ID   TBG_CANAX               Reviewed;         502 AA.
AC   O93807;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Tubulin gamma chain;
DE   AltName: Full=Gamma-tubulin;
GN   Name=TUB4;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Akashi T.;
RT   "A divergent gamma-tubulin gene of the yeast Candida albicans.";
RL   Submitted (SEP-1998) 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.
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; AB017784; BAA74797.1; -; Genomic_DNA.
DR   PDB; 7ANZ; EM; 3.60 A; A/B=1-502.
DR   PDBsum; 7ANZ; -.
DR   AlphaFoldDB; O93807; -.
DR   SMR; O93807; -.
DR   ChEMBL; CHEMBL3988634; -.
DR   VEuPathDB; FungiDB:C4_05570C_A; -.
DR   VEuPathDB; FungiDB:CAWG_03265; -.
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; 3.40.50.1440; -; 1.
DR   InterPro; IPR002454; Gamma_tubulin.
DR   InterPro; IPR008280; Tub_FtsZ_C.
DR   InterPro; IPR000217; Tubulin.
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   SUPFAM; SSF52490; SSF52490; 1.
DR   SUPFAM; SSF55307; SSF55307; 1.
DR   PROSITE; PS00227; TUBULIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Cytoskeleton; GTP-binding; Microtubule;
KW   Nucleotide-binding.
FT   CHAIN           1..502
FT                   /note="Tubulin gamma chain"
FT                   /id="PRO_0000048449"
FT   REGION          51..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          473..502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..70
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         169..175
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   502 AA;  56481 MW;  5B9E499258CA4BD4 CRC64;
     MPGETITLQV GQCGNQVGLQ YWQQLATEHG IQSDGSSTPY PKDINDLQLQ ELNNSGSSPQ
     SYPQQTKPNG KYRNDHPELF FTLSDSNTYT PRSILIDMEP SVIAKSTSAL PMFNPRNVHL
     SNQGNGAANN WINGYKYGTE EEETLLNLID REVDKCDNLS NFQLFHSVAG GTGSGVGSKM
     LEVISDRYGH KKLLNTFSIF PSNEDTSDVV VQPYNTILTL KRLIDYSDAT FVFHNDSLNR
     IENILFNNNS NIQHDDNDLF LGANKLIALV SASVSNPLRF PGYMYSSMES IVSNLIPTPD
     LKFLTSSIAP FSTQKHNYLN EYDMLLELSN DRYKTNRVGG DTSYISMLNY LIGYNLDQRE
     IRKGILKSQQ RISFVPWVAR SVLVVHGKKS PYLKNTNLEG IQVTNNTSMI DVFTKILKQF
     DLLIKRKAYL NRYYSSVEEE NEVMEMFNES RESVKSIIDE YKACKEITYL DDDDEDDLED
     GDGGGGGNGN GYNNIDDADM GI