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Conserved domains on  [gi|1251770415|ref|NP_001343398|]
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thialysine N-epsilon-acetyltransferase isoform 2 [Mus musculus]

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
3-106 1.12e-11

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 57.70  E-value: 1.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770415   3 STRIREARESDCGDIMRMIRELAEFEKLSHQVKISEEALRADGFGE--NPFFHCLVAEiipAPGEsqgslVVGYgLYYFI 80
Cdd:COG1247     1 EMTIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAilAPGRPVLVAE---EDGE-----VVGF-ASLGP 71

                          90       100
                  ....*....|....*....|....*..
gi 1251770415  81 YSTWTG-RNVYLEDIYVMPQYRGTGWG 106
Cdd:COG1247    72 FRPRPAyRGTAEESIYVDPDARGRGIG 98
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
3-106 1.12e-11

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 57.70  E-value: 1.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770415   3 STRIREARESDCGDIMRMIRELAEFEKLSHQVKISEEALRADGFGE--NPFFHCLVAEiipAPGEsqgslVVGYgLYYFI 80
Cdd:COG1247     1 EMTIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAilAPGRPVLVAE---EDGE-----VVGF-ASLGP 71

                          90       100
                  ....*....|....*....|....*..
gi 1251770415  81 YSTWTG-RNVYLEDIYVMPQYRGTGWG 106
Cdd:COG1247    72 FRPRPAyRGTAEESIYVDPDARGRGIG 98
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 71-106 6.76e-03

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: 33.65  E-value: 6.76e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1251770415  71 VVGYGLYYFIYSTWtgRNVYLEDIYVMPQYRGTGWG 106
Cdd:pfam00583  44 LVGFASLSIIDDEP--PVGEIEGLAVAPEYRGKGIG 77
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 71-106 7.34e-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: 32.63  E-value: 7.34e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1251770415  71 VVGYGLYYFIYstWTGRNVYLEDIYVMPQYRGTGWG 106
Cdd:cd04301    10 IVGFASLSPDG--SGGDTAYIGDLAVLPEYRGKGIG 43
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
3-106 1.12e-11

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 57.70  E-value: 1.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770415   3 STRIREARESDCGDIMRMIRELAEFEKLSHQVKISEEALRADGFGE--NPFFHCLVAEiipAPGEsqgslVVGYgLYYFI 80
Cdd:COG1247     1 EMTIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAilAPGRPVLVAE---EDGE-----VVGF-ASLGP 71

                          90       100
                  ....*....|....*....|....*..
gi 1251770415  81 YSTWTG-RNVYLEDIYVMPQYRGTGWG 106
Cdd:COG1247    72 FRPRPAyRGTAEESIYVDPDARGRGIG 98
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
6-104 2.00e-06

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 43.54  E-value: 2.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770415   6 IREARESDCGDIMRMIRELAEFEKLSHQVkiseEALRADGfgenPFFHCLVAEIipapgesqGSLVVGYGLYYFIYSTWT 85
Cdd:COG3153     1 IRPATPEDAEAIAALLRAAFGPGREAELV----DRLREDP----AAGLSLVAED--------DGEIVGHVALSPVDIDGE 64

                          90
                  ....*....|....*....
gi 1251770415  86 GRNVYLEDIYVMPQYRGTG 104
Cdd:COG3153    65 GPALLLGPLAVDPEYRGQG 83
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 5-106 1.39e-04

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: 38.43  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770415   5 RIREARESDCGDIMRMIRELAEFEKLSHqvkiseealradgfgenpffhCLVAEiipapgesQGSLVVGYGLYYFIystw 84
Cdd:COG1246     2 TIRPATPDDVPAILELIRPYALEEEIGE---------------------FWVAE--------EDGEIVGCAALHPL---- 48

                          90       100
                  ....*....|....*....|..
gi 1251770415  85 TGRNVYLEDIYVMPQYRGTGWG 106
Cdd:COG1246    49 DEDLAELRSLAVHPDYRGRGIG 70
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 71-106 6.76e-03

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: 33.65  E-value: 6.76e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1251770415  71 VVGYGLYYFIYSTWtgRNVYLEDIYVMPQYRGTGWG 106
Cdd:pfam00583  44 LVGFASLSIIDDEP--PVGEIEGLAVAPEYRGKGIG 77
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 71-106 7.34e-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: 32.63  E-value: 7.34e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1251770415  71 VVGYGLYYFIYstWTGRNVYLEDIYVMPQYRGTGWG 106
Cdd:cd04301    10 IVGFASLSPDG--SGGDTAYIGDLAVLPEYRGKGIG 43
 
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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