ID A0A1I5R433_9FIRM Unreviewed; 354 AA.
AC A0A1I5R433;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=SAMN04487928_103111 {ECO:0000313|EMBL:SFP53245.1};
OS Butyrivibrio proteoclasticus.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=43305 {ECO:0000313|EMBL:SFP53245.1, ECO:0000313|Proteomes:UP000182624};
RN [1] {ECO:0000313|Proteomes:UP000182624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P18 {ECO:0000313|Proteomes:UP000182624};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; FOXO01000003; SFP53245.1; -; Genomic_DNA.
DR RefSeq; WP_074884170.1; NZ_FOXO01000003.1.
DR AlphaFoldDB; A0A1I5R433; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000182624; 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};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00093}.
FT DOMAIN 226..242
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT MOD_RES 233
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00093"
SQ SEQUENCE 354 AA; 40318 MW; C428BB46AAD73588 CRC64;
MFDKIEDILR RYEDITMELN DPYVVSDQNK FRNLMKEQKS LEALVECYQE YKKCKQTIDD
SLQLLDEESD PDMKEMLREE LSEAKERIPE LENQLKILLL PKDPNDEKNV IVEIRAGVGG
EEAALFAADM YRLYTRYAER KNWRVETMSV EDTGIGGIKD VSFMIKGEGA YSRLKFEGGV
HRVQRIPATE SGGRIHTSAI TVAIMPEVED VEVEIDMNDC KFDVFRASGN GGQCVNTTDS
AVRLTHLPTG IVISCQDEKS QQQNKAKALK VLRAKLYELE EQKKHNSEAA LRKSQVGSGD
RSDKIRTYNF HQGRVTDHRI NLTLYKIDQI MDGDLDEIID SLIAADQAEK LAAE
//
