ID   TBB_EUPFO               Reviewed;         444 AA.
AC   Q9N2N6;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Tubulin beta chain;
DE   AltName: Full=Beta-tubulin;
OS   Euplotes focardii.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Hypotrichia; Euplotida; Euplotidae; Euplotes.
OX   NCBI_TaxID=36767;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=TN1;
RX   PubMed=8087111; DOI=10.1111/j.1550-7408.1994.tb06100.x;
RA   Miceli C., Ballarini P., Di Giuseppe G., Valbonesi A., Luporini P.;
RT   "Identification of the tubulin gene family and sequence determination of
RT   one beta-tubulin gene in a cold-poikilotherm protozoan, the antarctic
RT   ciliate Euplotes focardii.";
RL   J. Eukaryot. Microbiol. 41:420-427(1994).
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; S72098; AAB31932.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9N2N6; -.
DR   SMR; Q9N2N6; -.
DR   PRIDE; Q9N2N6; -.
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..444
FT                   /note="Tubulin beta chain"
FT                   /id="PRO_0000048295"
FT   REGION          423..444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..444
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   444 AA;  49807 MW;  1F50D2FA60B9DB06 CRC64;
     MREIVHIQAG QCGNQIGAKF WEVISDEHGV DPTGTYHGDS DLQLERINVY FNEATGRKIC
     PRAMLMDLEP GTMDSVRAGP FGQLFRPDNF VFGQSGAGNN WAKGHYTEGA ELIDSVLDVV
     RKEAEGCDCL QGFQITHSLG GGTGSGMGTL LISKIREKYP DRIMETFSVF PSPKVSDTVV
     EPYNATLSVH QLVENADEVM CIDNEALYDI CFRTLKPTTP TYGDLNHLVS AVISGVTSCL
     RFPGQLNSDL RKLAVNLIPF PRLHFFMIGF APLTSRGSQQ YRALTVPELT QQMFDAKNMM
     CASDPRHGRY LTASAMFRGR MSTKEVDEQM LNVQNKNSSY FVEWIPNNIK SSVCDIPPKG
     LKMSSTFIGN STAIQEMFKR VAEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
     EYQQYQDATA EEEGEFDDEE EMDV