ID   RF1_ANAD2               Reviewed;         370 AA.
AC   B8JAU2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 64.
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=A2cp1_0396;
OS   Anaeromyxobacter dehalogenans (strain 2CP-1 / ATCC BAA-258).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=455488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-1 / ATCC BAA-258;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Beliaev A.S., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-1.";
RL   Submitted (JAN-2009) 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; CP001359; ACL63753.1; -; Genomic_DNA.
DR   RefSeq; WP_012631807.1; NC_011891.1.
DR   AlphaFoldDB; B8JAU2; -.
DR   SMR; B8JAU2; -.
DR   EnsemblBacteria; ACL63753; ACL63753; A2cp1_0396.
DR   KEGG; acp:A2cp1_0396; -.
DR   HOGENOM; CLU_036856_0_1_7; -.
DR   OMA; ISDHRVG; -.
DR   Proteomes; UP000007089; 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..370
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_1000193466"
FT   REGION          286..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         237
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   370 AA;  41158 MW;  59433F4AEB8F169E CRC64;
     MLSPDVLKKL EAIEQRFEEL TQLLSDPAVA GNGDRFRKVA KERASIEQTV TALRAYRKLL
     EDVEGNEALL ADKDPELREL AKEELAQLRP QVDPAEEQLK LYLVPKDPND EKDVIVEIRA
     GAGGDEAGLF AAEVMRMYVR YAERRGWRVE LMDTSGGALG GVKEATLTVS GDAVYSSLKY
     ESGVHRVQRV PATEAQGRIH TSTVTVAVMP EAEEIDVQVN PADVEMDVFR STGSGGQSVN
     TTDSAVRLTH KPTGIVVKCQ QEKSQLKNRT MAMKMLRAKL FEIEQERQRS ARDATRKSQV
     GTGDRSEKIR TYNFPQDRLT DHRVNYTRHN LPAVMDGDVQ DVIDACRTFY AAQALREASR
     GEAGAAERRA