ID   TBG_PLAFO               Reviewed;         452 AA.
AC   P34787;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Tubulin gamma chain;
DE   AltName: Full=Gamma-tubulin;
GN   Name=G-TUB;
OS   Plasmodium falciparum (isolate NF54).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=5843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8366893; DOI=10.1016/0166-6851(93)90025-s;
RA   Maessen G.D.F., Wesseling J.G., Smits M.A., Konings R.N.H.,
RA   Schoenmakers J.G.G.;
RT   "The gamma-tubulin gene of the malaria parasite Plasmodium falciparum.";
RL   Mol. Biochem. Parasitol. 60:27-36(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, centrosome {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR   EMBL; X62393; CAA44265.1; -; mRNA.
DR   AlphaFoldDB; P34787; -.
DR   SMR; P34787; -.
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..452
FT                   /note="Tubulin gamma chain"
FT                   /id="PRO_0000048477"
FT   BINDING         142..148
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   452 AA;  51538 MW;  3C16D41534A03294 CRC64;
     MPREIITLQC GQCGNQIGVE FWKQLCNEHN IDQEGILKNN NFLNEDRKDI FFYQADDEHF
     IPGALLFDLE PRVINSIQTS EYRNLYNPEN MFISKEGGGA GNNWGCGYSQ GHKVEEEIID
     MIDREVDNSD NLEGFILSHS IAGGTGSGMG SYLLELLNDN YSKKMIQTFS VFPLLTNESS
     DVVVQPYNSI LTLKRLILST DSVVVIDNTS LNRIFVERLK LNNPTFQQTN TIISNVMSAS
     TTTLRYPGSM NNDMISLISS LIINPKCHFL ITSYTPITID KHISNVQKTT VLDVMKRLLH
     TKNIMVSAPV RRGMYISILN IIRGETDPTQ VHKGLQRIRD RKLVNFIKWN PASIQVTLAK
     QSPHVVSQHK VCGLMMANHT SISTLFERCV TQFDRLYKRR AFLENYKKES MFSSADGQGN
     FEEMESSKEI TQNLIDEYKS AERDDYFTNT YI