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Conserved domains on  [gi|1934100058|ref|WP_195331402|]
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acyltransferase [Barnesiella intestinihominis]

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];
7-281 3.56e-27

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


:

Pssm-ID: 442505 [Multi-domain]  Cd Length: 345  Bit Score: 109.31  E-value: 3.56e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934100058   7 KPQERSSNIELLRILSMFLVLMIHYIPSRTLPTHDTLAHDTLGTLFdleLRSISFVCVNCFILISGYFG--------IRW 78
Cdd:COG3274     4 SKKKRIVYLDLLRVLAIFAVVLIHVTAPFVSSPGLIGSLNWWVANL---LDSLSRFAVPLFFMISGALLldrkkedlKDF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934100058  79 KLKSFSNLLFQILFWAIV--CPVIVFAATDSLNMTDLFKTLYHNTFSR--WFIEAYIGLYILAPMINRFIEKSTHRELGI 154
Cdd:COG3274    81 YKKRLRRILIPLLFWSLIylLFFTFLGGFSFNSLSEFLKNLLTGGVSYhlWFLYMIIGLYLFTPLLRKLVRKASKRELLY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934100058 155 FILAFYLFSTLFGYLGKAYDFNKGMSI---ISLVGLYLIGAYLRRKQDgIFDLSKYVYLGVYLVTGFIMVAIAALILKAG 231
Cdd:COG3274   161 FLLLWLILSLLLPYLNTLLGIDLFFTLtlfLGYLGYFLLGYYLARYKA-RLKKRRLIALLLFLVGLALTFLGTYLLSLQT 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1934100058 232 --FTITPYSYLNPLIVLESIALFLFFKKLNIGS---IKWINYIAVSSFAVYLIHN 281
Cdd:COG3274   240 gkFNELFYSYLSPNVVLMSVALFLLLKNLSFRSsklSRLLSRLSKYSFGIYLIHP 294
 
Name Accession Description Interval E-value
WecH COG3274
Surface polysaccharide O-acyltransferase WecH [Cell wall/membrane/envelope biogenesis];
7-281 3.56e-27

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


Pssm-ID: 442505 [Multi-domain]  Cd Length: 345  Bit Score: 109.31  E-value: 3.56e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934100058   7 KPQERSSNIELLRILSMFLVLMIHYIPSRTLPTHDTLAHDTLGTLFdleLRSISFVCVNCFILISGYFG--------IRW 78
Cdd:COG3274     4 SKKKRIVYLDLLRVLAIFAVVLIHVTAPFVSSPGLIGSLNWWVANL---LDSLSRFAVPLFFMISGALLldrkkedlKDF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934100058  79 KLKSFSNLLFQILFWAIV--CPVIVFAATDSLNMTDLFKTLYHNTFSR--WFIEAYIGLYILAPMINRFIEKSTHRELGI 154
Cdd:COG3274    81 YKKRLRRILIPLLFWSLIylLFFTFLGGFSFNSLSEFLKNLLTGGVSYhlWFLYMIIGLYLFTPLLRKLVRKASKRELLY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934100058 155 FILAFYLFSTLFGYLGKAYDFNKGMSI---ISLVGLYLIGAYLRRKQDgIFDLSKYVYLGVYLVTGFIMVAIAALILKAG 231
Cdd:COG3274   161 FLLLWLILSLLLPYLNTLLGIDLFFTLtlfLGYLGYFLLGYYLARYKA-RLKKRRLIALLLFLVGLALTFLGTYLLSLQT 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1934100058 232 --FTITPYSYLNPLIVLESIALFLFFKKLNIGS---IKWINYIAVSSFAVYLIHN 281
Cdd:COG3274   240 gkFNELFYSYLSPNVVLMSVALFLLLKNLSFRSsklSRLLSRLSKYSFGIYLIHP 294
Acyl_transf_3 pfam01757
Acyltransferase family; This family includes a range of acyltransferase enzymes. This domain ...
15-280 8.02e-08

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: 53.32  E-value: 8.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934100058  15 IELLRILSMFLVLMIHyipsrTLPTHDTLAHDTLGTLFDLELRSISFVCVNCFILISGYFG----------IRWKLKSFS 84
Cdd:pfam01757   4 LDLLRGIAILLVVIGH-----VLLAFGYGGFGLPLELALLFLVFLGRFGVPLFFFISGYLLaalrrrrrslFKFIKKRLL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934100058  85 NLLFQILFWAIVCPVIVFAATDSLNMTDLFKTLYHNTFSR---------WFIEAYIGLYILAPMINRFIEKSTHRELGIF 155
Cdd:pfam01757  79 RLLIPYLLWSLLYALLLLLVAGLSVGGALLLLLLLNNGPLfflgvnghlWFLSALFVFYLLLPLLLRLLRKLKKSLLLLL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934100058 156 ILAFYLFSTLFGY--LGKAYDFNKGMSIISLVGLYLIGAYLRRKQDGI--FDLSKYVYLGVYLVTGFIMVAIAALILKAG 231
Cdd:pfam01757 159 LLLLLLLFLLYILilLVGVPFTVLVLFIFLYLPFFLLGALLARYRKRIrsKRLKLLIIILLALALLALILLLLFLFGLDP 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1934100058 232 FTITPYSYLNPLIVLESIALFLFFKKLN---IGSIKWINYIAVSSFAVYLIH 280
Cdd:pfam01757 239 LALEFYGYPSLLLLLLGILLLLLLALLLanlRSLRRLLSYLGKYSFGIYLIH 290
 
Name Accession Description Interval E-value
WecH COG3274
Surface polysaccharide O-acyltransferase WecH [Cell wall/membrane/envelope biogenesis];
7-281 3.56e-27

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


Pssm-ID: 442505 [Multi-domain]  Cd Length: 345  Bit Score: 109.31  E-value: 3.56e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934100058   7 KPQERSSNIELLRILSMFLVLMIHYIPSRTLPTHDTLAHDTLGTLFdleLRSISFVCVNCFILISGYFG--------IRW 78
Cdd:COG3274     4 SKKKRIVYLDLLRVLAIFAVVLIHVTAPFVSSPGLIGSLNWWVANL---LDSLSRFAVPLFFMISGALLldrkkedlKDF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934100058  79 KLKSFSNLLFQILFWAIV--CPVIVFAATDSLNMTDLFKTLYHNTFSR--WFIEAYIGLYILAPMINRFIEKSTHRELGI 154
Cdd:COG3274    81 YKKRLRRILIPLLFWSLIylLFFTFLGGFSFNSLSEFLKNLLTGGVSYhlWFLYMIIGLYLFTPLLRKLVRKASKRELLY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934100058 155 FILAFYLFSTLFGYLGKAYDFNKGMSI---ISLVGLYLIGAYLRRKQDgIFDLSKYVYLGVYLVTGFIMVAIAALILKAG 231
Cdd:COG3274   161 FLLLWLILSLLLPYLNTLLGIDLFFTLtlfLGYLGYFLLGYYLARYKA-RLKKRRLIALLLFLVGLALTFLGTYLLSLQT 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1934100058 232 --FTITPYSYLNPLIVLESIALFLFFKKLNIGS---IKWINYIAVSSFAVYLIHN 281
Cdd:COG3274   240 gkFNELFYSYLSPNVVLMSVALFLLLKNLSFRSsklSRLLSRLSKYSFGIYLIHP 294
Acyl_transf_3 pfam01757
Acyltransferase family; This family includes a range of acyltransferase enzymes. This domain ...
15-280 8.02e-08

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: 53.32  E-value: 8.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934100058  15 IELLRILSMFLVLMIHyipsrTLPTHDTLAHDTLGTLFDLELRSISFVCVNCFILISGYFG----------IRWKLKSFS 84
Cdd:pfam01757   4 LDLLRGIAILLVVIGH-----VLLAFGYGGFGLPLELALLFLVFLGRFGVPLFFFISGYLLaalrrrrrslFKFIKKRLL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934100058  85 NLLFQILFWAIVCPVIVFAATDSLNMTDLFKTLYHNTFSR---------WFIEAYIGLYILAPMINRFIEKSTHRELGIF 155
Cdd:pfam01757  79 RLLIPYLLWSLLYALLLLLVAGLSVGGALLLLLLLNNGPLfflgvnghlWFLSALFVFYLLLPLLLRLLRKLKKSLLLLL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934100058 156 ILAFYLFSTLFGY--LGKAYDFNKGMSIISLVGLYLIGAYLRRKQDGI--FDLSKYVYLGVYLVTGFIMVAIAALILKAG 231
Cdd:pfam01757 159 LLLLLLLFLLYILilLVGVPFTVLVLFIFLYLPFFLLGALLARYRKRIrsKRLKLLIIILLALALLALILLLLFLFGLDP 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1934100058 232 FTITPYSYLNPLIVLESIALFLFFKKLN---IGSIKWINYIAVSSFAVYLIH 280
Cdd:pfam01757 239 LALEFYGYPSLLLLLLGILLLLLLALLLanlRSLRRLLSYLGKYSFGIYLIH 290
 
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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