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Conserved domains on  [gi|489971004|ref|WP_003874227|]
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GNAT family N-acetyltransferase [Mycobacterium avium]

Protein Classification

N-acetyltransferase( domain architecture ID 1000386)

N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate; similar to Drosophila melanogaster arylalkylamine N-acetyltransferase 1 that catalyzes N-acetylation of tryptamine, tyramine, dopamine, serotonin, and octopamine

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];
118-194 4.71e-11

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


:

Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 58.17  E-value: 4.71e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489971004 118 VHPEEPHWYLAVIGSDPGVRGQGFGQALMRSRLDRCDAEHCPAYLESTKPENVPYYQRFGFTVTREIVLPDGGPSMW 194
Cdd:COG3153   61 IDGEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLPFYERFGFRPAGELGLTLGPDEVF 137
Eis super family cl34773
Predicted acetyltransferase [General function prediction only];
4-181 9.86e-03

Predicted acetyltransferase [General function prediction only];


The actual alignment was detected with superfamily member COG4552:

Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 36.03  E-value: 9.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489971004   4 QVRPADRADIRALSATLARAFYDDPVMvwLFPDRRKRIARLSRVFAtmtrhhhlagggvevacagagigaaaLWDPphrw 83
Cdd:COG4552    2 EIRPLTEDDLDAFARLLAYAFGPEPDD--EELEAYRPLLEPGRVLG--------------------------VFDD---- 49

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489971004  84 rETPRAQLAMTPTYLRVfglrsmRGRAVqelmksvhpeePHWYLAVIGSDPGVRGQGFGQALMRSRLDRCDAEHCP-AYL 162
Cdd:COG4552   50 -GELVGTLALYPFTLNV------GGARV-----------PMAGITGVAVAPEHRRRGVARALLREALAELRERGQPlSAL 111

                        170
                 ....*....|....*....
gi 489971004 163 ESTKPenvPYYQRFGFTVT 181
Cdd:COG4552  112 YPFEP---GFYRRFGYELA 127
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
118-194 4.71e-11

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 58.17  E-value: 4.71e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489971004 118 VHPEEPHWYLAVIGSDPGVRGQGFGQALMRSRLDRCDAEHCPAYLESTKPENVPYYQRFGFTVTREIVLPDGGPSMW 194
Cdd:COG3153   61 IDGEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLPFYERFGFRPAGELGLTLGPDEVF 137
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 124-180 2.16e-06

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 43.98  E-value: 2.16e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 489971004  124 HWYLAVigsDPGVRGQGFGQALMRSRLDRCDAEHCPAYLESTKPENVPYYQRFGFTV 180
Cdd:pfam13508  31 ELRLAV---HPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRAAAFYEKLGFEE 84
PRK10314 PRK10314
GNAT family N-acetyltransferase;
110-193 1.12e-03

GNAT family N-acetyltransferase;


Pssm-ID: 182373 [Multi-domain]  Cd Length: 153  Bit Score: 37.90  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489971004 110 AVQELMKSVHPEEPHWYLAVIGSDpGVRGQGFGQALMRSRLDRCdAEHCP---AYLeSTKPENVPYYQRFGFTVTREIVL 186
Cdd:PRK10314  61 AYARILKSDDDLEPVVIGRVIVSE-ALRGEKVGQQLMSKTLESC-TRHWPdkpVYL-GAQAHLQNFYQSFGFIPVTEVYE 137


                 ....*..
gi 489971004 187 PDGGPSM 193
Cdd:PRK10314 138 EDGIPHI 144
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 120-159 6.92e-03

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: 33.79  E-value: 6.92e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 489971004 120 PEEPHWYLAVIGSDPGVRGQGFGQALMRSRLDRCDAEHCP 159
Cdd:cd04301   21 SGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAK 60
Eis COG4552
Predicted acetyltransferase [General function prediction only];
4-181 9.86e-03

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 36.03  E-value: 9.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489971004   4 QVRPADRADIRALSATLARAFYDDPVMvwLFPDRRKRIARLSRVFAtmtrhhhlagggvevacagagigaaaLWDPphrw 83
Cdd:COG4552    2 EIRPLTEDDLDAFARLLAYAFGPEPDD--EELEAYRPLLEPGRVLG--------------------------VFDD---- 49

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489971004  84 rETPRAQLAMTPTYLRVfglrsmRGRAVqelmksvhpeePHWYLAVIGSDPGVRGQGFGQALMRSRLDRCDAEHCP-AYL 162
Cdd:COG4552   50 -GELVGTLALYPFTLNV------GGARV-----------PMAGITGVAVAPEHRRRGVARALLREALAELRERGQPlSAL 111

                        170
                 ....*....|....*....
gi 489971004 163 ESTKPenvPYYQRFGFTVT 181
Cdd:COG4552  112 YPFEP---GFYRRFGYELA 127
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
118-194 4.71e-11

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 58.17  E-value: 4.71e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489971004 118 VHPEEPHWYLAVIGSDPGVRGQGFGQALMRSRLDRCDAEHCPAYLESTKPENVPYYQRFGFTVTREIVLPDGGPSMW 194
Cdd:COG3153   61 IDGEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLPFYERFGFRPAGELGLTLGPDEVF 137
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 117-199 5.15e-08

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 48.88  E-value: 5.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489971004 117 SVHPEEPHWYLAVIGSDPGVRGQGFGQALMRSRLDRCDAEHCP-AYLEsTKPENVP---YYQRFGFTVTREIVLPDGGPS 192
Cdd:COG0456    6 GLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARrLRLE-VREDNEAaiaLYEKLGFEEVGERPNYYGDDA 84


                 ....*..
gi 489971004 193 MWaMWRP 199
Cdd:COG0456   85 LV-MEKE 90
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 124-180 2.16e-06

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 43.98  E-value: 2.16e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 489971004  124 HWYLAVigsDPGVRGQGFGQALMRSRLDRCDAEHCPAYLESTKPENVPYYQRFGFTV 180
Cdd:pfam13508  31 ELRLAV---HPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRAAAFYEKLGFEE 84
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 121-191 6.33e-06

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 43.89  E-value: 6.33e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489971004 121 EEPHWYLAVIGSDPGVRGQGFGQALMRSRLDRCDAEHCpAYLEST----KPENVPYYQRFGFTVTREIVLPDGGP 191
Cdd:COG0454   55 DDKVLELKRLYVLPEYRGKGIGKALLEALLEWARERGC-TALELDtldgNPAAIRFYERLGFKEIERYVAYVGGE 128
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 121-189 1.96e-05

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: 42.67  E-value: 1.96e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489971004 121 EEPHWYLAVIGSDPGVRGQGFGQALMRSRLDRCDAEHCPA-YLESTkPENVPYYQRFGFTVTREIVLPDG 189
Cdd:COG1246   49 DEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRlFLLTT-SAAIHFYEKLGFEEIDKEDLPYA 117
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 118-178 4.10e-05

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: 41.35  E-value: 4.10e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489971004  118 VHPEEPHWYLAVIGSDPGVRGQGFGQALMRSRLDRCDAEHCPAYLESTKPEN---VPYYQRFGF 178
Cdd:pfam00583  53 IDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNlaaIALYEKLGF 116
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
118-201 3.18e-04

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 39.01  E-value: 3.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489971004 118 VHPEEPHWY----LAVigsDPGVRGQGFGQALMRSRLDRCDAEHC-PAYLESTKpENVPYYQRFGFTVTREIVLPDGGPS 192
Cdd:COG2153   51 LLPPGDGEAkigrVAV---LPEYRGQGLGRALMEAAIEEARERGArRIVLSAQA-HAVGFYEKLGFVPVGEEFLEAGIPH 126


                 ....*....
gi 489971004 193 MWaMWRPPR 201
Cdd:COG2153  127 ID-MRKPLS 134
PRK10314 PRK10314
GNAT family N-acetyltransferase;
110-193 1.12e-03

GNAT family N-acetyltransferase;


Pssm-ID: 182373 [Multi-domain]  Cd Length: 153  Bit Score: 37.90  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489971004 110 AVQELMKSVHPEEPHWYLAVIGSDpGVRGQGFGQALMRSRLDRCdAEHCP---AYLeSTKPENVPYYQRFGFTVTREIVL 186
Cdd:PRK10314  61 AYARILKSDDDLEPVVIGRVIVSE-ALRGEKVGQQLMSKTLESC-TRHWPdkpVYL-GAQAHLQNFYQSFGFIPVTEVYE 137


                 ....*..
gi 489971004 187 PDGGPSM 193
Cdd:PRK10314 138 EDGIPHI 144
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 120-159 6.92e-03

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: 33.79  E-value: 6.92e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 489971004 120 PEEPHWYLAVIGSDPGVRGQGFGQALMRSRLDRCDAEHCP 159
Cdd:cd04301   21 SGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAK 60
Eis COG4552
Predicted acetyltransferase [General function prediction only];
4-181 9.86e-03

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 36.03  E-value: 9.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489971004   4 QVRPADRADIRALSATLARAFYDDPVMvwLFPDRRKRIARLSRVFAtmtrhhhlagggvevacagagigaaaLWDPphrw 83
Cdd:COG4552    2 EIRPLTEDDLDAFARLLAYAFGPEPDD--EELEAYRPLLEPGRVLG--------------------------VFDD---- 49

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489971004  84 rETPRAQLAMTPTYLRVfglrsmRGRAVqelmksvhpeePHWYLAVIGSDPGVRGQGFGQALMRSRLDRCDAEHCP-AYL 162
Cdd:COG4552   50 -GELVGTLALYPFTLNV------GGARV-----------PMAGITGVAVAPEHRRRGVARALLREALAELRERGQPlSAL 111

                        170
                 ....*....|....*....
gi 489971004 163 ESTKPenvPYYQRFGFTVT 181
Cdd:COG4552  112 YPFEP---GFYRRFGYELA 127
 
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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