ID   RF1_MICAN               Reviewed;         366 AA.
AC   B0JYC5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=MAE_53410;
OS   Microcystis aeruginosa (strain NIES-843 / IAM M-2473).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Microcystaceae; Microcystis.
OX   NCBI_TaxID=449447;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-843 / IAM M-247;
RX   PubMed=18192279; DOI=10.1093/dnares/dsm026;
RA   Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M.,
RA   Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A.,
RA   Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M.,
RA   Nakazaki N., Nakayama S., Yamada M., Tabata S., Watanabe M.M.;
RT   "Complete genomic structure of the bloom-forming toxic cyanobacterium
RT   Microcystis aeruginosa NIES-843.";
RL   DNA Res. 14:247-256(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; AP009552; BAG05163.1; -; Genomic_DNA.
DR   RefSeq; WP_002796124.1; NC_010296.1.
DR   AlphaFoldDB; B0JYC5; -.
DR   SMR; B0JYC5; -.
DR   STRING; 449447.MAE_53410; -.
DR   PaxDb; B0JYC5; -.
DR   EnsemblBacteria; BAG05163; BAG05163; MAE_53410.
DR   KEGG; mar:MAE_53410; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_3; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
DR   BioCyc; MAER449447:MAE_RS23220-MON; -.
DR   Proteomes; UP000001510; 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..366
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_1000075503"
FT   MOD_RES         239
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   366 AA;  41132 MW;  E2EBAB87D5818672 CRC64;
     MAESYLLDKL QSVEQTYKEL TRRLADPDVT GNPGELHRLA KSRASLEETV NTYEIWQKSQ
     EDLIGAKQIF KESASDPELR EMAALEVAEL EEKIATLEDQ LTILLLPRDP LDEKNIMLEI
     RAGTGGDEAS IWAGDLVRLY SKYAETQNWK VSLLSESQAD MGGFKEAILE IKGDNVYSKL
     KFEAGVHRVQ RVPLTEASGR VHTSTATVAI MPEVDDVEVH IDPKDIELTT ARSGGAGGQN
     VNKVETAVDL IHKPTGIRVF CTEERSQLQN RERAMQILRA KLYDMKLQEQ QEAVSSMRRS
     QVGTGSRSEK IRTYNYKDNR LTDHRLNQNF SLDRILDGDI EEVIQSCIAK DQQEKLAELA
     AAQETA