ID   RF1_NITSB               Reviewed;         354 AA.
AC   A6Q162;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 76.
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=NIS_0104;
OS   Nitratiruptor sp. (strain SB155-2).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Nautiliales;
OC   Nitratiruptoraceae; Nitratiruptor; unclassified Nitratiruptor.
OX   NCBI_TaxID=387092;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB155-2;
RX   PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA   Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA   Horikoshi K.;
RT   "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT   emergence of pathogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(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; AP009178; BAF69221.1; -; Genomic_DNA.
DR   RefSeq; WP_011979647.1; NC_009662.1.
DR   AlphaFoldDB; A6Q162; -.
DR   SMR; A6Q162; -.
DR   STRING; 387092.NIS_0104; -.
DR   EnsemblBacteria; BAF69221; BAF69221; NIS_0104.
DR   KEGG; nis:NIS_0104; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_7; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000001118; 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..354
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_1000004922"
FT   REGION          284..308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        284..299
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         231
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   354 AA;  40360 MW;  8CBE6124291CAC53 CRC64;
     MLKEKLHPFI QRYNEINELL SSPEITQDIK KMTALSKEQS EIEPIVEKAK EYMNILEAIE
     ENRSLIEDEE LGELAKEELK ELEPKKEQLE EEIKVLLISK DPNDEKDIYL EIRAGTGGEE
     AALFASDLFK AYARYAEKKG WRVEIVSSSE SDSGGYKEII AKIKGQGVYS RLKYEAGTHR
     VQRVPETESQ GRIHTSAVTV AIMPEVDDVD VEINPNDLKI DVYRSSGHGG QSVNTTDSAV
     RITHIPTGIV VAMQDEKSQH KNKEKALKIL KARIFEKRMR EQQEALAKDR KEQVGSGDRS
     ERIRTYNFPQ NRVTDHRIGL TLYKLEEVMQ GDLDQIIEPL IAHYQAQKIQ EAGL