SYNM_YEAST
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 03-AUG-2022, entry version 175.
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; 170.
DR DIP; DIP-2597N; -.
DR IntAct; P25345; 4.
DR MINT; P25345; -.
DR STRING; 4932.YCR024C; -.
DR MaxQB; P25345; -.
DR PaxDb; P25345; -.
DR PRIDE; P25345; -.
DR EnsemblFungi; YCR024C_mRNA; YCR024C; YCR024C.
DR GeneID; 850388; -.
DR KEGG; sce:YCR024C; -.
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 BioCyc; YEAST:G3O-29339-MON; -.
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 Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.930.10; -; 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 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; TIGR00457; asnS; 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
