ID A0A1F5N297_9BACT Unreviewed; 371 AA.
AC A0A1F5N297;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=tyrosine--tRNA ligase {ECO:0000256|ARBA:ARBA00013160};
DE EC=6.1.1.1 {ECO:0000256|ARBA:ARBA00013160};
DE AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00033323};
GN ORFNames=A3H40_01635 {ECO:0000313|EMBL:OGE71693.1};
OS Candidatus Daviesbacteria bacterium RIFCSPLOWO2_02_FULL_38_15.
OC Bacteria; Candidatus Daviesbacteria.
OX NCBI_TaxID=1797794 {ECO:0000313|EMBL:OGE71693.1, ECO:0000313|Proteomes:UP000177057};
RN [1] {ECO:0000313|EMBL:OGE71693.1, ECO:0000313|Proteomes:UP000177057}
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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-
CC tyrosyl-tRNA(Tyr); Xref=Rhea:RHEA:10220, Rhea:RHEA-COMP:9706,
CC Rhea:RHEA-COMP:9707, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58315, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78536, ChEBI:CHEBI:456215; EC=6.1.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000069};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|RuleBase:RU363036}.
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:OGE71693.1}.
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DR EMBL; MFDV01000015; OGE71693.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5N297; -.
DR STRING; 1797794.A3H40_01635; -.
DR Proteomes; UP000177057; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004831; F:tyrosine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:InterPro.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 1.10.240.10; Tyrosyl-Transfer RNA Synthetase; 1.
DR InterPro; IPR002305; aa-tRNA-synth_Ic.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR002307; Tyr-tRNA-ligase.
DR InterPro; IPR023617; Tyr-tRNA-ligase_arc/euk-type.
DR NCBIfam; TIGR00234; tyrS; 1.
DR PANTHER; PTHR46264:SF4; TYROSINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR46264; TYROSINE-TRNA LIGASE; 1.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PIRSF; PIRSF006588; TyrRS_arch_euk; 1.
DR PRINTS; PR01040; TRNASYNTHTYR.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363036};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363036};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363036};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363036};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363036}.
SQ SEQUENCE 371 AA; 41925 MW; 547466658CCD85BC CRC64;
MSPDEKFKLI TRNLEEVLTE EELKSLIESG TPLKHYIGFE ISGKLHLGSL FTLLKVKDLQ
DAGARTIIWL ADLHSAINDK LDGKLETIQK AAKGYFTEAF KALFISIGGN PDKLIFKLCS
ETYAQNPDFW LTLLEIGKTT TLARTKRSIT IMGRGELDDN IPTDKLFYPI MQAADIFLLD
INIAHAGLDQ RKVHVIARDS ANQVKTHALK DNKGNQIKPV AIHHPILLSL TGLPQNVQGE
KDEIAMKSKM SKSKAGSGIS IHDSPEDIQN KINQAYAPEG IIENNPVLNW TKYLVFYEPN
FDFTIKRPEK WGGDLSYSSY EHLEKDYAEK KLHPQDLKAA LAEWLIKKLE PVRKYFEDPT
KKALLDFIIL L
//
