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Database: UniProt
Entry: A0A0V0Z833_9BILA
LinkDB: A0A0V0Z833_9BILA
Original site: A0A0V0Z833_9BILA 
ID   A0A0V0Z833_9BILA        Unreviewed;       534 AA.
AC   A0A0V0Z833;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
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};
DE   Flags: Fragment;
GN   Name=yars {ECO:0000313|EMBL:KRY08656.1};
GN   ORFNames=T12_9986 {ECO:0000313|EMBL:KRY08656.1};
OS   Trichinella patagoniensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY08656.1, ECO:0000313|Proteomes:UP000054783};
RN   [1] {ECO:0000313|EMBL:KRY08656.1, ECO:0000313|Proteomes:UP000054783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS2496 {ECO:0000313|EMBL:KRY08656.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
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: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|RuleBase:RU361234}.
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:KRY08656.1}.
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DR   EMBL; JYDQ01000317; KRY08656.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0Z833; -.
DR   STRING; 990121.A0A0V0Z833; -.
DR   Proteomes; UP000054783; 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:UP000054783};
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          372..475
FT                   /note="TRNA-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50886"
FT   NON_TER         534
FT                   /evidence="ECO:0000313|EMBL:KRY08656.1"
SQ   SEQUENCE   534 AA;  60000 MW;  B97EC63A0A4608F8 CRC64;
     MSSLAADEKF QLITRNLQEV LGETVLKDIL KTRNVKIYWG TATTGRPHVG YFVPMSKIAD
     FLKADCEVFT YFIAGDEFGA VTILFADLHA YLDNMKAPWE LLKLRTQYYE TVIKLLLQTV
     GVPLEKLKFV RGTEFQLSRE YTLDVYRISS LVTQHDAKKA GAEVVKQVEY PLLSGLLYPC
     LQALDEEYLK VDAQFGGVDQ RKIFTFSEKY LPSLGYAKRI HLMNPMVPGL TCDKMSASIE
     DSKIDLLDDP ETVKKKLKKA FCEPGNLEKN AVLDFCKHVI FPLLHGEEFS VERDAQAGGN
     IAFSNFSALS ASFADKALHP ADLKTAVAVF INKMLTPIRE KMSEPEMAKL VEAAYPSSKL
     KLNKQKQEAE LTVGRLDMRV GKIVRVRQHE EAENLFVEEI DVGENEPRTV VSGLAQHYHL
     DDLCDRFVVV LCNLKPAKLR GILSNGMVLC ASSESPRRVQ LIEPPDGSSP GDVIYAEGIE
     RHPDDVLNPK KKVWEKIQAD LRTSHNGEPI WKDSILKTNR GPLKKSSLLL TPIK
//
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