ID   TBG_COCH5               Reviewed;         459 AA.
AC   P40633; M2SYV7;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2013, sequence version 3.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Tubulin gamma chain;
DE   AltName: Full=Gamma-tubulin;
GN   Name=TUB4; ORFNames=COCHEDRAFT_1179534;
OS   Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) (Southern
OS   corn leaf blight fungus) (Bipolaris maydis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=701091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC 48332 / race O;
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC 48332 / race O;
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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 66-330.
RC   STRAIN=C5 / ATCC 48332 / race O;
RA   Parkinson C., Luo H., Knight A., Ahlquist J., Perlin M.H.;
RL   Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Tubulin is the major constituent of microtubules. The gamma
CC       chain is found at microtubule organizing centers (MTOC) such as the
CC       spindle poles or the centrosome, suggesting that it is involved in the
CC       minus-end nucleation of microtubule assembly (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, spindle pole body {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR   EMBL; KB445578; EMD90570.1; -; Genomic_DNA.
DR   EMBL; X74455; CAA52464.1; -; Genomic_DNA.
DR   PIR; S40209; S40209.
DR   AlphaFoldDB; P40633; -.
DR   SMR; P40633; -.
DR   STRING; 701091.P40633; -.
DR   EnsemblFungi; EMD90570; EMD90570; COCHEDRAFT_1179534.
DR   eggNOG; KOG1374; Eukaryota.
DR   HOGENOM; CLU_015718_1_0_1; -.
DR   OMA; EHGINKE; -.
DR   Proteomes; UP000016936; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0000930; C:gamma-tubulin complex; IEA:InterPro.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005816; C:spindle pole body; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:InterPro.
DR   GO; GO:0007020; P:microtubule nucleation; IEA:InterPro.
DR   GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR   CDD; cd02188; gamma_tubulin; 1.
DR   Gene3D; 1.10.287.600; -; 1.
DR   Gene3D; 3.30.1330.20; -; 1.
DR   Gene3D; 3.40.50.1440; -; 1.
DR   InterPro; IPR002454; Gamma_tubulin.
DR   InterPro; IPR008280; Tub_FtsZ_C.
DR   InterPro; IPR000217; Tubulin.
DR   InterPro; IPR037103; Tubulin/FtsZ-like_C.
DR   InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR   InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR   InterPro; IPR023123; Tubulin_C.
DR   InterPro; IPR017975; Tubulin_CS.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR   PANTHER; PTHR11588; PTHR11588; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   Pfam; PF03953; Tubulin_C; 1.
DR   PRINTS; PR01164; GAMMATUBULIN.
DR   PRINTS; PR01161; TUBULIN.
DR   SMART; SM00864; Tubulin; 1.
DR   SMART; SM00865; Tubulin_C; 1.
DR   SUPFAM; SSF52490; SSF52490; 1.
DR   SUPFAM; SSF55307; SSF55307; 1.
DR   PROSITE; PS00227; TUBULIN; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..459
FT                   /note="Tubulin gamma chain"
FT                   /id="PRO_0000048452"
FT   REGION          440..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        441..459
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         142..148
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        67
FT                   /note="L -> A (in Ref. 3; CAA52464)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        119
FT                   /note="L -> W (in Ref. 3; CAA52464)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        221
FT                   /note="N -> T (in Ref. 3; CAA52464)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        246..248
FT                   /note="GYM -> AYS (in Ref. 3; CAA52464)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        274
FT                   /note="Missing (in Ref. 3; CAA52464)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        312
FT                   /note="K -> SH (in Ref. 3; CAA52464)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        325..330
FT                   /note="GEADPS -> AKPTPQ (in Ref. 3; CAA52464)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   459 AA;  51489 MW;  EC25A2DAC8423199 CRC64;
     MPREIITLQA GQCGNSVGQQ FWQQLCQEHG INKDGNLEDF ATEGGDRKDV FFYQSDDTRY
     IPRAILLDLE PRVLHSIQAS PYKNIYNPEN FYIHKDGTGA GNNWGMGYSM GEQVHEDILD
     MIDREADGSD SLEGFMMLHS IAGGTGSGLG SYMLERLNDR FPKKLIQTYS VFPNTQDGDI
     VVQPYNSLLS MRRLTQNADS VVVLDNGALT RIAADRLHVM NPSFEQTNQL VSTVMSASTT
     TLRYPGYMHN DLVGIVASLI PTPRCHFLMT SYTPFSGENV EQAKTVRKTT VLDVMRRLLQ
     PKNRMVSTNP TKKSCYMSIL NIIQGEADPS DVHKSLMRIR ERRLATFIPW GPASIQVALT
     KKSPYVTSSH RVSGLMLANH TGIATLFKRI VAQYSTLRKR NAFLESYKRE VPFKDGLGEF
     DEAKEVVQGL IAEYEEAEDA DYLTKETAPT DEAEDKRAG