ID   TBB_COCHE               Reviewed;         447 AA.
AC   Q4R9N3;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Tubulin beta chain;
DE   AltName: Full=Beta-tubulin;
GN   Name=TUB1;
OS   Cochliobolus heterostrophus (Southern corn leaf blight fungus) (Bipolaris
OS   maydis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=5016;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=HITO7711;
RX   PubMed=12501431; DOI=10.2323/jgam.44.217;
RA   Gafur A., Tanaka C., Shimizu K., Ouchi S., Tsuda M.;
RT   "Molecular analysis and characterization of the Cochliobolus heterostrophus
RT   beta-tubulin gene and its possible role in coferring resistance to
RT   benomyl.";
RL   J. Gen. Appl. Microbiol. 44:217-223(1998).
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; AB009971; BAD99947.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4R9N3; -.
DR   SMR; Q4R9N3; -.
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   3: Inferred from homology;
KW   Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding.
FT   CHAIN           1..447
FT                   /note="Tubulin beta chain"
FT                   /id="PRO_0000048400"
FT   REGION          424..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        431..447
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:0000250"
SQ   SEQUENCE   447 AA;  49902 MW;  52E9B5492EC8CB7F CRC64;
     MREIVHLQTG QCGNQIGAAF WQTISGEHGL DGSGVYNGTS DLQLERMNVY FNEASNNKFV
     PRAVLVDLEP GTMDAVRAGP FGQLFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDQVLDVV
     RREAEGCDCL QGFQITHSLG GGTGAGMGTL LISKIREEFP DRMMATYSVV PSPKVSDTVV
     EPYNATLSIH QLVENSDETF CIDNEALYDI CMRTLKLNNP SYGDLNHLVS AVMSGVTTCL
     RFPGQLNSDL RKLAVNMVPF PRLHFFMVGF APLTSRGAHS FRAVTVPELT QQMFDPKNMM
     AASDFRNGRY LTCSAYFRGK VSMKEVEDQM RNVQNKNSSY FVEWIPNNVQ TALCSIPPRG
     LKMSSTFVGN STSIQELFKR VGDQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
     EYQQYQEASV SEGEEEYDEE APLEAEE