ID   TBB1_HYPRU              Reviewed;         446 AA.
AC   P31864;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Tubulin beta-1 chain;
DE   AltName: Full=Beta-1-tubulin;
GN   Name=tub1;
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; Z15054; CAA78764.1; -; Genomic_DNA.
DR   PIR; S35191; S35191.
DR   AlphaFoldDB; P31864; -.
DR   SMR; P31864; -.
DR   PRIDE; P31864; -.
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-1 chain"
FT                   /id="PRO_0000048436"
FT   REGION          421..446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..446
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         142..148
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   446 AA;  49626 MW;  B43E7B478B11CE13 CRC64;
     MREIVSVHLQ TGQCGNQVGS AFWQTISGEH GLDSSGVYGG TSDQQLDRLN VYFNEASNNK
     YVPRAVLVDL EPGTMDAVRS GPFGQLFRPD NFVFGQSGAG NNWAKGHYTE GAELVDQVLD
     VVRREAENCE CLQGFQITHS LGGGTGSGMG TLLISKIREE FPDRMMATFS VVPSPKVSDT
     VVEPYNATLS MHQLVENSDK TFCIDNEALY DICMRTLKLS NPSYGDLNHL VSAVMSGVST
     SLRFPGQLNS DLRKLAVNMV PFPRLHFFMV GFAPLTSPGA HSFRAVTVPE LTQQMMDPKN
     MMAASDFRNG RYLTCSTIFR GKVAMKEVED QMRTVQNKNS AYFVEWIPNN IQTACALSPP
     RGLKISSTFV GNSTAIQEIF RRVGEQFSAM FRRQAFLHWY TSEGMDEMEF TEAESNMNDL
     VSEYQQYQDA SADDGEEYEE DAPMEE