(data stored in ACNUC7421 zone)

SWISSPROT: C5BHI3_EDWI9

ID   C5BHI3_EDWI9            Unreviewed;       148 AA.
AC   C5BHI3;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 48.
DE   RecName: Full=Ribosomal-protein-alanine acetyltransferase {ECO:0000256|RuleBase:RU363094};
DE            EC=2.3.1.128 {ECO:0000256|RuleBase:RU363094};
GN   OrderedLocusNames=NT01EI_0553 {ECO:0000313|EMBL:ACR67782.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67782.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This enzyme acetylates the N-terminal alanine of
CC       ribosomal protein S18. {ECO:0000256|RuleBase:RU363094}.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + ribosomal-protein L-alanine = CoA
CC       + ribosomal-protein N-acetyl-L-alanine.
CC       {ECO:0000256|RuleBase:RU363094}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU363094}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. RimI
CC       subfamily. {ECO:0000256|RuleBase:RU363094}.
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DR   EMBL; CP001600; ACR67782.1; -; Genomic_DNA.
DR   RefSeq; WP_015869982.1; NC_012779.2.
DR   ProteinModelPortal; C5BHI3; -.
DR   STRING; 634503.NT01EI_0553; -.
DR   EnsemblBacteria; ACR67782; ACR67782; NT01EI_0553.
DR   GeneID; 7961574; -.
DR   KEGG; eic:NT01EI_0553; -.
DR   PATRIC; fig|634503.3.peg.499; -.
DR   eggNOG; ENOG4105KEG; Bacteria.
DR   eggNOG; COG0456; LUCA.
DR   HOGENOM; HOG000078523; -.
DR   KO; K03789; -.
DR   OMA; GERYLNY; -.
DR   OrthoDB; POG091H02FM; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008999; F:ribosomal-protein-alanine N-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006474; P:N-terminal protein amino acid acetylation; IEA:InterPro.
DR   InterPro; IPR006464; AcTrfase_RimI/Ard1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   TIGRFAMs; TIGR01575; rimI; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5BHI3.
DR   SWISS-2DPAGE; C5BHI3.
KW   Acyltransferase {ECO:0000313|EMBL:ACR67782.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Cytoplasm {ECO:0000256|RuleBase:RU363094};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
KW   Transferase {ECO:0000313|EMBL:ACR67782.1}.
FT   DOMAIN        3    148       N-acetyltransferase.
FT                                {ECO:0000259|PROSITE:PS51186}.
SQ   SEQUENCE   148 AA;  16426 MW;  FDE971C844C27BFD CRC64;
     MSNTISSLIP ADTDAAYAVE CASHAFPWTH STFLSNQGER YYNLKLESQG QLAAFAITQV
     VLDEATLFNV AVAPAYQRQG LGRTLLQRLI DDLTERGVMT LWLEVRDSNR AAIALYHALG
     FSEVSLRRNY YPTADGREDA RIMALPLG
//

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