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Database: UniProt
Entry: A0A2S4W1R2_9BASI
LinkDB: A0A2S4W1R2_9BASI
Original site: A0A2S4W1R2_9BASI 
ID   A0A2S4W1R2_9BASI        Unreviewed;       446 AA.
AC   A0A2S4W1R2;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
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=PSTT_01881 {ECO:0000313|EMBL:POW15720.1};
OS   Puccinia striiformis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=27350 {ECO:0000313|EMBL:POW15720.1, ECO:0000313|Proteomes:UP000239156};
RN   [1] {ECO:0000313|EMBL:POW15720.1, ECO:0000313|Proteomes:UP000239156}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-210 {ECO:0000313|EMBL:POW15720.1,
RC   ECO:0000313|Proteomes:UP000239156};
RA   Xia C.;
RT   "Gene loss provides genomic basis for host adaptation in cereal stripe rust
RT   fungi.";
RL   Submitted (DEC-2017) 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}.
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:POW15720.1}.
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DR   EMBL; PKSL01000011; POW15720.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S4W1R2; -.
DR   VEuPathDB; FungiDB:PSHT_04546; -.
DR   VEuPathDB; FungiDB:PSTT_01881; -.
DR   Proteomes; UP000239156; 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:UP000239156}.
FT   REGION          369..401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          411..430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..401
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   446 AA;  49987 MW;  FA7DF1B47AFCA7E9 CRC64;
     MSTNAETLNA NERYELITRN LGEVLGSQEL LKLCQEEGRI ITCYWGTATT GRPHIGYFVP
     LTKIADFLRA GVRVKVLLAD VHAFLDNLKA PLELINQRVS YYSHILRAVF TSIGVPIDRL
     EFITGSSYQY STPYNKDCLK LASLVSERDA RKAGSEVVKE SDAPPLSGLL YPLLQALDEE
     YLGVDFQFGG IDQRKIFTFA ELYLPRLGYA KRIHLMNTMV PGLTGTKMSS SDAKSKIDFL
     DTPEDVKKKI KDAVCVPGEI NGNGILAFLE SVLLPIADLK RNMNEDRKSP FASSDAPEGT
     LFSVVRKREK DVLHYTSYTD IVRDYQTEEP VGSGSFKLFP SDLKLSVTNA ILTLLAPIRE
     TYENDPQFKE ANRLAYPDDF QNSSGDGKKK KDKKFTPKPD WVIEKRTSKS IDSMKEVESN
     PDTGFNQNSF DFLKNETCSH NANPIS
//
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