SYNM_SCHPO
ID SYNM_SCHPO Reviewed; 441 AA.
AC Q9P6I0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Asparagine--tRNA ligase, mitochondrial;
DE EC=6.1.1.22;
DE AltName: Full=Asparaginyl-tRNA synthetase;
DE Short=AsnRS;
GN Name=slm5; ORFNames=SPBC1198.10c;
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 -!- 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: Mitochondrion {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; CAB91185.1; -; Genomic_DNA.
DR RefSeq; NP_595079.1; NM_001020985.2.
DR AlphaFoldDB; Q9P6I0; -.
DR SMR; Q9P6I0; -.
DR BioGRID; 276188; 11.
DR STRING; 4896.SPBC1198.10c.1; -.
DR MaxQB; Q9P6I0; -.
DR PaxDb; Q9P6I0; -.
DR EnsemblFungi; SPBC1198.10c.1; SPBC1198.10c.1:pep; SPBC1198.10c.
DR GeneID; 2539632; -.
DR KEGG; spo:SPBC1198.10c; -.
DR PomBase; SPBC1198.10c; slm5.
DR VEuPathDB; FungiDB:SPBC1198.10c; -.
DR eggNOG; KOG0554; Eukaryota.
DR HOGENOM; CLU_004553_2_0_1; -.
DR InParanoid; Q9P6I0; -.
DR OMA; DNMDLAE; -.
DR PhylomeDB; Q9P6I0; -.
DR PRO; PR:Q9P6I0; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005759; C:mitochondrial matrix; IC:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0004816; F:asparagine-tRNA ligase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0000049; F:tRNA binding; IC:PomBase.
DR GO; GO:0006421; P:asparaginyl-tRNA aminoacylation; ISS:UniProtKB.
DR GO; GO:0032543; P:mitochondrial 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; Ligase; Mitochondrion;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..441
FT /note="Asparagine--tRNA ligase, mitochondrial"
FT /id="PRO_0000315955"
SQ SEQUENCE 441 AA; 50508 MW; 9F4E037F8157C46C CRC64;
MNKFQLPKTL KSLWHHPHNG ELISINGWVR SIRKLKNVCF AMVSDGTCQQ ALQVVTSPEQ
SKKLSYGASV NIEGQLAVSK NAKLGLQQYE LLAEKIKIYG QINDDNYPIQ KKHLTTEMLR
QIPHLRLRTA KQGEIFRLRS DSLKALRQFF SSKDFTETNP PIITSSDCEG AGEVFTLTPQ
ETHKNKSFER DDQKHFFDRP AFLTVSTQLH LEALALGLSR VYTISPAFRA EQSHTSRHLA
EFWMLEAEVA FMTSLSQLTS LMEDMIKYTL NSLMEQNYHR DHWDQLLKPW KCMTYSEAIE
ELSAVKKTWK YPPKWGNDLS SEHEKYLCEI LHKTPVFVTD YPQKIKPFYM KSSGPDTVAA
VDLLVPQVGE LAGGSLRKDH LDEYKTYPPE LQWYLDLMKY SNAPHGGFGL GIERLIAFLE
GENTNVKETI PFPRSVGSIF A
