ID   TBB_GIBFU               Reviewed;         446 AA.
AC   P53374;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Tubulin beta chain;
DE   AltName: Full=Beta-tubulin;
GN   Name=TUB2;
OS   Gibberella fujikuroi (Bakanae and foot rot disease fungus) (Fusarium
OS   fujikuroi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=5127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A 102;
RX   PubMed=8702300; DOI=10.1128/aem.62.8.3053-3056.1996;
RA   Yan K., Dickman M.B.;
RT   "Isolation of a beta-tubulin gene from Fusarium moniliforme that confers
RT   cold-sensitive benomyl resistance.";
RL   Appl. Environ. Microbiol. 62:3053-3056(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}.
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; U27303; AAB18275.1; -; Genomic_DNA.
DR   AlphaFoldDB; P53374; -.
DR   SMR; P53374; -.
DR   eggNOG; KOG1375; Eukaryota.
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   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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   Antibiotic resistance; Cytoplasm; Cytoskeleton; GTP-binding; Microtubule;
KW   Nucleotide-binding.
FT   CHAIN           1..446
FT                   /note="Tubulin beta chain"
FT                   /id="PRO_0000048414"
FT   REGION          421..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:0000250"
FT   VARIANT         50
FT                   /note="Y -> N (in benomyl-resistant strain)"
SQ   SEQUENCE   446 AA;  49905 MW;  80DD6B4BF5A6F951 CRC64;
     MREIVHLQTG QCGNQIGAAF WQTISGEHGL DSNGVYNGTS ELQLERMSVY FNERSGNKYV
     PRAVLVDLEP GTMDAVRAGP FGQLFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDQVLDVV
     RREAEGCDCL QGFQITHSLG GGTGAGMGTL LISKIREEFP DRMMATFSVV PSPKVSDTVV
     EPYNATLSVH QLVENSDETF CIDNEALYDI CMRTLKLSNP SYGDLNYLVS AVMSGVTTCL
     RFPGQLNSDL RKLAVNMVPF PRLHFFMVGF APLTSRGAHS FRAVSVPELT QQMFDPKNMM
     AASDFRNGRY LTCSAIFRGR VAMKEVEDQM RNVQNKNSSY FVEWIPNNIQ TALCAIPPRG
     LTMSSTFIGN STSIQELFKR VGEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
     EYQQYQDAGI DEEEEEYEEE LPEGEE