UniProt: G3I189

Database: UniProt
Entry: G3I189_CRIGR

LinkDB:  G3I189_CRIGR 
Original site:  G3I189_CRIGR

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Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (5)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   ENSEMBL-UP (3)   
Protein sequence (2)   
   RefSeq(pep) (2)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (5)   
   InterPro (3)   
   Pfam (1)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (17)   

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ID   G3I189_CRIGR            Unreviewed;       215 AA.
AC   G3I189;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=N-terminal amino-acid N(alpha)-acetyltransferase NatA {ECO:0000256|ARBA:ARBA00026110};
DE            EC=2.3.1.255 {ECO:0000256|ARBA:ARBA00026110};
GN   Name=Naa11 {ECO:0000313|Ensembl:ENSCGRP00001001562.1,
GN   ECO:0000313|RefSeq:XP_027243409.1};
GN   ORFNames=I79_017139 {ECO:0000313|EMBL:EGW10743.1};
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW10743.1, ECO:0000313|Proteomes:UP000001075};
RN   [1] {ECO:0000313|Proteomes:UP000001075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX   PubMed=21804562; DOI=10.1038/nbt.1932;
RA   Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA   Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA   Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA   Famili I., Palsson B.O., Wang J.;
RT   "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL   Nat. Biotechnol. 29:735-741(2011).
RN   [2] {ECO:0000313|EMBL:EGW10743.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA   Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA   Fan C.H., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA   Famili I., Palsson B.O., Wang J.;
RT   "The genomic sequence of the Chinese hamster ovary CHO-K1 cell line.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSCGRP00001001562.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
RN   [4] {ECO:0000313|RefSeq:XP_027243409.1}
RP   IDENTIFICATION.
RC   STRAIN=17A/GY {ECO:0000313|RefSeq:XP_027243409.1};
RC   TISSUE=Liver {ECO:0000313|RefSeq:XP_027243409.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N-terminal L-alanyl-[protein] = CoA + H(+) + N-
CC         terminal N(alpha)-acetyl-L-alanyl-[protein]; Xref=Rhea:RHEA:50500,
CC         Rhea:RHEA-COMP:12701, Rhea:RHEA-COMP:12702, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64718,
CC         ChEBI:CHEBI:83683; EC=2.3.1.255;
CC         Evidence={ECO:0000256|ARBA:ARBA00024449};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N-terminal L-cysteinyl-[protein] = CoA + H(+) +
CC         N-terminal N(alpha)-acetyl-L-cysteinyl-[protein];
CC         Xref=Rhea:RHEA:50512, Rhea:RHEA-COMP:12707, Rhea:RHEA-COMP:12708,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:65250, ChEBI:CHEBI:133372; EC=2.3.1.255;
CC         Evidence={ECO:0000256|ARBA:ARBA00024588};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N-terminal L-seryl-[protein] = CoA + H(+) + N-
CC         terminal N(alpha)-acetyl-L-seryl-[protein]; Xref=Rhea:RHEA:50504,
CC         Rhea:RHEA-COMP:12703, Rhea:RHEA-COMP:12704, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64738,
CC         ChEBI:CHEBI:83690; EC=2.3.1.255;
CC         Evidence={ECO:0000256|ARBA:ARBA00024482};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N-terminal L-threonyl-[protein] = CoA + H(+) + N-
CC         terminal N(alpha)-acetyl-L-threonyl-[protein]; Xref=Rhea:RHEA:50516,
CC         Rhea:RHEA-COMP:12709, Rhea:RHEA-COMP:12710, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64739,
CC         ChEBI:CHEBI:133375; EC=2.3.1.255;
CC         Evidence={ECO:0000256|ARBA:ARBA00024610};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N-terminal L-valyl-[protein] = CoA + H(+) + N-
CC         terminal N(alpha)-acetyl-L-valyl-[protein]; Xref=Rhea:RHEA:50508,
CC         Rhea:RHEA-COMP:12705, Rhea:RHEA-COMP:12706, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64741,
CC         ChEBI:CHEBI:133371; EC=2.3.1.255;
CC         Evidence={ECO:0000256|ARBA:ARBA00024591};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N-terminal glycyl-[protein] = CoA + H(+) + N-
CC         terminal N(alpha)-acetylglycyl-[protein]; Xref=Rhea:RHEA:50496,
CC         Rhea:RHEA-COMP:12666, Rhea:RHEA-COMP:12700, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64723,
CC         ChEBI:CHEBI:133369; EC=2.3.1.255;
CC         Evidence={ECO:0000256|ARBA:ARBA00024451};
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. ARD1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00025786}.
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DR   EMBL; JH001055; EGW10743.1; -; Genomic_DNA.
DR   RefSeq; XP_003509102.1; XM_003509054.2.
DR   RefSeq; XP_027243409.1; XM_027387608.1.
DR   STRING; 10029.G3I189; -.
DR   PaxDb; 10029-XP_007606539-1; -.
DR   Ensembl; ENSCGRT00001001729.1; ENSCGRP00001001562.1; ENSCGRG00001001343.1.
DR   GeneID; 100770650; -.
DR   KEGG; cge:100770650; -.
DR   CTD; 84779; -.
DR   eggNOG; KOG3235; Eukaryota.
DR   GeneTree; ENSGT00940000164242; -.
DR   OMA; LPENYFM; -.
DR   OrthoDB; 275667at2759; -.
DR   Proteomes; UP000001075; Unassembled WGS sequence.
DR   Proteomes; UP000694386; Unplaced.
DR   Proteomes; UP001108280; Chromosome 1.
DR   GO; GO:0031415; C:NatA complex; IEA:InterPro.
DR   GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; IEA:InterPro.
DR   CDD; cd04301; NAT_SF; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR045047; Ard1-like.
DR   InterPro; IPR000182; GNAT_dom.
DR   PANTHER; PTHR23091:SF282; N-ALPHA-ACETYLTRANSFERASE 11; 1.
DR   PANTHER; PTHR23091; N-TERMINAL ACETYLTRANSFERASE; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001075};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..152
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
FT   REGION          175..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        198..215
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   215 AA;  24344 MW;  FF89E089B686B42A CRC64;
     MNIRNARPDD LMNMQHCNLL CLPENYQMKY YFYHGLSWPQ LSYIAEDEDG KIVGYVLAKM
     EEDPDDVPHG HITSLAVKRS HRRLGLAQKL MDQASRAMIE NFSAKYVSLH VRKSNRAALH
     LYSNTLNFQV SEVEPKYYAD GEDAYAMKRD LSQMADELRR QLVLKKGKYV VLGSSENQEV
     QDSTLPGAEE ACQLESPAGD STDDQGSSED LDSTS
//

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