SYNC_YEAST
ID SYNC_YEAST Reviewed; 554 AA.
AC P38707; D3DKW4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Asparagine--tRNA ligase, cytoplasmic {ECO:0000303|PubMed:9605503};
DE EC=6.1.1.22 {ECO:0000269|PubMed:9605503};
DE AltName: Full=Asparaginyl-tRNA synthetase {ECO:0000303|PubMed:9605503};
DE Short=AsnRS {ECO:0000303|PubMed:9605503};
GN Name=DED81 {ECO:0000303|PubMed:9605503}; OrderedLocusNames=YHR019C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [2]
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 [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9605503;
RX DOI=10.1002/(sici)1097-0061(19980430)14:6<527::aid-yea253>3.0.co;2-3;
RA Landrieu I., Vandenbol M., Leberman R., Portetelle D., Hartlein M.;
RT "Identification of YHR019 in Saccharomyces cerevisiae chromosome VIII as
RT the gene for the cytosolic asparaginyl-tRNA synthetase.";
RL Yeast 14:527-533(1998).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Catalyzes the attachment of asparagine to tRNA(Asn) in a two-
CC step reaction: asparagine is first activated by ATP to form Asn-AMP and
CC then transferred to the acceptor end of tRNA(Asn).
CC {ECO:0000269|PubMed:9605503}.
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:9605503};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:9605503}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; U10399; AAB68874.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06708.1; -; Genomic_DNA.
DR PIR; S46775; S46775.
DR RefSeq; NP_011883.1; NM_001179149.1.
DR AlphaFoldDB; P38707; -.
DR SMR; P38707; -.
DR BioGRID; 36448; 275.
DR DIP; DIP-5575N; -.
DR IntAct; P38707; 64.
DR MINT; P38707; -.
DR STRING; 4932.YHR019C; -.
DR iPTMnet; P38707; -.
DR MaxQB; P38707; -.
DR PaxDb; P38707; -.
DR PRIDE; P38707; -.
DR EnsemblFungi; YHR019C_mRNA; YHR019C; YHR019C.
DR GeneID; 856412; -.
DR KEGG; sce:YHR019C; -.
DR SGD; S000001061; DED81.
DR VEuPathDB; FungiDB:YHR019C; -.
DR eggNOG; KOG0555; Eukaryota.
DR GeneTree; ENSGT01030000234618; -.
DR HOGENOM; CLU_004553_2_10_1; -.
DR InParanoid; P38707; -.
DR OMA; CKQHTVR; -.
DR BioCyc; YEAST:G3O-31080-MON; -.
DR PRO; PR:P38707; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38707; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IC: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 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; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..554
FT /note="Asparagine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000176501"
SQ SEQUENCE 554 AA; 62207 MW; 169B6859F694D29C CRC64;
MSSLYIKEAT GVDELTTAGS QDHPFKTPAY ALFASQQKSD ATEPKLFVFK TEDNEYQEIS
ASALKKARKG CDGLKKKAVK QKEQELKKQQ KEAENAAKQL SALNITIKED ESLPAAIKTR
IYDSYSKVGQ RVKVSGWIHR LRSNKKVIFV VLRDGSGFIQ CVLSGDLALA QQTLDLTLES
TVTLYGTIVK LPEGKTAPGG VELNVDYYEV VGLAPGGEDS FTNKIAEGSD PSLLLDQRHL
ALRGDALSAV MKVRAALLKS VRRVYDEEHL TEVTPPCMVQ TQVEGGSTLF KMNYYGEEAY
LTQSSQLYLE TCLASLGDVY TIQESFRAEK SHTRRHLSEY THIEAELAFL TFDDLLQHIE
TLIVKSVQYV LEDPIAGPLV KQLNPNFKAP KAPFMRLQYK DAITWLNEHD IKNEEGEDFK
FGDDIAEAAE RKMTDTIGVP IFLTRFPVEI KSFYMKRCSD DPRVTESVDV LMPNVGEITG
GSMRIDDMDE LMAGFKREGI DTDAYYWFID QRKYGTCPHG GYGIGTERIL AWLCDRFTVR
DCSLYPRFSG RCKP
