ID   TBG_ENTHI               Reviewed;         451 AA.
AC   P54401;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Tubulin gamma chain;
DE   AltName: Full=Gamma-tubulin;
OS   Entamoeba histolytica.
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=5759;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ATCC 30459 / HM-1:IMSS;
RX   PubMed=9497056; DOI=10.1016/s0166-6851(97)00157-6;
RA   Ray S.S., Gangopadhyay S.S., Pande G., Samuelson J.C., Lohia A.;
RT   "Primary structure of Entamoeba histolytica gamma-tubulin and localisation
RT   of amoebic microtubule organising centres.";
RL   Mol. Biochem. Parasitol. 90:331-336(1997).
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; U20322; AAC08441.1; -; mRNA.
DR   AlphaFoldDB; P54401; -.
DR   SMR; P54401; -.
DR   STRING; 5759.rna_EHI_008240-1; -.
DR   VEuPathDB; AmoebaDB:EHI5A_150010; -.
DR   VEuPathDB; AmoebaDB:EHI7A_112330; -.
DR   VEuPathDB; AmoebaDB:EHI8A_121620; -.
DR   VEuPathDB; AmoebaDB:EHI_008240; -.
DR   VEuPathDB; AmoebaDB:KM1_191480; -.
DR   eggNOG; KOG1374; Eukaryota.
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; 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.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding.
FT   CHAIN           1..451
FT                   /note="Tubulin gamma chain"
FT                   /id="PRO_0000048458"
FT   BINDING         139..145
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   451 AA;  51955 MW;  1DA5422E0134B256 CRC64;
     MPREIITLNV GQCGNQLGSE FFKKICSEHG ILPDGSLSTN EFIDDRKDVF FYQADDQRYV
     PRSINIDLEP RVLDSIRTSE WRNFYNPENF IIPTNNGAGN SWANGYYTTE KMSEIEEIID
     REVEHCDSLE GFFFCHSICG GTGSGLGSKI MEMISEKYPK NILTSFSVMV KENPDVVVSP
     YNSILTLRRL ITECQSVVVF DNSALADITH TQFGVDEATV FDMNSIISSS MSAFTANLRF
     PSTLYNSLNS LMIHLCPSRF SHFLMTSYTP LRQVNQISSR TSAIDVMKRL IQPQNIMART
     RLKEGKYISM CDFFQGDVSY DEINEALQRF TDRRLAEFVP WNKEAIKVVH TRVSPLVKRG
     NRMSGMLLAN NTSIRYYFQD ILKAFDQMFK KRVYLQTDRD NLRKFPEFEE SKEIVKCVIE
     EYAKAESIEY SHYSYPIHKY LKGIAKEKIA E