ID A0A0J5M753_PLUGE Unreviewed; 360 AA.
AC A0A0J5M753;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
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:KMK16511.1};
GN ORFNames=ABW06_00780 {ECO:0000313|EMBL:KMK16511.1};
OS Pluralibacter gergoviae (Enterobacter gergoviae).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Pluralibacter.
OX NCBI_TaxID=61647 {ECO:0000313|EMBL:KMK16511.1, ECO:0000313|Proteomes:UP000036196};
RN [1] {ECO:0000313|EMBL:KMK16511.1, ECO:0000313|Proteomes:UP000036196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS81F13 {ECO:0000313|EMBL:KMK16511.1,
RC ECO:0000313|Proteomes:UP000036196};
RA Greninger A.L., Miller S.;
RT "Genome sequences of Pluralibacter gergoviae.";
RL Submitted (MAY-2015) 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:KMK16511.1}.
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DR EMBL; LDZF01000001; KMK16511.1; -; Genomic_DNA.
DR RefSeq; WP_048274108.1; NZ_VWRP01000001.1.
DR AlphaFoldDB; A0A0J5M753; -.
DR STRING; 61647.LG71_14955; -.
DR PATRIC; fig|61647.15.peg.166; -.
DR eggNOG; COG0216; Bacteria.
DR Proteomes; UP000036196; 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.
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:UP000036196}.
FT DOMAIN 228..244
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT REGION 285..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 235
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00093"
SQ SEQUENCE 360 AA; 40308 MW; 326521F27496DEC8 CRC64;
MKPSIVAKLE ALHERHEEVQ ALLGDAGTIA DQDRFRALSR EYAQLSDVSK CFTDWQQVQE
DIETAQMMLD DPEMREMAQE ELRDAKEKGE QLEAQLQVLL LPKDPDDERN AFVEVRAGTG
GDEAALFAGD LFRMYSRYAE SRRWRVEIMS ASEGEHGGFK EVIAKISGEG VYGRLKFESG
GHRVQRVPAT ESQGRIHTSA CTVAVMPEVP EAEMPDINPA DLRIDTFRSS GAGGQHVNTT
DSAIRITHLP TGIVVECQDE RSQHKNKAKA LSVLGSRIRA AEIAKRQQAE ASTRRNLLGS
GDRSDRNRTY NFPQGRVTDH RINLTLYRLD EAMEGKLDML IEPIVQEYQA DQLAALSDQE
//
