ID A0A0G1UEL0_9BACT Unreviewed; 626 AA.
AC A0A0G1UEL0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 22-FEB-2023, entry version 34.
DE RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814};
DE EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
GN ORFNames=UY22_C0034G0013 {ECO:0000313|EMBL:KKU92544.1};
OS Candidatus Amesbacteria bacterium GW2011_GWC1_48_10.
OC Bacteria; Candidatus Amesbacteria.
OX NCBI_TaxID=1618365 {ECO:0000313|EMBL:KKU92544.1, ECO:0000313|Proteomes:UP000034877};
RN [1] {ECO:0000313|EMBL:KKU92544.1, ECO:0000313|Proteomes:UP000034877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKU92544.1}.
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DR EMBL; LCPE01000034; KKU92544.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1UEL0; -.
DR PATRIC; fig|1618365.3.peg.761; -.
DR Proteomes; UP000034877; 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; 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 ECO:0000313|EMBL:KKU92544.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KKU92544.1};
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 313..386
FT /note="B5"
FT /evidence="ECO:0000259|PROSITE:PS51483"
SQ SEQUENCE 626 AA; 70502 MW; 9D3C88A1759EEDE1 CRC64;
MNILIPDSWL REFLDTDATP QQIQSALSLC GPSIERLIKF APPLKLRGGE RGGNTDWIYD
IEITTNRVDC MSVIGFAREA VAILPQFKRR ARLIKSPFAT KPSLKTSTQV PYLEVKVDQT
LCPRFTAVLI QNVTIGPSPD WLAKRLELVG MRPLNAIVDI SNYLMHELGQ PIHTFDYDKI
TNRRMTLRAS RKGEKITTLD GKTHTLHGGD IVIEDGSGKL IDLCGIMGGL NSAVDTKTKN
VLLFVQTYDP VRIRKTSMSL AHRTQAAVLF EKKLSPDSVL PTTQSAIQLF ILLTHGQPSD
KVLDIYTPGK TKDALTTSFS LPEFINSRLG INLSAPQISQ FLAGLGFLVL SDRKVEIPWY
RTGDISIPED LVEEVARIYG YHNLPSQIMS GPLPTNRNDK VFYWEHRLKT LLVHLGFTEV
YTWSLVEIDT GLKLKNPLTS EWSYLRTTLT PSHLKIHTEN AGKADQFDFF EITSVYLPRR
NDLPLEEPRL IISTNSGNYS KFKGIIETVL SEMGIADFPI RIQTHSNILV WETPLLPLIS
QATTTRTYTA ISQYPPIMED VNITHNRPYA EIIKSIQKIS SLIKQIDLID KFGDKLTLRL
TFHSASKQLS SLDIIPIRDK IANIQL
//
