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Database: UniProt
Entry: A0A1F6C1V0_9BACT
LinkDB: A0A1F6C1V0_9BACT
Original site: A0A1F6C1V0_9BACT 
ID   A0A1F6C1V0_9BACT        Unreviewed;       383 AA.
AC   A0A1F6C1V0;
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:OGG43174.1};
GN   ORFNames=A3G50_01285 {ECO:0000313|EMBL:OGG43174.1};
OS   Candidatus Jorgensenbacteria bacterium RIFCSPLOWO2_12_FULL_42_11.
OC   Bacteria; Candidatus Jorgensenbacteria.
OX   NCBI_TaxID=1798473 {ECO:0000313|EMBL:OGG43174.1};
RN   [1] {ECO:0000313|EMBL:OGG43174.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U.,
RA   Brodie E.L., Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected
RT   biogeochemical processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(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:OGG43174.1}.
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DR   EMBL; MFKM01000021; OGG43174.1; -; 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      138    292       AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:
FT                                PS50862}.
FT   DOMAIN      289    383       FDX-ACB. {ECO:0000259|PROSITE:PS51447}.
SQ   SEQUENCE   383 AA;  44736 MW;  CF1408F3528CBDC9 CRC64;
     MSTKRRNLTI NDPEMPAVLS KLQNKTDFKS LRIKQLLALP DLTKTNDSPI KFLIDAIVNL
     RRFKNFDIIN VPEIVSVRNN FDLLNAPADH PSRQETDTYY PEKDWVLRTH TTVMWPYYFS
     EENMKKLETE GEIGALCFGK VYRKDEIDRS HYPAFHQIDG LYICRKDKKI IGILELTEVL
     VDIAKNIYGT DVEYQISEDT FPFTDPSLQI AIKGKNQWLE IVGAGVVHTR VLKNLDIDPS
     VYNGWAFGFG LERLAMIKME IPDIRIFWST DKRITGQFKD LNSRFQEISK YPMTYRDISF
     VVGKDTSLNN YYEIIRDCAG NLVEEVSLLD KYENKEKFGE NNISYTFHIV YRSNERTLTN
     DEVDKIQRLL IDRTRKELNA LVR
//
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