NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1002249257|ref|XP_015628808|]
View 

probable acetyltransferase NATA1-like [Oryza sativa Japonica Group]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11441181)

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
115-211 7.58e-19

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 80.04  E-value: 7.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002249257 115 GGRVtAGFVICFPnYSTFLSKPGLYVEDIFVRAPWRRRGLGRMMLSAVAGKAAELGMGRVEWCVLDWNKNAIDFYEGMGA 194
Cdd:COG1247    60 DGEV-VGFASLGP-FRPRPAYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGF 137
                          90
                  ....*....|....*...
gi 1002249257 195 EVLPQWR-ICRLTGAALD 211
Cdd:COG1247   138 EEVGTLPeVGFKFGRWLD 155
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
115-211 7.58e-19

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 80.04  E-value: 7.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002249257 115 GGRVtAGFVICFPnYSTFLSKPGLYVEDIFVRAPWRRRGLGRMMLSAVAGKAAELGMGRVEWCVLDWNKNAIDFYEGMGA 194
Cdd:COG1247    60 DGEV-VGFASLGP-FRPRPAYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGF 137
                          90
                  ....*....|....*...
gi 1002249257 195 EVLPQWR-ICRLTGAALD 211
Cdd:COG1247   138 EEVGTLPeVGFKFGRWLD 155
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
115-193 3.19e-13

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: 64.08  E-value: 3.19e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002249257 115 GGRVtAGFVICFPNYSTFlskPGLYVEDIFVRAPWRRRGLGRMMLSAVAGKAAELGMGRVEWCVLDWNKNAIDFYEGMG 193
Cdd:pfam00583  41 DGEL-VGFASLSIIDDEP---PVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLG 115
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
115-175 2.19e-07

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 46.50  E-value: 2.19e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002249257 115 GGRVtAGFVICFPNYStflSKPGLYVEDIFVRAPWRRRGLGRMMLSAVAGKAAELGMGRVE 175
Cdd:cd04301     7 DGEI-VGFASLSPDGS---GGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLR 63
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
115-211 7.58e-19

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 80.04  E-value: 7.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002249257 115 GGRVtAGFVICFPnYSTFLSKPGLYVEDIFVRAPWRRRGLGRMMLSAVAGKAAELGMGRVEWCVLDWNKNAIDFYEGMGA 194
Cdd:COG1247    60 DGEV-VGFASLGP-FRPRPAYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGF 137
                          90
                  ....*....|....*...
gi 1002249257 195 EVLPQWR-ICRLTGAALD 211
Cdd:COG1247   138 EEVGTLPeVGFKFGRWLD 155
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
121-196 3.33e-16

Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 71.23  E-value: 3.33e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002249257 121 GFVICFPNYStflsKPGLYVEDIFVRAPWRRRGLGRMMLSAVAGKAAELGMGRVEWCVLDWNKNAIDFYEGMGAEV 196
Cdd:COG0456     1 GFALLGLVDG----GDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEE 72
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
115-193 3.19e-13

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: 64.08  E-value: 3.19e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002249257 115 GGRVtAGFVICFPNYSTFlskPGLYVEDIFVRAPWRRRGLGRMMLSAVAGKAAELGMGRVEWCVLDWNKNAIDFYEGMG 193
Cdd:pfam00583  41 DGEL-VGFASLSIIDDEP---PVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLG 115
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
116-207 4.22e-13

N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, General function prediction only];


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 63.92  E-value: 4.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002249257 116 GRVTAGFVICFPNYStFLSKPGLYVEDIFVRAPWRRRGLGRMMLSAVAGKAAELGMGRVEWCVLDWNKNAIDFYEGMGAE 195
Cdd:COG0454    38 AVDDKGEPIGFAGLR-RLDDKVLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFK 116
                          90
                  ....*....|..
gi 1002249257 196 VLPQWRICRLTG 207
Cdd:COG0454   117 EIERYVAYVGGE 128
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
115-202 8.43e-10

Predicted N-acetyltransferase YhbS [General function prediction only];


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 55.09  E-value: 8.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002249257 115 GGRVtAGFVICFPNYSTFlSKPGLYVEDIFVRAPWRRRGLGRMMLSAVAGKAAELGMGRVewcVLDWNKNAIDFYEGMGA 194
Cdd:COG3153    47 DGEI-VGHVALSPVDIDG-EGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAV---VLLGDPSLLPFYERFGF 121

                  ....*...
gi 1002249257 195 EVLPQWRI 202
Cdd:COG3153   122 RPAGELGL 129
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
139-206 2.86e-08

Predicted acetyltransferase, GNAT family [General function prediction only];


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 49.52  E-value: 2.86e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002249257 139 YVEDIFVRAPWRRRGLGRMMLSAVAGKAAELGMGRVEWCVLDWNKNAIDFYEGMGAEVLPQWRICRLT 206
Cdd:COG3393    17 EISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVGEYATVLFR 84
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
115-175 2.19e-07

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 46.50  E-value: 2.19e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002249257 115 GGRVtAGFVICFPNYStflSKPGLYVEDIFVRAPWRRRGLGRMMLSAVAGKAAELGMGRVE 175
Cdd:cd04301     7 DGEI-VGFASLSPDGS---GGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLR 63
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
139-199 5.77e-07

N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism]; N-acetylglutamate synthase or related acetyltransferase, GNAT family is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440859 [Multi-domain]  Cd Length: 132  Bit Score: 47.29  E-value: 5.77e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002249257 139 YVEDIFVRAPWRRRGLGRMMLSAVAGKAAELGMGRVEWCVldwNKNAIDFYEGMGAEVLPQ 199
Cdd:COG1246    54 ELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLT---TSAAIHFYEKLGFEEIDK 111
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
120-193 1.13e-06

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 45.14  E-value: 1.13e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002249257 120 AGFVICFPNYSTFlskpGLYVEDIFVRAPWRRRGLGRMMLSAVAGKAAELGMGRVEwcvLDWNKNAIDFYEGMG 193
Cdd:pfam13508  15 VGFAALLPLDDEG----ALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLE---LETTNRAAAFYEKLG 81
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
139-193 1.01e-04

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


Pssm-ID: 463953 [Multi-domain]  Cd Length: 128  Bit Score: 40.72  E-value: 1.01e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1002249257 139 YVEDIFVRAPWRRRGLGRMMLSAVAGKAAELGMGRVEwCVLDWNKNAIDFYEGMG 193
Cdd:pfam13673  53 HISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSE-LTVNASPYAVPFYEKLG 106
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
143-195 1.06e-04

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: 41.52  E-value: 1.06e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1002249257 143 IFVRAPWRRRGLGRMMLSAVAGKA-AELGMGRVEWCVLDWNKNAIDFYEGMGAE 195
Cdd:COG1670    93 YWLAPAYWGKGYATEALRALLDYAfEELGLHRVEAEVDPDNTASIRVLEKLGFR 146
COG3818 COG3818
Predicted N-acetyltransferase, GNAT superfamily [General function prediction only];
73-174 2.58e-04

Predicted N-acetyltransferase, GNAT superfamily [General function prediction only];


Pssm-ID: 443030 [Multi-domain]  Cd Length: 168  Bit Score: 40.30  E-value: 2.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002249257  73 ILDLSPSPLP-------ASGPSTiashcLDLSASPLAD--PEAAAFASPRGGGRVtAGFVICF--------PNYSTFLSK 135
Cdd:COG3818     7 IRDAREHDLDavlalnnAAVPAV-----SPLDAARLARlhEQAAYARVAEVDGEV-AGFLLAFgpgadydsPNYRWFAER 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1002249257 136 --PGLYVEDIFVRAPWRRRGLGRMMLSAVAGKAAELGMGRV 174
Cdd:COG3818    81 ydNFLYIDRIVVAPSARGRGLGRALYADVFSYARARGVPRV 121
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
143-193 6.12e-04

Predicted N-acyltransferase, GNAT family [General function prediction only];


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 38.63  E-value: 6.12e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1002249257 143 IFVRAPWRRRGLGRMMLSAVAGKAAELGMGRVewcVLDWNKNAIDFYEGMG 193
Cdd:COG2153    64 VAVLPEYRGQGLGRALMEAAIEEARERGARRI---VLSAQAHAVGFYEKLG 111
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
125-197 2.47e-03

FR47-like protein; The members of this family are similar to the C-terminal region of the D. melanogaster hypothetical protein FR47. This protein has been found to consist of two N-acyltransferase-like domains swapped with the C-terminal strands.


Pssm-ID: 117022 [Multi-domain]  Cd Length: 86  Bit Score: 35.77  E-value: 2.47e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002249257 125 CFPNYSTFLSkpGLYVEDIFvrapwRRRGLGRMMLSAVAGKAAELGMGRVEWCVLDwNKNAIDFYEGMGAEVL 197
Cdd:pfam08445  16 CLRLPGGELG--ALQTLPEH-----RRRGLGSRLVAALARGIAERGITPFAVVVAG-NTPSRRLYEKLGFRKI 80
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH