ID A0A401XJT4_9FLAO Unreviewed; 364 AA.
AC A0A401XJT4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 18-JUN-2025, entry version 21.
DE RecName: Full=Peptide chain release factor 1 {ECO:0000256|HAMAP-Rule:MF_00093, ECO:0000256|NCBIfam:TIGR00019};
DE Short=RF-1 {ECO:0000256|HAMAP-Rule:MF_00093};
GN Name=prfA {ECO:0000256|HAMAP-Rule:MF_00093,
GN ECO:0000313|EMBL:GCD77276.1};
GN ORFNames=JCM31826_07580 {ECO:0000313|EMBL:GCD77276.1};
OS Thermaurantimonas aggregans.
OC Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Schleiferiaceae; Thermaurantimonas.
OX NCBI_TaxID=2173829 {ECO:0000313|EMBL:GCD77276.1, ECO:0000313|Proteomes:UP000286715};
RN [1] {ECO:0000313|EMBL:GCD77276.1, ECO:0000313|Proteomes:UP000286715}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LA {ECO:0000313|EMBL:GCD77276.1,
RC ECO:0000313|Proteomes:UP000286715};
RA Iino T., Ohkuma M., Haruta S.;
RT "Schleiferia aggregans sp. nov., a moderately thermophilic heterotrophic
RT bacterium isolated from microbial mats at a terrestrial hot spring.";
RL Submitted (NOV-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCD77276.1}.
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DR EMBL; BHZE01000005; GCD77276.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401XJT4; -.
DR Proteomes; UP000286715; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016149; F:translation release factor activity, codon specific; IEA:UniProtKB-UniRule.
DR FunFam; 3.30.160.20:FF:000004; Peptide chain release factor 1; 1.
DR FunFam; 3.30.70.1660:FF:000002; Peptide chain release factor 1; 1.
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; IPR050057; Prokaryotic/Mito_RF.
DR InterPro; IPR004373; RF-1.
DR NCBIfam; TIGR00019; prfA; 1.
DR NCBIfam; NF001859; PRK00591.1; 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.
DR PROSITE; PS00745; RF_PROK_I; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00093};
KW Methylation {ECO:0000256|ARBA:ARBA00022481, ECO:0000256|HAMAP-
KW Rule:MF_00093};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00093}; Reference proteome {ECO:0000313|Proteomes:UP000286715}.
FT DOMAIN 233..249
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT MOD_RES 240
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00093"
SQ SEQUENCE 364 AA; 41456 MW; DA89BA877C4969F4 CRC64;
MLKEMDSLIE KIEALELKFQ DVADQIVQPH IIADQKKYVA LNREYKELEA IVEKGKQFKN
LYNSIQEAKE ILKTEKDPEL REIALAEIEE GEPRLEQLRE EIRLLLLPKD PEDARGCTME
IRAGTGGDEA AIFAGDLFRM YSKYCEKRGW KVEVLDYNEG TSGGYKEIIF KVNGEGAYGV
LKYESGVHRV QRVPQTETQG RIHTSAATVA VLPEADEISF ELNPADVEMQ TARSGGAGGQ
NVNKVETKVM LTHRPTGIVV TCQVERSQHA NRERAMQMLR DKLFEIEYTK RMEEVASKRK
TMVSTGDRSA KIRTYNYPQS RVTDHRIGLT VYNLDEIMNG DLFKFSEELE LAENAERLKE
SAEV
//