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Database: UniProt
Entry: A0A3F2V164_9GAMM
LinkDB: A0A3F2V164_9GAMM
Original site: A0A3F2V164_9GAMM 
ID   A0A3F2V164_9GAMM        Unreviewed;       358 AA.
AC   A0A3F2V164;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, 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   ECO:0000313|EMBL:RLP53593.1};
GN   ORFNames=D6160_14665 {ECO:0000313|EMBL:RLP53593.1};
OS   Ketobacter sp.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Ketobacteraceae; Ketobacter.
OX   NCBI_TaxID=2083498 {ECO:0000313|EMBL:RLP53593.1, ECO:0000313|Proteomes:UP000280615};
RN   [1] {ECO:0000313|EMBL:RLP53593.1, ECO:0000313|Proteomes:UP000280615}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BinD {ECO:0000313|EMBL:RLP53593.1};
RA   Xu J.;
RT   "Metagenomic reconstruction reveals the metabolic diversity of the novel
RT   genus Ketobacter and the trajectory of genomic evolution within the
RT   Alcanivoraceae family.";
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:RLP53593.1}.
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DR   EMBL; RAHY01000013; RLP53593.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3F2V164; -.
DR   Proteomes; UP000280615; 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:UP000280615}.
FT   DOMAIN          228..244
FT                   /note="Prokaryotic-type class I peptide chain release
FT                   factors"
FT                   /evidence="ECO:0000259|PROSITE:PS00745"
FT   REGION          280..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        281..302
FT                   /note="Basic and acidic 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   358 AA;  40610 MW;  DAB8B417626FA690 CRC64;
     MKESLRTKLA GRSERYEEVG LLLSQPEVIM DQNQFRKLSQ EYAEIEPIVH CYREYDQVLK
     NIEEAKSWLA DPDLKEMGEE ELEANQKKSE LLEAELQKLM LPKDPFDGSN VFLEVRAGTG
     GDEAAIFAGD LYRMYSRYGE SLGWRIEAVS QNEGEHGGYK EIICRVIGDN VYSKLKFESG
     AHRVQRVPAT ESQGRIHTSA CTVAILPEAD EVTDIEVRNE DLRIDTYRSS GAGGQHVNTT
     DSAVRIVHLP SGVVVECQDE RSQHKNKAKA MSLLKSRLLQ HAQDKQQKET SDARRNLVGS
     GDRSERIRTY NYPQGRVTDH RINLTLYRLP EIMEGSLEEV IQPLVNEYQA DLLAALEE
//
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