ID   RF1_DESAL               Reviewed;         355 AA.
AC   B8FEA2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 64.
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=Dalk_5213;
OS   Desulfatibacillum aliphaticivorans.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Desulfatibacillum.
OX   NCBI_TaxID=218208;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK-01;
RX   PubMed=21651686; DOI=10.1111/j.1462-2920.2011.02516.x;
RA   Callaghan A.V., Morris B.E., Pereira I.A., McInerney M.J., Austin R.N.,
RA   Groves J.T., Kukor J.J., Suflita J.M., Young L.Y., Zylstra G.J., Wawrik B.;
RT   "The genome sequence of Desulfatibacillum alkenivorans AK-01: a blueprint
RT   for anaerobic alkane oxidation.";
RL   Environ. Microbiol. 14:101-113(2012).
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; CP001322; ACL06883.1; -; Genomic_DNA.
DR   RefSeq; WP_015949919.1; NC_011768.1.
DR   AlphaFoldDB; B8FEA2; -.
DR   SMR; B8FEA2; -.
DR   EnsemblBacteria; ACL06883; ACL06883; Dalk_5213.
DR   KEGG; dal:Dalk_5213; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_7; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000000739; 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..355
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_1000117234"
FT   REGION          282..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         232
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   355 AA;  39694 MW;  509372549C9414FC CRC64;
     MLDRLEGVEQ RFLEVESLLS DPKIVGDQKV YQKYVREHAD LSKVVEAYRE YKQVLEGLEE
     SKELLKDPDP DIKDLAKEEI DRLDKEQVRL EDELKILLLP KDPNDDKNVI LEIRAGTGGD
     EAGLFAADLF RMYSRYAETR GWKVETLSEH LTGVGGIKEI AAMITGQGVY SAFKFESGTH
     RVQRVPVTEA QGRIHTSACT VAVLPEAEEV DIQIDPSEIR VDVYRSQGAG GQHVNTTDSA
     VRLTHLPTGV VVTCQDEKSQ HKNKAKAMKV LRARLLDHAV QEQNASISAE RKSQVGSGDR
     SERIRTYNYP QGRVTDHRIG LTLYKLESIM AGQISEIVDA LTTHYNAEAL QEGGL