ID A0A426CIE5_9BACT Unreviewed; 373 AA.
AC A0A426CIE5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
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=Ga0100231_017930 {ECO:0000313|EMBL:RRJ95866.1};
OS Opitutaceae bacterium TAV4.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae.
OX NCBI_TaxID=278959 {ECO:0000313|EMBL:RRJ95866.1, ECO:0000313|Proteomes:UP000078325};
RN [1] {ECO:0000313|EMBL:RRJ95866.1, ECO:0000313|Proteomes:UP000078325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TAV4 {ECO:0000313|EMBL:RRJ95866.1,
RC ECO:0000313|Proteomes:UP000078325};
RA Rodrigues J., Kotak M., Lin J.;
RT "Draft genome sequences of strains TAV3 and TAV4 (Verrucomicrobial:
RT Opitutaceae) isolated from a wood-feeding termite and in silico analysis of
RT their polysaccharide-degrading enzymes.";
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:RRJ95866.1}.
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DR EMBL; LXWU02000003; RRJ95866.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A426CIE5; -.
DR STRING; 278959.Ga0100231_12480; -.
DR Proteomes; UP000078325; 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; -; 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 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:UP000078325}.
FT DOMAIN 229..245
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT MOD_RES 236
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00093"
SQ SEQUENCE 373 AA; 41583 MW; 33298BC6A7EEF6D1 CRC64;
MQSLPDISLF QRRADELDAQ MRSPTFYNDA RAAAAVTREH QQVTQLLADH AAHRKTLAEI
AEAQALIKDP SADPDLRELA EAELPELEAR RERLFRTVLA GMIPPEPTDS RDTVLEIRAG
TGGEEAALFA AELARMYHRY AEDRGWTVEP TGSSESERGG FREVSFIIRG QDVYKQLKFE
SGVHRVQRVP LTEANGRIHT STVTVAVLPE AQEVDIRIDP QDLEITVQRA SGPGGQGVNT
TDSAVRIVHK PTGMIVYCAD GRSQQKNKAS AMSVLRARLL QRKQDEEAAK YAAQRRGQIG
TGDRSERIRT YNFPQNRLTD HRIGLTLYSL TQVMEGALNE VVQPLQKAEF EEKLALLTGQ
PYDRRRAASG DDD
//
