ID   TBB_TOXGO               Reviewed;         449 AA.
AC   P10878;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Tubulin beta chain;
DE   AltName: Full=Beta-tubulin;
OS   Toxoplasma gondii.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX   NCBI_TaxID=5811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3412377; DOI=10.1016/0166-6851(88)90081-3;
RA   Nagel S.D., Boothroyd J.C.;
RT   "The alpha- and beta-tubulins of Toxoplasma gondii are encoded by single
RT   copy genes containing multiple introns.";
RL   Mol. Biochem. Parasitol. 29:261-273(1988).
CC   -!- FUNCTION: Tubulin is the major constituent of microtubules. It binds
CC       two moles of GTP, one at an exchangeable site on the beta chain and one
CC       at a non-exchangeable site on the alpha chain.
CC   -!- SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is a
CC       hollow water-filled tube with an outer diameter of 25 nm and an inner
CC       diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to
CC       form protofilaments running lengthwise along the microtubule wall with
CC       the beta-tubulin subunit facing the microtubule plus end conferring a
CC       structural polarity. Microtubules usually have 13 protofilaments but
CC       different protofilament numbers can be found in some organisms and
CC       specialized cells.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR   EMBL; M20025; AAA30146.1; -; Genomic_DNA.
DR   PIR; S16340; S16340.
DR   AlphaFoldDB; P10878; -.
DR   SMR; P10878; -.
DR   PRIDE; P10878; -.
DR   VEuPathDB; ToxoDB:TGARI_266960; -.
DR   VEuPathDB; ToxoDB:TGCAST_266960; -.
DR   VEuPathDB; ToxoDB:TGCOUG_266960; -.
DR   VEuPathDB; ToxoDB:TGDOM2_266960; -.
DR   VEuPathDB; ToxoDB:TGFOU_266960; -.
DR   VEuPathDB; ToxoDB:TGGT1_266960; -.
DR   VEuPathDB; ToxoDB:TGMAS_266960; -.
DR   VEuPathDB; ToxoDB:TGME49_266960; -.
DR   VEuPathDB; ToxoDB:TGP89_266960; -.
DR   VEuPathDB; ToxoDB:TGPRC2_266960; -.
DR   VEuPathDB; ToxoDB:TGRH88_011050; -.
DR   VEuPathDB; ToxoDB:TGRUB_266960; -.
DR   VEuPathDB; ToxoDB:TGVAND_266960; -.
DR   VEuPathDB; ToxoDB:TGVEG_266960; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR   GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR   Gene3D; 1.10.287.600; -; 1.
DR   Gene3D; 3.30.1330.20; -; 1.
DR   Gene3D; 3.40.50.1440; -; 1.
DR   InterPro; IPR013838; Beta-tubulin_BS.
DR   InterPro; IPR002453; Beta_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; PR01163; BETATUBULIN.
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.
DR   PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding.
FT   CHAIN           1..449
FT                   /note="Tubulin beta chain"
FT                   /id="PRO_0000048318"
FT   REGION          426..449
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..449
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         140..146
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   449 AA;  50059 MW;  B3EBB10C1B4A66F5 CRC64;
     MREIVHVQGG QCGNQIGAKF WEVISDEHGI DPTGTYCGDS DLQLERINVF YNEATGGRFV
     PRAILMDLEP GTMDSVRAGP FGQLFRPDNF VFGQTGAGNN WAKGHYTEGA ELIDSVLDVV
     RKEAEGCDCL QGFQITHSLG GGTGSGMGTL LISKVREEYP DRIMETFSVF PSPKVSDTVV
     EPYNATLSVH QLVENADEVQ VIDNEALYDI CFRTLKLTTP TYGDLNHLVS AAMSGVTCCL
     RFPGQLNSDL RKLAVNLVPF PRLHFFLIGF APLTSRGSQQ YRALSVPELT QQMFDAKNMM
     CASDPRHGRY LTASAMFRGR MSTKEVDEQM LNVQNKNSSY FVEWIPNNMK SSVCDIPPKG
     LKMSVTFVGN STAIQEMFKR VSDQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
     EYQQYQDATA EEEGEFDEEE GEMGAEEGA