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Conserved domains on  [gi|17562856|ref|NP_505333|]
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Acyltransferase [Caenorhabditis elegans]

Protein Classification

acyltransferase family protein( domain architecture ID 15196437)

acyltransferase family protein, containing a SGNH/GDSL hydrolase domain, may catalyze the acylation of one of a variety of substrates such as peptidoglycans or sugars

EC:  2.3.1.-
Gene Ontology:  GO:0016747

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
OafA COG1835
Peptidoglycan/LPS O-acetylase OafA/YrhL, contains acyltransferase and SGNH-hydrolase domains ...
2-336 2.77e-45

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: 163.28  E-value: 2.77e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562856   2 RTDIQCLRGIAIILVFLFHL--------LPNLFVNGFLGVDIFFVISGFLMAKILTKSSLRSVQDITAFYFRRFRRILTL 73
Cdd:COG1835   8 LPSLDGLRGLAALLVVLYHAfllfppgpLGGLLSGGFLGVDVFFVLSGFLITRSLLRRLERGGFSLRRFYLRRFLRIYPA 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562856  74 YLFTIFLTvimihlylpnflwetnnryslaslflvtnqlvihdqadyfnefrtslsssnafLHLWSLSVEMQFYILAPIV 153
Cdd:COG1835  88 YLVVLLLT-----------------------------------------------------GHLWSLSVELQFYLLFPLL 114
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562856 154 FFGLQFLKNDYLKLVAVSITSVVGFICFVLIFDQFAFNFMLL-RLWQFSAG-FVSLFWSKIRVNRLPNkieenetrlfef 231
Cdd:COG1835 115 LLLLRRLRRRLLALLALLALASLLLLALLLTGDPSAAYFLTLtRLWEFLLGaLLALLYRRLRRLRRLL------------ 182
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562856 232 pflkedMVIILIAVIGLCFIPTKLDVLILRPLVTTATALIIGC---EYHNNQILKSKILGYIGDISYVMYLVHWPIITIF 308
Cdd:COG1835 183 ------ALAGLALLLAALLLLDGAPFPGFGLLPLLAALLVLAAaagSGLLSRLLSSRPLVFLGDISYSLYLWHWPVLVLL 256
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 17562856 309 LS--------NTVKSYIFCTSLTILSSVVLHHTFEK 336
Cdd:COG1835 257 LAllgrllgpAPLLLLLLALALSLALAALSYRLVER 292
SGNH pfam19040
SGNH domain (fused to AT3 domains); This entry include SGNH domains that are found fused to ...
413-631 1.34e-24

SGNH domain (fused to AT3 domains); This entry include SGNH domains that are found fused to membrane domains from the AT3 families pfam01757.


:

Pssm-ID: 436916  Cd Length: 245  Bit Score: 103.14  E-value: 1.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562856   413 FGYCKYPQGRGNVSIMTIGNSYALSFADLIIEQFKLNYSNYTYVSIDEGYGFFTDSPGSS----LALSVFRKLVAEHKPD 488
Cdd:pfam19040  13 LGACRLGDGAGPPSVLLWGDSHAAALAPGLDEAAKERGVSVLQITRSGCPPLLLRLPDAAcaafNAAILEALALLPSKPD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562856   489 ILFITPRYSSSLQSR-----------IRKNDDYIHQMSENIQFYESIAKKIYILGSHPLYNINHLNTFLHYLIQNSDELE 557
Cdd:pfam19040  93 TVVLAARWSLYLEGPafndegigrdlSNTIAAFAAALRATVAALAAAGKKVVLLGPVPEYVPRNARCLARAGGLLRDPLC 172
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17562856   558 SLHLNRFksDDDMRCVKKRFEKV--KCKKCQFFDLSHVF-VEGDKYLTFDRDSLisYVDNtIHLTSAGLKLCQPVFE 631
Cdd:pfam19040 173 SIPRAEY--RARNARVNAALDELaaKPGKVRVIDPSPLFcDDGGRCSALDGTPL--YFDD-NHLSPAGARLLAPLFA 244
 
Name Accession Description Interval E-value
OafA COG1835
Peptidoglycan/LPS O-acetylase OafA/YrhL, contains acyltransferase and SGNH-hydrolase domains ...
2-336 2.77e-45

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: 163.28  E-value: 2.77e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562856   2 RTDIQCLRGIAIILVFLFHL--------LPNLFVNGFLGVDIFFVISGFLMAKILTKSSLRSVQDITAFYFRRFRRILTL 73
Cdd:COG1835   8 LPSLDGLRGLAALLVVLYHAfllfppgpLGGLLSGGFLGVDVFFVLSGFLITRSLLRRLERGGFSLRRFYLRRFLRIYPA 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562856  74 YLFTIFLTvimihlylpnflwetnnryslaslflvtnqlvihdqadyfnefrtslsssnafLHLWSLSVEMQFYILAPIV 153
Cdd:COG1835  88 YLVVLLLT-----------------------------------------------------GHLWSLSVELQFYLLFPLL 114
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562856 154 FFGLQFLKNDYLKLVAVSITSVVGFICFVLIFDQFAFNFMLL-RLWQFSAG-FVSLFWSKIRVNRLPNkieenetrlfef 231
Cdd:COG1835 115 LLLLRRLRRRLLALLALLALASLLLLALLLTGDPSAAYFLTLtRLWEFLLGaLLALLYRRLRRLRRLL------------ 182
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562856 232 pflkedMVIILIAVIGLCFIPTKLDVLILRPLVTTATALIIGC---EYHNNQILKSKILGYIGDISYVMYLVHWPIITIF 308
Cdd:COG1835 183 ------ALAGLALLLAALLLLDGAPFPGFGLLPLLAALLVLAAaagSGLLSRLLSSRPLVFLGDISYSLYLWHWPVLVLL 256
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 17562856 309 LS--------NTVKSYIFCTSLTILSSVVLHHTFEK 336
Cdd:COG1835 257 LAllgrllgpAPLLLLLLALALSLALAALSYRLVER 292
SGNH pfam19040
SGNH domain (fused to AT3 domains); This entry include SGNH domains that are found fused to ...
413-631 1.34e-24

SGNH domain (fused to AT3 domains); This entry include SGNH domains that are found fused to membrane domains from the AT3 families pfam01757.


Pssm-ID: 436916  Cd Length: 245  Bit Score: 103.14  E-value: 1.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562856   413 FGYCKYPQGRGNVSIMTIGNSYALSFADLIIEQFKLNYSNYTYVSIDEGYGFFTDSPGSS----LALSVFRKLVAEHKPD 488
Cdd:pfam19040  13 LGACRLGDGAGPPSVLLWGDSHAAALAPGLDEAAKERGVSVLQITRSGCPPLLLRLPDAAcaafNAAILEALALLPSKPD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562856   489 ILFITPRYSSSLQSR-----------IRKNDDYIHQMSENIQFYESIAKKIYILGSHPLYNINHLNTFLHYLIQNSDELE 557
Cdd:pfam19040  93 TVVLAARWSLYLEGPafndegigrdlSNTIAAFAAALRATVAALAAAGKKVVLLGPVPEYVPRNARCLARAGGLLRDPLC 172
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17562856   558 SLHLNRFksDDDMRCVKKRFEKV--KCKKCQFFDLSHVF-VEGDKYLTFDRDSLisYVDNtIHLTSAGLKLCQPVFE 631
Cdd:pfam19040 173 SIPRAEY--RARNARVNAALDELaaKPGKVRVIDPSPLFcDDGGRCSALDGTPL--YFDD-NHLSPAGARLLAPLFA 244
Acyl_transf_3 pfam01757
Acyltransferase family; This family includes a range of acyltransferase enzymes. This domain ...
4-308 2.59e-17

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: 83.37  E-value: 2.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562856     4 DIQCLRGIAIILVFLFHLLPN----------------LFVNGFLGVDIFFVISGFLMAkiltkSSLRSVQDITAFYFRRF 67
Cdd:pfam01757   3 YLDLLRGIAILLVVIGHVLLAfgyggfglplelallfLVFLGRFGVPLFFFISGYLLA-----ALRRRRRSLFKFIKKRL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562856    68 RRILTLYLFTIFLTVIMIHLYLPNFLWETNNRYSLASLFLvtnqlvihdqadyfnefrtsLSSSNAFLHLWSLSVEMQFY 147
Cdd:pfam01757  78 LRLLIPYLLWSLLYALLLLLVAGLSVGGALLLLLLLNNGP--------------------LFFLGVNGHLWFLSALFVFY 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562856   148 ILAPIVFFGLQFLKNDYLKLVAVSITsVVGFICFVLIFDQFAFNFMLLRLWQFSAGFVSLFWSKIRVNRLPNKIEENETR 227
Cdd:pfam01757 138 LLLPLLLRLLRKLKKSLLLLLLLLLL-LLFLLYILILLVGVPFTVLVLFIFLYLPFFLLGALLARYRKRIRSKRLKLLII 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562856   228 LFEFPFLKEDMVIILIAVIGLCFIPTKLDVLILRPLVTTATALIIGCEYHNNQILKSKILGYIGDISYVMYLVHWPIITI 307
Cdd:pfam01757 217 ILLALALLALILLLLFLFGLDPLALEFYGYPSLLLLLLGILLLLLLALLLANLRSLRRLLSYLGKYSFGIYLIHPPILLL 296

                  .
gi 17562856   308 F 308
Cdd:pfam01757 297 L 297
 
Name Accession Description Interval E-value
OafA COG1835
Peptidoglycan/LPS O-acetylase OafA/YrhL, contains acyltransferase and SGNH-hydrolase domains ...
2-336 2.77e-45

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: 163.28  E-value: 2.77e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562856   2 RTDIQCLRGIAIILVFLFHL--------LPNLFVNGFLGVDIFFVISGFLMAKILTKSSLRSVQDITAFYFRRFRRILTL 73
Cdd:COG1835   8 LPSLDGLRGLAALLVVLYHAfllfppgpLGGLLSGGFLGVDVFFVLSGFLITRSLLRRLERGGFSLRRFYLRRFLRIYPA 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562856  74 YLFTIFLTvimihlylpnflwetnnryslaslflvtnqlvihdqadyfnefrtslsssnafLHLWSLSVEMQFYILAPIV 153
Cdd:COG1835  88 YLVVLLLT-----------------------------------------------------GHLWSLSVELQFYLLFPLL 114
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562856 154 FFGLQFLKNDYLKLVAVSITSVVGFICFVLIFDQFAFNFMLL-RLWQFSAG-FVSLFWSKIRVNRLPNkieenetrlfef 231
Cdd:COG1835 115 LLLLRRLRRRLLALLALLALASLLLLALLLTGDPSAAYFLTLtRLWEFLLGaLLALLYRRLRRLRRLL------------ 182
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562856 232 pflkedMVIILIAVIGLCFIPTKLDVLILRPLVTTATALIIGC---EYHNNQILKSKILGYIGDISYVMYLVHWPIITIF 308
Cdd:COG1835 183 ------ALAGLALLLAALLLLDGAPFPGFGLLPLLAALLVLAAaagSGLLSRLLSSRPLVFLGDISYSLYLWHWPVLVLL 256
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 17562856 309 LS--------NTVKSYIFCTSLTILSSVVLHHTFEK 336
Cdd:COG1835 257 LAllgrllgpAPLLLLLLALALSLALAALSYRLVER 292
SGNH pfam19040
SGNH domain (fused to AT3 domains); This entry include SGNH domains that are found fused to ...
413-631 1.34e-24

SGNH domain (fused to AT3 domains); This entry include SGNH domains that are found fused to membrane domains from the AT3 families pfam01757.


Pssm-ID: 436916  Cd Length: 245  Bit Score: 103.14  E-value: 1.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562856   413 FGYCKYPQGRGNVSIMTIGNSYALSFADLIIEQFKLNYSNYTYVSIDEGYGFFTDSPGSS----LALSVFRKLVAEHKPD 488
Cdd:pfam19040  13 LGACRLGDGAGPPSVLLWGDSHAAALAPGLDEAAKERGVSVLQITRSGCPPLLLRLPDAAcaafNAAILEALALLPSKPD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562856   489 ILFITPRYSSSLQSR-----------IRKNDDYIHQMSENIQFYESIAKKIYILGSHPLYNINHLNTFLHYLIQNSDELE 557
Cdd:pfam19040  93 TVVLAARWSLYLEGPafndegigrdlSNTIAAFAAALRATVAALAAAGKKVVLLGPVPEYVPRNARCLARAGGLLRDPLC 172
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17562856   558 SLHLNRFksDDDMRCVKKRFEKV--KCKKCQFFDLSHVF-VEGDKYLTFDRDSLisYVDNtIHLTSAGLKLCQPVFE 631
Cdd:pfam19040 173 SIPRAEY--RARNARVNAALDELaaKPGKVRVIDPSPLFcDDGGRCSALDGTPL--YFDD-NHLSPAGARLLAPLFA 244
Acyl_transf_3 pfam01757
Acyltransferase family; This family includes a range of acyltransferase enzymes. This domain ...
4-308 2.59e-17

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: 83.37  E-value: 2.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562856     4 DIQCLRGIAIILVFLFHLLPN----------------LFVNGFLGVDIFFVISGFLMAkiltkSSLRSVQDITAFYFRRF 67
Cdd:pfam01757   3 YLDLLRGIAILLVVIGHVLLAfgyggfglplelallfLVFLGRFGVPLFFFISGYLLA-----ALRRRRRSLFKFIKKRL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562856    68 RRILTLYLFTIFLTVIMIHLYLPNFLWETNNRYSLASLFLvtnqlvihdqadyfnefrtsLSSSNAFLHLWSLSVEMQFY 147
Cdd:pfam01757  78 LRLLIPYLLWSLLYALLLLLVAGLSVGGALLLLLLLNNGP--------------------LFFLGVNGHLWFLSALFVFY 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562856   148 ILAPIVFFGLQFLKNDYLKLVAVSITsVVGFICFVLIFDQFAFNFMLLRLWQFSAGFVSLFWSKIRVNRLPNKIEENETR 227
Cdd:pfam01757 138 LLLPLLLRLLRKLKKSLLLLLLLLLL-LLFLLYILILLVGVPFTVLVLFIFLYLPFFLLGALLARYRKRIRSKRLKLLII 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562856   228 LFEFPFLKEDMVIILIAVIGLCFIPTKLDVLILRPLVTTATALIIGCEYHNNQILKSKILGYIGDISYVMYLVHWPIITI 307
Cdd:pfam01757 217 ILLALALLALILLLLFLFGLDPLALEFYGYPSLLLLLLGILLLLLLALLLANLRSLRRLLSYLGKYSFGIYLIHPPILLL 296

                  .
gi 17562856   308 F 308
Cdd:pfam01757 297 L 297
WecH COG3274
Surface polysaccharide O-acyltransferase WecH [Cell wall/membrane/envelope biogenesis];
8-325 8.43e-07

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


Pssm-ID: 442505 [Multi-domain]  Cd Length: 345  Bit Score: 51.53  E-value: 8.43e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562856   8 LRGIAIILVFLFHLLPN----------------LFVNGFL--GVDIFFVISGFLMAKiltksslRSVQDITAFYFRRFRR 69
Cdd:COG3274  15 LRVLAIFAVVLIHVTAPfvsspgligslnwwvaNLLDSLSrfAVPLFFMISGALLLD-------RKKEDLKDFYKKRLRR 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562856  70 ILTLYLFtifltvimihlylpnflWetnnryslASLFLVTNQLVIHDQADYFNEFRTSLSSSNAFLHLWSLSVEMQFYIL 149
Cdd:COG3274  88 ILIPLLF-----------------W--------SLIYLLFFTFLGGFSFNSLSEFLKNLLTGGVSYHLWFLYMIIGLYLF 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562856 150 APIVFFGLQFLKNDYLKLVAVSITSVVGFICFVLIFDQFAFNFMLLRLWQFSAGFVSLFWSKIRVNRLPNkieeNETRLF 229
Cdd:COG3274 143 TPLLRKLVRKASKRELLYFLLLWLILSLLLPYLNTLLGIDLFFTLTLFLGYLGYFLLGYYLARYKARLKK----RRLIAL 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562856 230 EFPFLkeDMVIILIAVIGLCFIPTKLDVL---ILRPLVTTAT-ALIIGCEYHNNQILK-SKILGYIGDISYVMYLVHWPI 304
Cdd:COG3274 219 LLFLV--GLALTFLGTYLLSLQTGKFNELfysYLSPNVVLMSvALFLLLKNLSFRSSKlSRLLSRLSKYSFGIYLIHPLV 296
                       330       340
                ....*....|....*....|.
gi 17562856 305 ITIFLSNTVKSYIFCTSLTIL 325
Cdd:COG3274 297 LDLLTKLGLNLLNINPLLGIP 317
YfiQ COG3936
Membrane-bound acyltransferase YfiQ, involved in biofilm formation [Carbohydrate transport and ...
5-347 3.69e-03

Membrane-bound acyltransferase YfiQ, involved in biofilm formation [Carbohydrate transport and metabolism];


Pssm-ID: 443137  Cd Length: 334  Bit Score: 39.94  E-value: 3.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562856   5 IQCLRGIAIILVFLFHLLPNLFVN-----------------GFLGVDIFFVISGFLMAKILTKSSLRSvqditaFYFRRF 67
Cdd:COG3936   8 TFYLRGILCLSIVLHHIITMTTLKsdvslnqvevlfifrllLMFATPVFIFLSEFLLAYSYKQNYPKG------FLKKRL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562856  68 RRILTLYLFTIFLTVIMIHLYLPNflwetnnryslaslflvtnqlvihdqADYFNEFRTSLSSSNafLHLWSLSVEMQFY 147
Cdd:COG3936  82 QYIFIPYLIIALIYAIYESLIKTN--------------------------ADFVDSFLTNIFLGN--WHGWFILVIFQFY 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562856 148 ILAPIVFFGLQFLKNDYLKLVAVSITsvVGFICFVLIFDQFafnfmLLRLWQFSAGFVSLFWSKIRvNRLPNKIEENetr 227
Cdd:COG3936 134 LLFYLFFKFLKKYNPAVVVLLSLLIN--YVYLAYFNNFGAK-----TIFLGWLFYFVLGYYMGKNY-ERFLKFLEKY--- 202
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562856 228 LFEFPFLKEDMVIILIAVIGLCFIPtklDVLILRPLVTTATALIIGCEYH--NNQILKSKILGYIGDISYVMYLVHWPII 305
Cdd:COG3936 203 RIFIVIFAILAFGFFIYGALSGNLT---EVTSKRFDLIPYTISVIFLVFLllMKVKLVPKFLNFISNYSFEIYLIHPLIL 279
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 17562856 306 TIFLSNTVK---SYIFCTSLTILSSVVLHHTFEKLYLKLNWKSLI 347
Cdd:COG3936 280 ILLGSFFVSledSPLLYVLLVFLLTVGSAILVSKLLNKLPFGKLI 324
OpgC_C pfam10129
OpgC protein; This domain, found in various hypothetical and OpgC prokaryotic proteins. It is ...
2-97 5.77e-03

OpgC protein; This domain, found in various hypothetical and OpgC prokaryotic proteins. It is likely to act as an acyltransferase enzyme.


Pssm-ID: 431075  Cd Length: 358  Bit Score: 39.51  E-value: 5.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562856     2 RTDIQCLRGIAIILVFLFHLlPNLFVNGFL--------GVDIFFVISGFLMAKILTKSSLRsvQDITAFYFRRFRRILTL 73
Cdd:pfam10129   2 DLRLDFFRGLALVFIFVDHI-PGNVLSWLTlrnfgfsdAAEVFVFLSGYAAGMAYGRAMAR--RGWLAAAARILRRAWQL 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 17562856    74 YLFTIFLTVIMI--------HLYLPNFLWETN 97
Cdd:pfam10129  79 YVAHIALFVLVLaliallalLFDNPDYIDEFN 110
 
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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