ID   SYV_SCHPO               Reviewed;         980 AA.
AC   O75005;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Valine--tRNA ligase;
DE            EC=6.1.1.9;
DE   AltName: Full=Valyl-tRNA synthetase;
DE            Short=ValRS;
GN   Name=vas2; ORFNames=SPBC1709.02c, SPBC1734.18c;
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: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CU329671; CAA21312.1; -; Genomic_DNA.
DR   PIR; T39630; T39630.
DR   RefSeq; NP_595435.1; NM_001021343.2.
DR   AlphaFoldDB; O75005; -.
DR   SMR; O75005; -.
DR   BioGRID; 276730; 4.
DR   STRING; 4896.SPBC1709.02c.1; -.
DR   iPTMnet; O75005; -.
DR   MaxQB; O75005; -.
DR   PaxDb; O75005; -.
DR   PRIDE; O75005; -.
DR   EnsemblFungi; SPBC1709.02c.1; SPBC1709.02c.1:pep; SPBC1709.02c.
DR   GeneID; 2540197; -.
DR   KEGG; spo:SPBC1709.02c; -.
DR   PomBase; SPBC1709.02c; -.
DR   VEuPathDB; FungiDB:SPBC1709.02c; -.
DR   eggNOG; KOG0432; Eukaryota.
DR   HOGENOM; CLU_001493_0_1_1; -.
DR   InParanoid; O75005; -.
DR   OMA; FATKLWN; -.
DR   PhylomeDB; O75005; -.
DR   BRENDA; 6.1.1.9; 5613.
DR   PRO; PR:O75005; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; IGI:PomBase.
DR   GO; GO:0005829; C:cytosol; 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:0002181; P:cytoplasmic translation; NAS:PomBase.
DR   GO; GO:0061475; P:cytosolic 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   HAMAP; MF_02004; Val_tRNA_synth_type1; 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; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..980
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000035838"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           139..149
FT                   /note="'HIGH' region"
FT   MOTIF           652..656
FT                   /note="'KMSKS' region"
FT   COMPBIAS        22..40
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         655
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   980 AA;  111317 MW;  BB91FAF976030C3C CRC64;
     MADKGCEAAQ SKDSSAPGSG EPRPKTEKEL ERERQKAAKL EKYHAKLAAK KAKEEARKPK
     LDKKAKIASP VAEYVEKTTP GEKKVLQDLD SPALKSYNPK AVESAWYDWW VKSGFFEPEF
     GPDGKPKKEG VFVITSPPPN VTGALHIGHA LTIAIQDSLA RWNRMLGKTV LFLGGFDHAG
     LSTQSVVEKK LWYTQKKTRH DYPRDKFVDI VWEWKEEYHN RIKNQMSRLG GSFDWTREAF
     TMDENLSRAV VETFVRLHEE NIIYRANRLV NWCTALQTTL SNLEVENVDV PGRTLLKVPG
     YDEPVEVGVL TSIAYAVEGS DERIVIATTR PETLLGDTAV AVHPQDPRYK HLHGKFVKHP
     FCNRSIPIIC DDIIVDMEFG TGAVKITPAH DPNDYEVGKR HNLEFINIFT DDGLLNENCG
     EFAGMKRFTA RVKVVERLKE LGLFVGTKEN PMVIPLCGKT SDIIEPVMKP QWWVNQKEMA
     AAAAEVVKSG EIEIAPDMSR REFIRWMENI QDWCISRQLW WGHRIPAYFV NLADEPSQDR
     SEGRYWVTGR TLEQAEEKAK AAFPGKSFTL EQDEDVLDTW FSSGLWPFST LGWPKDTSDY
     ENFYPTTLME TGWDILFFWI ARMVMLGLKL TGKIPFKRVF CHALVRDAQG RKMSKSLGNV
     VDPIDVIEGI SLQALHDKLL VGNLDSREVE KAKKGQRLSY PKGIPQCGTD ALRFTLCSLT
     TGGRDLNLDI LRVEGYRKFC NKLYNATKFA LGRLGSNFVP NKTADLTGNE SLVEKWIFHR
     LNIAAAAMNK NMEEMNFLQA TSAVHQFWLY ELCDVYIENS KYLLSDGTEV QQESAKQTLY
     TVLDNALRLM HPFMPYVTEE MWQRLPRRPG DKTQTIVKAA FPVERVDYSN EIAAKYYESI
     ITVVHSTRSM MAENGIKSDA VVYIHPDEEH SKLITSESAS IQSLIKKCKT LSIVDNTFDS
     DKCVKNEVLE GSTIFLERNN