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Database: UniProt
Entry: C5DCJ7_LACTC
LinkDB: C5DCJ7_LACTC
Original site: C5DCJ7_LACTC 
ID   C5DCJ7_LACTC            Unreviewed;       405 AA.
AC   C5DCJ7;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 73.
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   OrderedLocusNames=KLTH0B03608g {ECO:0000313|EMBL:CAR21508.1};
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR21508.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR21508.1, ECO:0000313|Proteomes:UP000002036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC   {ECO:0000313|Proteomes:UP000002036};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA   Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA   Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA   Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA   Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA   Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA   Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA   Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA   Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
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; CU928166; CAR21508.1; -; Genomic_DNA.
DR   RefSeq; XP_002551946.1; XM_002551900.1.
DR   AlphaFoldDB; C5DCJ7; -.
DR   STRING; 559295.C5DCJ7; -.
DR   GeneID; 8290779; -.
DR   KEGG; lth:KLTH0B03608g; -.
DR   eggNOG; KOG2144; Eukaryota.
DR   HOGENOM; CLU_035267_0_1_1; -.
DR   InParanoid; C5DCJ7; -.
DR   OMA; RKIHMLA; -.
DR   OrthoDB; 1405752at2759; -.
DR   Proteomes; UP000002036; Chromosome B.
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   CDD; cd00805; TyrRS_core; 1.
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:UP000002036}.
FT   REGION          354..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   405 AA;  45167 MW;  EA7178E5B1ECBDFC CRC64;
     MTGESQTIQD PQAAYELITK NLQEVLNPQI IKNVLEVEKR PLKLYWGTAP TGRPHCGYFV
     PMTKLADFLK AGCEVRVLLA DLHAFLDNMK APLEVVKYRA KYYECVIKSL LRSINVPIEK
     LDFVVGSSYQ LSSEYTMDIF KISNVVSQND AKRAGADVVK QVANPLLSGL IYPLMQALDE
     EHLGVDVQFG GVDQRKIFVL AEENLPSLGY KKRAHLMNPM VPGLTQGGKM SASDPNSKID
     ILEEPKQVKK KINTAFCAPG VVEDNGLLSF IEYVVAPIQE LKHGANYFKF YIDRPEKFGG
     PVTYNSFKEL VEDFKNEKLA PPDLKTGVSD IINELLAPIR EDFAKDPEFQ EAQAKGYPVV
     STEKVKKQKK PKNKGTRYPG GQAPNNDPTA VVAEKLEQTE LKESS
//
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