ID A0A0C2XHS0_HEBCY Unreviewed; 430 AA.
AC A0A0C2XHS0;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Tyrosine--tRNA ligase {ECO:0000256|ARBA:ARBA00013160, ECO:0000256|RuleBase:RU361234};
DE EC=6.1.1.1 {ECO:0000256|ARBA:ARBA00013160, ECO:0000256|RuleBase:RU361234};
DE AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00033323, ECO:0000256|RuleBase:RU361234};
GN ORFNames=M413DRAFT_30884 {ECO:0000313|EMBL:KIM37418.1};
OS Hebeloma cylindrosporum h7.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hymenogastraceae; Hebeloma.
OX NCBI_TaxID=686832 {ECO:0000313|EMBL:KIM37418.1, ECO:0000313|Proteomes:UP000053424};
RN [1] {ECO:0000313|EMBL:KIM37418.1, ECO:0000313|Proteomes:UP000053424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=h7 {ECO:0000313|Proteomes:UP000053424};
RG DOE Joint Genome Institute;
RA Kuo A., Gay G., Dore J., Kohler A., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=h7 {ECO:0000313|Proteomes:UP000053424};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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 ECO:0000256|RuleBase:RU361234};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|RuleBase:RU361234}.
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DR EMBL; KN831797; KIM37418.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2XHS0; -.
DR STRING; 686832.A0A0C2XHS0; -.
DR HOGENOM; CLU_035267_0_1_1; -.
DR OrthoDB; 1405752at2759; -.
DR Proteomes; UP000053424; 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 CDD; cd00805; TyrRS_core; 1.
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:RU361234};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361234};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU361234};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361234};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU361234};
KW Reference proteome {ECO:0000313|Proteomes:UP000053424}.
FT REGION 372..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 430 AA; 47574 MW; 978BCB9F01DF3E5A CRC64;
MTTAEEKYDL ITRRLQEVLG GDSIKAILAE GRQPKCYWGT APTGRPHIGY FVPLTKIADF
LRAGVHVTVL LADVHAFLDN LKAPLELVAH RTKYYEFLLT TVLTSLGIPT SSLRFVEGSS
YQLTREYNLD NYKLCATVSE HDAKKAGAEV VKQVDSPLLS GLLYPGLQAL DEQYLDVDFQ
FGGVDQRKNF TFAELYLPRL GYAKRAHLMN AMVPGLAGGK MSASDPNSKI DFLDSPEVVR
KKLKSAFCEE GNVQENGVLA FVEAVLIPIS QLRLERTSAG SSTVLESGLG DQRPFISDDA
PEGTVFSVER DEKFGGSTHY KTFEEMKVDF ENKQLHPKDL KTSVANGIIR LLEPVRKAFE
ENEEWQRIEK LAYPDPNAKV DKKKKKEKVY HPPPPGKGKT AKPVVDGPSD AAVAHAEAEA
AKQHPEPNSS
//
