ID   RF1_MAGMM               Reviewed;         361 AA.
AC   A0LDT7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=Mmc1_3645;
OS   Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Magnetococcales;
OC   Magnetococcaceae; Magnetococcus.
OX   NCBI_TaxID=156889;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1;
RX   PubMed=19465526; DOI=10.1128/aem.02874-08;
RA   Schubbe S., Williams T.J., Xie G., Kiss H.E., Brettin T.S., Martinez D.,
RA   Ross C.A., Schuler D., Cox B.L., Nealson K.H., Bazylinski D.A.;
RT   "Complete genome sequence of the chemolithoautotrophic marine magnetotactic
RT   coccus strain MC-1.";
RL   Appl. Environ. Microbiol. 75:4835-4852(2009).
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; CP000471; ABK46130.1; -; Genomic_DNA.
DR   RefSeq; WP_011715183.1; NC_008576.1.
DR   AlphaFoldDB; A0LDT7; -.
DR   SMR; A0LDT7; -.
DR   STRING; 156889.Mmc1_3645; -.
DR   EnsemblBacteria; ABK46130; ABK46130; Mmc1_3645.
DR   KEGG; mgm:Mmc1_3645; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_5; -.
DR   OMA; ISDHRVG; -.
DR   Proteomes; UP000002586; 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..361
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_1000117244"
FT   REGION          286..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         236
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   361 AA;  39806 MW;  81AED217F92F2113 CRC64;
     MAIEEKLESL TSRHAELSAH LADPTTVSDS KRFAAYSKEF SDLEPVVAAW QAHLAILQQL
     AETDEMLAEA GDDAEMRQMA REERETLKNK LEQSQKHLHL MLLPKDPNDD KNVILEIRAG
     TGGEEAALFV SDLFRMYGRF AEIKGWRIEM LSSSATDLGG YKELIAMVQG KGAYMGLKYE
     SGVHRVQRIP VTETGGRIHT SAVTVAILPE ADEVELHIED KDLRIDVYRS SGPGGQSVNT
     TDSAVRITHL PTGLVVICQD EKSQHKNKAK AMKVLQARLL DAQQQAADSQ RAEARKGQVG
     SGDRSERIRT YNFPQSRVTD HRINLTLHKL DQVLQGGLAE VVDALTAHDQ ASKLAHLGGG
     D