ID   SYNM_YEAST              Reviewed;         492 AA.
AC   P25345; D6VR33;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   27-MAR-2024, entry version 182.
DE   RecName: Full=Asparagine--tRNA ligase, mitochondrial;
DE            EC=6.1.1.22 {ECO:0000269|PubMed:9030748};
DE   AltName: Full=Asparaginyl-tRNA synthetase;
DE            Short=AsnRS;
DE   Flags: Precursor;
GN   Name=SLM5; OrderedLocusNames=YCR024C; ORFNames=YCR242, YCR24C;
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].
RX   PubMed=1574926; DOI=10.1002/yea.320080306;
RA   Bolle P.-A., Gilliquet V., Berben G., Dumont J., Hilger F.;
RT   "The complete sequence of K3B, a 7.9 kb fragment between PGK1 and CRY1 on
RT   chromosome III, reveals the presence of seven open reading frames.";
RL   Yeast 8:205-213(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=1574125; DOI=10.1038/357038a0;
RA   Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA   Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA   Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA   Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA   Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA   Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA   Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA   Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA   Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA   Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA   Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA   Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA   Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA   Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA   Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA   Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA   Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA   Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA   Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA   Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA   Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA   Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA   Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA   Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA   Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA   Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA   Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA   Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA   Sgouros J.G.;
RT   "The complete DNA sequence of yeast chromosome III.";
RL   Nature 357:38-46(1992).
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   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=9030748; DOI=10.1111/j.1432-1033.1997.0268a.x;
RA   Landrieu I., Vandenbol M., Hartlein M., Portetelle D.;
RT   "Mitochondrial asparaginyl-tRNA synthetase is encoded by the yeast nuclear
RT   gene YCR24c.";
RL   Eur. J. Biochem. 243:268-273(1997).
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   -!- FUNCTION: Catalyzes the attachment of asparagine to tRNA(Asn) in the
CC       mitochondrion. {ECO:0000269|PubMed:9030748}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + H(+) + L-
CC         asparaginyl-tRNA(Asn); Xref=Rhea:RHEA:11180, Rhea:RHEA-COMP:9659,
CC         Rhea:RHEA-COMP:9674, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58048, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78515, ChEBI:CHEBI:456215; EC=6.1.1.22;
CC         Evidence={ECO:0000269|PubMed:9030748};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11181;
CC         Evidence={ECO:0000269|PubMed:9030748};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000305|PubMed:9030748}.
CC   -!- MISCELLANEOUS: Present with 784 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; X59720; CAA42316.1; -; Genomic_DNA.
DR   EMBL; BK006937; DAA07502.1; -; Genomic_DNA.
DR   PIR; S19435; S19435.
DR   RefSeq; NP_009953.1; NM_001178738.1.
DR   AlphaFoldDB; P25345; -.
DR   SMR; P25345; -.
DR   BioGRID; 31006; 179.
DR   DIP; DIP-2597N; -.
DR   IntAct; P25345; 4.
DR   MINT; P25345; -.
DR   STRING; 4932.YCR024C; -.
DR   MaxQB; P25345; -.
DR   PaxDb; 4932-YCR024C; -.
DR   PeptideAtlas; P25345; -.
DR   EnsemblFungi; YCR024C_mRNA; YCR024C; YCR024C.
DR   GeneID; 850388; -.
DR   KEGG; sce:YCR024C; -.
DR   AGR; SGD:S000000618; -.
DR   SGD; S000000618; SLM5.
DR   VEuPathDB; FungiDB:YCR024C; -.
DR   eggNOG; KOG0554; Eukaryota.
DR   GeneTree; ENSGT01030000234618; -.
DR   HOGENOM; CLU_004553_2_0_1; -.
DR   InParanoid; P25345; -.
DR   OMA; DNMDLAE; -.
DR   OrthoDB; 2786597at2759; -.
DR   BioCyc; YEAST:G3O-29339-MONOMER; -.
DR   BioGRID-ORCS; 850388; 7 hits in 10 CRISPR screens.
DR   PRO; PR:P25345; -.
DR   Proteomes; UP000002311; Chromosome III.
DR   RNAct; P25345; Protein.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IMP:SGD.
DR   GO; GO:0004816; F:asparagine-tRNA ligase activity; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006421; P:asparaginyl-tRNA aminoacylation; IDA:SGD.
DR   GO; GO:0070145; P:mitochondrial asparaginyl-tRNA aminoacylation; IMP:SGD.
DR   CDD; cd00776; AsxRS_core; 1.
DR   CDD; cd04318; EcAsnRS_like_N; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR004522; Asn-tRNA-ligase.
DR   InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   NCBIfam; TIGR00457; asnS; 1.
DR   PANTHER; PTHR22594:SF34; ASPARAGINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 1.
DR   PRINTS; PR01042; TRNASYNTHASP.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 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;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..492
FT                   /note="Asparagine--tRNA ligase, mitochondrial"
FT                   /id="PRO_0000035801"
SQ   SEQUENCE   492 AA;  56785 MW;  E20C6F921C9BAA9C CRC64;
     MFHAFTFLKG GRFYSSLTVK SLYEQVHHTS HDPISINGWI KSIRLLKRIA FLDLQDGTSV
     NPLRIVIPLT NTDEVQFLKI LKTGQTLSIS NATWQSTPNR KQPFELQIKN PVKSIKLVGP
     VSENYPLQKK YQTLRYLRSL PTLKYRTAYL SAILRLRSFV EFQFMLYFQK NHFTKVSPPI
     LTSNDCEGAG ELFQVSTNTS PTASSYFGKP TYLTVSTQLH LEILALSLSR CWTLSPCFRA
     EKSDTPRHLS EFWMLEVEMC FVNSVNELTS FVETTIKHII KACIDNQQEL LPKQFISSQE
     NNASSELSIN QETQQIKTRW EDLINEKWHN ITYTNAIEIL KKRHNEVSHF KYEPKWGQPL
     QTEHEKFLAG EYFKSPVFVT DYPRLCKPFY MKQNSTPDDT VGCFDLLVPG MGEIIGGSLR
     EDDYDKLCRE MKARGMNRSG ELDWYVSLRK EGSAPHGGFG LGFERFISYL YGNHNIKDAI
     PFYRTSAESI DF
//