ID   RF1_GLAP5               Reviewed;         360 AA.
AC   B8F526;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 67.
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=HAPS_0792;
OS   Glaesserella parasuis serovar 5 (strain SH0165) (Haemophilus parasuis).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Glaesserella.
OX   NCBI_TaxID=557723;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH0165;
RX   PubMed=19074396; DOI=10.1128/jb.01682-08;
RA   Yue M., Yang F., Yang J., Bei W., Cai X., Chen L., Dong J., Zhou R.,
RA   Jin M., Jin Q., Chen H.;
RT   "Complete genome sequence of Haemophilus parasuis SH0165.";
RL   J. Bacteriol. 191:1359-1360(2009).
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; CP001321; ACL32428.1; -; Genomic_DNA.
DR   RefSeq; WP_005713004.1; NC_011852.1.
DR   AlphaFoldDB; B8F526; -.
DR   SMR; B8F526; -.
DR   STRING; 557723.HAPS_0792; -.
DR   EnsemblBacteria; ACL32428; ACL32428; HAPS_0792.
DR   GeneID; 66619089; -.
DR   KEGG; hap:HAPS_0792; -.
DR   HOGENOM; CLU_036856_0_1_6; -.
DR   OMA; ISDHRVG; -.
DR   Proteomes; UP000006743; 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..360
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_1000193491"
FT   REGION          285..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        285..302
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   360 AA;  40598 MW;  7F54792E1A1899AF CRC64;
     MKASIINKLD SLSERHEELQ ALLGDATIIS DQEKFCAYSK EYSQLEEVVS TFNRWKKLHS
     DIEEAQILLD DPDMKEIAAE EIEANKAEIE QLEQNLQILL LPKDPNDEYN CFLEIRAGTG
     GDEAGIFAGD LYRMYSRYAE SKRWRIEELS ANESEQGGYK EIIVKISGEG VYGQLKFESG
     GHRVQRVPKT ESQGRIHTSA CTVAVMPELP ESEMPEINPA DLRIDTYRSS GAGGQHVNTT
     DSAVRITHIP TGIVVECQDE RSQHKNKAKA LAVLASRIVQ VEKEKQAQEQ ADTRRNLLGS
     GDRSDKIRTY NYPQGRVTDH RINLTVYRLD EVMNGKIDEL IQPIITEYQA DQLAALSDQN