ID A0A0G1HYG0_9BACT Unreviewed; 661 AA.
AC A0A0G1HYG0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 36.
DE RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814};
DE EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
DE AltName: Full=Phenylalanyl-tRNA synthetase beta subunit {ECO:0000256|ARBA:ARBA00033189};
GN ORFNames=UW44_C0005G0037 {ECO:0000313|EMBL:KKT51995.1};
OS Candidatus Collierbacteria bacterium GW2011_GWB2_44_22.
OC Bacteria; Candidatus Collierbacteria.
OX NCBI_TaxID=1618387 {ECO:0000313|EMBL:KKT51995.1, ECO:0000313|Proteomes:UP000034006};
RN [1] {ECO:0000313|EMBL:KKT51995.1, ECO:0000313|Proteomes:UP000034006}
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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) +
CC L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413, Rhea:RHEA-COMP:9668,
CC Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58095, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78531, ChEBI:CHEBI:456215; EC=6.1.1.20;
CC Evidence={ECO:0000256|ARBA:ARBA00000395};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000256|ARBA:ARBA00011209}.
CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC family. Type 1 subfamily. {ECO:0000256|ARBA:ARBA00008653}.
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:KKT51995.1}.
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DR EMBL; LCIH01000005; KKT51995.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1HYG0; -.
DR STRING; 1618387.UW44_C0005G0037; -.
DR PATRIC; fig|1618387.3.peg.449; -.
DR Proteomes; UP000034006; 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; IPR004532; Phe-tRNA-ligase_IIc_bsu_bact.
DR InterPro; IPR020825; Phe-tRNA_synthase-like_B3/B4.
DR InterPro; IPR041616; PheRS_beta_core.
DR InterPro; IPR005147; tRNA_synthase_B5-dom.
DR NCBIfam; TIGR00472; pheT_bact; 1.
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 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KKT51995.1};
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 296..372
FT /note="B5"
FT /evidence="ECO:0000259|PROSITE:PS51483"
FT DOMAIN 586..661
FT /note="FDX-ACB"
FT /evidence="ECO:0000259|PROSITE:PS51447"
SQ SEQUENCE 661 AA; 74323 MW; 6D9826558DC369EA CRC64;
MDIVITDSSI RKFLDTPADS EMLSQNVSLC GPTFDRIKKI DGDFVYEIEA ITNRVDTASA
QGVAREAATI LTQFNIPAKF INDPYKENLS FPDSQAKQFN LNIERDLVIR LVALSLENIS
VKPSSKETQS FLENCGQRPL NNCVDITNEL TLLYGLPSHI FDLDKLAAQN LTIRESKRGE
SITTLDDKKN ILIDGDIVIE DGSDRLVDLC GIMGGQVAEV DDHTKNILLI VPVYNPQKIR
KTSLRLQKRT LAAQIFEKQP DPELCLPVLS KAVQLFKERT GAVISSPLFD YYPANRSPKI
ISLDFNWLNT FVGLDIKKET VIDILASLGF GGTKEGNGLA CSVPSWRYHD INIREDLAEE
VARIYGYFRL PSVLPCVNLP AEPKNHLFKT ELKSKIFLSD IGYHEIYNNS LISLQAIEKS
GQDSSRFIKL KNSLSQDFEY LRTSLIPSAL ENHKHNQGKA DKQIKTFEIA NCYQKTEGQE
LPKEISYLAI LSEGDYRKTK GDLEALFQKL RVKDISFEPS KVLPPFYNTV ATADIYSEKL
MIGYIGSIKS AVSRNFGLTN SLIATEINLD SLVSKISQEY VYHPISEYPS IIEDLTVASE
KSLGDIIEAI KSTSKLVKDI QYLDSFKGKH SFRISFQNNE KNLEQAEINS LKEIILDLFK
V
//
