ID   RF1_ACHLI               Reviewed;         354 AA.
AC   A9NEP7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=ACL_0201;
OS   Acholeplasma laidlawii (strain PG-8A).
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC   Acholeplasma.
OX   NCBI_TaxID=441768;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG-8A;
RX   PubMed=21784942; DOI=10.1128/jb.05059-11;
RA   Lazarev V.N., Levitskii S.A., Basovskii Y.I., Chukin M.M., Akopian T.A.,
RA   Vereshchagin V.V., Kostrjukova E.S., Kovaleva G.Y., Kazanov M.D.,
RA   Malko D.B., Vitreschak A.G., Sernova N.V., Gelfand M.S., Demina I.A.,
RA   Serebryakova M.V., Galyamina M.A., Vtyurin N.N., Rogov S.I., Alexeev D.G.,
RA   Ladygina V.G., Govorun V.M.;
RT   "Complete genome and proteome of Acholeplasma laidlawii.";
RL   J. Bacteriol. 193:4943-4953(2011).
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; CP000896; ABX80827.1; -; Genomic_DNA.
DR   RefSeq; WP_012242158.1; NC_010163.1.
DR   AlphaFoldDB; A9NEP7; -.
DR   SMR; A9NEP7; -.
DR   STRING; 441768.ACL_0201; -.
DR   PRIDE; A9NEP7; -.
DR   EnsemblBacteria; ABX80827; ABX80827; ACL_0201.
DR   GeneID; 66293196; -.
DR   KEGG; acl:ACL_0201; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_14; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000008558; 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..354
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_1000117228"
FT   MOD_RES         231
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   354 AA;  40085 MW;  A90DE0BD3ED785C6 CRC64;
     MFERLEVMRK TYYALQEKLA SGISDVKEIT KLMKELKSLE DAVVAYEKYL SLKEQLKDLE
     ELLELETESS VLEMAKAEEK SLESDIENLE ESLRILLLPK DPDDDKNVII EIKGAAGGDE
     GNIFAGDLFK MYSKYAESMG WKVTLVNTTP GSSGGFAGIE FIISGENAFS YLKHESGVHR
     VQRVPETESQ GRIHTSTAVV LALPEQEDIE YDVKWEDIRF DTYNSSGAGG QSVNTTYSAV
     RLTHIPTNVV VTSQEERSQH ANKDRAYKLL VTRIYDKIQQ EQLEKEGESR KALIGRGNRS
     EKIRTYNYPQ NRVTDHRIGL TINRLDAIME GRIDLIIEPL INEIQKEALE GQSK