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Database: UniProt
Entry: A0A1J4WNG1_9BACT
LinkDB: A0A1J4WNG1_9BACT
Original site: A0A1J4WNG1_9BACT 
ID   A0A1J4WNG1_9BACT        Unreviewed;       380 AA.
AC   A0A1J4WNG1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   13-FEB-2019, entry version 7.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OIO50684.1};
GN   ORFNames=AUJ45_02685 {ECO:0000313|EMBL:OIO50684.1};
OS   Parcubacteria group bacterium CG1_02_50_68.
OC   Bacteria; unclassified Parcubacteria group.
OX   NCBI_TaxID=1805312 {ECO:0000313|EMBL:OIO50684.1};
RN   [1] {ECO:0000313|EMBL:OIO50684.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CG1_02_50_68 {ECO:0000313|EMBL:OIO50684.1};
RX   PubMed=27112493;
RA   Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA   Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C.,
RA   Banfield J.F.;
RT   "Genomic resolution of a cold subsurface aquifer community provides
RT   metabolic insights for novel microbes adapted to high CO
RT   concentrations.";
RL   Environ. Microbiol. 0:0-0(2016).
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:OIO50684.1}.
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DR   EMBL; MNWM01000032; OIO50684.1; -; Genomic_DNA.
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      134    290       AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:
FT                                PS50862}.
FT   DOMAIN      286    380       FDX-ACB. {ECO:0000259|PROSITE:PS51447}.
SQ   SEQUENCE   380 AA;  43533 MW;  76064580C6F67CAD CRC64;
     MEITVSRDGE RQLRADVENR NDFEALRIRR YLAMPDLSRT VGSPIHELTE RIRAIPGFKE
     YDVINVPEIM STDIVFDLFD FPKDHPARSR SDSYFIDDVH VLRTHTTVMW YYWLKEKSVR
     EKIAAGTAVG AISFGKVYRK DEIDRRHMNV FHQIDGWYLA PKKEKSITID DLKKVLSDIA
     IAAFGPKVKY RFNPDIFPYT DPSLEMEIDK DGNNTWVEVL GAGVVKGSVL DNLGVDSSVW
     NGWAFGFGLE RLAIISMELP DIRLLWSSDE RVKKQLTLGA KFKEVSKYPP IVRDISFIVA
     KGFVPNNYFD LVREVAGDLV EQVELLDTYE NEKKFGAGKV SYAYRITYRS IDKTLTNEEV
     GVLHTNLETA TAKNFDAVIR
//
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