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Database: UniProt
Entry: G3WEK4_SARHA
LinkDB: G3WEK4_SARHA
Original site: G3WEK4_SARHA 
ID   G3WEK4_SARHA            Unreviewed;       514 AA.
AC   G3WEK4;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 2.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=Tyrosine--tRNA ligase {ECO:0000256|RuleBase:RU361234};
DE            EC=6.1.1.1 {ECO:0000256|RuleBase:RU361234};
DE   AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000256|RuleBase:RU361234};
GN   Name=YARS1 {ECO:0000313|Ensembl:ENSSHAP00000013859.2};
OS   Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX   NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000013859.2, ECO:0000313|Proteomes:UP000007648};
RN   [1] {ECO:0000313|Ensembl:ENSSHAP00000013859.2, ECO:0000313|Proteomes:UP000007648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA   Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA   Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA   Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA   Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA   Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA   Jones M.E., Schuster S.C.;
RT   "Genetic diversity and population structure of the endangered marsupial
RT   Sarcophilus harrisii (Tasmanian devil).";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN   [2] {ECO:0000313|Ensembl:ENSSHAP00000013859.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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:ARBA00034238};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10221;
CC         Evidence={ECO:0000256|ARBA:ARBA00034238};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU361234}.
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DR   AlphaFoldDB; G3WEK4; -.
DR   STRING; 9305.ENSSHAP00000013859; -.
DR   Ensembl; ENSSHAT00000013976.2; ENSSHAP00000013859.2; ENSSHAG00000011851.2.
DR   eggNOG; KOG2144; Eukaryota.
DR   eggNOG; KOG2241; Eukaryota.
DR   GeneTree; ENSGT00940000156949; -.
DR   HOGENOM; CLU_035267_3_0_1; -.
DR   OrthoDB; 1405752at2759; -.
DR   TreeFam; TF300898; -.
DR   Proteomes; UP000007648; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004831; F:tyrosine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd02799; tRNA_bind_EMAP-II_like; 1.
DR   CDD; cd00805; TyrRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 1.10.240.10; Tyrosyl-Transfer RNA Synthetase; 1.
DR   InterPro; IPR002305; aa-tRNA-synth_Ic.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR002547; tRNA-bd_dom.
DR   InterPro; IPR002307; Tyr-tRNA-ligase.
DR   NCBIfam; TIGR00234; tyrS; 1.
DR   PANTHER; PTHR11586; TRNA-AMINOACYLATION COFACTOR ARC1 FAMILY MEMBER; 1.
DR   PANTHER; PTHR11586:SF33; TYROSINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   Pfam; PF00579; tRNA-synt_1b; 1.
DR   Pfam; PF01588; tRNA_bind; 1.
DR   PRINTS; PR01040; TRNASYNTHTYR.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   PROSITE; PS50886; TRBD; 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}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU361234};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007648};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU00209};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|PROSITE-
KW   ProRule:PRU00209}.
FT   DOMAIN          350..454
FT                   /note="TRNA-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50886"
FT   REGION          325..344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   514 AA;  57790 MW;  9F24950B3A02FFC2 CRC64;
     MKRIQEVLGE EKLKEILKQR ELKVYWGTAT TGKPHVAYFV PMSKIADFLK AGCEVTILFA
     DLHAYLDNMK APWELLELRT FYYENVIKAM LESIGVSLEK LKFVKGTDYQ LSKKYTLDVY
     RLSSMVTQHD AKKAGAEVVK QVEHPLLSGL LYPGLQALDE EYLNVDAQFG GVDQRKIFTF
     AEKYLPTLGY SKRIHLMNPM VPGLTGSKMS SSEEESKIDL LDRKEDVKKK LKKAFCEPGN
     VENNGVLAFI RHVLFPLKSE FVILREEKWG GNKTYTAYSE LEKDFANQVV HPGDLKNSVE
     VALNKLLDPI REKFNAPALK KLSSAAYPDP TKQKPAAKAS AKNMEPDVVV PSRLDIRVGK
     VISVEKHPDA DTLYLEKIDV GEPEPRTVVS GLVHFVPKEE LQDRLVVVLC NLKPQKMRGV
     ESQGMLLCAS TEGANRQVEL LDPPQGSAPG ERVFVEGYEQ GQPDEELKPK KKVFEKLQAD
     FQISSERIAQ WKQTNLMTKL GCVSCKTLKG GNIS
//
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