ID   RF1_PROM5               Reviewed;         364 AA.
AC   A2BYQ7;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=P9515_17111;
OS   Prochlorococcus marinus (strain MIT 9515).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167542;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9515;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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; CP000552; ABM72918.1; -; Genomic_DNA.
DR   RefSeq; WP_011821010.1; NC_008817.1.
DR   AlphaFoldDB; A2BYQ7; -.
DR   SMR; A2BYQ7; -.
DR   STRING; 167542.P9515_17111; -.
DR   PRIDE; A2BYQ7; -.
DR   EnsemblBacteria; ABM72918; ABM72918; P9515_17111.
DR   KEGG; pmc:P9515_17111; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_3; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000001589; 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..364
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_1000093489"
FT   MOD_RES         239
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   364 AA;  40956 MW;  F803C73645AB0407 CRC64;
     MEYTTLIARL KTASKSFVNL EMQLADPDIA NNPKKLELIA KERAKLEPLV LDFNQLLDTD
     KEIDDSRQLL KDNRNDKDME LLINEELCNL EVLKNSLIQK VTIALLPKDP RDERSVMLEI
     RAGAGGNEAC IWAGDLARMY ERYGQKIGWS VKPISASESD MGGFKELVIS IKGDSVYSQL
     KFEAGVHRVQ RVPATESQGR VHTSTATVAV MPEADPVEVK IDPSDLEIGT ARSGGAGGQN
     VNKVETAIDL IHKPTGIRVF CTQERSQLQN RERAMEILRA KLYEIQLKEA NDKERSQRLM
     QVGTGDRSEK IRTYNFKDNR TTDHRLGSNF ALEPILAGQL DEVIDACIAQ EQKRIMEDFN
     ENEN