ID   TBG_USTVI               Reviewed;         469 AA.
AC   P32348;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Tubulin gamma chain;
DE   AltName: Full=Gamma-tubulin;
GN   Name=TUB4;
OS   Microbotryum violaceum (Anther smut fungus) (Ustilago violacea).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX   NCBI_TaxID=5272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A(1) Yellow;
RX   PubMed=8299946; DOI=10.1016/0378-1119(93)90005-n;
RA   Luo H., Perlin M.H.;
RT   "The gamma-tubulin-encoding gene from the basidiomycete fungus, Ustilago
RT   violacea, has a long 5'-untranslated region.";
RL   Gene 137:187-194(1993).
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; X68132; CAA48239.1; -; Genomic_DNA.
DR   PIR; S31727; S31727.
DR   AlphaFoldDB; P32348; -.
DR   SMR; P32348; -.
DR   PRIDE; P32348; -.
DR   PhylomeDB; P32348; -.
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.
FT   CHAIN           1..469
FT                   /note="Tubulin gamma chain"
FT                   /id="PRO_0000048482"
FT   BINDING         142..148
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   469 AA;  52622 MW;  A6AC39B7112D16FC CRC64;
     MPREILTVSA GQAGNQIGSE FWSQLCAEHG ISKEGVLEDW ATDMTDRKDV FFYQADDEHY
     IPRAVMIDLE PRVLDSIKSG PYKNLYNPEN FFYDPQGGGA GNNWAKGYAA GERVYEEVME
     MIDREAEGSD SLEGFMLLHS IAGGTGSGLG SYLLERMNDR YPKKLIQTYS VFPDADSGDV
     VVQPYNSLLS MKRLTNHADS VIVLDNAALS KICQDRLHVQ VASFAQTNQL VSTVMSASTQ
     TLRYPGYMNN DLVGMIASLI PTPRCHFLTT SYTPFTSDKI EQAKAVRKTT VLDVMRRLLQ
     PKNRLVSMPT TPSRHACYIS ILNIIQGEVD PTDVHKSLLR IRERNSATFI PWGPASIQVA
     LTKQSPYVQT THKVSGLMLA NHTNIASIFK RTVAQYDQLR KRNAFMPQYQ KEAMFEKNLD
     EFDEARATVQ DLIEEYQACE KADYIDYGAG PGYVKGEDRR EKGREAVEG