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Database: UniProt
Entry: A0A0G1BC44_9BACT
LinkDB: A0A0G1BC44_9BACT
Original site: A0A0G1BC44_9BACT 
ID   A0A0G1BC44_9BACT        Unreviewed;       375 AA.
AC   A0A0G1BC44;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   13-FEB-2019, entry version 15.
DE   SubName: Full=Phenylalanyl-tRNA synthetase {ECO:0000313|EMBL:KKS43926.1};
GN   ORFNames=UV07_C0019G0006 {ECO:0000313|EMBL:KKS43926.1};
OS   Candidatus Azambacteria bacterium GW2011_GWB1_42_17.
OC   Bacteria; Candidatus Azambacteria.
OX   NCBI_TaxID=1618615 {ECO:0000313|EMBL:KKS43926.1};
RN   [1] {ECO:0000313|EMBL:KKS43926.1}
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:KKS43926.1}.
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DR   EMBL; LCDB01000019; KKS43926.1; -; Genomic_DNA.
DR   EnsemblBacteria; KKS43926; KKS43926; UV07_C0019G0006.
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   ECO:0000313|EMBL:KKS43926.1};
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      131    285       AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:
FT                                PS50862}.
FT   DOMAIN      281    375       FDX-ACB. {ECO:0000259|PROSITE:PS51447}.
SQ   SEQUENCE   375 AA;  43972 MW;  0288E389B7B6A63B CRC64;
     MADNKTEEKL IEVLRKRRDP EAKRLKRFLD MSDLTRTPGS PLAELVKRIV NLPRFSDFEV
     LKAPEIIPYD ISFNLFNFPA DHPARNPSDT YFVDKDHILR THTTVMWYYH LALPGVWNKI
     KKGESVSALS YGKVYRKDEI DRSHMNVFHQ MDGWYLCRRK DHIITINDLK DVLIEIAQAI
     FGKNTKYRFN TDKFPYTDPS IEMEIQVSER WVEVLGAGVV RKVVLENLGV DPKRYNGWAF
     GFGLERLAIT SMDLPDIRLL WSQDERVKKQ LKLGNKYKEV SKFPPITRDI SFIAGKDFVP
     NNYFDLIRDI GGILVEEVRL IDKYEDLIKF GPDRSSYTYR LIYRSSDRTL LSNEVDKIQE
     KIYSETAKQF NAKLR
//
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