ID   TBB_PLAFK               Reviewed;         445 AA.
AC   P14643;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Tubulin beta chain;
DE   AltName: Full=Beta-tubulin;
OS   Plasmodium falciparum (isolate K1 / Thailand).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=5839;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2693902; DOI=10.1111/j.1365-2958.1989.tb00137.x;
RA   Delves C.J., Ridely R.G., Goman M., Holloway S.P., Hyde J.E., Scaife J.G.;
RT   "Cloning of a beta-tubulin gene from Plasmodium falciparum.";
RL   Mol. Microbiol. 3:1511-1519(1989).
CC   -!- FUNCTION: Tubulin is the major constituent of microtubules (By
CC       similarity). It binds two moles of GTP, one at an exchangeable site on
CC       the beta chain and one at a non-exchangeable site on the alpha chain
CC       (Probable). {ECO:0000250|UniProtKB:Q7KQL5, ECO:0000305}.
CC   -!- SUBUNIT: Dimer of alpha and beta chains (By similarity). A typical
CC       microtubule is a hollow water-filled tube with an outer diameter of 25
CC       nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate
CC       head-to-tail to form protofilaments running lengthwise along the
CC       microtubule wall with the beta-tubulin subunit facing the microtubule
CC       plus end conferring a structural polarity. Microtubules usually have 13
CC       protofilaments but different protofilament numbers can be found in some
CC       organisms and specialized cells (Probable). Interacts with
CC       DCX/apicortin; the interaction stabilizes microtubule assembly (By
CC       similarity). {ECO:0000250|UniProtKB:Q7KQL5, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q7KQL5}. Note=Localizes to the parasite surface
CC       in subpellicular regions in trophozoites and schizonts (By similarity).
CC       In merozoites, localize to the apical end of the parasite (By
CC       similarity). {ECO:0000250|UniProtKB:Q7KQL5}.
CC   -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR   EMBL; X16075; CAA34207.1; -; Genomic_DNA.
DR   PIR; S07460; UBZQF.
DR   AlphaFoldDB; P14643; -.
DR   SMR; P14643; -.
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..445
FT                   /note="Tubulin beta chain"
FT                   /id="PRO_0000048312"
FT   REGION          426..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..445
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   445 AA;  49751 MW;  15A33134F357FFDE CRC64;
     MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPSGTYCGDS DLQLERVDVF YNEATGGRYV
     PRAILMDLEP GTMDSVRAGP FGQLFRPDNF VFGQTGAGNN WAKGHYTEGA ELIDAVLDVV
     RKEAEGCDCL QGFQITHSLG GGTGSGMGTL LISKIREEYP DRIMETFSVF PSPKVSDTVV
     EPYNATLSVH QLVENADEVQ VIDNEALYDI CFRTLKLTTP TYGDLNHLVS AAMSGVTCSL
     RFPGQLNSDL RKLAVNLIPF PRLHFFMIGF APLTSRGSQQ YRALTVPELT QQMFDAKNMM
     CASDPRHGRY LTACAMFRGR MSTKEVDEQM LNVQNKNSSY FVEWIPHNTK SSVCDIPPKG
     LKMAVTFVGN STAIQEMFKR VSDQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
     EYQQYQDATA EEEGEFEEEE GDVEA