ID   RF1_CYAP4               Reviewed;         364 AA.
AC   B8HXV0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 65.
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=Cyan7425_1003;
OS   Cyanothece sp. (strain PCC 7425 / ATCC 29141).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Cyanothecaceae; Cyanothece; unclassified Cyanothece.
OX   NCBI_TaxID=395961;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7425 / ATCC 29141;
RX   PubMed=21972240; DOI=10.1128/mbio.00214-11;
RA   Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA   Sherman L.A., Pakrasi H.B.;
RT   "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT   unicellular nitrogen-fixing Cyanobacteria.";
RL   MBio 2:E214-E214(2011).
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; CP001344; ACL43389.1; -; Genomic_DNA.
DR   RefSeq; WP_012626487.1; NC_011884.1.
DR   AlphaFoldDB; B8HXV0; -.
DR   SMR; B8HXV0; -.
DR   STRING; 395961.Cyan7425_1003; -.
DR   PRIDE; B8HXV0; -.
DR   EnsemblBacteria; ACL43389; ACL43389; Cyan7425_1003.
DR   KEGG; cyn:Cyan7425_1003; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_3; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
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..364
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_1000193484"
FT   REGION          291..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        291..310
FT                   /note="Polar 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;  41063 MW;  C994D691A7BA1344 CRC64;
     MAESYLLDKL KSVELTFHEL TRRLADPEVA TDPEEFQRVA KARASLEETV DTYDTWKTVQ
     QHLAEARQIA REAASDPELQ EMAVQEVNEL TEKSAHLEQR LKILLLPRDP NDDKNIMLEI
     RAGTGGDEAS IWAGDLVRLY SRYAESQRWR VKLVSESLGE MGGFKEAILE IQGEQVYSKL
     KYEAGVHRVQ RVPATEASGR VHTSTATVAI MPEVDEVEVK IDPKDIELTT ARSGGAGGQN
     VNKVETAVDL FHKPTGIRIF CTEERSQLQN KERAMQILRA KLYEMKLQEQ QSEITSRRRS
     QVGTGSRSEK IRTYNYKDNR ATDHRLGQNF PLNQVLEGDI EGIIQACITQ DQQEQLAELA
     AATA