ID A0A380NFQ9_9FIRM Unreviewed; 361 AA.
AC A0A380NFQ9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
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 ECO:0000313|EMBL:SUP39939.1};
GN ORFNames=NCTC12020_00171 {ECO:0000313|EMBL:SUP39939.1};
OS Veillonella criceti.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Veillonella.
OX NCBI_TaxID=103891 {ECO:0000313|EMBL:SUP39939.1, ECO:0000313|Proteomes:UP000255367};
RN [1] {ECO:0000313|EMBL:SUP39939.1, ECO:0000313|Proteomes:UP000255367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12020 {ECO:0000313|EMBL:SUP39939.1,
RC ECO:0000313|Proteomes:UP000255367};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-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}.
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DR EMBL; UHIO01000001; SUP39939.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A380NFQ9; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000255367; 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 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};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00093}; Reference proteome {ECO:0000313|Proteomes:UP000255367}.
FT DOMAIN 65..180
FT /note="Peptide chain release factor"
FT /evidence="ECO:0000259|SMART:SM00937"
FT COILED 77..104
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 236
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00093"
SQ SEQUENCE 361 AA; 40630 MW; C5F8B78528F860B2 CRC64;
MVLVDKLQVI EDKYMDLEQR ISDPEVIARQ QEWQKLTRQH ASLTETVEAF REYKQVLTGI
DEALEVLEDK TMDEEFREMA QEELKELKER KDELEERLHI LLLPKDPNDE KNVIVEIRGG
AGGDEAALFA GDLFRMYTKY AEAQGWRCEI IDANAPELGG FKEVVFSVDG NSAYSKLKFE
SGVHRVQRVP ETESSGRIHT STVTVAVLPE AEDVDIEIND KDLQIDTYCA SGAGGQHVNR
TESAVRITHK PTGIVVACQD ERSQLKNKDK AMRVLRAKLQ DKAEQEAAAS VAADRKSQVG
TGDRSERIRT YNYPQGRVTD HRINLTLYKL DAVLNGDLDE LIQALIAADQ AAKMQEADQN
A
//
