ID   SYV_NEUCR               Reviewed;        1093 AA.
AC   P28350; Q7RVK3;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 155.
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=cyt-20; Synonyms=un-3; ORFNames=NCU01965;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF ARG-201.
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=1830127; DOI=10.1128/mcb.11.8.4022-4035.1991;
RA   Kubelik A.R., Turcq B., Lambowitz A.M.;
RT   "The Neurospora crassa cyt-20 gene encodes cytosolic and mitochondrial
RT   valyl-tRNA synthetases and may have a second function in addition to
RT   protein synthesis.";
RL   Mol. Cell. Biol. 11:4022-4035(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- FUNCTION: May have a second function in addition to protein synthesis.
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. Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=Mitochondrial;
CC         IsoId=P28350-1; Sequence=Displayed;
CC       Name=Cytoplasmic;
CC         IsoId=P28350-2; Sequence=VSP_018909;
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; M64703; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CM002236; EAA35093.3; -; Genomic_DNA.
DR   PIR; A41251; A41251.
DR   RefSeq; XP_964329.3; XM_959236.3. [P28350-1]
DR   AlphaFoldDB; P28350; -.
DR   SMR; P28350; -.
DR   STRING; 5141.EFNCRP00000001058; -.
DR   EnsemblFungi; EAA35093; EAA35093; NCU01965. [P28350-1]
DR   GeneID; 3880494; -.
DR   KEGG; ncr:NCU01965; -.
DR   VEuPathDB; FungiDB:NCU01965; -.
DR   HOGENOM; CLU_001493_0_1_1; -.
DR   InParanoid; P28350; -.
DR   Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004832; F:valine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd07962; Anticodon_Ia_Val; 1.
DR   Gene3D; 1.10.287.380; -; 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; IPR037118; Val-tRNA_synth_C_sf.
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   1: Evidence at protein level;
KW   Alternative initiation; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm;
KW   Ligase; Mitochondrion; Nucleotide-binding; Protein biosynthesis;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..44
FT                   /note="Mitochondrion"
FT   CHAIN           45..1093
FT                   /note="Valine--tRNA ligase, mitochondrial"
FT                   /id="PRO_0000035836"
FT   REGION          40..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           179..189
FT                   /note="'HIGH' region"
FT   MOTIF           692..696
FT                   /note="'KMSKS' region"
FT   COMPBIAS        68..84
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         695
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..43
FT                   /note="Missing (in isoform Cytoplasmic)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_018909"
FT   MUTAGEN         201
FT                   /note="R->C: Gross deficiency of both mitochondrial and
FT                   cytoplasmic ValRS activities."
FT                   /evidence="ECO:0000269|PubMed:1830127"
SQ   SEQUENCE   1093 AA;  123352 MW;  3492E40668CAB42C CRC64;
     MPLSLWRLAI GSSRRHSLLK ITSTRVLPVP RPYSTYSNNK KVIMPGEDQP AAAPAAAPAA
     QDAPGAPAPK KNDKKEKAKA DKAAKFAAKQ AAAKAKQPAA QSAPKEKKEK TPALPPYEDS
     TPAGEKKVIQ SFEHPHFSAY NPSAVEAAWY QWWEKAGYFK PESCRKPSAG KFVIPLPPPN
     VTGALHCGHA LANSLQDTLI RWYRMKGYET LWVPGCDHAG ISTQSVVEKM LWKKEKKIRQ
     ELGREKFTDL VWEWKGEYHQ RINNAQKLMG GSMDWSREAF TMDKNLTAAT METFCRLHDE
     GLIYRSNRLV NWCTHLNTAL SGLEVETKEI TGRTLLDVPG YDKKVEFGVL THFKYQIDGS
     EETIEVATTR PETMLGDTGI AVNPEDPRYT HLVGKFARHP FVDRLLPIVT DNYVDKEFGT
     GAVKLTPAHD FNDYQLGQRH NLEFINILNE NGTLNDNAGP FKGQKRFDAR YTVVEELTKL
     GLFVKKEPNP MKIPLCEKSK DVIEPMMTEQ WWVRMKEMGE AALQVVEEGK VKISPESATK
     SYKRWLADIQ DWCISRQLWW GHRIPAYRVI FEGEEGQREN EKSEWVVGRT QEEAQAKAEA
     KFAGRKFTLE QDPDCLDTWF SSGLWPMAIL GWPNTENLDF KKFFPTSMLE TGWDILFFWV
     SRMIMLSLKM TGEVPFTEVY CHSLIRDSEG RKMSKSLGNV IDPLDIIRGI ELEDLHAKLL
     VGNLKEEEVA RATKYQKTAF PGGIPECGAD AMRFTLLSYT TGGGDINFDI RVMHAYRRFC
     NKIWQASKYV LGKLPQDFMP KGELDTANFS VPEKWILHRM NVAVKGMNEA LEAREFSRAT
     KVAYQFFYDE LCDVFIENSK GILSDGTPEE QQSVQQTLYH ALDVALRLLH PIMPYITEEL
     WQRLPRKQGD GETIMLAPYP AFESQLEFAT EAEDYELGLK CAGGIRSLAA DYNIKSDGRA
     FIKATTADSL ATVSAQLAAI RTLCGKGVKE VNVLGADEEL PRGCAVYVIN AEITVLLQVG
     GSISDIDAEI KKITTKLQKT DLTIKKQQEL LSKDGFEKVS EAVQESEKQK LADAQAAKEN
     YQRTLEEFSK LKI