ID   RF1_RHOP2               Reviewed;         361 AA.
AC   Q2J423;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   25-MAY-2022, entry version 84.
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=RPB_0075;
OS   Rhodopseudomonas palustris (strain HaA2).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HaA2;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Pelletier D.A.,
RA   Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris HaA2.";
RL   Submitted (JAN-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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABD04787.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000250; ABD04787.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011438977.1; NC_007778.1.
DR   AlphaFoldDB; Q2J423; -.
DR   SMR; Q2J423; -.
DR   STRING; 316058.RPB_0075; -.
DR   PRIDE; Q2J423; -.
DR   EnsemblBacteria; ABD04787; ABD04787; RPB_0075.
DR   KEGG; rpb:RPB_0075; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_5; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000008809; 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..361
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_0000263337"
FT   REGION          286..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..304
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         235
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   361 AA;  39826 MW;  54AF5FF2A0CC62CA CRC64;
     MSNLPEAKLD VLLAHHASLE AQLLGEVAAN DYVRITRELS ELNPLVEAVK AYREVRDELG
     DIDDLLEDPA TDPEMRAMAE AERDALDAHR EDLIQQIRVA LLPKDAMDER NVMLEIRAGT
     GGDEASLFAG DLFRMYEKFA ALQGWSVEVI SASEGTVGGF KEIIAEVKGR GAFAKLKFES
     GVHRVQRVPD TETQGRIHTS AATVAVLPEV EEVDVDIKPD DLKIDTMRAQ GAGGQHVNKT
     ESAIRITHLP TGIVVMMQDS RSQHKNRASA MNILRSRIYD AEQQRIDSAR SAERKQKVGS
     GDRSERIRTY NFPQGRVTDH RINLTLYKLP QVIAGEALGE LIDALTTEHQ VAQLAAQGHA
     A