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Database: UniProt
Entry: A0A1G1CN06_9BACT
LinkDB: A0A1G1CN06_9BACT
Original site: A0A1G1CN06_9BACT 
ID   A0A1G1CN06_9BACT        Unreviewed;       670 AA.
AC   A0A1G1CN06;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   22-FEB-2023, entry version 23.
DE   RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814};
DE            EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
GN   ORFNames=A2W24_04750 {ECO:0000313|EMBL:OGV96410.1};
OS   Microgenomates group bacterium RBG_16_45_19.
OC   Bacteria.
OX   NCBI_TaxID=1817747 {ECO:0000313|EMBL:OGV96410.1, ECO:0000313|Proteomes:UP000178440};
RN   [1] {ECO:0000313|EMBL:OGV96410.1, ECO:0000313|Proteomes:UP000178440}
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:OGV96410.1}.
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DR   EMBL; MHDC01000028; OGV96410.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G1CN06; -.
DR   STRING; 1817747.A2W24_04750; -.
DR   Proteomes; UP000178440; 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.
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          296..379
FT                   /note="B5"
FT                   /evidence="ECO:0000259|PROSITE:PS51483"
SQ   SEQUENCE   670 AA;  74533 MW;  C02F419CCC901320 CRC64;
     MNFRLPHSWL LEFLQTPAKP KAIASSLSLC GPSVERLEMI EHEPVYELEV TTNRVDMMSV
     RGIAREAAAI LPRFGFKAAL KPLPPAPAIP KILPPTSLKI TNDSTLCRRI LAIELGQISL
     KPSPAWLQTR LRQVGLRPLN NAIDITNYAM WAIGHPIHAF DLDKLTATNR LIVRQAKPGE
     TFTTLENLSY TTVGGEVIFD DGTGHIIDLP GIMGTKNTVV SASTKRIYLW IEDVDPVKIR
     FASMTHALRS QAAILNEKSV DPELALPTLM YAINLYQDLC SAKINSQLVD IYPSPPKIKS
     VTLDSGLLDT YLGTSLEVAT VSGIFTALGC QVQPAATPRP PHRFSLHLTP PSYRAKDLLT
     PPDFIEEVAR IEGYHNLASR VMATPIPLHP SPVQFDLEFQ VKQWLAGWGA TEVYTYSMIS
     PKLALASGFP LNQHLEIKNP YSAEWVYLRR SLIPSLVAVF AHNPPTSITI FELQHVYHPS
     PKPRALPQEE LHLTLLTSNT YSHLKGLLEA LVQKWHLPEP EILTSKTIPA PFAPSQSGRL
     QLHHDILGYL GAHKSTNNFC LDLDWSVFQK YAKTHPTLKP LLPHPPIIED LTFTLPPKTP
     LGPVLTTIKQ LDPMIDSVKL SVRYQQNYTF TLTYQDVNRQ LATQDLATLR QKIVAALAKT
     YHAPLVGSLT
//
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