ID   SYVM_SCHPO              Reviewed;         950 AA.
AC   O14160;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 2.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Valine--tRNA ligase, mitochondrial;
DE            EC=6.1.1.9;
DE   AltName: Full=Valyl-tRNA synthetase;
DE            Short=ValRS;
DE   Flags: Precursor;
GN   Name=vas1; ORFNames=SPAC4A8.08c;
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-valine + tRNA(Val) = AMP + diphosphate + L-valyl-
CC         tRNA(Val); Xref=Rhea:RHEA:10704, Rhea:RHEA-COMP:9672, Rhea:RHEA-
CC         COMP:9708, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57762,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78537, ChEBI:CHEBI:456215; EC=6.1.1.9;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; CU329670; CAB38577.1; -; Genomic_DNA.
DR   PIR; T38777; T38777.
DR   RefSeq; NP_593819.1; NM_001019249.2.
DR   AlphaFoldDB; O14160; -.
DR   SMR; O14160; -.
DR   BioGRID; 280018; 2.
DR   STRING; 4896.SPAC4A8.08c.1; -.
DR   MaxQB; O14160; -.
DR   PaxDb; O14160; -.
DR   PRIDE; O14160; -.
DR   EnsemblFungi; SPAC4A8.08c.1; SPAC4A8.08c.1:pep; SPAC4A8.08c.
DR   GeneID; 2543603; -.
DR   KEGG; spo:SPAC4A8.08c; -.
DR   PomBase; SPAC4A8.08c; -.
DR   VEuPathDB; FungiDB:SPAC4A8.08c; -.
DR   eggNOG; KOG0432; Eukaryota.
DR   HOGENOM; CLU_001493_0_2_1; -.
DR   InParanoid; O14160; -.
DR   OMA; VMETGWD; -.
DR   PhylomeDB; O14160; -.
DR   BRENDA; 6.1.1.9; 5613.
DR   PRO; PR:O14160; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005759; C:mitochondrial matrix; IC:PomBase.
DR   GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR   GO; GO:0004832; F:valine-tRNA ligase activity; IDA:PomBase.
DR   GO; GO:0070185; P:mitochondrial valyl-tRNA aminoacylation; EXP:PomBase.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd07962; Anticodon_Ia_Val; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   Gene3D; 3.90.740.10; -; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR033705; Anticodon_Ia_Val.
DR   InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   InterPro; IPR002303; Valyl-tRNA_ligase.
DR   PANTHER; PTHR11946; PTHR11946; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   PRINTS; PR00986; TRNASYNTHVAL.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00422; valS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Mitochondrion;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..90
FT                   /note="Mitochondrion"
FT   CHAIN           91..950
FT                   /note="Valine--tRNA ligase, mitochondrial"
FT                   /id="PRO_0000352849"
FT   MOTIF           67..77
FT                   /note="'HIGH' region"
FT   MOTIF           556..560
FT                   /note="'KMSKS' region"
FT   BINDING         559
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   950 AA;  109627 MW;  923B080350E3F40B CRC64;
     MFHFQRSFSS RKAHGLLSFK NRNYIHIEAP FDIAAIQDGW NIIRKHIHYP KPKSIEAPMF
     PILLPPPNIT GKLHIGHALT ITIQDALARF YAMHGYKVSF RPGTDHAGIA TQSVVEKYLQ
     KKGVYRNQLS KDELLSSIHS WQVKYQKSII NQLKSFEAIF DWDNIFYTMD QNRSEAVNEA
     FISLFNAGLI YRANRFVNWC PKLESAVSDI EVESQQINKP VTKYVDNTPV EFGWLYEISY
     QLEGSDNEQL NVSTTRPETI FGDRAIAVSP HDERYKKYVG RFVKHPLIDD LLIPVICDNA
     VDRHFGTGVL KITPMHSIVD YEIAKRHNID CVSIMDKSGN LINCSKEVNG MNRLKARSKI
     VRLLQQRNRL VEQVPHSLIL SVCSRTGDVI EPVMVPQWYL SVDSLKKEVL KSSNKLKLVP
     SLARKEWDSW FKKMGDWCIS RQIWWGHQIP VWKILEEDKW IAAPNYEKAL QLSVGKSVSQ
     DSDVLDTWFS SALLPLSAFG WPKSKDIQPL PFIESGQDIL FFWIARMALL CKYFSNELPF
     KEIILHPLVR DSEGRKMSKS LGNVIDPMDI INGVTLENMK KALLEGNLPI SEVHKSSKQM
     EKAFPNGIPA QGIDIFRYGL FLCLHHEQRI LLDMNSFSDA HRFVSKLWNL ARYFNQYKDK
     ENPLKLTDSQ RQRISLLKMA TYSKLHHAVE GVKESFEQRK FFNAADIMKN FLLNDLSSVY
     VELTRFDVKD SKSSAYEVYR VFSDILHIFL KLIHPIVPCI SGVMLHSKII PERKNSEFLS
     FPTSQQECLL VHDNQAEVVV QNAYDVLIQL RKLESPLNKS PSREHTVYIS TSLEPLKYFY
     DAIEQSTNLK LKSISQEDTI DLMRNQTFIL SRISSDTILL VPKKLYPSKR KKLRKNLDDL
     QKKLDKIQHT TSSSGYEKAP SYIKLKNCEL QKDILVKIQD IKQALLNTEI