ID   RF1_SYNR3               Reviewed;         364 AA.
AC   A5GVY9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 73.
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};
GN   OrderedLocusNames=SynRCC307_2145;
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=316278;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307;
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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; CT978603; CAK29048.1; -; Genomic_DNA.
DR   RefSeq; WP_011936559.1; NC_009482.1.
DR   AlphaFoldDB; A5GVY9; -.
DR   SMR; A5GVY9; -.
DR   STRING; 316278.SynRCC307_2145; -.
DR   EnsemblBacteria; CAK29048; CAK29048; SynRCC307_2145.
DR   KEGG; syr:SynRCC307_2145; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_3; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000001115; 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..364
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_1000004963"
FT   REGION          292..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        303..326
FT                   /note="Basic and acidic residues"
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   364 AA;  40357 MW;  C277A99397377D6F CRC64;
     MDQSFVTERL EATCRTFNAL ERQLADPSVA ADPEQLLTLA KERSRLEPLV LDYQRLQQLH
     AEHQQAQQLL KESKGDAELE ALAQEELQQL SSEQEQLNQR LKVALLPSDP RDERSVMLEI
     RAGAGGDEAC LWAGDLARMY ERHAQTCGWQ VNPVSASEAE LGGFKELILA IRGDAVFSQL
     KYEAGVHRVQ RVPATESQGR VHTSTATVAV MPEADPVDVQ IDPKDLDIST ARSGGAGGQN
     VNKVETAVDL LHKPTGIRVF CTQERSQLQN RERAMEILRA KLLAKEEEEA AAAESSARRA
     QVGSGDRSEK IRTYNYKDNR TTDHRLGKNF PLETVLNGQL SDLIEACTHA DQQQKLEELA
     ASES