ID   RF1_HAES1               Reviewed;         360 AA.
AC   Q0I3B5;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 83.
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=HS_0950;
OS   Haemophilus somnus (strain 129Pt) (Histophilus somni).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=205914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=129Pt;
RX   PubMed=17172329; DOI=10.1128/jb.01422-06;
RA   Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O.,
RA   Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N.,
RA   Xie G., Inzana T.J.;
RT   "Complete genome sequence of Haemophilus somnus (Histophilus somni) strain
RT   129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus
RT   influenzae Rd.";
RL   J. Bacteriol. 189:1890-1898(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; CP000436; ABI25225.1; -; Genomic_DNA.
DR   RefSeq; WP_011609104.1; NC_008309.1.
DR   AlphaFoldDB; Q0I3B5; -.
DR   SMR; Q0I3B5; -.
DR   STRING; 205914.HS_0950; -.
DR   EnsemblBacteria; ABI25225; ABI25225; HS_0950.
DR   KEGG; hso:HS_0950; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_6; -.
DR   OMA; ISDHRVG; -.
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..360
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_0000263283"
FT   REGION          284..312
FT                   /note="Disordered"
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;  40813 MW;  B77A56DB9202D182 CRC64;
     MKASIISKLE SLKERHEELE ALLGEPSVIN DQDKFRAYSK EYAQLEDVVK CFARWNWLNN
     NIEETQLLLD DPDMKEMAEL EIEESKAEIE NAEQQLQILL LPKDPNDEYN AYLEIRAGTG
     GDEAGIFAGD LFRMYSRYAE SKRWRVEVLN ANESEQGGYK EIIVKVNGEG VYGQLKFESG
     GHRVQRVPKT ESQGRIHTSA CTVAVMPELP ENEMPEINPS DLRIDTYRSS GAGGQHVNTT
     DSAVRITHIP TGIVVECQDE RSQHKNKAKA LSVLASRIAQ AEQERQAQAQ ADTRRNLLGS
     GDRSDKIRTY NYPQGRVTDH RINLTVYRLD EVMNGKIDEL IQPIITEYQA DQLAMLSEQN