ID   TBG_CANGA               Reviewed;         465 AA.
AC   Q6FNU9;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Tubulin gamma chain;
DE   AltName: Full=Gamma-tubulin;
GN   Name=TUB4; OrderedLocusNames=CAGL0J08888g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR380956; CAG61046.1; -; Genomic_DNA.
DR   RefSeq; XP_448095.1; XM_448095.1.
DR   AlphaFoldDB; Q6FNU9; -.
DR   SMR; Q6FNU9; -.
DR   STRING; 5478.XP_448095.1; -.
DR   EnsemblFungi; CAG61046; CAG61046; CAGL0J08888g.
DR   GeneID; 2889469; -.
DR   KEGG; cgr:CAGL0J08888g; -.
DR   CGD; CAL0133032; CAGL0J08888g.
DR   VEuPathDB; FungiDB:CAGL0J08888g; -.
DR   eggNOG; KOG1374; Eukaryota.
DR   HOGENOM; CLU_015718_1_0_1; -.
DR   InParanoid; Q6FNU9; -.
DR   OMA; EHGINKE; -.
DR   Proteomes; UP000002428; Chromosome J.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0008275; C:gamma-tubulin small complex; IEA:EnsemblFungi.
DR   GO; GO:0005822; C:inner plaque of spindle pole body; IEA:EnsemblFungi.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005824; C:outer plaque of spindle pole body; IEA:EnsemblFungi.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:EnsemblFungi.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:InterPro.
DR   GO; GO:0051417; P:microtubule nucleation by spindle pole body; IEA:EnsemblFungi.
DR   GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR   GO; GO:0007052; P:mitotic spindle organization; IEA:EnsemblFungi.
DR   GO; GO:2000767; P:positive regulation of cytoplasmic translation; IEA:EnsemblFungi.
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..465
FT                   /note="Tubulin gamma chain"
FT                   /id="PRO_0000048450"
FT   BINDING         144..150
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   465 AA;  52344 MW;  730825BE406D0F75 CRC64;
     MTGEIITIQV GQCGNHVGKY FWNQLLKEHG IDKDGYSKYN DDLTHIREDD TNPFFKQITN
     NRYVPRAIMI DLEPAAVTDV QSSFNDLFNP RNTWVSSEGL GAGNSWSTGY DRGVQNQDRI
     MDIIDRELDS TDNFEGFQLL HSVAGGTGSG LGSSLLEALT DRYSKSFITT YSVFPSKQSE
     VVVGPYNTVL TLRRLCEDAD ASIIFDNNAL LNLTARTFRD PNTSYEHTNQ LISSALSSIT
     NSLRFPSYMY NSMASIFSTL IPTPELHFLT PNFTPFTPDY IIGGQRYKKN TAYDVLLDLL
     DPFNSLVTQR SDMVTHFNVF STVIGEVDQN HILRALPKMQ QRLNMPSWST SALNVNIGRR
     SPYLPPLESR ENSVSGLMLS NTSAITSVFE RSASAFDKLF YKGAFLNQFE SGQLFQNGLD
     EFVESREVIT RMMEEYSNAE QDTYLDDILN EDDIMIGGFD NEGDS