SYDM_YEAST
ID SYDM_YEAST Reviewed; 658 AA.
AC P15179; D6W3R3;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Aspartate--tRNA ligase, mitochondrial;
DE EC=6.1.1.12 {ECO:0000305|PubMed:2668951};
DE AltName: Full=Aspartyl-tRNA synthetase;
DE Short=AspRS;
GN Name=MSD1; OrderedLocusNames=YPL104W; ORFNames=LPG5W;
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], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=2668951; DOI=10.1073/pnas.86.16.6023;
RA Gampel A., Tzagoloff A.;
RT "Homology of aspartyl- and lysyl-tRNA synthetases.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:6023-6027(1989).
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 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 -!- FUNCTION: Catalyzes the attachment of aspartate to tRNA(Asp) in the
CC mitochondrion. {ECO:0000269|PubMed:2668951}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-
CC aspartyl-tRNA(Asp); Xref=Rhea:RHEA:19649, Rhea:RHEA-COMP:9660,
CC Rhea:RHEA-COMP:9678, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78516,
CC ChEBI:CHEBI:456215; EC=6.1.1.12;
CC Evidence={ECO:0000305|PubMed:2668951};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19650;
CC Evidence={ECO:0000305|PubMed:2668951};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000305|PubMed:2668951}.
CC -!- MISCELLANEOUS: Present with 1550 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type 1 subfamily. {ECO:0000305}.
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DR EMBL; M26020; AAA35137.1; -; Genomic_DNA.
DR EMBL; M24418; AAA35173.1; -; Genomic_DNA.
DR EMBL; U43281; AAB68196.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11329.1; -; Genomic_DNA.
DR PIR; S61963; SYBYDM.
DR RefSeq; NP_015221.1; NM_001183918.1.
DR AlphaFoldDB; P15179; -.
DR SMR; P15179; -.
DR BioGRID; 36077; 83.
DR DIP; DIP-6339N; -.
DR IntAct; P15179; 5.
DR STRING; 4932.YPL104W; -.
DR MaxQB; P15179; -.
DR PaxDb; P15179; -.
DR PRIDE; P15179; -.
DR EnsemblFungi; YPL104W_mRNA; YPL104W; YPL104W.
DR GeneID; 856000; -.
DR KEGG; sce:YPL104W; -.
DR SGD; S000006025; MSD1.
DR VEuPathDB; FungiDB:YPL104W; -.
DR eggNOG; KOG2411; Eukaryota.
DR GeneTree; ENSGT01030000234618; -.
DR HOGENOM; CLU_014330_4_1_1; -.
DR InParanoid; P15179; -.
DR OMA; YQLDVEM; -.
DR BioCyc; YEAST:G3O-34006-MON; -.
DR SABIO-RK; P15179; -.
DR PRO; PR:P15179; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P15179; protein.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IMP:SGD.
DR GO; GO:0004815; F:aspartate-tRNA ligase activity; IMP:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IBA:GO_Central.
DR GO; GO:0070146; P:mitochondrial aspartyl-tRNA aminoacylation; IMP:SGD.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.1360.30; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00044; Asp_tRNA_synth_type1; 1.
DR InterPro; IPR004364; Aa-tRNA-synt_II.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004524; Asp-tRNA-ligase_1.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR004115; GAD-like_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR PANTHER; PTHR22594:SF5; PTHR22594:SF5; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR PRINTS; PR01042; TRNASYNTHASP.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00459; aspS_bact; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Mitochondrion;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..658
FT /note="Aspartate--tRNA ligase, mitochondrial"
FT /id="PRO_0000111015"
FT REGION 226..229
FT /note="Aspartate"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 248..250
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 553
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 560
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 604..607
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 658 AA; 75461 MW; 664081ED6DE24964 CRC64;
MLARSRVCLQ TITRRLADFP EANAIKKKFL FRKDTSTIKQ LKGLSSGQKI VLNGWIEQKP
KRVGKNLIFG LLRDSNGDII QLVDNKSLLK GFTLEDVVQA VGILSLKRKL SNEDADEYEV
QLEDITVLNA SNKKPAQMQD FKLSAIYPPE FRYLQLRNPK YQDFLKKRSS ISKEIRNSFN
NFDFTEVETP MLFKATPEGA REFLVPTRTK RSDGKPSFYA LDQSPQQYKQ LLMASGVNKY
YQMARCFRDE DLRADRQPEF TQVDMEMAFA NSEDVMKIIE KTVSGVWSKF SKKRGLLTLD
SKGTLVPAKK ENGTVSIFRM TYEQAMTSYG IDKPDLRAPD LKIINLGEFN AFSHLNKKFP
VFEVIILRSA FSNMEEYKER WSFLTNNSNY NYRVPIVLPI ENDEQANSNW FENFHAIATF
ENPHLITKFL KLKKGDIVCG CTREPNHSIF ENPTPLGRLR QLVLQSEHGK NIYHAVNKDV
ASWIVDFPLF SPVIIEDKSG KKEKLAYPEY EKDRLCSTHH PFTMVKLKDY EKLEKTPEKC
LGRHYDLVVN GVELGGGSTR IHDPRLQDYI FEDILKIDNA YELFGHLLNA FDMGTPPHAG
FAIGFDRMCA MICETESIRD VIAFPKSITG ADLVVKSPSV IPESILEPYN IKYSNSKK
