ID   RF1_HALMA               Reviewed;         418 AA.
AC   Q5UXY3;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Peptide chain release factor subunit 1 {ECO:0000255|HAMAP-Rule:MF_00424};
DE   AltName: Full=Translation termination factor aRF1 {ECO:0000255|HAMAP-Rule:MF_00424};
GN   Name=prf1 {ECO:0000255|HAMAP-Rule:MF_00424}; OrderedLocusNames=rrnAC3164;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=272569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=15520287; DOI=10.1101/gr.2700304;
RA   Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA   Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA   Hood L., Ng W.V.;
RT   "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT   Dead Sea.";
RL   Genome Res. 14:2221-2234(2004).
CC   -!- FUNCTION: Directs the termination of nascent peptide synthesis
CC       (translation) in response to the termination codons UAA, UAG and UGA.
CC       {ECO:0000255|HAMAP-Rule:MF_00424}.
CC   -!- SUBUNIT: Heterodimer of two subunits, one of which binds GTP.
CC       {ECO:0000255|HAMAP-Rule:MF_00424}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00424}.
CC   -!- SIMILARITY: Belongs to the eukaryotic release factor 1 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00424}.
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DR   EMBL; AY596297; AAV47870.1; -; Genomic_DNA.
DR   RefSeq; WP_011224646.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q5UXY3; -.
DR   SMR; Q5UXY3; -.
DR   STRING; 272569.rrnAC3164; -.
DR   EnsemblBacteria; AAV47870; AAV47870; rrnAC3164.
DR   GeneID; 40153972; -.
DR   KEGG; hma:rrnAC3164; -.
DR   PATRIC; fig|272569.17.peg.3704; -.
DR   eggNOG; arCOG01742; Archaea.
DR   HOGENOM; CLU_035759_3_0_2; -.
DR   OMA; GQEMEVV; -.
DR   Proteomes; UP000001169; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016149; F:translation release factor activity, codon specific; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1330.30; -; 1.
DR   Gene3D; 3.30.420.60; -; 1.
DR   Gene3D; 3.30.960.10; -; 1.
DR   HAMAP; MF_00424; Rel_fact_arch_1; 1.
DR   InterPro; IPR042226; eFR1_2_sf.
DR   InterPro; IPR005140; eRF1_1_Pelota.
DR   InterPro; IPR024049; eRF1_1_sf.
DR   InterPro; IPR005141; eRF1_2.
DR   InterPro; IPR005142; eRF1_3.
DR   InterPro; IPR029064; L30e-like.
DR   InterPro; IPR020918; Peptide_chain-rel_aRF1.
DR   InterPro; IPR004403; Peptide_chain-rel_eRF1/aRF1.
DR   PANTHER; PTHR10113; PTHR10113; 1.
DR   Pfam; PF03463; eRF1_1; 1.
DR   Pfam; PF03464; eRF1_2; 1.
DR   Pfam; PF03465; eRF1_3; 1.
DR   SMART; SM01194; eRF1_1; 1.
DR   SUPFAM; SSF55315; SSF55315; 1.
DR   SUPFAM; SSF55481; SSF55481; 1.
DR   TIGRFAMs; TIGR03676; aRF1/eRF1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..418
FT                   /note="Peptide chain release factor subunit 1"
FT                   /id="PRO_0000143170"
SQ   SEQUENCE   418 AA;  46641 MW;  0F9A77B9817455A6 CRC64;
     MSEQQEQEQS DKQKYEFRKV IEELKGYQGS GTQLVSIYIP EGKLISDVVA HVTQEHSEAS
     NIKSKDTRTA VQDALTSIKD RLRYYDVRPP DNGLVVFSGA FDTGGGRTDM VTKVLESPPD
     PIESFRYHCD SEFLTEPLEH MLADKGLFGL IVLDRREANV GWLKGKRVEP VKSASSLVPG
     KQRKGGQSAQ RFARLRLEAI DNFYQEVAGM ANDLFVADRH EIDGILVGGP SPTKDEFLDG
     DYLHHELQDM VLGKFDVAYT DESGLYDLVD AADDVLAEHE MLRDKELMED FFKQLHNGDK
     ATYGFDQTRQ NLNMGAVEQL LISEDLRKDV VAYTCENGHD EYDLINSSAG TDDHECSRCG
     ATVDADDGER EDAIDHLMEL ADQRGTETVF ISTDFEKGEQ LLTAFGGVAG LLRYSTGV