ID   RF1_PARMW               Reviewed;         365 AA.
AC   Q7U4H2;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 104.
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}; Synonyms=sueB;
GN   OrderedLocusNames=SYNW2096;
OS   Parasynechococcus marenigrum (strain WH8102).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Parasynechococcus; Parasynechococcus marenigrum.
OX   NCBI_TaxID=84588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH8102;
RX   PubMed=12917641; DOI=10.1038/nature01943;
RA   Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P.,
RA   Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T.,
RA   Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT   "The genome of a motile marine Synechococcus.";
RL   Nature 424:1037-1042(2003).
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; BX569694; CAE08611.1; -; Genomic_DNA.
DR   RefSeq; WP_011128953.1; NC_005070.1.
DR   AlphaFoldDB; Q7U4H2; -.
DR   SMR; Q7U4H2; -.
DR   STRING; 84588.SYNW2096; -.
DR   EnsemblBacteria; CAE08611; CAE08611; SYNW2096.
DR   KEGG; syw:SYNW2096; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_3; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000001422; 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..365
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_0000177759"
FT   REGION          289..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         239
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   365 AA;  40738 MW;  449B0AE015192C85 CRC64;
     MDASTLLARL EAATASFRNL ERQLADPDVA ADPTRLEKIA RERARLEPLV LDFEELQVLE
     GEQKQSRELL KECRGDAAME ELAQDDLASL NRRHAELTEK LTVALLPRDP RDERSVMLEI
     RAGAGGDEAC IWAGDLARMY ERYSQKLGWN VQPISSNEAD LGGFRELILS VKGDSVFSQL
     KFEAGVHRVQ RVPATESQGR VHTSTATVAV MPEADAVEVQ LDPKDLEIST ARSGGAGGQN
     VNKVETAVDL LHKPSGIRVF CTQERSQLQN RERALEILRA KLLEQEQREA AARESSDRRA
     QVGSGDRSEK IRTYNYKDNR TTDHRLGRNF SLDPVLDGQL EDLIGACIAE EQRQKLEALS
     QQNED