ID A0A2P2BRI5_9FIRM Unreviewed; 354 AA.
AC A0A2P2BRI5;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=FRIFI_0050 {ECO:0000313|EMBL:CEI71604.1};
OS Romboutsia hominis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Romboutsia.
OX NCBI_TaxID=1507512 {ECO:0000313|EMBL:CEI71604.1, ECO:0000313|Proteomes:UP000245695};
RN [1] {ECO:0000313|EMBL:CEI71604.1, ECO:0000313|Proteomes:UP000245695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FRIFI {ECO:0000313|EMBL:CEI71604.1,
RC ECO:0000313|Proteomes:UP000245695};
RA Hornung B.V.;
RL Submitted (SEP-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; LN650648; CEI71604.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P2BRI5; -.
DR Proteomes; UP000245695; Chromosome Chromosome1.
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; -; 2.
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.
DR PROSITE; PS00745; RF_PROK_I; 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:UP000245695}.
FT DOMAIN 226..242
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT COILED 62..94
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 233
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00093"
SQ SEQUENCE 354 AA; 39939 MW; 013309529E65BCB9 CRC64;
MLKKLDVLED KYKDLTEKIS DPEIINDQKT WQKYMKEHSD LEPIVMKYRE YKNVLTSIAD
SKEILQEESD EELRDLAKME LSELEEQVEP LEAELKILLL PKDPNDEKNV IVEIRGGAGG
DEAALFAGDL FRMYSRYAER RRWKMELLSA SDTGVGGYKE VSFLIKGKGA YSRLKYESGV
HRVQRIPSTE SGGRIHTSTA TVAVLPEVET VEVNINPNDL RIDVFRSSGN GGQSVNTTDS
AVRITHIPTG EVVSCQDGKS QLKNKEQALK ILVARLNDKA IAEQNKDIAA ERKSQVGTGD
RSERIRTYNF PQGRVSDHRI NLTLYKLDSF LDGDIDEMID ALITVDQTEK MASL
//
