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Conserved domains on  [gi|446116477|ref|WP_000194332|]
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MULTISPECIES: acyltransferase [Bacillus]

Protein Classification

acyltransferase( domain architecture ID 10007154)

acyltransferase similar to Escherichia coli O-acetyltransferase WecH that catalyzes the acetylation of both cyclic ECA (ECA(CYC)) and phosphoglyceride-linked ECA (ECA(PG))

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
WecH COG3274
Surface polysaccharide O-acyltransferase WecH [Cell wall/membrane/envelope biogenesis];
6-359 2.07e-24

Surface polysaccharide O-acyltransferase WecH [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442505 [Multi-domain]  Cd Length: 345  Bit Score: 102.37  E-value: 2.07e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446116477   6 PEFKVLQSIAFLAVVLQ-SSLLYTMNQGNVLLEQSLIMGMLFNLAKFSAPAFIFIVGFHLIrhYTKQLVYKEYISEKATH 84
Cdd:COG3274   10 VYLDLLRVLAIFAVVLIhVTAPFVSSPGLIGSLNWWVANLLDSLSRFAVPLFFMISGALLL--DRKKEDLKDFYKKRLRR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446116477  85 LLIPYFFWSILYLL-----TTNDLITLQGGIKSLLLGTAAPHLWYVIMMFQIHLLFPLLCTLFYWFQKRTenkkdiykym 159
Cdd:COG3274   88 ILIPLLFWSLIYLLfftflGGFSFNSLSEFLKNLLTGGVSYHLWFLYMIIGLYLFTPLLRKLVRKASKRE---------- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446116477 160 tffaCLYFLLMWFSSHYIFNGEKLTSSTILHYTDRSFLFYSFYFVMGGiaavALKTWRLFVMKHIPLITILFFILFLFIN 239
Cdd:COG3274  158 ----LLYFLLLWLILSLLLPYLNTLLGIDLFFTLTLFLGYLGYFLLGY----YLARYKARLKKRRLIALLLFLVGLALTF 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446116477 240 YELFSFYGAN-SIHLTVSTYLKPSMFLYIVCeiiiLYVLSIMIVQRRGFLYKTLRFIGNYTYGAYLAHLFFLQLCTKFLs 318
Cdd:COG3274  230 LGTYLLSLQTgKFNELFYSYLSPNVVLMSVA----LFLLLKNLSFRSSKLSRLLSRLSKYSFGIYLIHPLVLDLLTKLG- 304
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 446116477 319 LFTLQENTILYSLLLFVLTAIISISTMVICSTIPFHTWITG 359
Cdd:COG3274  305 LNLLNINPLLGIPLVALLTFVLSLLIVLLLRKIPLLRKLVG 345
 
Name Accession Description Interval E-value
WecH COG3274
Surface polysaccharide O-acyltransferase WecH [Cell wall/membrane/envelope biogenesis];
6-359 2.07e-24

Surface polysaccharide O-acyltransferase WecH [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442505 [Multi-domain]  Cd Length: 345  Bit Score: 102.37  E-value: 2.07e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446116477   6 PEFKVLQSIAFLAVVLQ-SSLLYTMNQGNVLLEQSLIMGMLFNLAKFSAPAFIFIVGFHLIrhYTKQLVYKEYISEKATH 84
Cdd:COG3274   10 VYLDLLRVLAIFAVVLIhVTAPFVSSPGLIGSLNWWVANLLDSLSRFAVPLFFMISGALLL--DRKKEDLKDFYKKRLRR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446116477  85 LLIPYFFWSILYLL-----TTNDLITLQGGIKSLLLGTAAPHLWYVIMMFQIHLLFPLLCTLFYWFQKRTenkkdiykym 159
Cdd:COG3274   88 ILIPLLFWSLIYLLfftflGGFSFNSLSEFLKNLLTGGVSYHLWFLYMIIGLYLFTPLLRKLVRKASKRE---------- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446116477 160 tffaCLYFLLMWFSSHYIFNGEKLTSSTILHYTDRSFLFYSFYFVMGGiaavALKTWRLFVMKHIPLITILFFILFLFIN 239
Cdd:COG3274  158 ----LLYFLLLWLILSLLLPYLNTLLGIDLFFTLTLFLGYLGYFLLGY----YLARYKARLKKRRLIALLLFLVGLALTF 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446116477 240 YELFSFYGAN-SIHLTVSTYLKPSMFLYIVCeiiiLYVLSIMIVQRRGFLYKTLRFIGNYTYGAYLAHLFFLQLCTKFLs 318
Cdd:COG3274  230 LGTYLLSLQTgKFNELFYSYLSPNVVLMSVA----LFLLLKNLSFRSSKLSRLLSRLSKYSFGIYLIHPLVLDLLTKLG- 304
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 446116477 319 LFTLQENTILYSLLLFVLTAIISISTMVICSTIPFHTWITG 359
Cdd:COG3274  305 LNLLNINPLLGIPLVALLTFVLSLLIVLLLRKIPLLRKLVG 345
Acyl_transf_3 pfam01757
Acyltransferase family; This family includes a range of acyltransferase enzymes. This domain ...
10-346 1.32e-16

Acyltransferase family; This family includes a range of acyltransferase enzymes. This domain is found in a wide range of acyltransferase enzymes, including, mainly, bacterial proteins which catalyze the transfer of acyl groups, other than amino-acyl, from one compound to another, such as Glucans biosynthesis protein C (OPGC) or protein OatA from Listeria monocytogenes serovar 1/2a and Staphylococcus aureus, an integral membrane protein which is responsible for O-acetylation at the C6-hydroxyl group of N-acetylmuramyl residues, forming the corresponding N,6-O-diacetylmuramic acid of the peptidoglycan, a modification that determines lysozyme resistance. This domain is also present in eukaryotic proteins, namely O-acyltransferase like protein (OACYL) from mouse and RHY1 (Regulator of hypoxia-inducible factor 1) and NRF6 (Nose resistant to fluoxetine protein 6) from Caenorhabditis elegans.


Pssm-ID: 426413 [Multi-domain]  Cd Length: 330  Bit Score: 79.90  E-value: 1.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446116477   10 VLQSIAFLAVVLqSSLLYTMNQGNVLLEQSLIMGMLFNLAKFSAPAFIFIVGFHLIRHYTKQLVYKEYISEKATHLLIPY 89
Cdd:pfam01757   6 LLRGIAILLVVI-GHVLLAFGYGGFGLPLELALLFLVFLGRFGVPLFFFISGYLLAALRRRRRSLFKFIKKRLLRLLIPY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446116477   90 FFWSILYLLTTNDLITLQGGIKSLLLGTA----------APHLWYVIMMFQIHLLFPLlctlfywFQKRTENKKDIYKYM 159
Cdd:pfam01757  85 LLWSLLYALLLLLVAGLSVGGALLLLLLLnngplfflgvNGHLWFLSALFVFYLLLPL-------LLRLLRKLKKSLLLL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446116477  160 TFFACLYFLLMWFSSHYIFNGEKLTSSTILHytdrsflfYSFYFVMGGIAAVALKTWRLFVMKHIPLITILFFILFLfin 239
Cdd:pfam01757 158 LLLLLLLLFLLYILILLVGVPFTVLVLFIFL--------YLPFFLLGALLARYRKRIRSKRLKLLIIILLALALLAL--- 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446116477  240 yeLFSFYGANSIHLTVSTYLKPSMFLYIVCEIIILYVLSIMIVQRRGFLyKTLRFIGNYTYGAYLAHLFFLQLCTKFLSL 319
Cdd:pfam01757 227 --ILLLLFLFGLDPLALEFYGYPSLLLLLLGILLLLLLALLLANLRSLR-RLLSYLGKYSFGIYLIHPPILLLLGKLLGL 303
                         330       340
                  ....*....|....*....|....*..
gi 446116477  320 FTLQENTILYSLLLFVLTAIISISTMV 346
Cdd:pfam01757 304 LGLPLLPILLFLLLLVLTLLVSVLLAR 330
 
Name Accession Description Interval E-value
WecH COG3274
Surface polysaccharide O-acyltransferase WecH [Cell wall/membrane/envelope biogenesis];
6-359 2.07e-24

Surface polysaccharide O-acyltransferase WecH [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442505 [Multi-domain]  Cd Length: 345  Bit Score: 102.37  E-value: 2.07e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446116477   6 PEFKVLQSIAFLAVVLQ-SSLLYTMNQGNVLLEQSLIMGMLFNLAKFSAPAFIFIVGFHLIrhYTKQLVYKEYISEKATH 84
Cdd:COG3274   10 VYLDLLRVLAIFAVVLIhVTAPFVSSPGLIGSLNWWVANLLDSLSRFAVPLFFMISGALLL--DRKKEDLKDFYKKRLRR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446116477  85 LLIPYFFWSILYLL-----TTNDLITLQGGIKSLLLGTAAPHLWYVIMMFQIHLLFPLLCTLFYWFQKRTenkkdiykym 159
Cdd:COG3274   88 ILIPLLFWSLIYLLfftflGGFSFNSLSEFLKNLLTGGVSYHLWFLYMIIGLYLFTPLLRKLVRKASKRE---------- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446116477 160 tffaCLYFLLMWFSSHYIFNGEKLTSSTILHYTDRSFLFYSFYFVMGGiaavALKTWRLFVMKHIPLITILFFILFLFIN 239
Cdd:COG3274  158 ----LLYFLLLWLILSLLLPYLNTLLGIDLFFTLTLFLGYLGYFLLGY----YLARYKARLKKRRLIALLLFLVGLALTF 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446116477 240 YELFSFYGAN-SIHLTVSTYLKPSMFLYIVCeiiiLYVLSIMIVQRRGFLYKTLRFIGNYTYGAYLAHLFFLQLCTKFLs 318
Cdd:COG3274  230 LGTYLLSLQTgKFNELFYSYLSPNVVLMSVA----LFLLLKNLSFRSSKLSRLLSRLSKYSFGIYLIHPLVLDLLTKLG- 304
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 446116477 319 LFTLQENTILYSLLLFVLTAIISISTMVICSTIPFHTWITG 359
Cdd:COG3274  305 LNLLNINPLLGIPLVALLTFVLSLLIVLLLRKIPLLRKLVG 345
Acyl_transf_3 pfam01757
Acyltransferase family; This family includes a range of acyltransferase enzymes. This domain ...
10-346 1.32e-16

Acyltransferase family; This family includes a range of acyltransferase enzymes. This domain is found in a wide range of acyltransferase enzymes, including, mainly, bacterial proteins which catalyze the transfer of acyl groups, other than amino-acyl, from one compound to another, such as Glucans biosynthesis protein C (OPGC) or protein OatA from Listeria monocytogenes serovar 1/2a and Staphylococcus aureus, an integral membrane protein which is responsible for O-acetylation at the C6-hydroxyl group of N-acetylmuramyl residues, forming the corresponding N,6-O-diacetylmuramic acid of the peptidoglycan, a modification that determines lysozyme resistance. This domain is also present in eukaryotic proteins, namely O-acyltransferase like protein (OACYL) from mouse and RHY1 (Regulator of hypoxia-inducible factor 1) and NRF6 (Nose resistant to fluoxetine protein 6) from Caenorhabditis elegans.


Pssm-ID: 426413 [Multi-domain]  Cd Length: 330  Bit Score: 79.90  E-value: 1.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446116477   10 VLQSIAFLAVVLqSSLLYTMNQGNVLLEQSLIMGMLFNLAKFSAPAFIFIVGFHLIRHYTKQLVYKEYISEKATHLLIPY 89
Cdd:pfam01757   6 LLRGIAILLVVI-GHVLLAFGYGGFGLPLELALLFLVFLGRFGVPLFFFISGYLLAALRRRRRSLFKFIKKRLLRLLIPY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446116477   90 FFWSILYLLTTNDLITLQGGIKSLLLGTA----------APHLWYVIMMFQIHLLFPLlctlfywFQKRTENKKDIYKYM 159
Cdd:pfam01757  85 LLWSLLYALLLLLVAGLSVGGALLLLLLLnngplfflgvNGHLWFLSALFVFYLLLPL-------LLRLLRKLKKSLLLL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446116477  160 TFFACLYFLLMWFSSHYIFNGEKLTSSTILHytdrsflfYSFYFVMGGIAAVALKTWRLFVMKHIPLITILFFILFLfin 239
Cdd:pfam01757 158 LLLLLLLLFLLYILILLVGVPFTVLVLFIFL--------YLPFFLLGALLARYRKRIRSKRLKLLIIILLALALLAL--- 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446116477  240 yeLFSFYGANSIHLTVSTYLKPSMFLYIVCEIIILYVLSIMIVQRRGFLyKTLRFIGNYTYGAYLAHLFFLQLCTKFLSL 319
Cdd:pfam01757 227 --ILLLLFLFGLDPLALEFYGYPSLLLLLLGILLLLLLALLLANLRSLR-RLLSYLGKYSFGIYLIHPPILLLLGKLLGL 303
                         330       340
                  ....*....|....*....|....*..
gi 446116477  320 FTLQENTILYSLLLFVLTAIISISTMV 346
Cdd:pfam01757 304 LGLPLLPILLFLLLLVLTLLVSVLLAR 330
OafA COG1835
Peptidoglycan/LPS O-acetylase OafA/YrhL, contains acyltransferase and SGNH-hydrolase domains ...
118-342 1.12e-05

Peptidoglycan/LPS O-acetylase OafA/YrhL, contains acyltransferase and SGNH-hydrolase domains [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441440  Cd Length: 309  Bit Score: 46.56  E-value: 1.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446116477 118 AAPHLWYVIMMFQIHLLFPLLCTLFYWFQKRtenkkdiykYMTFFACLYFLLMWFSSHYIFngeklTSSTILHYtdrSFL 197
Cdd:COG1835   94 LTGHLWSLSVELQFYLLFPLLLLLLRRLRRR---------LLALLALLALASLLLLALLLT-----GDPSAAYF---LTL 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446116477 198 FYSFYFVMGGIAAVALKTWRLFVMKHIPLITILFFILFLFINYELFSFYGansihltvstylkpsmFLYIVCEIIILYVL 277
Cdd:COG1835  157 TRLWEFLLGALLALLYRRLRRLRRLLALAGLALLLAALLLLDGAPFPGFG----------------LLPLLAALLVLAAA 220
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446116477 278 SIMIVQRRGFLYKTLRFIGNYTYGAYLAHLFFLQLCTKFLSLFtLQENTILYSLLLFVLTAIISI 342
Cdd:COG1835  221 AGSGLLSRLLSSRPLVFLGDISYSLYLWHWPVLVLLLALLGRL-LGPAPLLLLLLALALSLALAA 284
NolL COG3594
Fucose 4-O-acetylase or related acetyltransferase [Carbohydrate transport and metabolism];
51-144 2.26e-04

Fucose 4-O-acetylase or related acetyltransferase [Carbohydrate transport and metabolism];


Pssm-ID: 442813  Cd Length: 270  Bit Score: 42.65  E-value: 2.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446116477  51 FSAPAFIFIVGFhLIRHYTKQlvYKEYISEKATHLLIPYFFWSILYLLTTNDLITLQGGIKSLLLGTAAP--HLWYVIMM 128
Cdd:COG3594   48 FHMPLFFFISGY-FSKPSRNG--FKKFLKKKFKRLLVPYLIFQLIYSLFKFLVEGGEPLDLSLLLLLLDPngALWFLPAL 124
                         90
                 ....*....|....*.
gi 446116477 129 FQIHLLFPLLCTLFYW 144
Cdd:COG3594  125 FVWRLLLPLLRRLRRW 140
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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