ID F7XR47_TREPU Unreviewed; 553 AA.
AC F7XR47;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Phenylalanine--tRNA ligase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00282};
DE EC=6.1.1.20 {ECO:0000256|HAMAP-Rule:MF_00282};
DE AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00282};
DE Short=PheRS {ECO:0000256|HAMAP-Rule:MF_00282};
GN Name=pheS {ECO:0000256|HAMAP-Rule:MF_00282,
GN ECO:0000313|EMBL:AEH40897.1};
GN OrderedLocusNames=TPCCA_0973 {ECO:0000313|EMBL:AEH40897.1};
OS Treponema paraluiscuniculi (strain Cuniculi A).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=545776 {ECO:0000313|EMBL:AEH40897.1, ECO:0000313|Proteomes:UP000008317};
RN [1] {ECO:0000313|EMBL:AEH40897.1, ECO:0000313|Proteomes:UP000008317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cuniculi A {ECO:0000313|EMBL:AEH40897.1,
RC ECO:0000313|Proteomes:UP000008317};
RX PubMed=21655244; DOI=10.1371/journal.pone.0020415;
RA Smajs D., Zobanikova M., Strouhal M., Cejkova D., Dugan-Rocha S.,
RA Pospisilova P., Norris S.J., Albert T., Qin X., Hallsworth-Pepin K.,
RA Buhay C., Muzny D.M., Chen L., Gibbs R.A., Weinstock G.M.;
RT "Complete genome sequence of Treponema paraluiscuniculi, strain Cuniculi A:
RT the loss of infectivity to humans is associated with genome decay.";
RL PLoS ONE 6:E20415-E20415(2011).
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|HAMAP-Rule:MF_00282};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00282};
CC Note=Binds 2 magnesium ions per tetramer. {ECO:0000256|HAMAP-
CC Rule:MF_00282};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000256|HAMAP-Rule:MF_00282}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00282}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Phe-tRNA synthetase alpha subunit type 2 subfamily.
CC {ECO:0000256|ARBA:ARBA00006703, ECO:0000256|HAMAP-Rule:MF_00282}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00282}.
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DR EMBL; CP002103; AEH40897.1; -; Genomic_DNA.
DR RefSeq; WP_013945532.1; NC_015714.1.
DR AlphaFoldDB; F7XR47; -.
DR KEGG; tpl:TPCCA_0973; -.
DR PATRIC; fig|545776.3.peg.980; -.
DR HOGENOM; CLU_025086_2_2_12; -.
DR Proteomes; UP000008317; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00496; PheRS_alpha_core; 1.
DR HAMAP; MF_00282; Phe_tRNA_synth_alpha2; 1.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004529; Phe-tRNA-synth_IIc_asu.
DR InterPro; IPR022917; Phe_tRNA_ligase_alpha_bac/arc.
DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR NCBIfam; TIGR00468; pheS; 1.
DR PANTHER; PTHR11538:SF40; PHENYLALANINE--TRNA LIGASE ALPHA SUBUNIT; 1.
DR PANTHER; PTHR11538; PHENYLALANYL-TRNA SYNTHETASE; 1.
DR Pfam; PF01409; tRNA-synt_2d; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00282};
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00282};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00282};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_00282, ECO:0000313|EMBL:AEH40897.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00282};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00282}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00282};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00282}.
FT DOMAIN 305..544
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT BINDING 400
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00282"
FT BINDING 479
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00282"
FT BINDING 481
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="ligand shared with heterodimeric partner"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00282"
SQ SEQUENCE 553 AA; 61249 MW; 1443F688908A61AA CRC64;
MMPRMTGKAD LNTLVHKLHP LEIKVLKNCA MDEILSTSLL ISRLGFKEGH ANQAFSWLQS
KRIIEEHQRE QMRSFELTPC GYAAASDGTA EERMLTFLSS PPSLTAIADA AEHLHPRPPL
CNGLSLPELA HALTLAPKDV GSAFGILAQE GILRMDGEKR IHIVSPHVSD RMSLTRTLLQ
RAAARVASPS EVSDTPPGTL FESELSDDER RVMERIAKKR GASDSLFKVS VRERVTFTFT
PTARAVQEAL HTAGLTGNEI GALTVECLKS GAWKTQHLRR YNVHIPPARI IPGRSNAYAD
FLEHIKDRLV ALGFQEFDGP LVETDFWNAD ALFMPQFHPA RDIHDVYYLK HPTHAPTIPE
PFLSRVAATH ERGADSGSLG WRYSFDRDFT RRLLLRSQGT ALSARHLPTA HIPGKYFGIA
RCFRHDQVDA THLADFYQTE GIVLGTDVNV CTLLGMLKIL ATEIAGAQEV RYVGGYFPFT
EPSIELHALH PALGWFELGG AGLLRPEVTD PLGVHVPVMA WGLGVDRMAL LALGISDVRE
LFSPDIESVR LRV
//
