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Conserved domains on  [gi|1897676343|ref|WP_187328372|]
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N-acetyltransferase [Streptococcus sp. NSJ-72]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11418877)

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
PubMed:  27367672|26818562|15581578|10940244
SCOP:  3000403

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 72-139 8.32e-15

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 65.45  E-value: 8.32e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1897676343  72 PVAYIEGIAVVPVFQRHAIATQLLDFAQSWATEKGVSQLASDCDIDNAVSQAFHKKAGFKEISRTVHY 139
Cdd:COG0456    12 DEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNY 79
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 72-139 8.32e-15

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 65.45  E-value: 8.32e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1897676343  72 PVAYIEGIAVVPVFQRHAIATQLLDFAQSWATEKGVSQLASDCDIDNAVSQAFHKKAGFKEISRTVHY 139
Cdd:COG0456    12 DEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNY 79
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 44-130 1.67e-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: 62.54  E-value: 1.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897676343  44 FLYYIEGEAVAWVSLSMRSEYVegaeqlPVAYIEGIAVVPVFQRHAIATQLLDFAQSWATEKGVSQLASDCDIDNAVSQA 123
Cdd:pfam00583  36 FVAEEDGELVGFASLSIIDDEP------PVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIA 109


                  ....*..
gi 1897676343 124 FHKKAGF 130
Cdd:pfam00583 110 LYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 44-110 4.31e-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: 44.57  E-value: 4.31e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1897676343  44 FLYYIEGEAVAWVSLSMRSEyvegaeQLPVAYIEGIAVVPVFQRHAIATQLLDFAQSWATEKGVSQL 110
Cdd:cd04301     2 LVAEDDGEIVGFASLSPDGS------GGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRL 62
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 79-139 1.25e-03

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 36.83  E-value: 1.25e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1897676343  79 IAVVPVFQRHAIATQLLDFAQSWATEKGVSQLASDCDIDNAVSQAFHKKAGFKEISRTVHY 139
Cdd:PRK09491   69 IAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEVTIRRNY 129
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 72-139 8.32e-15

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 65.45  E-value: 8.32e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1897676343  72 PVAYIEGIAVVPVFQRHAIATQLLDFAQSWATEKGVSQLASDCDIDNAVSQAFHKKAGFKEISRTVHY 139
Cdd:COG0456    12 DEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNY 79
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 44-142 9.34e-15

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 66.23  E-value: 9.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897676343  44 FLYYIEGEAVAWVSLSMRSEyvegaeqlPVAYIEGIAVVPVFQRHAIATQLLDFAQSWATEKGVSQLASDCDIDNAVSQA 123
Cdd:COG0454    37 IAVDDKGEPIGFAGLRRLDD--------KVLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIR 108

                          90
                  ....*....|....*....
gi 1897676343 124 FHKKAGFKEISRTVHYTLN 142
Cdd:COG0454   109 FYERLGFKEIERYVAYVGG 127
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 44-130 1.67e-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: 62.54  E-value: 1.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897676343  44 FLYYIEGEAVAWVSLSMRSEYVegaeqlPVAYIEGIAVVPVFQRHAIATQLLDFAQSWATEKGVSQLASDCDIDNAVSQA 123
Cdd:pfam00583  36 FVAEEDGELVGFASLSIIDDEP------PVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIA 109


                  ....*..
gi 1897676343 124 FHKKAGF 130
Cdd:pfam00583 110 LYEKLGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
49-135 9.04e-11

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 56.54  E-value: 9.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897676343  49 EGEAVAWVSLSMRSEYvegaEQLPVAYIEGIAVVPVFQRHAIATQLLDFAQSWATEKGVSQLASDCDIDNAVSQAFHKKA 128
Cdd:COG1247    60 DGEVVGFASLGPFRPR----PAYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKL 135


                  ....*..
gi 1897676343 129 GFKEISR 135
Cdd:COG1247   136 GFEEVGT 142
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 44-138 5.88e-09

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: 51.15  E-value: 5.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897676343  44 FLYYIEGEAVAWVSLSMRSEyvegaeqlPVAYIEGIAVVPVFQRHAIATQLLDFAQSWATEKGVSQLASDCdidNAVSQA 123
Cdd:COG1246    31 WVAEEDGEIVGCAALHPLDE--------DLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLT---TSAAIH 99

                          90
                  ....*....|....*
gi 1897676343 124 FHKKAGFKEISRTVH 138
Cdd:COG1246   100 FYEKLGFEEIDKEDL 114
COG3818 COG3818
Predicted N-acetyltransferase, GNAT superfamily [General function prediction only];
74-138 1.97e-08

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


Pssm-ID: 443030 [Multi-domain]  Cd Length: 168  Bit Score: 50.32  E-value: 1.97e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1897676343  74 AYIEGIAVVPVFQRHAIATQLLDFAQSWATEKGVSQLASDCDID--NAVSQAFHKKAGFKEISRTVH 138
Cdd:COG3818    85 LYIDRIVVAPSARGRGLGRALYADVFSYARARGVPRVTCEVNLEppNPGSLAFHARLGFREVGQQRV 151
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
44-138 3.73e-08

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 49.31  E-value: 3.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897676343  44 FLYYIEGEAVAWVSLSmrseYVEGAEQLPVAYIEGIAVVPVFQRHAIATQLLDFAQSWATEKGVSQLASDCDIDNAvsqA 123
Cdd:COG3153    42 LVAEDDGEIVGHVALS----PVDIDGEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLL---P 114

                          90
                  ....*....|....*
gi 1897676343 124 FHKKAGFKEISRTVH 138
Cdd:COG3153   115 FYERFGFRPAGELGL 129
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 44-110 4.31e-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: 44.57  E-value: 4.31e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1897676343  44 FLYYIEGEAVAWVSLSMRSEyvegaeQLPVAYIEGIAVVPVFQRHAIATQLLDFAQSWATEKGVSQL 110
Cdd:cd04301     2 LVAEDDGEIVGFASLSPDGS------GGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRL 62
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 16-141 1.17e-05

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: 42.68  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897676343  16 WAYFAHLAWKIEK-KKLLVAFSEGKFPNEFLYYI-----EGEAVAWVSLSMRSEYVEGAEqlpvayIeGIAVVPVFQRHA 89
Cdd:COG1670    31 ARYLPGPPYSLEEaRAWLERLLADWADGGALPFAiedkeDGELIGVVGLYDIDRANRSAE------I-GYWLAPAYWGKG 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1897676343  90 IATQLLDFAQSWA-TEKGVSQLASDCDIDNAVSQAFHKKAGFKEISRTVHYTL 141
Cdd:COG1670   104 YATEALRALLDYAfEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALV 156
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 44-132 4.16e-05

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 39.75  E-value: 4.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897676343  44 FLYYIEGEAVAWVSLSMRSEYVEGAEqlpvayiEGIAVVPVFQRHAIATQLLDFAQSWATEKGVSQLASDCDIDNAvsqA 123
Cdd:pfam13508   6 FVAEDDGKIVGFAALLPLDDEGALAE-------LRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRAA---A 75


                  ....*....
gi 1897676343 124 FHKKAGFKE 132
Cdd:pfam13508  76 FYEKLGFEE 84
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 49-131 6.73e-04

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 37.71  E-value: 6.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897676343  49 EGEAVAWVSLSMRSEYVEGAEqlpvayIeGIAVVPVFQRHAIAT----QLLDFaqsWATEKGVSQLASDCDIDNAVSQAF 124
Cdd:pfam13302  63 DTGFIGSIGLYDIDGEPERAE------L-GYWLGPDYWGKGYATeavrALLEY---AFEELGLPRLVARIDPENTASRRV 132


                  ....*..
gi 1897676343 125 HKKAGFK 131
Cdd:pfam13302 133 LEKLGFK 139
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 79-139 1.25e-03

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 36.83  E-value: 1.25e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1897676343  79 IAVVPVFQRHAIATQLLDFAQSWATEKGVSQLASDCDIDNAVSQAFHKKAGFKEISRTVHY 139
Cdd:PRK09491   69 IAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEVTIRRNY 129
 
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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