ID   TBB_PLESA               Reviewed;         446 AA.
AC   Q92268; O13509;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Tubulin beta chain;
DE   AltName: Full=Beta-tubulin;
OS   Pleurotus sajor-caju (Oyster mushroom).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Lentinus.
OX   NCBI_TaxID=50053;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=MGL2084;
RA   Kim B.G.;
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=MGL2084;
RA   Kim B.G.;
RL   Submitted (JUN-1997) 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}.
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DR   EMBL; U64720; AAB61260.1; -; mRNA.
DR   EMBL; AF008134; AAB63288.1; -; mRNA.
DR   AlphaFoldDB; Q92268; -.
DR   SMR; Q92268; -.
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..446
FT                   /note="Tubulin beta chain"
FT                   /id="PRO_0000048426"
FT   REGION          423..446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        427..446
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"
FT   CONFLICT        13
FT                   /note="R -> G (in Ref. 2; AAB63288)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        82
FT                   /note="G -> A (in Ref. 2; AAB63288)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        97
FT                   /note="G -> A (in Ref. 2; AAB63288)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        270
FT                   /note="V -> L (in Ref. 2; AAB63288)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   446 AA;  50058 MW;  A6D50E6F36525D12 CRC64;
     MREIVHLQTG QCRNQIGAKF WEVVSDEHGI EPDGLYKGNN DLQLERISVY YNEVGANKYV
     PRAVLVDLEP GTMDSVRSGP LGSLFRPDNF VFGQSGGGNN WAKGHYTEGA ELVDAVLDVV
     RKEAEGTDCL QGFQITHSLG GGTGAGMGTL LISKIREEYP DRMMCTYSVV PSPKVSDTVV
     EPYNATLSVH QLVENSDETF CIDNEALYDI CFRTLKLTTP TYGDLNHLIS IVMSGITTCL
     RFPGQLNSDL RKLAVNMVPF PRLHFFMPGV CPLTARGSQQ YRAVTVPELT QQMFDAKNMM
     AASDPRHGRY LTVAAVFRGK VSMKEVEEQM QNVQNKNSAY FVEWIPNNVL TAQCDIPPRG
     CKMAVTFLGN STAIQELFKR VNDQFAAMFK RKAFLHWYTQ EGMDEMEFTE AESNMQDLVA
     EYQQYQDATA DEEEGEYEEE PAEEEQ