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Database: UniProt
Entry: A0A1F4YDT5_9BACT
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Original site: A0A1F4YDT5_9BACT 
ID   A0A1F4YDT5_9BACT        Unreviewed;       610 AA.
AC   A0A1F4YDT5;
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=A2876_02385 {ECO:0000313|EMBL:OGC92044.1};
OS   Candidatus Amesbacteria bacterium RIFCSPHIGHO2_01_FULL_48_32b.
OC   Bacteria; Candidatus Amesbacteria.
OX   NCBI_TaxID=1797253 {ECO:0000313|EMBL:OGC92044.1, ECO:0000313|Proteomes:UP000178176};
RN   [1] {ECO:0000313|EMBL:OGC92044.1, ECO:0000313|Proteomes:UP000178176}
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:OGC92044.1}.
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DR   EMBL; MEXH01000023; OGC92044.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F4YDT5; -.
DR   Proteomes; UP000178176; 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; 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          297..364
FT                   /note="B5"
FT                   /evidence="ECO:0000259|PROSITE:PS51483"
FT   DOMAIN          535..610
FT                   /note="FDX-ACB"
FT                   /evidence="ECO:0000259|PROSITE:PS51447"
SQ   SEQUENCE   610 AA;  69354 MW;  E365ACAD0FD16C84 CRC64;
     MQILIPDSWL REYLYTDAKP KEIQKALSLC GPSIERMQKV GDDYVYDIEV TTNRVDMMSV
     YGIAREAAAI LPRFNHQAKL LSDPFSAKLS FETSSFVDYL KVKVDPSLCL RFSAILIKNV
     SVKPSPDWIT KKLELVGMRG LNNVVDISNL LMHEFGQPIH TFDYDKIAYH TMTLRESRVG
     ESLTTLDGKT HKLPGHDIVI EDGSKKLIDL CGIMGGANSA VDDETKNVLF FVQTYEPSHI
     RKTSMALSHR TSAAVLFEKG LPIESVLPTM EKALPLFKEL TGGQPETTAI DIVNEKPYSK
     TLTAPPDFIN SRLGINLTPK EIRDILTNLG ITDKIPWWRK NDINIPEDFV EEVARIYGYH
     NLPARLMSGP LPTARTNDSE FYWISNIKSA LKHWGFVETY TYSLIPQDSG LKLKNPLSDD
     WKYLRTTLIP SLKSIIQENL GRVKELNLFE IANVYLPRKN DLPQEVLHLA IGTTRKDWFY
     LKGVVESLFN YELGITVGFN ENKEVFSYEN CLVFEINLQE QISRATSIRK FTPISQFPAI
     IEDMNVTLSS KYDTLISQIK KVSPLIKNIE LIDKYADKLT LRLTFHSDDR QLSSSDLAPV
     REKLSKLFAQ
//
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