ID   RF1_SYNJA               Reviewed;         361 AA.
AC   Q2JUK1;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 85.
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=CYA_1445;
OS   Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone
OS   A-Prime).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=321327;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA-3-3Ab;
RX   PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA   Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N.,
RA   Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT   "Population level functional diversity in a microbial community revealed by
RT   comparative genomic and metagenomic analyses.";
RL   ISME J. 1:703-713(2007).
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; CP000239; ABC99613.1; -; Genomic_DNA.
DR   RefSeq; WP_011430291.1; NC_007775.1.
DR   AlphaFoldDB; Q2JUK1; -.
DR   SMR; Q2JUK1; -.
DR   STRING; 321327.CYA_1445; -.
DR   EnsemblBacteria; ABC99613; ABC99613; CYA_1445.
DR   KEGG; cya:CYA_1445; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_3; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000008818; 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.
FT   CHAIN           1..361
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_0000263377"
FT   MOD_RES         240
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   361 AA;  40841 MW;  5ECDCA6004A0B839 CRC64;
     MASAQLIEQL KNVEATFQEL TVRLADPDVA TDPAELQRIA KARSSLEATV QTFHEWQKLT
     RELKQTEELL REVASDDPEL EAMARAELEQ LRVRQEQLEE KLTLLLLPRD PNDEKNIMLE
     IRAGTGGEEA ALWAADLARM YTRYAEKMGW SVRLASLSEG EMGGYKEAIL EIRGDQVYSK
     LKFEAGVHRV QRVPVTEAQG RVHTSTATVA VMPEVDEVEV VIDPKDIEIK TARSGGAGGQ
     NVNKVETAVD LLHKPTGIRV FCTEERSQLQ NRQRAMQILR AKLYEMKLQE QQASISSARR
     MQVGTGSRSE KIRTYNYKDN RVTDHRLNQN FLLEPILEGE LDELIQACIG LYQKELLAEL
     S