ID   RF1_CORJK               Reviewed;         358 AA.
AC   Q4JUI9;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=jk1346;
OS   Corynebacterium jeikeium (strain K411).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=306537;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K411;
RX   PubMed=15968079; DOI=10.1128/jb.187.13.4671-4682.2005;
RA   Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A.,
RA   Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F.,
RA   Rupp O., Schneiker S., Viehoever P., Puehler A.;
RT   "Complete genome sequence and analysis of the multiresistant nosocomial
RT   pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the
RT   human skin flora.";
RL   J. Bacteriol. 187:4671-4682(2005).
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; CR931997; CAI37518.1; -; Genomic_DNA.
DR   RefSeq; WP_011273827.1; NC_007164.1.
DR   AlphaFoldDB; Q4JUI9; -.
DR   SMR; Q4JUI9; -.
DR   STRING; 306537.jk1346; -.
DR   EnsemblBacteria; CAI37518; CAI37518; jk1346.
DR   KEGG; cjk:jk1346; -.
DR   PATRIC; fig|306537.10.peg.1366; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_6_11; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000000545; 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..358
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_0000263261"
FT   REGION          51..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..79
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         236
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   358 AA;  39968 MW;  EA35090995CE9664 CRC64;
     MSQSPSVIDD ILAEYQGLEM QLSDPELHND PAAARKVGKR FSELQPIIQT HQKLEQARED
     QEAASEMASE DKEFAEEAKR LEEEISELEE QLTDLLAPRD PHDGDDIVME IKSGAGGEEA
     ALFAGELARM YQRYAERHGF STEILGLNET DLGGVKDMTL SIRSKQPSRD GAWSEFKFEG
     GVHRVQRIPV TESQGRIQTS AAGVLVYPEP DEVEDVHIDD KDIRVDVYRS SGKGGQGVNT
     TDSAVRITHL PTNIVVTCQK ERSQIQNRAR AMQVLAARLQ QLKEEEAEAE AAEGRAAQIR
     TMDRSERIRT YNFPESRVSD HRIGYKANNL DSVLDGDLEA LLAALKEADR ARRLEAED