ID A0A1J4NZ38_9ACTN Unreviewed; 358 AA.
AC A0A1J4NZ38;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=WN71_011790 {ECO:0000313|EMBL:OIJ67745.1};
OS Streptomyces mangrovisoli.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1428628 {ECO:0000313|EMBL:OIJ67745.1, ECO:0000313|Proteomes:UP000034196};
RN [1] {ECO:0000313|EMBL:OIJ67745.1, ECO:0000313|Proteomes:UP000034196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC149T {ECO:0000313|Proteomes:UP000034196};
RA Lee L.-H., Ser H.-L.;
RT "Genome sequence of Streptomyces mangrovisoli MUSC 149.";
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}.
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:OIJ67745.1}.
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DR EMBL; LAVA02000023; OIJ67745.1; -; Genomic_DNA.
DR RefSeq; WP_046591568.1; NZ_LAVA02000023.1.
DR AlphaFoldDB; A0A1J4NZ38; -.
DR STRING; 1428628.WN71_011790; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000034196; 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:UP000034196}.
FT DOMAIN 230..246
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT COILED 259..301
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 237
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00093"
SQ SEQUENCE 358 AA; 39368 MW; EA4FC083160C88A5 CRC64;
MFEAVEELVV EHADLETKLA DPSVHADQAN ARKLNKRYAE LTPIVATFRS WKQTGDDIDT
ARELAADDPD FAAEVKELEK SREELTEKLR MLLVPRDPSD DKDVILEIKA GAGGDESALF
AGDLLRMYLR YAERVGWKTE IIDATESELG GYKDVQVAVK TKGGQGATEP GQGVWARMKY
EGGVHRVQRV PATESQGRIH TSAAGVLVTP EAEEVDVEIN PNDLRIDVYR SSGPGGQSVN
TTDSAVRITH LPTGVVASCQ NEKSQLQNKE QALRILRSRL LAAAQEEAER EAADARRSQV
RTVDRSEKIR TYNFPENRIS DHRVGFKSYN LDQVLDGDLD AVIQACVDAD SAAKLAAA
//
