ID A0A1L9TR53_9EURO Unreviewed; 387 AA.
AC A0A1L9TR53;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=ASPSYDRAFT_54868 {ECO:0000313|EMBL:OJJ61920.1};
OS Aspergillus sydowii CBS 593.65.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=1036612 {ECO:0000313|EMBL:OJJ61920.1, ECO:0000313|Proteomes:UP000184356};
RN [1] {ECO:0000313|Proteomes:UP000184356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 593.65 {ECO:0000313|Proteomes:UP000184356};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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; KV878583; OJJ61920.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9TR53; -.
DR STRING; 1036612.A0A1L9TR53; -.
DR VEuPathDB; FungiDB:ASPSYDRAFT_54868; -.
DR OrthoDB; 1405752at2759; -.
DR Proteomes; UP000184356; 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: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:UP000184356}.
FT REGION 342..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 387 AA; 42399 MW; 19D040756F06EE21 CRC64;
MDAAAKARLD LITENLAETL NPEIIESILA EGRNPRIYWG TATTGRPHTG YFVAAIKIAQ
LLAAGCEVVV LLADVHAFLD NLKAPLELVE NRAKYYSKVI TAILESVGVP TEKLEFVLGS
SYQKSPEYTM DVYKLSSLVS EHDAKKAGAE IVKQSANAPL SGLLYSILQV LDEEHLKVDA
QLGGMDQRKL FAAAVEWLPK IGYRKRAHLV TPMVAGLSGG KMSSSVHDSK IDLLDPPDVI
SKKIRKAEAA PKVIEDNGVI AMVEFVLLPA AGLKGKKEFV VERRDAEPLV YSDISKLKED
YQNDVLTPQQ LKPAVTAALT SLMAPITEAY QASPEWQQIT EQAYPPPVVE KKQKKVKSKG
TRHPGANKEQ TLPERPKPEA TETETQN
//
