RF1_SALPA
ID RF1_SALPA Reviewed; 360 AA.
AC Q5PCQ9;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Peptide chain release factor 1 {ECO:0000255|HAMAP-Rule:MF_00093};
DE Short=RF-1 {ECO:0000255|HAMAP-Rule:MF_00093};
GN Name=prfA {ECO:0000255|HAMAP-Rule:MF_00093}; OrderedLocusNames=SPA1097;
OS Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=295319;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9150 / SARB42;
RX PubMed=15531882; DOI=10.1038/ng1470;
RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA Warren W., Florea L., Spieth J., Wilson R.K.;
RT "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT restricted serovars of Salmonella enterica that cause typhoid.";
RL Nat. Genet. 36:1268-1274(2004).
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:0000255|HAMAP-Rule:MF_00093}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00093}.
CC -!- PTM: Methylated by PrmC. Methylation increases the termination
CC efficiency of RF1. {ECO:0000255|HAMAP-Rule:MF_00093}.
CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC family. {ECO:0000255|HAMAP-Rule:MF_00093}.
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DR EMBL; CP000026; AAV77066.1; -; Genomic_DNA.
DR RefSeq; WP_000804704.1; NC_006511.1.
DR AlphaFoldDB; Q5PCQ9; -.
DR SMR; Q5PCQ9; -.
DR EnsemblBacteria; AAV77066; AAV77066; SPA1097.
DR KEGG; spt:SPA1097; -.
DR HOGENOM; CLU_036856_0_1_6; -.
DR OMA; ISDHRVG; -.
DR Proteomes; UP000008185; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016149; F:translation release factor activity, codon specific; IEA:UniProtKB-UniRule.
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 Pfam; PF03462; PCRF; 1.
DR Pfam; PF00472; RF-1; 1.
DR SMART; SM00937; PCRF; 1.
DR SUPFAM; SSF75620; SSF75620; 1.
DR TIGRFAMs; TIGR00019; prfA; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methylation; Protein biosynthesis.
FT CHAIN 1..360
FT /note="Peptide chain release factor 1"
FT /id="PRO_0000263346"
FT REGION 285..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 235
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ SEQUENCE 360 AA; 40477 MW; 67AF15AD7AD698B5 CRC64;
MKPSIVAKLE ALHERHEEVQ ALLGDAGIIA DQDRFRALSR EYAQLSDVSR CFTDWQQVQD
DIETAQMMLD DPEMREMAQE ELREAKEKSE QLEQQLQVLL LPKDPDDERN AFLEVRAGTG
GDEAALFAGD LFRMYSRYAE ARRWRVEIMS MSEGEHGGYK EIIAKISGDG VYGRLKFESG
GHRVQRVPAT ESQGRIHTSA CTVAVMPELP EAELPDINPA DLRIDTFRSS GAGGQHVNTT
DSSIRITHLP TGIVVECQDE RSQHKNKAKA LSVLGARIHA AETAKRQQAE ASTRRNLLGS
GDRSDRNRTY NFPQGRVTDH RINLTLYRLD ETMEGKLDML IEPIVQEHQA DLLAALSEQE
