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Database: UniProt
Entry: A0A418XT60_9BURK
LinkDB: A0A418XT60_9BURK
Original site: A0A418XT60_9BURK 
ID   A0A418XT60_9BURK        Unreviewed;       358 AA.
AC   A0A418XT60;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 15.
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:RJG15856.1};
GN   ORFNames=D3872_11620 {ECO:0000313|EMBL:RJG15856.1};
OS   Massilia cavernae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=2320864 {ECO:0000313|EMBL:RJG15856.1, ECO:0000313|Proteomes:UP000284006};
RN   [1] {ECO:0000313|EMBL:RJG15856.1, ECO:0000313|Proteomes:UP000284006}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K1S02-61 {ECO:0000313|EMBL:RJG15856.1,
RC   ECO:0000313|Proteomes:UP000284006};
RA   Zhu H.;
RL   Submitted (SEP-2018) 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:RJG15856.1}.
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DR   EMBL; QYUP01000111; RJG15856.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A418XT60; -.
DR   OrthoDB; 9806673at2; -.
DR   Proteomes; UP000284006; 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};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00093}; Reference proteome {ECO:0000313|Proteomes:UP000284006}.
FT   DOMAIN          228..244
FT                   /note="Prokaryotic-type class I peptide chain release
FT                   factors"
FT                   /evidence="ECO:0000259|PROSITE:PS00745"
FT   MOD_RES         235
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   358 AA;  40105 MW;  12164A19FBE5C833 CRC64;
     MKPSMLAKLD QLANRLVELD ELLMHQEATS NMDNYRKMTR EHAEIGPLVG LYKEFQRAHG
     DIDEATTMLL DPDMKDFAQE EIEAGKARVA ELELDLQKML LPKDVNDERN IFLEIRAGTG
     GDESALFTGD LLRMYTRFAE RNRWQVEMVS ESASDLGGYR EVIVRIIGNG AYSKLKFESG
     GHRVQRVPAT ETQGRIHTSA CTVAVMPEAD EVEDVNINPA DLRIDTYRAS GAGGQHINKT
     DSAVRITHLP TGIVVECQDD RSQHKNKAQA LKVLAARIKD VQLREQQSKE AATRKSLIGS
     GDRSERIRTY NFPQGRMTDH RINLTLYKLD FIMDGDLSEL TNALAAEHQA ELLAALGD
//
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