ID A0A1F6CNQ4_9BACT Unreviewed; 605 AA.
AC A0A1F6CNQ4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 22-FEB-2023, entry version 21.
DE RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814};
DE EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
GN ORFNames=A2763_00685 {ECO:0000313|EMBL:OGG50839.1};
OS Candidatus Kaiserbacteria bacterium RIFCSPHIGHO2_01_FULL_54_36.
OC Bacteria; Candidatus Kaiserbacteria.
OX NCBI_TaxID=1798482 {ECO:0000313|EMBL:OGG50839.1, ECO:0000313|Proteomes:UP000178370};
RN [1] {ECO:0000313|EMBL:OGG50839.1, ECO:0000313|Proteomes:UP000178370}
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., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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:OGG50839.1}.
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DR EMBL; MFKV01000006; OGG50839.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6CNQ4; -.
DR STRING; 1798482.A2763_00685; -.
DR Proteomes; UP000178370; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:InterPro.
DR Gene3D; 3.30.56.10; -; 2.
DR Gene3D; 3.30.70.380; Ferrodoxin-fold anticodon-binding domain; 1.
DR Gene3D; 3.50.40.10; Phenylalanyl-trna Synthetase, Chain B, domain 3; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR005146; B3/B4_tRNA-bd.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR005121; Fdx_antiC-bd.
DR InterPro; IPR036690; Fdx_antiC-bd_sf.
DR InterPro; IPR045060; Phe-tRNA-ligase_IIc_bsu.
DR InterPro; IPR020825; Phe-tRNA_synthase-like_B3/B4.
DR InterPro; IPR041616; PheRS_beta_core.
DR InterPro; IPR005147; tRNA_synthase_B5-dom.
DR PANTHER; PTHR10947:SF0; PHENYLALANINE--TRNA LIGASE BETA SUBUNIT; 1.
DR PANTHER; PTHR10947; PHENYLALANYL-TRNA SYNTHETASE BETA CHAIN AND LEUCINE-RICH REPEAT-CONTAINING PROTEIN 47; 1.
DR Pfam; PF03483; B3_4; 1.
DR Pfam; PF03484; B5; 1.
DR Pfam; PF03147; FDX-ACB; 1.
DR Pfam; PF17759; tRNA_synthFbeta; 1.
DR SMART; SM00873; B3_4; 1.
DR SMART; SM00874; B5; 1.
DR SMART; SM00896; FDX-ACB; 1.
DR SUPFAM; SSF54991; Anticodon-binding domain of PheRS; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF56037; PheT/TilS domain; 1.
DR SUPFAM; SSF46955; Putative DNA-binding domain; 2.
DR PROSITE; PS51483; B5; 1.
DR PROSITE; PS51447; FDX_ACB; 1.
PE 4: Predicted;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 294..369
FT /note="B5"
FT /evidence="ECO:0000259|PROSITE:PS51483"
FT DOMAIN 509..605
FT /note="FDX-ACB"
FT /evidence="ECO:0000259|PROSITE:PS51447"
SQ SEQUENCE 605 AA; 66079 MW; 50E54AA593DD6FD4 CRC64;
MKISRAWLQT FFDAPLPDAA AIGDALTFHA FEIESTENVA GDDILDVKVT PNRGHDALSH
HAIAKELGAI LGIPHKSDPL QAVISLEPKT DAVKVAIENP DLCRRFTVAL IQGVHVGPSP
DWLRERLESI GQRSINNVVD ATNFVMFNIG QPLHAFDAGK LSSQNGHSLI VRKAKDKEKM
LGLDDKEYIL TGAMLAIADG HTNEVVSIAG IKGGKPTGID ETTSALILEA ANWDGVLIRK
TSQVLKLRTD ASERFQQVIS PELAAYGLHA AANLILELAG GEIVGFVDEY PMPQGKREVA
VSTEKVNHVL GTELSVEDVG NAFTRLGLPH AQVGDHFTVT VPFERLDITI PEDLIEEVAR
VLGYDKIPTL DLPPFPNAPE VNANYYAAEQ TREELMAKGY SEVYTSVFAD TGERAVANKV
DSVHPYLRSN LVDGLTQALR RNVHNKDLLG LTEVRLFEIG TVWTKKGEEM HAATVGEKEK
PEEQIVKPEA GDTYNTLALS IAARYQSFSK YPFIVRDIAL WVPKGSDPDA VLQIIRAAAG
ALLVRAELFD TFEKGDPSTG SGQVKLSLAF RLVFQSLEKT LTDIEANAAM ENVYSEAKNQ
GWEVR
//
