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Conserved domains on  [gi|1945285227|emb|CAD7025046|]
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N-acetyltransferase [Rhizobium sp. P007]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11447364)

GNAT family N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate

CATH:  3.40.630.30
EC:  2.3.-.-
Gene Ontology:  GO:0016746|GO:0008080
SCOP:  3000403

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
9-182 1.31e-41

Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 441276 [Multi-domain]  Cd Length: 173  Bit Score: 137.82  E-value: 1.31e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945285227   9 PLSTDRLVLREFTRGDFPGYSAYHSLQEVYRYLYAAPPTGDALREQFSAILAAPfeKDGDTYRLAVERKADNALVGEVLL 88
Cdd:COG1670     2 TLETERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAWLERLLADW--ADGGALPFAIEDKEDGELIGVVGL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945285227  89 KLASVDALQGEVGYIFNPEFAGNGYATEAVGAMVSIGFSSIGFHRIFARLDAANKGSVGVVERLGLRREAHLIQNDRFRD 168
Cdd:COG1670    80 YDIDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDG 159
                         170
                  ....*....|....
gi 1945285227 169 VWGDEYIYAVLASE 182
Cdd:COG1670   160 RYRDHVLYSLLREE 173
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
9-182 1.31e-41

Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441276 [Multi-domain]  Cd Length: 173  Bit Score: 137.82  E-value: 1.31e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945285227   9 PLSTDRLVLREFTRGDFPGYSAYHSLQEVYRYLYAAPPTGDALREQFSAILAAPfeKDGDTYRLAVERKADNALVGEVLL 88
Cdd:COG1670     2 TLETERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAWLERLLADW--ADGGALPFAIEDKEDGELIGVVGL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945285227  89 KLASVDALQGEVGYIFNPEFAGNGYATEAVGAMVSIGFSSIGFHRIFARLDAANKGSVGVVERLGLRREAHLIQNDRFRD 168
Cdd:COG1670    80 YDIDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDG 159
                         170
                  ....*....|....
gi 1945285227 169 VWGDEYIYAVLASE 182
Cdd:COG1670   160 RYRDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
14-155 1.39e-31

Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 111.28  E-value: 1.39e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945285227  14 RLVLREFTRGDFPGYSAYHSLQEVYRYLYAAPPTGDALREQFSAILAAPFEKDGdtYRLAVERKADNAlVGEVLLKLASV 93
Cdd:pfam13302   1 RLLLRPLTEEDAEALFELLSDPEVMRYGVPWPLTLEEAREWLARIWAADEAERG--YGWAIELKDTGF-IGSIGLYDIDG 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1945285227  94 DALQGEVGYIFNPEFAGNGYATEAVGAMVSIGFSSIGFHRIFARLDAANKGSVGVVERLGLR 155
Cdd:pfam13302  78 EPERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
71-169 1.32e-04

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 40.94  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945285227  71 RLAVERKADNAlvgeVLLKLASVDAL--QGEVGYIFNPEFAGNGYATEAVGAMVSIGFSSIGFHRIFARLDAANKGSVGV 148
Cdd:PRK15130   59 RFVVECDGEKA----GLVELVEINHVhrRAEFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHI 134
                          90       100
                  ....*....|....*....|....*
gi 1945285227 149 VERLGLRREAHLIQ----NDRFRDV 169
Cdd:PRK15130  135 YRKLGFEVEGELIHeffiNGEYRNT 159
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
9-182 1.31e-41

Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441276 [Multi-domain]  Cd Length: 173  Bit Score: 137.82  E-value: 1.31e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945285227   9 PLSTDRLVLREFTRGDFPGYSAYHSLQEVYRYLYAAPPTGDALREQFSAILAAPfeKDGDTYRLAVERKADNALVGEVLL 88
Cdd:COG1670     2 TLETERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAWLERLLADW--ADGGALPFAIEDKEDGELIGVVGL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945285227  89 KLASVDALQGEVGYIFNPEFAGNGYATEAVGAMVSIGFSSIGFHRIFARLDAANKGSVGVVERLGLRREAHLIQNDRFRD 168
Cdd:COG1670    80 YDIDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDG 159
                         170
                  ....*....|....
gi 1945285227 169 VWGDEYIYAVLASE 182
Cdd:COG1670   160 RYRDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
14-155 1.39e-31

Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 111.28  E-value: 1.39e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945285227  14 RLVLREFTRGDFPGYSAYHSLQEVYRYLYAAPPTGDALREQFSAILAAPFEKDGdtYRLAVERKADNAlVGEVLLKLASV 93
Cdd:pfam13302   1 RLLLRPLTEEDAEALFELLSDPEVMRYGVPWPLTLEEAREWLARIWAADEAERG--YGWAIELKDTGF-IGSIGLYDIDG 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1945285227  94 DALQGEVGYIFNPEFAGNGYATEAVGAMVSIGFSSIGFHRIFARLDAANKGSVGVVERLGLR 155
Cdd:pfam13302  78 EPERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
71-169 1.32e-04

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 40.94  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945285227  71 RLAVERKADNAlvgeVLLKLASVDAL--QGEVGYIFNPEFAGNGYATEAVGAMVSIGFSSIGFHRIFARLDAANKGSVGV 148
Cdd:PRK15130   59 RFVVECDGEKA----GLVELVEINHVhrRAEFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHI 134
                          90       100
                  ....*....|....*....|....*
gi 1945285227 149 VERLGLRREAHLIQ----NDRFRDV 169
Cdd:PRK15130  135 YRKLGFEVEGELIHeffiNGEYRNT 159
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
77-153 4.33e-04

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 38.27  E-value: 4.33e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1945285227  77 KADNALVGEVLLKLASVDALQGEVGYIF-NPEFAGNGYATEAVGAMVSIGFSSiGFHRIFARLDAANKGSVGVVERLG 153
Cdd:pfam00583  39 EEDGELVGFASLSIIDDEPPVGEIEGLAvAPEYRGKGIGTALLQALLEWARER-GCERIFLEVAADNLAAIALYEKLG 115
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
15-176 7.23e-04

L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 38.44  E-value: 7.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945285227  15 LVLREFTRGDFPGysayhsLQEVYRYLYA--------APPTGDALREQFSAILAapfekDGDTYRLAVErkaDNALVGEV 86
Cdd:COG1247     2 MTIRPATPEDAPA------IAAIYNEAIAegtatfetEPPSEEEREAWFAAILA-----PGRPVLVAEE---DGEVVGFA 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945285227  87 LLKLAS---VDALQGEVGYIFNPEFAGNGYATEAVGAMVSIgFSSIGFHRIFARLDAANKGSVGVVERLGLRREAHLIQN 163
Cdd:COG1247    68 SLGPFRprpAYRGTAEESIYVDPDARGRGIGRALLEALIER-ARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEV 146
                         170
                  ....*....|...
gi 1945285227 164 DRFRDVWGDEYIY 176
Cdd:COG1247   147 GFKFGRWLDLVLM 159
 
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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