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Conserved domains on  [gi|1015655944|gb|KZA06269|]
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hypothetical protein HMPREF1326_00119 [Akkermansia sp. KLE1605]

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];
28-151 5.24e-08

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


:

Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 48.93  E-value: 5.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655944  28 IRRPGAYERHLVADWVGLHFSPKWVSETKTAFARQP--ISCFIATREKQMIGFACYD-VTVRG-----FLGPMGVGEEAR 99
Cdd:COG3153     1 IRPATPEDAEAIAALLRAAFGPGREAELVDRLREDPaaGLSLVAEDDGEIVGHVALSpVDIDGegpalLLGPLAVDPEYR 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1015655944 100 KSGVGRVLLVSALRGLRDMGHAY-GIIGGVGPADFYARtVGAVPIEGSSPGIY 151
Cdd:COG3153    81 GQGIGRALMRAALEAARERGARAvVLLGDPSLLPFYER-FGFRPAGELGLTLG 132
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
28-151 5.24e-08

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 48.93  E-value: 5.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655944  28 IRRPGAYERHLVADWVGLHFSPKWVSETKTAFARQP--ISCFIATREKQMIGFACYD-VTVRG-----FLGPMGVGEEAR 99
Cdd:COG3153     1 IRPATPEDAEAIAALLRAAFGPGREAELVDRLREDPaaGLSLVAEDDGEIVGHVALSpVDIDGegpalLLGPLAVDPEYR 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1015655944 100 KSGVGRVLLVSALRGLRDMGHAY-GIIGGVGPADFYARtVGAVPIEGSSPGIY 151
Cdd:COG3153    81 GQGIGRALMRAALEAARERGARAvVLLGDPSLLPFYER-FGFRPAGELGLTLG 132
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 66-119 9.46e-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: 33.02  E-value: 9.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1015655944  66 CFIATREKQMIGFACY----DVTVRGFLGPMGVGEEARKSGVGRVLLVSALRGLRDMG 119
Cdd:cd04301     1 FLVAEDDGEIVGFASLspdgSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERG 58
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
28-151 5.24e-08

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 48.93  E-value: 5.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655944  28 IRRPGAYERHLVADWVGLHFSPKWVSETKTAFARQP--ISCFIATREKQMIGFACYD-VTVRG-----FLGPMGVGEEAR 99
Cdd:COG3153     1 IRPATPEDAEAIAALLRAAFGPGREAELVDRLREDPaaGLSLVAEDDGEIVGHVALSpVDIDGegpalLLGPLAVDPEYR 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1015655944 100 KSGVGRVLLVSALRGLRDMGHAY-GIIGGVGPADFYARtVGAVPIEGSSPGIY 151
Cdd:COG3153    81 GQGIGRALMRAALEAARERGARAvVLLGDPSLLPFYER-FGFRPAGELGLTLG 132
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
66-154 1.64e-04

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 39.98  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655944  66 CFIATREKQMIGFACYDvTVRGFLGPMGVGE-------EARKSGVGRVLLVSALRGLRDMGHAYgIIGGVGPA-----DF 133
Cdd:COG1247    54 VLVAEEDGEVVGFASLG-PFRPRPAYRGTAEesiyvdpDARGRGIGRALLEALIERARARGYRR-LVAVVLADneasiAL 131

                          90       100
                  ....*....|....*....|....*
gi 1015655944 134 Y----ARTVGAVPIEGSSPGIYVDI 154
Cdd:COG1247   132 YeklgFEEVGTLPEVGFKFGRWLDL 156
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 66-119 9.46e-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: 33.02  E-value: 9.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1015655944  66 CFIATREKQMIGFACY----DVTVRGFLGPMGVGEEARKSGVGRVLLVSALRGLRDMG 119
Cdd:cd04301     1 FLVAEDDGEIVGFASLspdgSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERG 58
 
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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