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Database: UniProt
Entry: A0A0G0RGR7_9BACT
LinkDB: A0A0G0RGR7_9BACT
Original site: A0A0G0RGR7_9BACT 
ID   A0A0G0RGR7_9BACT        Unreviewed;       398 AA.
AC   A0A0G0RGR7;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   05-JUN-2019, entry version 13.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KKR51889.1};
GN   ORFNames=UT89_C0005G0046 {ECO:0000313|EMBL:KKR51889.1};
OS   Parcubacteria group bacterium GW2011_GWE1_40_20.
OC   Bacteria; unclassified Parcubacteria group.
OX   NCBI_TaxID=1618946 {ECO:0000313|EMBL:KKR51889.1};
RN   [1] {ECO:0000313|EMBL:KKR51889.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a
RT   large radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. {ECO:0000256|SAAS:SAAS01110910}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KKR51889.1}.
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DR   EMBL; LBYN01000005; KKR51889.1; -; Genomic_DNA.
DR   EnsemblBacteria; KKR51889; KKR51889; UT89_C0005G0046.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:InterPro.
DR   Gene3D; 3.30.70.380; -; 1.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR005121; Fdx_antiC-bd.
DR   InterPro; IPR036690; Fdx_antiC-bd_sf.
DR   InterPro; IPR004530; Phe-tRNA-synth_IIc_mito.
DR   InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR   PANTHER; PTHR11538:SF41; PTHR11538:SF41; 1.
DR   Pfam; PF03147; FDX-ACB; 1.
DR   Pfam; PF01409; tRNA-synt_2d; 1.
DR   SMART; SM00896; FDX-ACB; 1.
DR   SUPFAM; SSF54991; SSF54991; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR   PROSITE; PS51447; FDX_ACB; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|SAAS:SAAS01110915};
KW   ATP-binding {ECO:0000256|SAAS:SAAS01110882};
KW   Ligase {ECO:0000256|SAAS:SAAS01110936};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS01110884};
KW   Protein biosynthesis {ECO:0000256|SAAS:SAAS01110938}.
FT   DOMAIN      151    288       AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:
FT                                PS50862}.
FT   DOMAIN      304    398       FDX-ACB. {ECO:0000259|PROSITE:PS51447}.
FT   REGION        1     21       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0G0RGR7}.
SQ   SEQUENCE   398 AA;  46332 MW;  7C6AB08D70C59FC9 CRC64;
     MTNEQNKTQE ELYGDASLSR KIYETPSEKE EKLLEELNHR TDTESSRMKQ YLAMKDLSRT
     PESPLFEMIE RVTNIPILKN FDLIKVPEIV TAEVTFDLFN FPLNHPARSK SDTYYLNENY
     ILRTHCTVMW YYYLALKEVR EQLKNGQAIG VLSHGKVYRK DEIDRNHMNI FHQIDGLYLC
     KTNKHVITQE DLKDVLSGIA KSVFGENVKY RFNDDTFPYT NQSIEMEIDK DGNWIEVLGA
     GVVQPAVLEK LGVDSKEYNG WAFGFGLERL AIISMELPDI RLLWSEDPRV TKQLKLGNKF
     VEVSKYPPIV RDISFVVKND FVPNDYFDLV RETAPNLVEE VHLLDKYENA EKFGENMVSY
     AFRITYRSTE RTLTSEEIDA VHKKLEKVTS ELFSATVR
//
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