ID A0A1V2RFN0_9ACTN Unreviewed; 356 AA.
AC A0A1V2RFN0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-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=STBA_19110 {ECO:0000313|EMBL:ONK11182.1};
OS Streptomyces sp. MP131-18.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1857892 {ECO:0000313|EMBL:ONK11182.1, ECO:0000313|Proteomes:UP000189065};
RN [1] {ECO:0000313|EMBL:ONK11182.1, ECO:0000313|Proteomes:UP000189065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP131-18 {ECO:0000313|EMBL:ONK11182.1,
RC ECO:0000313|Proteomes:UP000189065};
RA Paulus C., Rebets Y., Tokovenko B., Nadmid S., Terekhova L.P.,
RA Myronovskyi M., Zotchev S.B., Rueckert C., Kalinowski J., Luzhetskyy A.;
RT "New natural products identified by combined genomics-metabolomics
RT profiling of marine Streptomyces sp. MP131-18.";
RL Submitted (JUN-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}.
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:ONK11182.1}.
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DR EMBL; LZNS01000001; ONK11182.1; -; Genomic_DNA.
DR RefSeq; WP_077058819.1; NZ_LZNS01000001.1.
DR AlphaFoldDB; A0A1V2RFN0; -.
DR STRING; 1857892.STBA_19110; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000189065; 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 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}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00093};
KW Reference proteome {ECO:0000313|Proteomes:UP000189065}.
FT DOMAIN 227..243
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT REGION 284..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 256..283
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 286..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 234
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00093"
SQ SEQUENCE 356 AA; 39218 MW; 05CCB7ECBD9CC098 CRC64;
MFEAVEDLVG EHADLERRLA DPAVHADQGT ARRLGKRYAE LTPIIAAYRS WKRHGEDIET
ARELAAEDPD FAAEVKDLQA RREELTEELR LLLVPRDPSD DKDVILEIKA GEGGDESALF
AGDLLRMYLR YAERVGWRTE IIDGNESDLG GYKDVSVAVK TRGTPEPGQG VWARLKYEGG
VHRVQRVPAT ESQGRIHTSA AGVLVLPEAE DVDVEISTAD LRIDVYRSSG PGGQSVNTTD
SAVRITHLPT GIVVSCQNEK SQLQNKEQAL RILRARLLAA AQEGADREAS DARRSQVRTV
DRSERVRTYN YPENRISDHR VGFKAYNLDQ VLDGDLDPVI QACVDADSAA KLAAAG
//
