ID   RF1_RHOBA               Reviewed;         360 AA.
AC   Q7ULT3;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 97.
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=RB9305;
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=243090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX   PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA   Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA   Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA   Reinhardt R.;
RT   "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT   1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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; BX294149; CAD76186.1; -; Genomic_DNA.
DR   RefSeq; NP_868809.1; NC_005027.1.
DR   RefSeq; WP_007328933.1; NC_005027.1.
DR   AlphaFoldDB; Q7ULT3; -.
DR   SMR; Q7ULT3; -.
DR   STRING; 243090.RB9305; -.
DR   PRIDE; Q7ULT3; -.
DR   EnsemblBacteria; CAD76186; CAD76186; RB9305.
DR   KEGG; rba:RB9305; -.
DR   PATRIC; fig|243090.15.peg.4458; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_0; -.
DR   InParanoid; Q7ULT3; -.
DR   OMA; CHQDTRM; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000001025; 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.
PE   3: Inferred from homology;
KW   Cytoplasm; Methylation; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..360
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_0000263334"
FT   MOD_RES         237
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   360 AA;  40795 MW;  10FE0AFF0F91D194 CRC64;
     MSGSIRDILE EKLARFEKLE NDMSDPEVLS DGARMSATAR EHGGLNRLAN QYRTFKRLTD
     EIHQCVAMVA DAEDVDEREM AESEMESLRK ERETVWEDLL SLTVGGEDSH RTRCVMEIRA
     GTGGDEAALF ARDLFEMYTR YAEKVGWKTE LMDASPTEMG GFKDVTLTLE GDNVFRDLQY
     ESGGHRVQRV PETETQGRVH TSAATVAVMP EPEDVEIDLK PDDYRKDFFG ASGPGGQHVN
     KTDSAVRLTH HETGIVVQCQ DEKSQHKNLA KALRVLKARI YEKKREEEAA KQAEARKGLI
     GSGDRSQRIR TYNFPQNRLT DHRINLTIYK LDQIIAGDLN PVTEALIEYD RDQLRGDMID