ID   SYNC_SCHPO              Reviewed;         568 AA.
AC   O94567;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Probable asparagine--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.22;
DE   AltName: Full=Asparaginyl-tRNA synthetase;
DE            Short=AsnRS;
GN   Name=nrs1; Synonyms=ded81; ORFNames=SPBC1773.10c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Cytosolic asparaginyl-tRNA synthetase which catalyzes the
CC       specific attachment of asparagine to its cognate tRNA. {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; CU329671; CAA21915.1; -; Genomic_DNA.
DR   PIR; T39675; T39675.
DR   RefSeq; NP_595125.1; NM_001021032.2.
DR   AlphaFoldDB; O94567; -.
DR   SMR; O94567; -.
DR   BioGRID; 276584; 10.
DR   STRING; 4896.SPBC1773.10c.1; -.
DR   iPTMnet; O94567; -.
DR   MaxQB; O94567; -.
DR   PaxDb; O94567; -.
DR   PRIDE; O94567; -.
DR   EnsemblFungi; SPBC1773.10c.1; SPBC1773.10c.1:pep; SPBC1773.10c.
DR   GeneID; 2540046; -.
DR   KEGG; spo:SPBC1773.10c; -.
DR   PomBase; SPBC1773.10c; nrs1.
DR   VEuPathDB; FungiDB:SPBC1773.10c; -.
DR   eggNOG; KOG0555; Eukaryota.
DR   HOGENOM; CLU_004553_2_10_1; -.
DR   InParanoid; O94567; -.
DR   OMA; CKQHTVR; -.
DR   PhylomeDB; O94567; -.
DR   PRO; PR:O94567; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0004816; F:asparagine-tRNA ligase activity; ISS:PomBase.
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; IMP:PomBase.
DR   GO; GO:0002181; P:cytoplasmic translation; NAS:PomBase.
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   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..568
FT                   /note="Probable asparagine--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000176499"
SQ   SEQUENCE   568 AA;  63870 MW;  934483A10962BCAC CRC64;
     MAGLESKVSD MKIKSDVVFY IDEASGNDET GNGSQTSPFK TAIHALETDA NCTIFVKKNG
     SEEFEPITTN ALKKAKKGVE QAAKKKAKAA EAEAAAAARA AAAKEAEAKR LEAAKNIVLK
     EPKDAPAAKK IAIIDSTNFR DSRVRVNGWV HRMRTQKGII FIILRDGTGF LQCVLSGKVY
     DRASYDFINL GPESTVCLYG VIKELPEGKS APGNHELVVD YYQILHAAPT GEEAFTNRLN
     AEAEPSYLLD QRHLVIRGET ASSVLKVRAR ALRAMRDTFE NLKMTEVTPP CMVQTQVEGG
     ATLFKFNYYG QDAYLTQSSQ LYLEAALPAL GSVYTIQESF RAEKSLTRRH LSEFTHVEFE
     LPFVNFGEFL EIIEEFICQT IDRLLDDPIA TPLIKQLNPD FVKPSRPFMR LSYEDAIKYL
     NEHNILTPEG EQHKFGDDIA EAAERKMTDQ INRPIFLTYF PLEIKSFYMK RVVDRPELTE
     SVDCLMPNVG EIVGGSMRIS DIQELLAAYK REGIDPAPYY WFTEQRKYGT TEHGGCGLGL
     ERFLAWLCDR YTVRECCLFP RFTERCTP