ID A0A0X1KQV5_9THEM Unreviewed; 350 AA.
AC A0A0X1KQV5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Peptide chain release factor 1 {ECO:0000256|HAMAP-Rule:MF_00093};
DE Short=RF-1 {ECO:0000256|HAMAP-Rule:MF_00093};
GN Name=prfA {ECO:0000256|HAMAP-Rule:MF_00093};
GN ORFNames=AJ81_04640 {ECO:0000313|EMBL:AJC73611.1};
OS Pseudothermotoga hypogea DSM 11164 = NBRC 106472.
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC Pseudothermotoga.
OX NCBI_TaxID=1123384 {ECO:0000313|EMBL:AJC73611.1, ECO:0000313|Proteomes:UP000077469};
RN [1] {ECO:0000313|EMBL:AJC73611.1, ECO:0000313|Proteomes:UP000077469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11164 {ECO:0000313|EMBL:AJC73611.1,
RC ECO:0000313|Proteomes:UP000077469};
RA Zhang X., Alvare G., Fristensky B., Chen L., Suen T., Chen Q., Ma K.;
RT "Genome sequencing of Thermotog hypogea.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00002986, ECO:0000256|HAMAP-Rule:MF_00093}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00093}.
CC -!- PTM: Methylated by PrmC. Methylation increases the termination
CC efficiency of RF1. {ECO:0000256|HAMAP-Rule:MF_00093}.
CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC family. {ECO:0000256|ARBA:ARBA00010835, ECO:0000256|HAMAP-
CC Rule:MF_00093}.
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DR EMBL; CP007141; AJC73611.1; -; Genomic_DNA.
DR RefSeq; WP_031504845.1; NZ_JONI01000007.1.
DR AlphaFoldDB; A0A0X1KQV5; -.
DR STRING; 1123384.AJ81_04640; -.
DR PaxDb; 1123384-AJ81_04640; -.
DR KEGG; phy:AJ81_04640; -.
DR PATRIC; fig|1123384.7.peg.910; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000077469; 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; 3.30.160.20; -; 1.
DR Gene3D; 3.30.70.1660; -; 1.
DR Gene3D; 6.10.140.1950; -; 1.
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 NCBIfam; TIGR00019; prfA; 1.
DR PANTHER; PTHR43804; LD18447P; 1.
DR PANTHER; PTHR43804:SF7; LD18447P; 1.
DR Pfam; PF03462; PCRF; 1.
DR Pfam; PF00472; RF-1; 1.
DR SMART; SM00937; PCRF; 1.
DR SUPFAM; SSF75620; Release factor; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00093};
KW Methylation {ECO:0000256|ARBA:ARBA00022481, ECO:0000256|HAMAP-
KW Rule:MF_00093}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00093};
KW Reference proteome {ECO:0000313|Proteomes:UP000077469}.
FT DOMAIN 65..171
FT /note="Peptide chain release factor"
FT /evidence="ECO:0000259|SMART:SM00937"
FT COILED 2..94
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 227
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00093"
SQ SEQUENCE 350 AA; 40282 MW; 977811953D77DBF4 CRC64;
MKELVKSLVE KAKERLQELQ IELARADIDV EEMKRLSIEY SKLEEIVQLH EGLEELERDI
EFWQQVIAED PSAEKELAET KQEHEQKLSQ LISLLLPSDD YDSIIMEIRA GTGGEEAALF
AADLYRMYSR YAERKGWEVE LADFHDTGLG GFKEVVLFVR GKSVYKHLKW ESGVHRVQRI
PITESSGRIH TSTATVAILP EVTTVEVQID PKDLEIDTFK ASGHGGQYVN KTESAVRITH
LPTGITVSCQ SERSQHQNRE KALAILRAKL FQLKQEELMQ KISQQRKSQI KTAERSEKIR
TYNFPQNRVT DHRIDYTSYR LKEILDGDLD ELVSKLLEFE LAETAKRILS
//
