ID   TBB_CERBT               Reviewed;         447 AA.
AC   Q3KVN1; Q3KVN2;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Tubulin beta chain;
DE   AltName: Full=Beta-tubulin;
GN   Name=TUB1;
OS   Cercospora beticola (Sugarbeet leaf spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX   NCBI_TaxID=122368;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AD-762, and C-3;
RA   Davidson R.M., Hanson L.E., Franc G.D., Panella L., Spence R.M.;
RT   "Isolation of beta-tubulin gene fragments from benzimadizole-sensitive and
RT   tolerant Cercospora beticola.";
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY856373; AAX52521.1; -; Genomic_DNA.
DR   EMBL; AY856374; AAX52522.1; -; Genomic_DNA.
DR   PRIDE; Q3KVN1; -.
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_0000048399"
FT   REGION          422..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"
FT   VARIANT         198
FT                   /note="A -> E (in strain: C-3)"
SQ   SEQUENCE   447 AA;  49683 MW;  F1B86CDDA469E3F1 CRC64;
     MREIVHLQTG QCGNQIGAAF WQTISGEHGL DGSGVYNGTS DLQLERMNVY FNEASGNKYV
     PRAVLVDLEP GTMDAVRAGP XGQLFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDQVLDVV
     RREAEGCDCL QGFQITHSLG GGTGAGMGTL LISKIREEFP DRMMATFSVM PSPKVSDTVV
     EPYNATLSVH QLVENSDATF CIDNEALYDI CMRTLKLNNP SYGDLNHLVS AVMSGVTTCL
     RFPGQLNSDL RKLAVNMVPF PRLHFFMVGF APLTSRGAHS FRAVTVPELT QQIFDPKNMM
     AASDFRNGRY LTCSAIYRGK VSMKEVEDQI RNVQNKNTAY FVEWIPNNVQ TALCSIPPRG
     LKMSSTFVGN STSIQELFKR VGDQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
     EYQQYQEASV SEGEEEYDEE APLEGEE