ID   SYYM_PODAS              Reviewed;         640 AA.
AC   P28669;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Tyrosine--tRNA ligase, mitochondrial;
DE            EC=6.1.1.1;
DE   AltName: Full=Tyrosyl-tRNA synthetase;
DE            Short=TyrRS;
DE   Flags: Precursor;
GN   Name=YTS1;
OS   Podospora anserina (Pleurage anserina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Podosporaceae; Podospora.
OX   NCBI_TaxID=2587412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=s;
RX   PubMed=1531084; DOI=10.1128/mcb.12.2.499-511.1992;
RA   Kaempfer U., Kueck U., Cherniak A.D., Lambowitz A.M.;
RT   "The mitochondrial tyrosyl-tRNA synthetase of Podospora anserina is a
RT   bifunctional enzyme active in protein synthesis and RNA splicing.";
RL   Mol. Cell. Biol. 12:499-511(1992).
CC   -!- FUNCTION: Has both an aminoacyl-tRNA synthetase activity and is
CC       involved in the splicing of group I introns.
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   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; X54981; CAA38725.1; -; Genomic_DNA.
DR   PIR; A42019; A42019.
DR   AlphaFoldDB; P28669; -.
DR   SMR; P28669; -.
DR   PRIDE; P28669; -.
DR   VEuPathDB; FungiDB:PODANS_1_3320; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0004831; F:tyrosine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00805; TyrRS_core; 1.
DR   Gene3D; 3.10.290.10; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002305; aa-tRNA-synth_Ic.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR036986; S4_RNA-bd_sf.
DR   InterPro; IPR002307; Tyr-tRNA-ligase.
DR   InterPro; IPR024088; Tyr-tRNA-ligase_bac-type.
DR   InterPro; IPR032005; TyrRSs_C.
DR   PANTHER; PTHR11766; PTHR11766; 1.
DR   Pfam; PF00579; tRNA-synt_1b; 1.
DR   Pfam; PF16714; TyrRSs_C; 1.
DR   PRINTS; PR01040; TRNASYNTHTYR.
DR   TIGRFAMs; TIGR00234; tyrS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Mitochondrion;
KW   mRNA processing; Nucleotide-binding; Protein biosynthesis; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..640
FT                   /note="Tyrosine--tRNA ligase, mitochondrial"
FT                   /id="PRO_0000035834"
FT   MOTIF           105..114
FT                   /note="'HIGH' region"
FT   MOTIF           322..326
FT                   /note="'KMSKS' region"
FT   BINDING         100
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT   BINDING         104
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT   BINDING         144
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT   BINDING         248
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT   BINDING         252
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT   BINDING         255
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT   BINDING         274
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT   BINDING         325
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   640 AA;  72406 MW;  1DBA1C469FF5E3C6 CRC64;
     MSMSRGSVCR RCLLTMKSMA GGGPTSTYAQ QRGKKTWHGP KYQAKIDQAQ ADWEERAEKI
     KKGEIQHTWD MFVERGYVKD TAGSHETIRK LMLHKRIGAY TGIDPTAPSL HIGHLLPLMP
     IFWMYMHGYA GYTLIGGATA KIGDPTDRLV SRTPLKRTDL TMNLTKIHYQ LKALWMNVEE
     QARRRGFEKD WAWKRAVVNN STWWNSLPLI EVLKRLGDSM RMGPLLSRDT VKNKMSKGDG
     MSFSEFTYPL MQGWDWWHMY QANGIQMQIG GSDQYGNIVT GVETVKVVRD NEPDPAKKIE
     GGPFNDPVGF TVPLLTDSAG VKFGKSAGNA FLDKFQTSEF DLYGYFVRRS DQEVEKLLKL
     FTFLPMENIN EAMKIHSENP ARRVAQHLLA FEVVGLVHGM NAAHRTALNH QARYGKQIDI
     PGVTLRMPKA ATEDTPPSIL DAPKMDMQLP ESLIMGKSIG RILYAAGLAK SASEGHRLAT
     QQGAYIGAMP GHKRTEDNKV MDYSQLSFTP IKLWFPQETR NYLIDGKLLI LRKGKVQIRV
     IEMVSDEEWK ESGQTYPGEP GTGALRMLRQ QLKMLKSGML TPDEVKANLK NHVEEEAPPP
     GFMKFPDQDS YAIRRATQEL MDEIHQKEVG GDSPREERRE