RF1_PYRHO
ID RF1_PYRHO Reviewed; 417 AA.
AC O59264;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Peptide chain release factor subunit 1;
DE AltName: Full=Translation termination factor aRF1;
GN Name=prf1; OrderedLocusNames=PH1584;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
CC -!- FUNCTION: Directs the termination of nascent peptide synthesis
CC (translation) in response to the termination codons UAA, UAG and UGA.
CC {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer of two subunits, one of which binds GTP.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eukaryotic release factor 1 family.
CC {ECO:0000305}.
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DR EMBL; BA000001; BAA30696.1; -; Genomic_DNA.
DR PIR; H71036; H71036.
DR AlphaFoldDB; O59264; -.
DR SMR; O59264; -.
DR STRING; 70601.3258013; -.
DR PRIDE; O59264; -.
DR EnsemblBacteria; BAA30696; BAA30696; BAA30696.
DR KEGG; pho:PH1584; -.
DR eggNOG; arCOG01742; Archaea.
DR OMA; GQEMEVV; -.
DR Proteomes; UP000000752; 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 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.
FT CHAIN 1..417
FT /note="Peptide chain release factor subunit 1"
FT /id="PRO_0000143183"
SQ SEQUENCE 417 AA; 47788 MW; D1FC382530836205 CRC64;
MSKMTRHDAQ LYELKKKIEE LKKIRGRGTE LISLYIPAGY DLSKVMQQLR EEYSTAQNIK
SKTTRKNVLG ALERAMQHLK LYKQTPENGL ALFVGNVSEI EGNTDIRLWA IIPPEPLNVR
LYRCDQTFVT EPLEEMLRVK DAYGLITVEK NEATIGLLRG KRIELLDELT SNVPGKTRAG
GQSARRYERI REQETHEFMK RIGEHANRAF LPLLEKGELK GIIIGGPGPT KEEFVEGEYL
HHELKKKILG VVDISYHGEY GLRELVEKAS DILRDHEVIR EKKLVNEFLK HVVKDTGLAT
YGEREVRRAL EIGAVDVLLI SEGYNKVRVR VKCNHCGWEE LKTMSEEEYE VYRKKITKCP
KCGSQNLTIE KWDVAEELIK MAEEAGSDVE IISLDTEEGQ QFYRAFGGLG AILRFKI