RF1_PICTO
ID RF1_PICTO Reviewed; 410 AA.
AC Q6KZ24;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 90.
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=PTO1443;
OS Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS 100828).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Picrophilaceae; Picrophilus.
OX NCBI_TaxID=263820;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA Schepers B., Dock C., Antranikian G., Liebl W.;
RT "Genome sequence of Picrophilus torridus and its implications for life
RT around pH 0.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(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; AE017261; AAT44028.1; -; Genomic_DNA.
DR RefSeq; WP_011178244.1; NC_005877.1.
DR AlphaFoldDB; Q6KZ24; -.
DR SMR; Q6KZ24; -.
DR STRING; 263820.PTO1443; -.
DR EnsemblBacteria; AAT44028; AAT44028; PTO1443.
DR GeneID; 2844849; -.
DR KEGG; pto:PTO1443; -.
DR PATRIC; fig|263820.9.peg.1497; -.
DR eggNOG; arCOG01742; Archaea.
DR HOGENOM; CLU_035759_3_0_2; -.
DR OMA; GQEMEVV; -.
DR OrthoDB; 32191at2157; -.
DR Proteomes; UP000000438; 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; Reference proteome.
FT CHAIN 1..410
FT /note="Peptide chain release factor subunit 1"
FT /id="PRO_0000143179"
SQ SEQUENCE 410 AA; 46903 MW; 4C38702AB6FE83C0 CRC64;
MESEDYKRYE FKKALEELKD LHGRGTELIS LYIPPDKQIS DVVQYLREEY STSSNIKSKS
TRKNVLAAIE SIMSRLKYYK QPPETGLVFF VGHIATRGDQ TEMYTKIIEP PEPIQTFMYK
CDSNFHLEQL ESQLKEKDIY GLIVIDRKEA TVGFLKGTRI EVVDYEQSLV PSKHHQGGQS
SRRFERLIEI AANDFFKKIG EIANNAFMPL IKDINAVFIG GPGATKEYFL EKDYLRNEIK
QKVKDLFDIG YTDESGLREL VEKASESIKD MKISREKDII NRFLREIKKP EGGLGVYGED
AIINALKSKN LDLLIISDTL KKRRYTYKCP VCNDTKTFTE KPRETPLCDK DNSEMELVDE
DDLVEDLYKL ADEAGTNVVF VSEDSDEGRL IKTAFGGLAG IMRYVPAIAP