ID   RF1_KOCRD               Reviewed;         369 AA.
AC   B2GLX4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Peptide chain release factor 1 {ECO:0000255|HAMAP-Rule:MF_00093};
DE            Short=RF-1 {ECO:0000255|HAMAP-Rule:MF_00093};
GN   Name=prfA {ECO:0000255|HAMAP-Rule:MF_00093}; OrderedLocusNames=KRH_09680;
OS   Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / DC2201).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Kocuria.
OX   NCBI_TaxID=378753;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9341 / DSM 348 / NBRC 103217 / DC2201;
RX   PubMed=18408034; DOI=10.1128/jb.01853-07;
RA   Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S.,
RA   Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Complete genome sequence of the soil actinomycete Kocuria rhizophila.";
RL   J. Bacteriol. 190:4139-4146(2008).
CC   -!- FUNCTION: Peptide chain release factor 1 directs the termination of
CC       translation in response to the peptide chain termination codons UAG and
CC       UAA. {ECO:0000255|HAMAP-Rule:MF_00093}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00093}.
CC   -!- PTM: Methylated by PrmC. Methylation increases the termination
CC       efficiency of RF1. {ECO:0000255|HAMAP-Rule:MF_00093}.
CC   -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC       family. {ECO:0000255|HAMAP-Rule:MF_00093}.
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DR   EMBL; AP009152; BAG29315.1; -; Genomic_DNA.
DR   RefSeq; WP_012398036.1; NZ_VECX01000011.1.
DR   AlphaFoldDB; B2GLX4; -.
DR   SMR; B2GLX4; -.
DR   STRING; 378753.KRH_09680; -.
DR   EnsemblBacteria; BAG29315; BAG29315; KRH_09680.
DR   KEGG; krh:KRH_09680; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_11; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000008838; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016149; F:translation release factor activity, codon specific; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00093; Rel_fac_1; 1.
DR   InterPro; IPR005139; PCRF.
DR   InterPro; IPR000352; Pep_chain_release_fac_I.
DR   InterPro; IPR045853; Pep_chain_release_fac_I_sf.
DR   InterPro; IPR004373; RF-1.
DR   Pfam; PF03462; PCRF; 1.
DR   Pfam; PF00472; RF-1; 1.
DR   SMART; SM00937; PCRF; 1.
DR   SUPFAM; SSF75620; SSF75620; 1.
DR   TIGRFAMs; TIGR00019; prfA; 1.
DR   PROSITE; PS00745; RF_PROK_I; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methylation; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..369
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_1000093466"
FT   MOD_RES         234
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   369 AA;  40651 MW;  3B4712222C2AEA5D CRC64;
     MSDPVQPLLD EHAQLQRELA DPAVHADAGR ARKLGRRYSE LNGIVEAHRR VERLSEDLEA
     ARELGSMDPE LAAEVKPLEE ELAVAREALR RKLVPRDPDD GRNVILEVKA GEGGDESALF
     AGDLLRMYMR FAEQSGLKTE ILSSTPTELG GYKDVQLAVK GSSSDPSEGA WARFKYEGGV
     HRVQRVPVTE SQGRVHTSAA GVLVFPEVDE PDEIDISQND LKIDVYRSSG PGGQSVNTTD
     SAVRITHVPT GIVVSMQNEK SQLQNREAAM RVLRARLLAH QQEQIDAENA AARKSQVRTV
     DRSERIRTYN FPENRIADHR TGYKAYNLDH VLDGALEPVI ASAVELDEKA RLEQLGQDSA
     EQGSAGRRG