ID   TBG_EUPAE               Reviewed;         461 AA.
AC   P54402;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Tubulin gamma chain;
DE   AltName: Full=Gamma-tubulin;
OS   Euplotes aediculatus (Ciliate).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Hypotrichia; Euplotida; Euplotidae; Euplotes.
OX   NCBI_TaxID=5940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Tan M., Heckmann K., Weiligmann C.;
RL   Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Tan M., Heckmann K.;
RL   Submitted (NOV-1996) 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, centrosome {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR   EMBL; X85233; CAA59488.1; -; Genomic_DNA.
DR   EMBL; Y09549; CAA70740.1; -; mRNA.
DR   AlphaFoldDB; P54402; -.
DR   SMR; P54402; -.
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: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   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding.
FT   CHAIN           1..461
FT                   /note="Tubulin gamma chain"
FT                   /id="PRO_0000048459"
FT   BINDING         142..148
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   461 AA;  52102 MW;  C4352AED558F64CA CRC64;
     MPREIITCQV GQCGNQIGME FWKQLCMEHG INPEGILEDF AVNGEDRKDV FFYQADDEHY
     VPRAVLIDLE PRVINCIQKS TYSSLYNPEN IYIAKHGGGA GNNWGRGYTD AEKVQDEILE
     MIDREADGSD SLEGFVLTHS IAGGTGSGFG SYLLERINDH YPKKLIQTYS VFPIENDVVV
     QPYNCLLSIK RLTLNADCVV VLDNNALTSI AVDRLKILQP TFSQINSIVS TVMAASTTTL
     RYPGYMNNDM VGLIASLVPT PRCHFLMTGY TPLSLDQKYT SVRKTTFLDV MRRLLQTKNI
     MVTGAVKKGA YMSILNVIQG DVDPTQVHKS LQRIKERKLA NFIPWGPASI QVALAKKSPY
     IDSGHKVSGL MLANHTGIRS IFKVLYDQYR TFRKRDAYMN IFKQTKIFED NLDEFDSSDE
     VVKNLIDEYA AAEKMDYINW GNDDDDMQFD PREPPKFSNI Q