SYTM_YEAST
ID SYTM_YEAST Reviewed; 462 AA.
AC P07236; D6VX06;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Threonine--tRNA ligase, mitochondrial;
DE EC=6.1.1.3;
DE AltName: Full=Threonyl-tRNA synthetase;
DE Short=ThrRS;
DE Flags: Precursor;
GN Name=MST1; OrderedLocusNames=YKL194C;
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 [MRNA].
RX PubMed=2999113; DOI=10.1016/s0021-9258(18)95745-5;
RA Pape L.K., Koerner T.J., Tzagoloff A.;
RT "Characterization of a yeast nuclear gene (MST1) coding for the
RT mitochondrial threonyl-tRNA1 synthetase.";
RL J. Biol. Chem. 260:15362-15370(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
RC STRAIN=ATCC 200358 / YNN 295;
RX PubMed=7791785; DOI=10.1128/mcb.15.7.3777;
RA Mackelvie S.H., Andrews P.D., Stark M.J.R.;
RT "The Saccharomyces cerevisiae gene SDS22 encodes a potential regulator of
RT the mitotic function of yeast type 1 protein phosphatase.";
RL Mol. Cell. Biol. 15:3777-3785(1995).
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-
CC threonyl-tRNA(Thr); Xref=Rhea:RHEA:24624, Rhea:RHEA-COMP:9670,
CC Rhea:RHEA-COMP:9704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57926, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78534, ChEBI:CHEBI:456215; EC=6.1.1.3;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- MISCELLANEOUS: Present with 1240 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; M12087; AAA34808.1; -; mRNA.
DR EMBL; Z28194; CAA82038.1; -; Genomic_DNA.
DR EMBL; X83609; CAA58589.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA08972.1; -; Genomic_DNA.
DR PIR; S38031; YSBYTM.
DR RefSeq; NP_012727.1; NM_001179760.1.
DR PDB; 3UGQ; X-ray; 2.10 A; A=26-462.
DR PDB; 3UGT; X-ray; 3.60 A; A/B/C/D=26-462.
DR PDB; 3UH0; X-ray; 2.00 A; A=26-462.
DR PDB; 4EO4; X-ray; 2.87 A; A/B/C/D=26-462.
DR PDB; 4YYE; X-ray; 2.30 A; A/B=26-462.
DR PDBsum; 3UGQ; -.
DR PDBsum; 3UGT; -.
DR PDBsum; 3UH0; -.
DR PDBsum; 4EO4; -.
DR PDBsum; 4YYE; -.
DR AlphaFoldDB; P07236; -.
DR SMR; P07236; -.
DR BioGRID; 33927; 34.
DR DIP; DIP-4855N; -.
DR IntAct; P07236; 1.
DR MINT; P07236; -.
DR STRING; 4932.YKL194C; -.
DR MaxQB; P07236; -.
DR PaxDb; P07236; -.
DR PRIDE; P07236; -.
DR EnsemblFungi; YKL194C_mRNA; YKL194C; YKL194C.
DR GeneID; 853640; -.
DR KEGG; sce:YKL194C; -.
DR SGD; S000001677; MST1.
DR VEuPathDB; FungiDB:YKL194C; -.
DR eggNOG; KOG1637; Eukaryota.
DR HOGENOM; CLU_008554_2_1_1; -.
DR InParanoid; P07236; -.
DR OMA; QIDFHQP; -.
DR BioCyc; YEAST:G3O-31956-MON; -.
DR BRENDA; 6.1.1.3; 984.
DR PRO; PR:P07236; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P07236; protein.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004829; F:threonine-tRNA ligase activity; IDA:SGD.
DR GO; GO:0070159; P:mitochondrial threonyl-tRNA aminoacylation; IDA:SGD.
DR GO; GO:0006435; P:threonyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd00771; ThrRS_core; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR002320; Thr-tRNA-ligase_IIa.
DR InterPro; IPR033728; ThrRS_core.
DR PANTHER; PTHR11451; PTHR11451; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PRINTS; PR01047; TRNASYNTHTHR.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00418; thrS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Ligase;
KW Mitochondrion; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..45
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 46..462
FT /note="Threonine--tRNA ligase, mitochondrial"
FT /id="PRO_0000035827"
FT CONFLICT 265
FT /note="G -> S (in Ref. 1; AAA34808)"
FT /evidence="ECO:0000305"
FT HELIX 35..46
FT /evidence="ECO:0007829|PDB:3UH0"
FT HELIX 63..82
FT /evidence="ECO:0007829|PDB:3UH0"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:3UH0"
FT HELIX 97..102
FT /evidence="ECO:0007829|PDB:3UH0"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:3UH0"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:3UH0"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:3UGQ"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:3UGQ"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:3UH0"
FT HELIX 133..140
FT /evidence="ECO:0007829|PDB:3UH0"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:3UH0"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:3UH0"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:3UH0"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:3UH0"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:3UH0"
FT STRAND 176..187
FT /evidence="ECO:0007829|PDB:3UH0"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:3UH0"
FT HELIX 192..207
FT /evidence="ECO:0007829|PDB:3UH0"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:3UH0"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:3UH0"
FT HELIX 239..256
FT /evidence="ECO:0007829|PDB:3UH0"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:3UH0"
FT STRAND 273..279
FT /evidence="ECO:0007829|PDB:3UH0"
FT STRAND 285..295
FT /evidence="ECO:0007829|PDB:3UH0"
FT HELIX 296..300
FT /evidence="ECO:0007829|PDB:3UH0"
FT STRAND 316..325
FT /evidence="ECO:0007829|PDB:3UH0"
FT HELIX 326..337
FT /evidence="ECO:0007829|PDB:3UH0"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:3UH0"
FT STRAND 350..356
FT /evidence="ECO:0007829|PDB:3UH0"
FT HELIX 360..374
FT /evidence="ECO:0007829|PDB:3UH0"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:4EO4"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:3UH0"
FT HELIX 403..413
FT /evidence="ECO:0007829|PDB:3UH0"
FT STRAND 416..421
FT /evidence="ECO:0007829|PDB:3UH0"
FT HELIX 423..428
FT /evidence="ECO:0007829|PDB:3UH0"
FT STRAND 431..435
FT /evidence="ECO:0007829|PDB:3UH0"
FT HELIX 436..438
FT /evidence="ECO:0007829|PDB:3UH0"
FT STRAND 443..445
FT /evidence="ECO:0007829|PDB:3UH0"
FT HELIX 447..459
FT /evidence="ECO:0007829|PDB:3UH0"
SQ SEQUENCE 462 AA; 54092 MW; BC90DED57EB037BF CRC64;
MKIQLVRWHC SRNALWNRAF YSTRKATKNA SSATPATMTS MVSQRQDLFM TDPLSPGSMF
FLPNGAKIFN KLIEFMKLQQ KFKFGFNEVV TPLIYKKTLW EKSGHWENYA DDMFKVETTD
EEKEEYGLKP MNCPGHCLIF GKKDRSYNEL PLRFSDFSPL HRNEASGALS GLTRLRKFHQ
DDGHIFCTPS QVKSEIFNSL KLIDIVYNKI FPFVKGGSGA ESNYFINFST RPDHFIGDLK
VWNHAEQVLK EILEESGKPW KLNPGDGAFY GPKLDIMVTD HLRKTHQVAT IQLDFQLPER
FDLKFKDQDN SYKRPIMIHR ATFGSIERFM ALLIDSNEGR WPFWLNPYQA VIIPVNTKNV
QQLDMCTALQ KKLRNELEAD DMEPVPLNDW HFNVDLDIRN EPVGYRIKSA ILKNYSYLII
VGDEEVQLQK YNIRERDNRK SFEKLTMSQI WEKFIELEKN YK
