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Conserved domains on  [gi|1080530650|gb|OFN11322|]
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acetyltransferase [Staphylococcus sp. HMSC064E11]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10456837)

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:  15581578|10940244|9175471|27367672|26818562
SCOP:  3000403

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 21-144 7.58e-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: 63.69  E-value: 7.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080530650  21 DALNQFELSERQQIYSSLPQTVLDDALKDENRIANVALnKEGKVVGFFVLHRYYQHEgydtpnNVVYVRSLSVNEKFQGH 100
Cdd:pfam00583   2 EALYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAE-EDGELVGFASLSIIDDEP------PVGEIEGLAVAPEYRGK 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1080530650 101 GYGTKMMMFLPEYVQALfpDFTHLYLVVDAENQSAWNVYERAGF 144
Cdd:pfam00583  75 GIGTALLQALLEWARER--GCERIFLEVAADNLAAIALYEKLGF 116
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 21-144 7.58e-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: 63.69  E-value: 7.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080530650  21 DALNQFELSERQQIYSSLPQTVLDDALKDENRIANVALnKEGKVVGFFVLHRYYQHEgydtpnNVVYVRSLSVNEKFQGH 100
Cdd:pfam00583   2 EALYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAE-EDGELVGFASLSIIDDEP------PVGEIEGLAVAPEYRGK 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1080530650 101 GYGTKMMMFLPEYVQALfpDFTHLYLVVDAENQSAWNVYERAGF 144
Cdd:pfam00583  75 GIGTALLQALLEWARER--GCERIFLEVAADNLAAIALYEKLGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
46-165 2.51e-12

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 63.48  E-value: 2.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080530650  46 ALKDENRIANVALNkEGKVVGFFVLHRYYQHEGYDTpnnvVYVRSLSVNEKFQGHGYGTKMMMFLPEYVQALfpDFTHLY 125
Cdd:COG1247    46 AILAPGRPVLVAEE-DGEVVGFASLGPFRPRPAYRG----TAEESIYVDPDARGRGIGRALLEALIERARAR--GYRRLV 118

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1080530650 126 LVVDAENQSAWNVYERAGFMHTATKEEgpIGKERLYYLDL 165
Cdd:COG1247   119 AVVLADNEASIALYEKLGFEEVGTLPE--VGFKFGRWLDL 156
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 61-126 1.61e-06

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: 1.61e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080530650  61 EGKVVGFFVLHRYYQHEGYdtpnnvVYVRSLSVNEKFQGHGYGTKMMMFLPEYVQALfpDFTHLYL 126
Cdd:cd04301     7 DGEIVGFASLSPDGSGGDT------AYIGDLAVLPEYRGKGIGSALLEAAEEEARER--GAKRLRL 64
PRK10562 PRK10562
putative acetyltransferase; Provisional
 87-144 2.92e-04

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 40.05  E-value: 2.92e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1080530650  87 YVRSLSVNEKFQGHGYGTKMMmflpEYVQALFPdftHLYLVVDAENQSAWNVYERAGF 144
Cdd:PRK10562   70 FVGALFVAPKAVRRGIGKALM----QHVQQRYP---HLSLEVYQKNQRAVNFYHAQGF 120
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 21-144 7.58e-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: 63.69  E-value: 7.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080530650  21 DALNQFELSERQQIYSSLPQTVLDDALKDENRIANVALnKEGKVVGFFVLHRYYQHEgydtpnNVVYVRSLSVNEKFQGH 100
Cdd:pfam00583   2 EALYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAE-EDGELVGFASLSIIDDEP------PVGEIEGLAVAPEYRGK 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1080530650 101 GYGTKMMMFLPEYVQALfpDFTHLYLVVDAENQSAWNVYERAGF 144
Cdd:pfam00583  75 GIGTALLQALLEWARER--GCERIFLEVAADNLAAIALYEKLGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
46-165 2.51e-12

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 63.48  E-value: 2.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080530650  46 ALKDENRIANVALNkEGKVVGFFVLHRYYQHEGYDTpnnvVYVRSLSVNEKFQGHGYGTKMMMFLPEYVQALfpDFTHLY 125
Cdd:COG1247    46 AILAPGRPVLVAEE-DGEVVGFASLGPFRPRPAYRG----TAEESIYVDPDARGRGIGRALLEALIERARAR--GYRRLV 118

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1080530650 126 LVVDAENQSAWNVYERAGFMHTATKEEgpIGKERLYYLDL 165
Cdd:COG1247   119 AVVLADNEASIALYEKLGFEEVGTLPE--VGFKFGRWLDL 156
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 8-152 3.43e-11

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: 60.78  E-value: 3.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080530650   8 DDITVQVFEEKYRDALNQFELSERQQIYSSLPQTVLDDALKDENRIAN-----------VALNKEGKVVGFFVLHRYyqh 76
Cdd:COG1670     6 ERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAWLERLLAdwadggalpfaIEDKEDGELIGVVGLYDI--- 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080530650  77 egyDTPNNVVYVrSLSVNEKFQGHGYGTKMMMFLPEYVQALFpDFTHLYLVVDAENQSAWNVYERAGFMHTATKEE 152
Cdd:COG1670    83 ---DRANRSAEI-GYWLAPAYWGKGYATEALRALLDYAFEEL-GLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRD 153
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 66-166 9.33e-11

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 57.36  E-value: 9.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080530650  66 GFFVLHRYYQHegydtpnNVVYVRSLSVNEKFQGHGYGTKMMMFLPEYVQALfpDFTHLYLVVDAENQSAWNVYERAGFM 145
Cdd:COG0456     1 GFALLGLVDGG-------DEAEIEDLAVDPEYRGRGIGRALLEAALERARER--GARRLRLEVREDNEAAIALYEKLGFE 71

                          90       100
                  ....*....|....*....|.
gi 1080530650 146 HTATKEEGPIGKERLYYLDLD 166
Cdd:COG0456    72 EVGERPNYYGDDALVMEKELA 92
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
56-165 8.17e-09

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 53.17  E-value: 8.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080530650  56 VALnKEGKVVGFFVLHRYYQHEGYDtpnnVVYVRSLSVNEKFQGHGYGTKMMMFLPEYVQALfpDFTHLYLVVDAENQSa 135
Cdd:COG3153    43 VAE-DDGEIVGHVALSPVDIDGEGP----ALLLGPLAVDPEYRGQGIGRALMRAALEAARER--GARAVVLLGDPSLLP- 114

                          90       100       110
                  ....*....|....*....|....*....|
gi 1080530650 136 wnVYERAGFMHTATKEEGPIGKERLYYLDL 165
Cdd:COG3153   115 --FYERFGFRPAGELGLTLGPDEVFLAKEL 142
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 61-166 1.88e-08

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: 51.92  E-value: 1.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080530650  61 EGKVVGFFVLHRYyqhegydtPNNVVYVRSLSVNEKFQGHGYGTKMMMFLPEYVQALfpDFTHLYLVVdaeNQSAWNVYE 140
Cdd:COG1246    36 DGEIVGCAALHPL--------DEDLAELRSLAVHPDYRGRGIGRRLLEALLAEAREL--GLKRLFLLT---TSAAIHFYE 102

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1080530650 141 RAGFmHTATKEEGPIGK-----ERLYYLDLD 166
Cdd:COG1246   103 KLGF-EEIDKEDLPYAKvwqrdSVVMEKDLE 132
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 61-126 1.61e-06

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: 1.61e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080530650  61 EGKVVGFFVLHRYYQHEGYdtpnnvVYVRSLSVNEKFQGHGYGTKMMMFLPEYVQALfpDFTHLYL 126
Cdd:cd04301     7 DGEIVGFASLSPDGSGGDT------AYIGDLAVLPEYRGKGIGSALLEAAEEEARER--GAKRLRL 64
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
82-149 4.44e-05

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 41.05  E-value: 4.44e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080530650  82 PNNVVYVRSLSVNEKFQGHGYGTKMMMFLPEYVQALfpDFTHLYLVVDAENQSAWNVYERAGFMHTAT 149
Cdd:COG3393    12 SPGVAEISGVYTHPEYRGRGLASALVAALAREALAR--GARTPFLYVDADNPAARRLYERLGFRPVGE 77
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 56-144 5.59e-05

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 40.90  E-value: 5.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080530650  56 VALNkEGKVVGFFVLHRYYQHEgydtpnnVVYVRSLSVNEKFQGHGYGTKMMmflpEYVQALFPDFTHLYLVVDAENQSA 135
Cdd:pfam13508   7 VAED-DGKIVGFAALLPLDDEG-------ALAELRLAVHPEYRGQGIGRALL----EAAEAAAKEGGIKLLELETTNRAA 74


                  ....*....
gi 1080530650 136 wNVYERAGF 144
Cdd:pfam13508  75 -AFYEKLGF 82
PRK10562 PRK10562
putative acetyltransferase; Provisional
 87-144 2.92e-04

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 40.05  E-value: 2.92e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1080530650  87 YVRSLSVNEKFQGHGYGTKMMmflpEYVQALFPdftHLYLVVDAENQSAWNVYERAGF 144
Cdd:PRK10562   70 FVGALFVAPKAVRRGIGKALM----QHVQQRYP---HLSLEVYQKNQRAVNFYHAQGF 120
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 60-144 2.42e-03

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 37.33  E-value: 2.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080530650  60 KEGKVVGFFVLHRYyqhEGYDTPNNVVYvrslSVNEKFQGHGYGTKMM-MFLpEYVQALfPDFTHLYLVVDAENQSAWNV 138
Cdd:pfam13302  62 KDTGFIGSIGLYDI---DGEPERAELGY----WLGPDYWGKGYATEAVrALL-EYAFEE-LGLPRLVARIDPENTASRRV 132


                  ....*.
gi 1080530650 139 YERAGF 144
Cdd:pfam13302 133 LEKLGF 138
COG3981 COG3981
Predicted acetyltransferase [General function prediction only];
15-165 3.43e-03

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443180  Cd Length: 170  Bit Score: 37.58  E-value: 3.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080530650  15 FEEKYRDALNQFELSERQQIYSSLPQTVLDDALKD-----------ENRIAN---VALNKEGKVVGFF--------VLHR 72
Cdd:COG3981    11 DEESYLEYLAEFLKEHIDGSGYLVSFEDFEAWLERlldeekgeelpEGWVPAttyWLVDEDGRIVGAInlrhelneFLLR 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080530650  73 YYQHEGYdtpnnvvyvrslSVNEKFQGHGYGTKMMMFLPEYVQALfpDFTHLYLVVDAENQSAWNVYERAG--FMHTATK 150
Cdd:COG3981    91 VGGHIGY------------GVRPSERGKGYATEMLRLALEEAREL--GLDRVLITCDKDNIASRKVIEANGgvLEDEVVD 156

                         170
                  ....*....|....*
gi 1080530650 151 EEGPIGKERlYYLDL 165
Cdd:COG3981   157 EEDGRPVRR-YWIDL 170
 
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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