ID   W6ZCA4_COCMI            Unreviewed;       471 AA.
AC   W6ZCA4;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Tubulin-tyrosine ligase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=COCMIDRAFT_24749 {ECO:0000313|EMBL:EUC47433.1};
OS   Bipolaris oryzae ATCC 44560.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=930090 {ECO:0000313|EMBL:EUC47433.1};
RN   [1] {ECO:0000313|EMBL:EUC47433.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC47433.1};
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA   Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA   Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA   LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA   Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector coding
RT   capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(2013).
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DR   EMBL; KI963953; EUC47433.1; -; Genomic_DNA.
DR   RefSeq; XP_007686076.1; XM_007687886.1.
DR   AlphaFoldDB; W6ZCA4; -.
DR   STRING; 930090.W6ZCA4; -.
DR   GeneID; 19120633; -.
DR   KEGG; bor:COCMIDRAFT_24749; -.
DR   eggNOG; KOG2157; Eukaryota.
DR   HOGENOM; CLU_031301_0_0_1; -.
DR   OrthoDB; 100598at2759; -.
DR   Proteomes; UP000054032; Unassembled WGS sequence.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR027746; TTL.
DR   InterPro; IPR004344; TTL/TTLL_fam.
DR   PANTHER; PTHR47551; TUBULIN--TYROSINE LIGASE PBY1-RELATED; 1.
DR   PANTHER; PTHR47551:SF1; TUBULIN--TYROSINE LIGASE PBY1-RELATED; 1.
DR   Pfam; PF03133; TTL; 2.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   PROSITE; PS51221; TTL; 1.
PE   4: Predicted;
FT   REGION          190..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        190..206
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   471 AA;  52877 MW;  9B74CC9C9567E469 CRC64;
     MASSGSKIGD KIYALINYED LYVQPLILSA LEKRLPTSSY ELITSLSQLP TPSSPLLQFV
     QYESIDFDHL MEYSSTSLAN AYVIRKALIR KHYLSTTIAN WITKYPDSVL KKHVKPSVEF
     EVDYAEFLDD ALVEAWELKE SWARNEELGD DEDGASSSKK EWWILKPGMS DRGQGIRLFS
     SEQELTEIFE EWDPDSDDED EEEDARSDSN AQQLKIEKDE DNGIITSQLR HFIAQPYIHP
     PLLLTPPNNP TSDLRKFHIR TYILAAGALK LYVYKPMLAL FAAHPYLPPW SADVEPNSQK
     AMRAHLTNTC LQDSGDREGS VGLFWDLPDS LPAQPDFSGS SNSEGGDAER KVNVPSNWKD
     AIFQQICDIT GSTFEAAARG MSIHFQPLPN SFEVFGLDFM VGLDEETGGL NTWLLEVNAF
     PDFRQTGSDL QGLVNGLMEG VVEKGIKPFF GLEGAENEDM VEVLNVDLGR R
//