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Conserved domains on  [gi|515632337|ref|WP_017064937|]
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MULTISPECIES: GNAT family N-acetyltransferase [Vibrio]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10006981)

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
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
7-165 4.99e-20

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


:

Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 81.67  E-value: 4.99e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515632337   7 FRQYNSNEIETITQVFTQTFTDSEgenEGKTLGELANDlltttaPTELFCFVVEDDSsesdadsTIVGSIIFTSLSFDDE 86
Cdd:COG3153    1 IRPATPEDAEAIAALLRAAFGPGR---EAELVDRLRED------PAAGLSLVAEDDG-------EIVGHVALSPVDIDGE 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515632337  87 TKAYLLSPVAVSTQVQKRGIGQRLINSGLQLLKEQGIELAVTYGDPN---YYSKVGFEQITVEQVPAPFElsfsHGWLAQ 163
Cdd:COG3153   65 GPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSllpFYERFGFRPAGELGLTLGPD----EVFLAK 140


                 ..
gi 515632337 164 SL 165
Cdd:COG3153  141 EL 142
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
7-165 4.99e-20

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 81.67  E-value: 4.99e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515632337   7 FRQYNSNEIETITQVFTQTFTDSEgenEGKTLGELANDlltttaPTELFCFVVEDDSsesdadsTIVGSIIFTSLSFDDE 86
Cdd:COG3153    1 IRPATPEDAEAIAALLRAAFGPGR---EAELVDRLRED------PAAGLSLVAEDDG-------EIVGHVALSPVDIDGE 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515632337  87 TKAYLLSPVAVSTQVQKRGIGQRLINSGLQLLKEQGIELAVTYGDPN---YYSKVGFEQITVEQVPAPFElsfsHGWLAQ 163
Cdd:COG3153   65 GPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSllpFYERFGFRPAGELGLTLGPD----EVFLAK 140


                 ..
gi 515632337 164 SL 165
Cdd:COG3153  141 EL 142
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 72-142 1.00e-06

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 44.75  E-value: 1.00e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515632337   72 IVGsiiFTSLSFDDETKAYLLSPVAVSTQVQKRGIGQRLINSGLQLLKEQGI---ELAVTYGDPNYYSKVGFEQ 142
Cdd:pfam13508  14 IVG---FAALLPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIkllELETTNRAAAFYEKLGFEE 84
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 71-124 9.10e-05

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: 39.18  E-value: 9.10e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 515632337  71 TIVGSIIFTSlsFDDETKAYLLSPVAVSTQVQKRGIGQRLINSGLQLLKEQGIE 124
Cdd:cd04301    9 EIVGFASLSP--DGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAK 60
PRK07757 PRK07757
N-acetyltransferase;
95-149 1.56e-04

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 40.18  E-value: 1.56e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515632337  95 VAVSTQVQKRGIGQRLINSGLQLLKEQGIE--LAVTYgDPNYYSKVGFEQITVEQVP 149
Cdd:PRK07757  71 LAVSEDYRGQGIGRMLVEACLEEARELGVKrvFALTY-QPEFFEKLGFREVDKEALP 126
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
7-165 4.99e-20

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 81.67  E-value: 4.99e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515632337   7 FRQYNSNEIETITQVFTQTFTDSEgenEGKTLGELANDlltttaPTELFCFVVEDDSsesdadsTIVGSIIFTSLSFDDE 86
Cdd:COG3153    1 IRPATPEDAEAIAALLRAAFGPGR---EAELVDRLRED------PAAGLSLVAEDDG-------EIVGHVALSPVDIDGE 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515632337  87 TKAYLLSPVAVSTQVQKRGIGQRLINSGLQLLKEQGIELAVTYGDPN---YYSKVGFEQITVEQVPAPFElsfsHGWLAQ 163
Cdd:COG3153   65 GPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSllpFYERFGFRPAGELGLTLGPD----EVFLAK 140


                 ..
gi 515632337 164 SL 165
Cdd:COG3153  141 EL 142
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 72-152 8.58e-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: 48.83  E-value: 8.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515632337  72 IVGsiiFTSLSFDDETKAYLLSpVAVSTQVQKRGIGQRLINSGLQLLKEQGIE---LAVTYGDPNYYSKVGFEQITVEQV 148
Cdd:COG1246   39 IVG---CAALHPLDEDLAELRS-LAVHPDYRGRGIGRRLLEALLAEARELGLKrlfLLTTSAAIHFYEKLGFEEIDKEDL 114


                 ....
gi 515632337 149 PAPF 152
Cdd:COG1246  115 PYAK 118
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 72-142 1.00e-06

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 44.75  E-value: 1.00e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515632337   72 IVGsiiFTSLSFDDETKAYLLSPVAVSTQVQKRGIGQRLINSGLQLLKEQGI---ELAVTYGDPNYYSKVGFEQ 142
Cdd:pfam13508  14 IVG---FAALLPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIkllELETTNRAAAFYEKLGFEE 84
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 71-140 9.56e-06

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: 42.89  E-value: 9.56e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515632337   71 TIVGSIIFTSlsFDDETKAYLLSPVAVSTQVQKRGIGQRLINSGLQLLKEQG---IELAVTYGDP---NYYSKVGF 140
Cdd:pfam00583  43 ELVGFASLSI--IDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGcerIFLEVAADNLaaiALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 78-143 1.84e-05

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 41.56  E-value: 1.84e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515632337  78 FTSLSFDDETKAYLLSPVAVSTQVQKRGIGQRLINSGLQLLKEQG---IELAVTYGDP---NYYSKVGFEQI 143
Cdd:COG0456    2 FALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGarrLRLEVREDNEaaiALYEKLGFEEV 73
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 71-124 9.10e-05

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: 39.18  E-value: 9.10e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 515632337  71 TIVGSIIFTSlsFDDETKAYLLSPVAVSTQVQKRGIGQRLINSGLQLLKEQGIE 124
Cdd:cd04301    9 EIVGFASLSP--DGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAK 60
PRK07757 PRK07757
N-acetyltransferase;
95-149 1.56e-04

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 40.18  E-value: 1.56e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515632337  95 VAVSTQVQKRGIGQRLINSGLQLLKEQGIE--LAVTYgDPNYYSKVGFEQITVEQVP 149
Cdd:PRK07757  71 LAVSEDYRGQGIGRMLVEACLEEARELGVKrvFALTY-QPEFFEKLGFREVDKEALP 126
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
4-148 9.88e-03

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 35.36  E-value: 9.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515632337   4 TMKFRQYNSNEIETITQVFTQTFTDSEG--ENEGKTLGELAnDLLTTTAPTELFCFVVEDDSsesdadsTIVGSIIFTSL 81
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIYNEAIAEGTAtfETEPPSEEERE-AWFAAILAPGRPVLVAEEDG-------EVVGFASLGPF 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515632337  82 S-FDDETKAYLLSpVAVSTQVQKRGIGQRLINSGLQLLKEQGI-ELAVTYGDPN-----YYSKVGFEQI-TVEQV 148
Cdd:COG1247   73 RpRPAYRGTAEES-IYVDPDARGRGIGRALLEALIERARARGYrRLVAVVLADNeasiaLYEKLGFEEVgTLPEV 146
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
95-143 9.95e-03

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 34.77  E-value: 9.95e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515632337  95 VAVSTQVQKRGIGQRLINSGLQLLKEQG---IEL-----AVtygdpNYYSKVGFEQI 143
Cdd:COG2153   64 VAVLPEYRGQGLGRALMEAAIEEARERGarrIVLsaqahAV-----GFYEKLGFVPV 115
 
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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