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Conserved domains on  [gi|17541550|ref|NP_502069|]
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N-acetyltransferase domain-containing protein [Caenorhabditis elegans]

Protein Classification

GNAT family protein( domain architecture ID 106742)

GNAT (Gcn5-related N-acetyltransferase) family protein similar to N-acetyltransferases that catalyze the transfer of an acetyl group from acetyl-CoA to a substrate

PubMed:  15581578

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NAT_SF super family cl17182
N-Acyltransferase superfamily: Various enyzmes that characteristicly catalyze the transfer of ...
 82-193 1.12e-03

N-Acyltransferase superfamily: Various enyzmes that characteristicly 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, 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 mechanism is an ordered Bi-Bi ternary complex kinetic mechanism for most GNATs: 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 then 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/ph enylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


The actual alignment was detected with superfamily member pfam00583:

Pssm-ID: 473072 [Multi-domain]  Cd Length: 116  Bit Score: 37.50  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541550    82 MLNSVWRRDESLCTPGEEDKDFEFHTIRKEVAMVAEILNELhESFWSLRPDQDVVLHFEISSVSV--NHRRQGLASKFMN 159
Cdd:pfam00583   4 LYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGEL-VGFASLSIIDDEPPVGEIEGLAVapEYRGKGIGTALLQ 82

                          90       100       110
                  ....*....|....*....|....*....|....
gi 17541550   160 WTENKKFLDTFGATGIATEASSLANQALLAKRGY 193
Cdd:pfam00583  83 ALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 82-193 1.12e-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: 37.50  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541550    82 MLNSVWRRDESLCTPGEEDKDFEFHTIRKEVAMVAEILNELhESFWSLRPDQDVVLHFEISSVSV--NHRRQGLASKFMN 159
Cdd:pfam00583   4 LYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGEL-VGFASLSIIDDEPPVGEIEGLAVapEYRGKGIGTALLQ 82

                          90       100       110
                  ....*....|....*....|....*....|....
gi 17541550   160 WTENKKFLDTFGATGIATEASSLANQALLAKRGY 193
Cdd:pfam00583  83 ALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 82-193 1.12e-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: 37.50  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541550    82 MLNSVWRRDESLCTPGEEDKDFEFHTIRKEVAMVAEILNELhESFWSLRPDQDVVLHFEISSVSV--NHRRQGLASKFMN 159
Cdd:pfam00583   4 LYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGEL-VGFASLSIIDDEPPVGEIEGLAVapEYRGKGIGTALLQ 82

                          90       100       110
                  ....*....|....*....|....*....|....
gi 17541550   160 WTENKKFLDTFGATGIATEASSLANQALLAKRGY 193
Cdd:pfam00583  83 ALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
 
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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