ID   TBB2_HYPRU              Reviewed;         446 AA.
AC   P31863;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Tubulin beta-2 chain;
DE   AltName: Full=Beta-2-tubulin;
GN   Name=tub2;
OS   Hypocrea rufa (Trichoderma viride).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=5547;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=T9 BR47;
RX   PubMed=8341264; DOI=10.1007/bf00276886;
RA   Goldman G.H., Temmerman W., Herrera-Estrella A., Jacobs D., Contreras R.,
RA   van Montagu M.;
RT   "A nucleotide substitution in one of the beta-tubulin genes of Trichoderma
RT   viride confers resistance to the antimitotic drug methyl benzimidazole-2-
RT   yl-carbamate.";
RL   Mol. Gen. Genet. 240:73-80(1993).
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; Z15055; CAA78765.1; -; Genomic_DNA.
DR   PIR; S35192; S25554.
DR   AlphaFoldDB; P31863; -.
DR   SMR; P31863; -.
DR   PRIDE; P31863; -.
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..446
FT                   /note="Tubulin beta-2 chain"
FT                   /id="PRO_0000048437"
FT   BINDING         140..146
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   446 AA;  49975 MW;  95C470CB903A39A9 CRC64;
     MREIVYIQTG QCGNQIGAAF WQTISGEHGL DSNGIYNGSS ELQLERMNVY FNEASNNKYV
     PRAVLVDLEP GTMDAVRAGP FGQLFRPDNF IFGQSSAGNN WAKGHYTEGA ELVDQVLDVV
     RREAEGCDCL QGFQITHSLG GGTGSGMGTL LLSKIREEFP DRMMATFSVV PSPKVSDTVV
     EPYNATLSVH QLVENSDETF CIDNEALYDI CMRTLKLNNP AYGDLNYLVS AVMSGITTCL
     RFPGQLNSDL RKLAVNMVPF PRLHFFMVGF APLTSPGAHS FRAVTVPELT QQMFDPKNMM
     AASDFRNGRY LTCCSIFRGK VAMKEVEDQM RNVQNKNSTY FVEWIPNNIQ TALCAIPPRG
     LKMSSTFIGN STSIQELFKR VGEQFSAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
     EYQQYQEAGI DEEEEYEDEA PMEAEE