ID   L0AWL9_THEEQ            Unreviewed;       564 AA.
AC   L0AWL9;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Tubulin-tyrosine ligase family member protein {ECO:0000313|EMBL:AFZ79935.1};
DE            EC=6.3.2.25 {ECO:0000313|EMBL:AFZ79935.1};
GN   ORFNames=BEWA_027840 {ECO:0000313|EMBL:AFZ79935.1};
OS   Theileria equi strain WA.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Theileriidae; Theileria.
OX   NCBI_TaxID=1537102 {ECO:0000313|EMBL:AFZ79935.1, ECO:0000313|Proteomes:UP000031512};
RN   [1] {ECO:0000313|EMBL:AFZ79935.1, ECO:0000313|Proteomes:UP000031512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WA {ECO:0000313|EMBL:AFZ79935.1,
RC   ECO:0000313|Proteomes:UP000031512};
RX   PubMed=23137308; DOI=10.1186/1471-2164-13-603;
RA   Kappmeyer L.S., Thiagarajan M., Herndon D.R., Ramsay J.D., Caler E.,
RA   Djikeng A., Gillespie J.J., Lau A.O., Roalson E.H., Silva J.C., Silva M.G.,
RA   Suarez C.E., Ueti M.W., Nene V.M., Mealey R.H., Knowles D.P., Brayton K.A.;
RT   "Comparative genomic analysis and phylogenetic position of Theileria
RT   equi.";
RL   BMC Genomics 13:603-603(2012).
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DR   EMBL; CP001669; AFZ79935.1; -; Genomic_DNA.
DR   RefSeq; XP_004829601.1; XM_004829544.1.
DR   AlphaFoldDB; L0AWL9; -.
DR   STRING; 1537102.L0AWL9; -.
DR   EnsemblProtists; AFZ79935; AFZ79935; BEWA_027840.
DR   GeneID; 15807129; -.
DR   KEGG; beq:BEWA_027840; -.
DR   VEuPathDB; PiroplasmaDB:BEWA_027840; -.
DR   eggNOG; KOG2158; Eukaryota.
DR   OrthoDB; 100598at2759; -.
DR   Proteomes; UP000031512; Chromosome 1.
DR   GO; GO:0004835; F:tubulin-tyrosine ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR004344; TTL/TTLL_fam.
DR   PANTHER; PTHR12241; TUBULIN POLYGLUTAMYLASE; 1.
DR   PANTHER; PTHR12241:SF154; TUBULIN POLYGLUTAMYLASE TTLL11; 1.
DR   Pfam; PF03133; TTL; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   PROSITE; PS51221; TTL; 1.
PE   4: Predicted;
KW   Ligase {ECO:0000313|EMBL:AFZ79935.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031512}.
SQ   SEQUENCE   564 AA;  64514 MW;  87A0074AB035E5C8 CRC64;
     MSLVDENAEE SETTLCSPQK YYYKKRPNVN LSQAKNDTCL LGSCLKSLRW KVCNHNVGDI
     YWYGMSITAS QIIDLCSSNK CSNYSKFAVN RYPNLQDATR KDYFYKLLQL HLHYKCNGDE
     HEHGTNAYPP SFTIPRDMKH IVNLLDYKIP FILKPSGGSM GQGVRVATVP EDVTDDLNDY
     IAQEYIANPL LLDGKKFDIR IYILLTGTFE DFSAFISKSS LVRVCTAFYE YPSANNSCNS
     FMHLTNYSIN RLNLSQYHRG KDIYDVNNNK RPLDSVLNHL EKYGYKKKNI WTQIKQIAEN
     VASALYPHIS INSGCLSGTR NPPKLFQILG LDVIIDIYGK AWLLEVNSNP SLKTTYCDGN
     ITRDDPVDLS IKLPVVRDFL TIVNNSLSNV DAIPESCEVI KVTIPTQVHI FVQLYKLTKL
     GTWTSCRITR TEWLAFCRRT KLVELAKVYA LLRSHNVPQG DENHETNVTG KRILLDLFSE
     YRRENGVPGV CFLRFSQMLE SLALIFYENF ALLRPSAVER LCGLTGVPSQ LLLNWSVNQP
     DILDKKGIKQ ATQRLFYHFK QQFL
//