ID   Q4U9A6_THEAN            Unreviewed;       774 AA.
AC   Q4U9A6;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=valine--tRNA ligase {ECO:0000256|ARBA:ARBA00013169};
DE            EC=6.1.1.9 {ECO:0000256|ARBA:ARBA00013169};
DE   AltName: Full=Valyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00029936};
GN   ORFNames=TA09105 {ECO:0000313|EMBL:CAI76597.1};
OS   Theileria annulata.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Theileriidae; Theileria.
OX   NCBI_TaxID=5874 {ECO:0000313|EMBL:CAI76597.1, ECO:0000313|Proteomes:UP000001950};
RN   [1] {ECO:0000313|EMBL:CAI76597.1, ECO:0000313|Proteomes:UP000001950}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ankara {ECO:0000313|Proteomes:UP000001950};
RX   PubMed=15994557; DOI=10.1126/science.1110418;
RA   Pain A., Renauld H., Berriman M., Murphy L., Yeats C.A., Weir W.,
RA   Kerhornou A., Aslett M., Bishop R., Bouchier C., Cochet M., Coulson R.M.R.,
RA   Cronin A., de Villiers E.P., Fraser A., Fosker N., Gardner M., Goble A.,
RA   Griffiths-Jones S., Harris D.E., Katzer F., Larke N., Lord A., Maser P.,
RA   McKellar S., Mooney P., Morton F., Nene V., O'Neil S., Price C.,
RA   Quail M.A., Rabbinowitsch E., Rawlings N.D., Rutter S., Saunders D.,
RA   Seeger K., Shah T., Squares R., Squares S., Tivey A., Walker A.R.,
RA   Woodward J., Dobbelaere D.A.E., Langsley G., Rajandream M.A., McKeever D.,
RA   Shiels B., Tait A., Barrell B.G., Hall N.;
RT   "Genome of the host-cell transforming parasite Theileria annulata compared
RT   with T. parva.";
RL   Science 309:131-133(2005).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363035}.
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DR   EMBL; CR940353; CAI76597.1; -; Genomic_DNA.
DR   RefSeq; XP_953222.1; XM_948129.1.
DR   AlphaFoldDB; Q4U9A6; -.
DR   STRING; 5874.Q4U9A6; -.
DR   GeneID; 3863234; -.
DR   KEGG; tan:TA09105; -.
DR   VEuPathDB; PiroplasmaDB:TA09105; -.
DR   eggNOG; KOG0432; Eukaryota.
DR   InParanoid; Q4U9A6; -.
DR   OMA; SNCDFVD; -.
DR   OrthoDB; 227753at2759; -.
DR   Proteomes; UP000001950; Chromosome 4.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004832; F:valine-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:InterPro.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   InterPro; IPR002303; Valyl-tRNA_ligase.
DR   PANTHER; PTHR11946:SF93; VALINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR   PANTHER; PTHR11946; VALYL-TRNA SYNTHETASES; 1.
DR   Pfam; PF00133; tRNA-synt_1; 2.
DR   PRINTS; PR00986; TRNASYNTHVAL.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|RuleBase:RU363035};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363035};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363035};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU363035};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001950}.
FT   DOMAIN          60..415
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          425..514
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   REGION          585..605
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   774 AA;  89872 MW;  0F4E1C195CD447D3 CRC64;
     MNIILICIIK SISCIKTYNF INHNFLNFNI NQDSTSLSHG SVNKLYDSTF ISDSITKGEN
     SLNNDKSEGT VRIITPPPNV TGDLHVGNLL NVVCCDVYKN YLKLKGFDVN INFSNDHAGQ
     SFQKVFDNTY PNLPSGSYKM EMAKLMCQNI RNRHLEDIRK LGIDWEYGHF TMDKHVESLA
     NSVLQRFKTL GLLKEKYWPT HCVNINGKFI PVCSSDIHYS NENITLHVMD KQFEDVNGDK
     INLKVCTPFQ EYYYATTALG VPNDIFQQLK DHQVDLPNLK RRVPIIPISN EINIPNFLKN
     KNMALMLSNG YNYYNPDDEM VILDWNELLN SKVEDIFNET INVTMEVPKY TKDINGKVVI
     LPVLQYVLDT KTLSKKALES LDKINVYPEN RKTMIYNRLK NIKDWCITRH AWWGIKPIID
     IGVDKNDNRV LDTWFTSSLW PIITWNGKTG TSILYTCYDI LENWIVKMLL VCANIDEDKL
     FNEIYLHGMV SDQFGKKMSK SHQNTLVLKD LMESEQTSFD HTLFNINDPD EMIKSNLVRL
     KLCSICSSSD FTKPLNNNFN YQNILFKYYQ IFKFRNSIRN YDSSPENSNS IVNNSNSGLE
     TPNSSPEYDN CGIDLEKIIK SKLFKLVDKI EQDIKKFEFS NCITNLNEYV KVFSEFLVPL
     IRLSVSTNVQ NLEHFDPYFS DLASIIYAFT PEFVNNFKLN DFIKEFKWPH LDTESNELFE
     ELVNIVTNVR KLVKNGQDDL NIKINPKLNT KFNTSYINYL IQLTYNKLPK INYM
//