ID   TBB_EIMTE               Reviewed;         449 AA.
AC   Q27380;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Tubulin beta chain;
DE   AltName: Full=Beta-tubulin;
OS   Eimeria tenella (Coccidian parasite).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX   NCBI_TaxID=5802;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=Wisconsin;
RX   PubMed=8920019; DOI=10.1016/0166-6851(95)02536-7;
RA   Zhu G., Keithly J.S.;
RT   "The beta tubulin gene of Eimeria tenella.";
RL   Mol. Biochem. Parasitol. 76:315-319(1996).
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; U19609; AAB41262.1; -; Genomic_DNA.
DR   EMBL; U19268; AAB41261.1; -; mRNA.
DR   RefSeq; XP_013228349.1; XM_013372895.1.
DR   AlphaFoldDB; Q27380; -.
DR   SMR; Q27380; -.
DR   PRIDE; Q27380; -.
DR   GeneID; 25249719; -.
DR   VEuPathDB; ToxoDB:ETH2_0401900; -.
DR   VEuPathDB; ToxoDB:ETH_00002520; -.
DR   OMA; VCSVAPK; -.
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   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding.
FT   CHAIN           1..449
FT                   /note="Tubulin beta chain"
FT                   /id="PRO_0000048293"
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;  49953 MW;  9C142BD11277AA71 CRC64;
     MREIVHVQGG QCGNQIGAKF WEVISDEHGI APTGTYKGDS DLQLERISVF YNEATGGRYV
     PRAVLMDLEP GTMDSVRSGP FGQLFRPDNF VFGQTGAGNN WAKGHYTEGA ELIDSVLDVV
     RKEAEGCDCL QGFQVTHSLG GGTGSGMGTL LISKVREEYP DRIMETFSVF PSPKVSDTVV
     EPYNATLSVH QLVENADEVQ VIDNEALYDI CFRTLKLTTP TYGDLNHLVS AAMSGVTCSL
     RFPGQLNSDL RKLAVNLVPF PRLHFFLIGF APLTSRGSQQ YRALTVPELT QQMFDAKNMM
     CASDPRHGRY LTACALFRGR MSTKEVDEQM LNVQNKNSSY FVEWIPNNMK SGVCDIPPKG
     LKMSVTFVGN STAIQEMFKR VSDQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
     EYQQYQDATA EEEGEFDEEE GVMDAEGAA