NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1025728039|gb|ANC57707|]
View 

acyltransferase, partial [Mesorhizobium sp. NWXJ42]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 1-157 2.41e-103

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 TIGR04245:

Pssm-ID: 473072  Cd Length: 193  Bit Score: 293.92  E-value: 2.41e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025728039   1 LADFFRKTYGPTGAFNAEPFEGNRSWVGARPELRAIGYDSKGIAAHLGLLRRFIKVGAVDLLVAELGLYGVRPDLEGLGI 80
Cdd:TIGR04245  20 LAEFFRKTYGPTGAFNAKPFEGGRSWAGARPELRAIGYDSRGVAAHMGLLRRFIKVGAVDLLVAELGLYGVRPDLEGLGI 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1025728039  81 ARSIHVMSPVLHELGVPFGFGTVRHALRNHLERFGRHGLMTVVSGVCVRSTHPQVHLHLSATRVEDVLVVVMPIARP 157
Cdd:TIGR04245 100 GHSIRAMYPVLQELGVPFAFGTVRHALRNHVERLCRNGLATIVSGVRVRSTLPDVHLDLPPTRIEDVLVVVFPIGRS 176
 
Name Accession Description Interval E-value
nodulat_NodA TIGR04245
N-acyltransferase NodA; Nodulation factors are lipo-chitooligosaccharides made by bacterial ...
 1-157 2.41e-103

N-acyltransferase NodA; Nodulation factors are lipo-chitooligosaccharides made by bacterial nitrogen-fixing bacteria as a signal to plant hosts. Nod factors differ slightly from system to system are serve as host range determinants. Because the N-acyl group varies from one NodA to another, the family treated as a subfamily, but all members of this family belong to NodABC systems.


Pssm-ID: 211968  Cd Length: 193  Bit Score: 293.92  E-value: 2.41e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025728039   1 LADFFRKTYGPTGAFNAEPFEGNRSWVGARPELRAIGYDSKGIAAHLGLLRRFIKVGAVDLLVAELGLYGVRPDLEGLGI 80
Cdd:TIGR04245  20 LAEFFRKTYGPTGAFNAKPFEGGRSWAGARPELRAIGYDSRGVAAHMGLLRRFIKVGAVDLLVAELGLYGVRPDLEGLGI 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1025728039  81 ARSIHVMSPVLHELGVPFGFGTVRHALRNHLERFGRHGLMTVVSGVCVRSTHPQVHLHLSATRVEDVLVVVMPIARP 157
Cdd:TIGR04245 100 GHSIRAMYPVLQELGVPFAFGTVRHALRNHVERLCRNGLATIVSGVRVRSTLPDVHLDLPPTRIEDVLVVVFPIGRS 176
PRK00756 PRK00756
acyltransferase NodA; Provisional
 1-157 2.26e-102

acyltransferase NodA; Provisional


Pssm-ID: 179111  Cd Length: 196  Bit Score: 291.61  E-value: 2.26e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025728039   1 LADFFRKTYGPTGAFNAEPFEGNRSWVGARPELRAIGYDSKGIAAHLGLLRRFIKVGAVDLLVAELGLYGVRPDLEGLGI 80
Cdd:PRK00756   23 LAEFFRKTYGPTGAFNAKPFEGGRSWAGARPELRAIAYDSHGVAAHMGLLRRFIKVGEVDLLVAELGLYGVRPDLEGLGI 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1025728039  81 ARSIHVMSPVLHELGVPFGFGTVRHALRNHLERFGRHGLMTVVSGVCVRSTHPQVHLHLSATRVEDVLVVVMPIARP 157
Cdd:PRK00756  103 AHSIRAMYPVLQELGVPFAFGTVRHALRNHVERLCRNGLATIVTGVRVRSTLPDVYLDLPPTRTEDVLVVVFPIGRP 179
NodA pfam02474
Nodulation protein A (NodA); Rhizobia nodulation (nod) genes control the biosynthesis of Nod ...
 1-157 2.27e-88

Nodulation protein A (NodA); Rhizobia nodulation (nod) genes control the biosynthesis of Nod factors required for infection and nodulation of their legume hosts. Nodulation protein A (NodA) is a N-acetyltransferase involved in production of Nod factors that stimulate mitosis in various plant protoplasts.


Pssm-ID: 426792  Cd Length: 195  Bit Score: 256.25  E-value: 2.27e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025728039   1 LADFFRKTYGPTGAFNAEPFEGNRSWVGARPELRAIGYDSKGIAAHLGLLRRFIKVGAVDLLVAELGLYGVRPDLEGLGI 80
Cdd:pfam02474  22 LAEFFRKSYGATGAFNAKPFEGGRSWAGARPELRIIGYDSRGVAAHMGVLRRFIKVGGVDLLVAELGLYAVRPDLEGLGI 101

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1025728039  81 ARSIHVMSPVLHELGVPFGFGTVRHALRNHLERFGRHGLMTVVSGVCVRSTHPQVHLHLSATRVEDVLVVVMPIARP 157
Cdd:pfam02474 102 GHSILVMTPVLKELGVPFGFGTVRHALRKHVERLCRNGLATIVSGVRVRSTLPDVYPDLPPTRIEDLLVVVLPVGRP 178
 
Name Accession Description Interval E-value
nodulat_NodA TIGR04245
N-acyltransferase NodA; Nodulation factors are lipo-chitooligosaccharides made by bacterial ...
 1-157 2.41e-103

N-acyltransferase NodA; Nodulation factors are lipo-chitooligosaccharides made by bacterial nitrogen-fixing bacteria as a signal to plant hosts. Nod factors differ slightly from system to system are serve as host range determinants. Because the N-acyl group varies from one NodA to another, the family treated as a subfamily, but all members of this family belong to NodABC systems.


Pssm-ID: 211968  Cd Length: 193  Bit Score: 293.92  E-value: 2.41e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025728039   1 LADFFRKTYGPTGAFNAEPFEGNRSWVGARPELRAIGYDSKGIAAHLGLLRRFIKVGAVDLLVAELGLYGVRPDLEGLGI 80
Cdd:TIGR04245  20 LAEFFRKTYGPTGAFNAKPFEGGRSWAGARPELRAIGYDSRGVAAHMGLLRRFIKVGAVDLLVAELGLYGVRPDLEGLGI 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1025728039  81 ARSIHVMSPVLHELGVPFGFGTVRHALRNHLERFGRHGLMTVVSGVCVRSTHPQVHLHLSATRVEDVLVVVMPIARP 157
Cdd:TIGR04245 100 GHSIRAMYPVLQELGVPFAFGTVRHALRNHVERLCRNGLATIVSGVRVRSTLPDVHLDLPPTRIEDVLVVVFPIGRS 176
PRK00756 PRK00756
acyltransferase NodA; Provisional
 1-157 2.26e-102

acyltransferase NodA; Provisional


Pssm-ID: 179111  Cd Length: 196  Bit Score: 291.61  E-value: 2.26e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025728039   1 LADFFRKTYGPTGAFNAEPFEGNRSWVGARPELRAIGYDSKGIAAHLGLLRRFIKVGAVDLLVAELGLYGVRPDLEGLGI 80
Cdd:PRK00756   23 LAEFFRKTYGPTGAFNAKPFEGGRSWAGARPELRAIAYDSHGVAAHMGLLRRFIKVGEVDLLVAELGLYGVRPDLEGLGI 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1025728039  81 ARSIHVMSPVLHELGVPFGFGTVRHALRNHLERFGRHGLMTVVSGVCVRSTHPQVHLHLSATRVEDVLVVVMPIARP 157
Cdd:PRK00756  103 AHSIRAMYPVLQELGVPFAFGTVRHALRNHVERLCRNGLATIVTGVRVRSTLPDVYLDLPPTRTEDVLVVVFPIGRP 179
NodA pfam02474
Nodulation protein A (NodA); Rhizobia nodulation (nod) genes control the biosynthesis of Nod ...
 1-157 2.27e-88

Nodulation protein A (NodA); Rhizobia nodulation (nod) genes control the biosynthesis of Nod factors required for infection and nodulation of their legume hosts. Nodulation protein A (NodA) is a N-acetyltransferase involved in production of Nod factors that stimulate mitosis in various plant protoplasts.


Pssm-ID: 426792  Cd Length: 195  Bit Score: 256.25  E-value: 2.27e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025728039   1 LADFFRKTYGPTGAFNAEPFEGNRSWVGARPELRAIGYDSKGIAAHLGLLRRFIKVGAVDLLVAELGLYGVRPDLEGLGI 80
Cdd:pfam02474  22 LAEFFRKSYGATGAFNAKPFEGGRSWAGARPELRIIGYDSRGVAAHMGVLRRFIKVGGVDLLVAELGLYAVRPDLEGLGI 101

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1025728039  81 ARSIHVMSPVLHELGVPFGFGTVRHALRNHLERFGRHGLMTVVSGVCVRSTHPQVHLHLSATRVEDVLVVVMPIARP 157
Cdd:pfam02474 102 GHSILVMTPVLKELGVPFGFGTVRHALRKHVERLCRNGLATIVSGVRVRSTLPDVYPDLPPTRIEDLLVVVLPVGRP 178
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH