ID   RF1_MAGSA               Reviewed;         354 AA.
AC   Q2W6V3;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=amb1618;
OS   Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Magnetospirillum.
OX   NCBI_TaxID=342108;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMB-1 / ATCC 700264;
RX   PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA   Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT   "Complete genome sequence of the facultative anaerobic magnetotactic
RT   bacterium Magnetospirillum sp. strain AMB-1.";
RL   DNA Res. 12:157-166(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; AP007255; BAE50422.1; -; Genomic_DNA.
DR   RefSeq; WP_011384027.1; NC_007626.1.
DR   AlphaFoldDB; Q2W6V3; -.
DR   SMR; Q2W6V3; -.
DR   STRING; 342108.amb1618; -.
DR   PRIDE; Q2W6V3; -.
DR   EnsemblBacteria; BAE50422; BAE50422; amb1618.
DR   KEGG; mag:amb1618; -.
DR   HOGENOM; CLU_036856_0_1_5; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000007058; 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..354
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_0000263293"
FT   REGION          283..308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         231
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   354 AA;  39538 MW;  DCE9A96E78D04A34 CRC64;
     MNLETQFDKV LYRHDEVRAQ LSSGEGMDSQ TIQRLSKELS ELDPVVTAVQ AFRKAREDMV
     QAAEMMNDPD MKDLAEEEFY ALKERLPALE REVQIMLLPK DEADEKNAII EVRAGTGGEE
     AALFAAELFR MYERYAGLHG WRFEVMDVND TGIGGVKEAS ATITGRNVFA RLKFESGVHR
     VQRVPATESQ GRIHTSAATV AIMPEAEEVD IQLNDSDLRF DVYRSQGSGG QSVNTTDSAV
     RVTHIPTGLA VACQQEKSQH KNKATALKLL RARLYERERS AKDAERAAAR KSQVGSGDRS
     ERIRTYNFPQ GRVTDHRINM TLYKIDAVMS GDALDELVEA LVAADQAERL AEME