGVYRPHNNPLFDWIQTRG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 168 REKSLYKCLDSKNFVSVIKSLKKGYTMWYAPDQDFglestGLENSIFAPFFG-KLCSTLTVTPWLAQKTGAVVIPAYYVR 246
Cdd:TIGR02207 165 RLRSNKAMIDRKDLRGMIKALKNGERIWYAPDHDY-----GRKSSVFVPFFAvPDAATTTGTSILARLSKCAVVPFTPRR 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1053731840 247 EKCLKKYKIVTGEPFEF--TGDSYKDAEMTNKFLEDAVRKYPEQYLWQHRRYRTRPN-GEPQIY 307
Cdd:TIGR02207 240 NEDGSGYRLKIDPPLDDfpGDDEIAAAARMNKIVEKMIMRAPEQYMWLHRRFKTRPDeGESSLY 303
|
|
| Lip_A_acyltrans |
pfam03279 |
Bacterial lipid A biosynthesis acyltransferase; |
8-298 |
5.95e-58 |
|
Bacterial lipid A biosynthesis acyltransferase;
Pssm-ID: 281296 [Multi-domain] Cd Length: 294 Bit Score: 187.94 E-value: 5.95e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 8 PKNWGIWIVVGIMNCGSKLPLFTHKYIVSTIGFIIKPFLKSRNDIARENLKIAFPEKSNKEIKKLVKKSYYSMVLSGAET 87
Cdd:pfam03279 10 PRYWLDWLGIAVLRLLALLPYSALRRIGKGLGRLAGRFLKRRRKIARRNLALCFPEMSEAEREQIIDKSFASVGRAIVET 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 88 TAAWFLSKKRFNKiEFEWEEgsRERFEKYHNDpEKKLIILGFHFHCIEIIGRYMGQEFSPFTVMYQKNGNDLIEELIKQY 167
Cdd:pfam03279 90 GRVWFWPDSRIAK-RFEVIG--LEHIKEALAQ-GRGAILVGPHFGNWDLGGRVLGQQYPGMAVYRPNLKNPLLDWLQTSG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 168 REKSLYKCLDSKN-FVSVIKSLKKGYTMWYAPDQDFglestGLENSIFAPFFGKLCSTLTVTPWLAQKTGAVVIPAYYVR 246
Cdd:pfam03279 166 RERFGGRMLPRQNgIKGLIKALRKGEVVWYLPDQDL-----GRKDSVFVPFFGVPAATTTGPAKLALKTKAAVIPVFPIR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1053731840 247 EKCLKKYKIVTGEPFEF--TGDSYKDAEMTNKFLEDAVRKYPEQYLWQHRRYRT 298
Cdd:pfam03279 241 NGDGSGYTVIVHPALDLtiTDDVEQIAQAMNQIVEKFIMPAPEQYFWLHRRWKT 294
|
|
| LPLAT_LABLAT-like |
cd07984 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LABLAT-like; ... |
110-297 |
1.20e-56 |
|
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: 181.26 E-value: 1.20e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 110 RERFEKYHNDpEKKLIILGFHFHCIEIIGRYMGQEFSPFTVMYQKNGNDLIEELIKQYREKSLYKCLDSKN-FVSVIKSL 188
Cdd:cd07984 9 LEHLEAALAK-GKGVILLTAHFGNWELAGLALALLGYPVTVVYRPLKNPLLDRLITRGRERFGARLIPRGGgLRELIRAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 189 KKGYTMWYAPDQDFGLEstgleNSIFAPFFGKLCSTLTVTPWLAQKTGAVVIPAYYVREKClKKYKIVTGEPFEF--TGD 266
Cdd:cd07984 88 KKGEIVGILPDQDPGRK-----GGVFVPFFGRPAATPTGPARLALKTGAPVVPAFAYRLPG-GGYRIEFEPPLENppSED 161
|
170 180 190
....*....|....*....|....*....|.
gi 1053731840 267 SYKDAEMTNKFLEDAVRKYPEQYLWQHRRYR 297
Cdd:cd07984 162 VEEDTQRLNDALEAAIREHPEQWLWFHRRWK 192
|
|
| PRK05646 |
PRK05646 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
6-307 |
1.65e-54 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 235543 [Multi-domain] Cd Length: 310 Bit Score: 179.62 E-value: 1.65e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 6 FSPKNWGIWIVVGIMNCGSKLPLFTHKYIVSTIGFIIKPFLKSRNDIARENLKIAFPEKSNKEIKKLVKKSYYSMVLSGA 85
Cdd:PRK05646 11 LHPRFWPLWLGLGLLWLVVQLPYRVLLWLGRALGALMYRLAGSRRRIAARNLELCFPEKSAAERERLLKENFASTGIAFF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 86 ETTAAWFLSKKRFNKIEFEweEGSrERFEKYHNDPEKkLIILGFHFHCIEIIGRYMGQEFSpFTVMYQKNGNDLIEELIK 165
Cdd:PRK05646 91 EMAMSWWWPKARLARLAHI--EGL-EHLQQAQQEGQG-VILMALHFTTLEIGAALLGQQHT-IDGMYREHKNPVFDFIQR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 166 QYREKslyKCLDS-----KNFVSVIKSLKKGYTMWYAPDQDFGLEStglenSIFAPFFGKLCSTLTVTPWLAQKTGAVVI 240
Cdd:PRK05646 166 RGRER---HNLDStaierEDVRGMLKLLRAGRAIWYAPDQDYGAKQ-----SIFVPLFGIPAATVTATTKFARLGRARVI 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1053731840 241 PAYYVREKCLKKYKIVTGEPFE-FTGDS-YKDAEMTNKFLEDAVRKYPEQYLWQHRRYRTRPNGEPQIY 307
Cdd:PRK05646 238 PFTQKRLADGSGYRLVIHPPLEdFPGESeEADCLRINQWVERVVRECPEQYLWAHRRFKSRPEGEPKLY 306
|
|
| PRK06860 |
PRK06860 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
5-307 |
2.54e-51 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 235880 [Multi-domain] Cd Length: 309 Bit Score: 171.25 E-value: 2.54e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 5 KFS-----PKNWGIWIVVGIMNCGSKLPLFTHKYIVSTIGFIIKPFLKSRNDIARENLKIAFPEKSNKEIKKLVKKSYYS 79
Cdd:PRK06860 8 KFSrallhPRYWLTWLGIGLLWLIVLLPYPVLYKLGRGLGKLALRFMKRRAKIARRNLELCFPEMSEQEREAIVVKNFES 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 80 MVLSGAETTAAWFLSKKRFNK-IEFEWEEGSRERfekyhnDPEKKLIIL-GFHFHCIEIIGRYMGQeFSPFTVMYQKNGN 157
Cdd:PRK06860 88 VGMALIETGMAWFWPDWRIKRwTEVEGLEHIREV------QAQGRGVLLvGVHFLTLELGARIFGM-HNPGIGVYRPNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 158 DLIEELIKQYREKSLYKCLDSKNFVSVIKSLKKGYTMWYAPDQDFglestGLENSIFAPFFG--KLCSTlTVTPWLAQKT 235
Cdd:PRK06860 161 PLYDWLQTWGRLRSNKSMLDRKDLKGMIKALKKGERIWYAPDHDY-----GPRSSVFVPFFAveQAATT-TGTWMLARMS 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1053731840 236 GAVVIPAYYVREKCLKKYKIVTGEP--FEFTGDSYKDAEMTNKFLEDAVRKYPEQYLWQHRRYRTRPNGEPQIY 307
Cdd:PRK06860 235 KAAVIPFVPRRKPDGKGYELIILPPedSPPLDDAEATAAWMNKVVEKCILMAPEQYMWLHRRFKTRPEGVPSRY 308
|
|
| PRK08025 |
PRK08025 |
kdo(2)-lipid IV(A) palmitoleoyltransferase; |
6-307 |
8.88e-48 |
|
kdo(2)-lipid IV(A) palmitoleoyltransferase;
Pssm-ID: 181200 Cd Length: 305 Bit Score: 162.21 E-value: 8.88e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 6 FSPKNWGIWIVVGIMNCGSKLPLFTHKYIVSTIGFIIKPFLKSRNDIARENLKIAFPEKSNKEIKKLVKKSYYSMVLSGA 85
Cdd:PRK08025 12 LHPRYWLTWFGLGVLWLLVQLPYPVLCFLGTRIGRMSRPFLKRRESIARKNLELCFPQMSAEEREKMIAENFRSLGMALL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 86 ETTAAWFLSKKRFNKiefeWEEGSRERFEKYHNDPEKKLIILGFHFHCIEIIGRYMGQeFSPFTVMYQKNGNDLIEELIK 165
Cdd:PRK08025 92 ETGMAWFWPDSRVRK----WFDVEGLDNLKRAQMQNRGVMVVGVHFMSLELGGRVMGL-CQPMMATYRPHNNKLMEWVQT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 166 QYREKSLYKCLDSKNFVSVIKSLKKGYTMWYAPDQDFGLEStglenSIFAPFFG-KLCSTLTVTPWLAQKTGAVVIPAYY 244
Cdd:PRK08025 167 RGRMRSNKAMIGRNNLRGIVGALKKGEAVWFAPDQDYGPKG-----SSFAPFFAvENVATTNGTYVLSRLSGAAMLTVTM 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1053731840 245 VREKCLKKYKIVTGEPFE-FTGDSYKDAEMTNKFLEDAVRKYPEQYLWQHRRYRTRPNGEPQIY 307
Cdd:PRK08025 242 VRKADYSGYRLFITPEMEgYPTDENQAAAYMNKIIEKEIMRAPEQYLWIHRRFKTRPVGESSLY 305
|
|
| PRK08733 |
PRK08733 |
LpxL/LpxP family Kdo(2)-lipid IV(A) lauroyl/palmitoleoyl acyltransferase; |
7-307 |
8.55e-44 |
|
LpxL/LpxP family Kdo(2)-lipid IV(A) lauroyl/palmitoleoyl acyltransferase;
Pssm-ID: 181542 [Multi-domain] Cd Length: 306 Bit Score: 151.59 E-value: 8.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 7 SPKNWGIWIVVGIMNCGSKLPLFTHKYIVSTIGFIIKPFLKSRNDIARENLKIAFPEKSNKEIKKLVKKSYYSMVLSGAE 86
Cdd:PRK08733 15 NPKHWPMYLGLAVMVLAARLPWTLQRALGRGVGWVAMRLAGTRRRAAEVNLKLCFPEQDDAWRARLLRDSFDALGVGLFE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 87 TTAAWFLSKKRFN-KIEFEweegSRERFEKYHNDPEKKLIILGfHFHCIEIIGRYMGQeFSPFTVMYQKNGNDLIEELIK 165
Cdd:PRK08733 95 FARAWWGSIDVIRpGVQIE----GLEHLQQLQQQGRGVLLVSG-HFMTLEMCGRLLCD-HVPLAGMYRRHRNPVFEWAVK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 166 QYREKSLYKCLDSKNFVSVIKSLKKGYTMWYAPDQDFGLESTglensIFAPFFGKLCSTLTVTPWLAQKTGAVVIPAYYV 245
Cdd:PRK08733 169 RGRLRYATHMFANEDLRATIKHLKRGGFLWYAPDQDMRGKDT-----VFVPFFGHPASTITATHQLARLTGCAVVPYFHR 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1053731840 246 REKclKKYKIVTGEPFEF--TGDSYKDAEMTNKFLEDAVRKYPEQYLWQHRRYRTRPNGEPQIY 307
Cdd:PRK08733 244 REG--GRYVLKIAPPLADfpSDDVIADTTRVNAAIEDMVREAPDQYLWIHRRFKRQPGGRSDFY 305
|
|
| PRK06946 |
PRK06946 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
12-307 |
9.42e-41 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 180770 [Multi-domain] Cd Length: 293 Bit Score: 143.29 E-value: 9.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 12 GIWIVVGIMNCGSKLPLFTHKYIVSTIGFIIKPFLKSRNDIARENLKIAFPEKSNKEIKKLVKKSYYSMVLSGAETTAAW 91
Cdd:PRK06946 5 GTALAIGLLKLLAFLPYGLTARFGDGLGWLLYRIPSRRRRIVHTNLKLCFPDWSDARREELARRHFRHVIRSYVERSVQW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 92 FLSKKRFNK-IEFEweegSRERFEKYHNDPEkklIILGFHFHCIEI----IGRYMGqefSPFTVMYQKNGNDLIEELIKQ 166
Cdd:PRK06946 85 FGSEKKLEKlVQVD----SAIDLTDPDGPPT---IFLGLHFVGIEAgsiwLNYSLR---RRVGSLYTPMSNPLLDAIAKA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 167 YREKSlykcldSKNFVS-------VIKSLKKGYTMWYAPDQDFGLEstgleNSIFAPFFGKLCSTLTVTPWLAQKTGAVV 239
Cdd:PRK06946 155 ARGRF------GAEMVSradsarqVLRWLRDGKPVMLGADMDFGLR-----DSTFVPFFGVPACTLTAVSRLARTGGAQV 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1053731840 240 IPAY---------YVrekcLKKYKIVTGEPfefTGDSYKDAEMTNKFLEDAVRKYPEQYLWQHRRYRTRPNGEPQIY 307
Cdd:PRK06946 224 VPFItevlpdykgYR----LRVFKPWENYP---TGDDDLDARRMNAFLEEQIRLMPEQYYWVHKRFKTRPPGEPSVY 293
|
|
| lipid_A_msbB |
TIGR02208 |
lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; This family consists of MsbB ... |
8-307 |
4.12e-39 |
|
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: 139.55 E-value: 4.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 8 PKNWGIWIVVGIMNCGSKLPLFTHKYIVSTIGFIIKPFLKSRNDIARENLKIAFPEKSNKEIKKLVKKSYYSMV---LSG 84
Cdd:TIGR02208 12 PKYWGTWLGVFALVLLAFMPAKLRDPIAKVLAKFVGPIAKKPRGRARINLSACFPEKSEAERETIIDNNFATFVqvmLSQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 85 AETTAAwflSK----KRFNKIEFEWEEGSRERfekyhndpEKKLIILGFHFHCIEIIGRYMGQEFSPFTVMYQKNGNDLI 160
Cdd:TIGR02208 92 AELAIR---SKahlrRRVNLMGLEHIEAAQAA--------GKPVIFLVPHGWAIDYAGLRLASQGLPMVTMFNNHKNPLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 161 EELIKQYREKSLYKCLDSKNFV-SVIKSLKKGYTMWYAPDQDFGLEstgleNSIFAPFFGKLCSTLTVTPWLAQKTGAVV 239
Cdd:TIGR02208 161 DWLWNRVRSRFGGHVYAREAGIkALLASLKRGESGYYLPDEDHGPE-----QSVFVPFFATYKATLPVVGRLAKAGNAQV 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 240 IPAYYVREKCLKKYKIVTGEPF--EFTGDSYKDAEMTNKFLEDAVRKYPEQYLWQHRRYRTRPNGEPQIY 307
Cdd:TIGR02208 236 VPVFPGYNQVTGKFELTVRPAMatELSVDPEQEARAMNKEVEQFILPYPEQYMWILRLLKTRPDGEASIY 305
|
|
| PRK08943 |
PRK08943 |
lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; Validated |
7-307 |
1.12e-36 |
|
lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; Validated
Pssm-ID: 236355 Cd Length: 314 Bit Score: 133.07 E-value: 1.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 7 SPKNWGIWIVVGIMNCGSKLPLFTHKYIVSTIGFIIKPFLKSRNDIARENLKIAFPEKSNKEIKKLVKKSYYSMV---LS 83
Cdd:PRK08943 20 HPRYWGTWLGIGALAGLALMPPRLRDPLAAKLGRLVGKLAKKARRRARINLSLCFPEKSEAEREAIIDEMFATAPqamLM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 84 GAETTaawFLSKKRFNK-IEFEWEEGSRErfekyHNDPEKKLIILGFHFHCIEIIGRYMGQEFSPFTVMYQKNGNDLIEE 162
Cdd:PRK08943 100 MAELA---LRSPKHLQRrVEWHGLEILEE-----ARANGENVIFLVPHGWAIDIPAMLLASQGQPMAAMFHNQRNPLFDW 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 163 LIKQYREK---SLYKCLDS-KNFvsvIKSLKKGYTMWYAPDQDFGLEstgleNSIFAPFFGKLCSTLTVTPWLAQKTGAV 238
Cdd:PRK08943 172 LWNRVRRRfggRLHAREDGiKPF---ISSVRQGYWGYYLPDEDHGPE-----HSVFVDFFATYKATLPGIGRLAKVCRAR 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1053731840 239 VIPAYYVREKCLKKYKIVTGEPF--EFTGDSYKDAEMTNKFLEDAVRKYPEQYLWQHRRYRTRPNGEPqIY 307
Cdd:PRK08943 244 VVPLFPVYNGKTHRLDIEIRPPMddLLSADDETIARRMNEEVEQFVGPHPEQYMWILKLLKTRKPGED-LY 313
|
|
| PRK08706 |
PRK08706 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
26-307 |
4.05e-35 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 169557 [Multi-domain] Cd Length: 289 Bit Score: 128.45 E-value: 4.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 26 LPLFTHKYIVSTIGFIIKPFLKSRNDIARENLKIAFPEKSNKEIKKLVKKSYYSMVLSGAETTAAWFLSKKRFNKIEfew 105
Cdd:PRK08706 14 LPFALLHKLADLTGLLAYLLVKPRRRIGEINLAKCFPEWDEEKRKTVLKQHFKHMAKLMLEYGLYWYAPAGRLKSLV--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 106 eegsreRFEKYH-----NDPEKKLIILGFHFHCIEIIGRYMGQEFsPFTVMYQKNGNDLIEELIKQYREK--SLYKCLDS 178
Cdd:PRK08706 91 ------RYRNKHylddaLAAGEKVIILYPHFTAFEMAVYALNQDV-PLISMYSHQKNKILDEQILKGRNRyhNVFLIGRT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 179 KNFVSVIKSLKKGYTMW-YAPDQDFGLEstgleNSIFAPFFGKLCSTLTVTPWLAQKTGAVVIPAYYVREKC----LKKY 253
Cdd:PRK08706 164 EGLRALVKQFRKSSAPFlYLPDQDFGRN-----DSVFVDFFGIQTATITGLSRIAALANAKVIPAIPVREADntvtLHFY 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1053731840 254 KIVTGEPfefTGDSYKDAEMTNKFLEDAVRKYPEQYLWQHRRYRTRPNGEPQIY 307
Cdd:PRK08706 239 PAWDSFP---SEDAQADAQRMNRFIEERVREHPEQYFWLHKRFKTRPEGSPDFY 289
|
|
| PRK08419 |
PRK08419 |
lipid A biosynthesis lauroyl acyltransferase; Reviewed |
25-307 |
3.77e-25 |
|
lipid A biosynthesis lauroyl acyltransferase; Reviewed
Pssm-ID: 181420 [Multi-domain] Cd Length: 298 Bit Score: 102.03 E-value: 3.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 25 KLPLFTHKYIVSTIGFIIKPFLKSRNDIARENLKIAFPE-KSNKEIKKLVKKSYYSMVLSGAETTAAWFLSK-KRFNKIE 102
Cdd:PRK08419 19 KMPHCIFLRLAKALAFIMRYLDKKRRKIAKANLDFCFGEsKSQEEKKRIIKKCYENFAFFGLDFIRNQNTTKeEILNKVT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 103 FEWEegsrERFEKYHNDpEKKLIILGFHFHCIEIIGRYMGQEFSPFTVMYQKNGNDLIEELIKQYREKSLYKCLDSKN-F 181
Cdd:PRK08419 99 FINE----ENLLDALKK-KRPIIVTTAHYGYWELFSLALAAYYGAVSIVGRLLKSAPINEMISKRREQFGIELIDKKGaM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 182 VSVIKSLKKGYTMWYAPDQDfglesTGLENSIFAPFFGKLCSTLTVTPWLAQKTGAVVIPAyYVREKCLKKYKIVTGEPF 261
Cdd:PRK08419 174 KELLKALKQGRALGILVDQN-----VVPKEGVEVKFFNKRVTHTTIASILARRYNALIIPV-FIFNDDYSHFTITFFPPI 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1053731840 262 --EFTGDSYKDAE----MTNKFLEDAVRKYPEQYLWQHRRYRtrpNGEPQIY 307
Cdd:PRK08419 248 rsKITDDAEADILeatqAQASACEEMIRKKPDEYFWFHRRFK---SFYPEIY 296
|
|
| PRK08905 |
PRK08905 |
lysophospholipid acyltransferase family protein; |
54-304 |
3.93e-18 |
|
lysophospholipid acyltransferase family protein;
Pssm-ID: 236348 [Multi-domain] Cd Length: 289 Bit Score: 82.73 E-value: 3.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 54 RENLKIAFPEkSNKEIKKLVKKSYYSMVLsgaETTAAWF---LSKKRFNKIEFEWEEGSRERFEKyhndpeKKLIILGFH 130
Cdd:PRK08905 40 RANLRQAGGD-PDPAMVKAAAAETGRMIL---ELPYVWFrkpEEIETMVKDDHGWEHVEAALAEG------RGILFLTPH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 131 FHCIEIIGRYMGQEFsPFTVMYQKNGNDLIEELIKQYREKSLYKCL--DSKNFVSVIKSLKKGYTMWYAPDQdfgLESTG 208
Cdd:PRK08905 110 LGCFEVTARYIAQRF-PLTAMFRPPRKAALRPLMEAGRARGNMRTApaTPQGVRMLVKALRRGEAVGILPDQ---VPSGG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 209 leNSIFAPFFGKLCSTLTVTPWLAQKTGAVVIPAYYVREKCLKKYKI---VTGEPFefTGDSYKDAEMTNKFLEDAVRKY 285
Cdd:PRK08905 186 --EGVWAPFFGRPAYTMTLVARLAEVTGVPVIFVAGERLPRGRGYRLhlrPVQEPL--PGDKAADAAVINAEIERLIRRF 261
|
250
....*....|....*....
gi 1053731840 286 PEQYLWQHRRYRtRPNGEP 304
Cdd:PRK08905 262 PTQYLWGYNRYK-RPRGAP 279
|
|
| PRK05645 |
PRK05645 |
lysophospholipid acyltransferase; |
15-307 |
9.29e-17 |
|
lysophospholipid acyltransferase;
Pssm-ID: 135493 [Multi-domain] Cd Length: 295 Bit Score: 78.79 E-value: 9.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 15 IVVGIMNCGSKLPLFTHKYIVSTIGFIIKPFLKSRNDIARENLKIAFPEKSNKEIKKLVKKSYYSMVLSGAETTAAWFLS 94
Cdd:PRK05645 8 LMVGALRLFALLPWRAVQGVGAGIGWLMWKLPNRSREVVRINLSKCFPELSPAELEKLVGQSLMDIGKTLTESACAWIWP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 95 KKRFNKI--EFEWEEGSRERFEKyhndpEKKLIILGFHFHCIEIIGRYMGQEFSPFtVMYQKNGNDLIEELIKQYREKSL 172
Cdd:PRK05645 88 PQKSLELvrEVEGLEVLEQALAS-----GKGVVGITSHLGNWEVLNHFYCSQCKPI-IFYRPPKLKAVDELLRKQRVQLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 173 YKCLDS--KNFVSVIKSLKKGYTMWYAPDQDFGlESTGlensIFAPFFGKLCSTLTVTPWLAQKTGAVVIPAYYVREKCL 250
Cdd:PRK05645 162 NRVAPStkEGILSVIKEVRKGGQVGIPADPEPA-ESAG----IFVPFLGTQALTSKFVPNMLAGGKAVGVFLHALRLPDG 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1053731840 251 KKYKIVTGEPFE--FTGDSYKDAEMTNKFLEDAVRKYPEQYLWQHRRYRTRPNGEPQIY 307
Cdd:PRK05645 237 SGYKVILEAAPEdmYSTDVEVSAAAMSKVVERYVRAYPSQYMWSMKRFKKRPAGEARWY 295
|
|
| PRK08734 |
PRK08734 |
lauroyl acyltransferase; |
36-307 |
3.65e-14 |
|
lauroyl acyltransferase;
Pssm-ID: 181543 [Multi-domain] Cd Length: 305 Bit Score: 71.45 E-value: 3.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 36 STIGFIIKPFLKSRND---------------IARENLKIAFPEKSNKEIKKLVKKSYYSMVLSGAETTAAWFlskkrfnk 100
Cdd:PRK08734 15 ALVGRLPWPLLKRLADllawswrklnaresrVTRRNLELAYPELSPQQRAQLHAQILRSTARQALEVLRTWT-------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 101 iefEWEEGSRERFEKYHNDP--------EKKLIILGFHFHCIEIIGRYMGqEFSPFTVMYQKNGNDLIEELIKQYREKSL 172
Cdd:PRK08734 87 ---HPPAENLARLRQRHGQElydaalasGRGVIVAAPHFGNWELLNQWLS-ERGPIAIVYRPPESEAVDGFLQLVRGGDN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 173 YKCLDSKNFV--SVIKSLKKGYTMWYAPDQdfgleSTGLENSIFAPFFGKLCSTLTVTPWLAQKTGAVVIPAYYVR---- 246
Cdd:PRK08734 163 VRQVRAEGPAvrQLFKVLKDGGAVGILPDQ-----QPKMGDGVFAPFFGIPALTMTLVNRLAERTGATVLYGWCERigpd 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1053731840 247 -EKCLkkyKIVTGEPFEFTGDSYKDAEMTNKFLEDAVRKYPEQYLWQHRRYRTRP--NGEPQIY 307
Cdd:PRK08734 238 lEFAL---HVQPADPAVADPDPLRAATALNAGIERIARRDPAQYQWTYKRYTLRPpgSGEHNPY 298
|
|
| PRK06553 |
PRK06553 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
34-297 |
4.04e-12 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 235827 [Multi-domain] Cd Length: 308 Bit Score: 65.38 E-value: 4.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 34 IVSTIGfiikPFLkSRNDIARENLKIAFPEKSNKEIKKLVKKSYYSMVLSGAETTaawFLSK--------KRFNKIEFEw 105
Cdd:PRK06553 50 LARLIG----PLL-PRHRVALDNLRAAFPEKSEAEIEAIALGMWDNLGRLGAEYA---FLDAifdydpeaPEPGRVEVR- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 106 eegSRERFEKYHNDPeKKLIILGFH---FHCIEIIGRYMGQEfspFTVMYQKNGNDLIEELIKQYREKSLYKCLDSKNFV 182
Cdd:PRK06553 121 ---GIEIFERLRDDG-KPALIFTAHlgnWELLAIAAAAFGLD---VTVLFRPPNNPYAARKVLEARRTTMGGLVPSGAGA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 183 S--VIKSLKKGYTMWYAPDQDF--GLESTglensifapFFGKLCSTLTVTPWLAQKTGAVVIPAYYVRekcL--KKYKIV 256
Cdd:PRK06553 194 AfaLAGVLERGGHVGMLVDQKFtrGVEVT---------FFGRPVKTNPLLAKLARQYDCPVHGARCIR---LpgGRFRLE 261
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1053731840 257 TGEPFEFTGDSYKD------AEMTNKFLEDAVRKYPEQYLWQHRRYR 297
Cdd:PRK06553 262 LTERVELPRDADGQidvqatMQALTDVVEGWVREYPGQWLWLHRRWR 308
|
|
| PRK06628 |
PRK06628 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
50-297 |
2.78e-07 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 102471 Cd Length: 290 Bit Score: 51.08 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 50 NDIARENLKIAFPEKSnkEIKKLVKKSYYSMVLSGAETTaawFLSKKRFNKIEFEWEEGSRERFEKYHNDPekkLIILGF 129
Cdd:PRK06628 50 NKIARRNIKAVFGDMC--DVEKIIDQTWDNFGRFIGEFT---YVNKMDEAELERRIEIIGIENIKKLEGQP---FLLFSG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 130 HFHCIEIIGRYMGQEFSPFTVMYQKNGNDLIEELIKQYREKSLYKCL--DSKNFVSVIKSLKKGYTMWYAPDQDfglest 207
Cdd:PRK06628 122 HFANWDISLKILHKFYPKVAVIYRKANNPYVNKLVNESRAGDKLRLIpkGPEGSRALVRAIKESESIVMLVDQK------ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 208 gLENSIFAPFFGKLCSTLTVTPWLAQKTGAVVIPAYYVREKclKKYKIVTGEP---FEFTGDSYKDAEMT----NKFLED 280
Cdd:PRK06628 196 -MNDGIEVPFLGHPAMTASAIAKIALQYKYPIIPCQIIRTK--GSYFKVIVHPqlkFEQTGDNKADCYNImlniNQMLGE 272
|
250
....*....|....*..
gi 1053731840 281 AVRKYPEQYLWQHRRYR 297
Cdd:PRK06628 273 WVKQNPAQWFWFHNRWK 289
|
|
| PRK05906 |
PRK05906 |
lipid A biosynthesis lauroyl acyltransferase; Provisional |
38-297 |
3.18e-07 |
|
lipid A biosynthesis lauroyl acyltransferase; Provisional
Pssm-ID: 168292 [Multi-domain] Cd Length: 454 Bit Score: 51.32 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 38 IGFIIKPFLKSRNDIARENLKIAFPEKSNKEIKKLVKKSYYSMVLSGAETTAAWFLSKKRFNKIEFEWEEGSRERF---- 113
Cdd:PRK05906 43 LGTLLFYFISDYRKTALTNLALAFPEKSFAERYQIARQSVQHVIITFLELLAVEKLAGHIDELIAIATSEDAPEGFfpee 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 114 --------EKYHNDPEKKLIILgFHFH-------CIEIIGRYMGQEFSpftvmyQKNGNDLIEELIKQYREKSLYKCLDS 178
Cdd:PRK05906 123 vssqqeleHTFSRLDEQEGAIL-FCGHqanwelpFLYITKRYPGLAFA------KPIKNRRLNKKIFSLRESFKGKIVPP 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731840 179 KNFV-SVIKSLKKGYTMWYAPDQDFglestgLENSIFAPFFGKLCSTLTVTPWLAQKTGAVVIPAYYVREKclKKYKIVT 257
Cdd:PRK05906 196 KNGInQALRALHQGEVVGIVGDQAL------LSSSYSYPLFGSQAFTTTSPALLAYKTGKPVIAVAIYRKP--NGYLVVP 267
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1053731840 258 GEPFeftgdsYKDAEMTNK------------FLEDAVRKYPEQYLWQHRRYR 297
Cdd:PRK05906 268 SKKF------YANKSLPIKesteqlmdrlmrFLEKGIACKPEQWMWLHKRWK 313
|
|
|