SYYM_YEAST
ID SYYM_YEAST Reviewed; 492 AA.
AC P48527; D6W3R9;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Tyrosine--tRNA ligase, mitochondrial;
DE EC=6.1.1.1 {ECO:0000250|UniProtKB:Q9Y2Z4};
DE AltName: Full=Tyrosyl-tRNA synthetase;
DE Short=TyrRS;
DE Flags: Precursor;
GN Name=MSY1; OrderedLocusNames=YPL097W; ORFNames=LPG11W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 24657 / D273-10B;
RA Hill J.E., Tzagoloff A.A.;
RT "The nuclear gene MSY1 of Saccharomyces cerevisiae codes for mitochondrial
RT tyrosyl-tRNA synthetase.";
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
CC -!- FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-
CC step reaction: tyrosine is first activated by ATP to form Tyr-AMP and
CC then transferred to the acceptor end of tRNA(Tyr).
CC {ECO:0000250|UniProtKB:Q9Y2Z4}.
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:0000250|UniProtKB:Q9Y2Z4};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9Y2Z4}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}.
CC -!- MISCELLANEOUS: Present with 996 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; L42333; AAA67122.1; -; Genomic_DNA.
DR EMBL; U43281; AAB68202.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11335.1; -; Genomic_DNA.
DR PIR; S59733; S59733.
DR RefSeq; NP_015228.1; NM_001183911.1.
DR AlphaFoldDB; P48527; -.
DR SMR; P48527; -.
DR BioGRID; 36083; 25.
DR DIP; DIP-3826N; -.
DR STRING; 4932.YPL097W; -.
DR MaxQB; P48527; -.
DR PaxDb; P48527; -.
DR PRIDE; P48527; -.
DR EnsemblFungi; YPL097W_mRNA; YPL097W; YPL097W.
DR GeneID; 856007; -.
DR KEGG; sce:YPL097W; -.
DR SGD; S000006018; MSY1.
DR VEuPathDB; FungiDB:YPL097W; -.
DR eggNOG; KOG2623; Eukaryota.
DR GeneTree; ENSGT00390000013709; -.
DR HOGENOM; CLU_024003_0_0_1; -.
DR InParanoid; P48527; -.
DR OMA; YMMAKDS; -.
DR BioCyc; YEAST:G3O-34000-MON; -.
DR PRO; PR:P48527; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P48527; protein.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IMP:SGD.
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; IGI:SGD.
DR GO; GO:0070184; P:mitochondrial tyrosyl-tRNA aminoacylation; IGI:SGD.
DR GO; GO:0043039; P:tRNA aminoacylation; IBA:GO_Central.
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 PANTHER; PTHR11766; PTHR11766; 1.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PRINTS; PR01040; TRNASYNTHTYR.
DR TIGRFAMs; TIGR00234; tyrS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Mitochondrion;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..492
FT /note="Tyrosine--tRNA ligase, mitochondrial"
FT /id="PRO_0000035835"
FT MOTIF 94..103
FT /note="'HIGH' region"
FT MOTIF 303..307
FT /note="'KMSKS' region"
FT BINDING 89
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 133
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 239
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 243
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 246
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 265
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 306
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 492 AA; 55287 MW; 2159116E1CB5ED2E CRC64;
MLELRSCSNL VNSSRRLVPL VTYSGLSAIT LPKSRFYSQP SALEVQGTSD SRSDNILDEL
KQRGLVSQVS QPESFLRTKL NGNDKIKLYC GVDPTAQSLH LGNLVPLMVL LHFYVKGHDI
VTVIGGATGK VGDPSGRKTE RDVMENDIRQ SNVASISQQL QRFFKNGLEY YRNRCALTED
VPSGKYTPRN NFNWWKDIKM LDFLADFGRH IRVQSMLARD SISSRLQTKN GLGFNEFTYQ
VLQAYDFYHL YKEENVTIQV GGNDQWGNIT AGIDLINRIQ PIKNKGLPFG ITVPLLTTAT
GEKFGKSAGN AVFIDPSINT AYDVYQFFYN TLDADVPKFL KIFTFLNSSE IKKIVETHIK
SPSLRYGQTL LAKEVTDMLY GVGSGSDSEA LSNIIFGRYD GTLSAAKLVD LCKKARILQY
ADREIDLIKL ICKLVNCSVS EARRKLSQGS VYLHHSKSKV NENISNLAPF LIDDRVLILR
IGKQKCFIIE MR
