ID   TBB1_COLGL              Reviewed;         448 AA.
AC   P32928;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Tubulin beta-1 chain;
DE   AltName: Full=Beta-1-tubulin;
GN   Name=TUB1;
OS   Colletotrichum gloeosporioides (Anthracnose fungus) (Glomerella cingulata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum gloeosporioides species complex.
OX   NCBI_TaxID=474922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Sp. aeschynomene;
RX   PubMed=8440473; DOI=10.1016/0378-1119(93)90771-t;
RA   Buhr T.L., Dickman M.B.;
RT   "Isolation and characterization of a beta-tubulin-encoding gene from
RT   Colletotrichum gloeosporioides f. sp. aeschynomene.";
RL   Gene 124:121-125(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; M90977; AAA33044.1; -; Genomic_DNA.
DR   AlphaFoldDB; P32928; -.
DR   SMR; P32928; -.
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..448
FT                   /note="Tubulin beta-1 chain"
FT                   /id="PRO_0000048401"
FT   REGION          424..448
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..448
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         143..149
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   448 AA;  50067 MW;  F2429CE158C11150 CRC64;
     MREIIHLQTG QCLIQGNQVG TAFWQTIHHE HGLDHDGYFR GESTQQSDRL SVYFAEASNN
     KYVPRAVLVD LEPATMDAIR SGPLGNFFRP DNMVHGQSGA GNNWAKGHYT EGAELVDQVL
     DVVRREAETC DSLQGFQITH SLGGGTGSGM GTLLIAKVRE EFPDRMMATF SVLPSPKVSE
     VVVEPYNATL SVHQLVENSD ETFCIDNEAL YDICRRTLKQ AHPSYGDLNK LVSRVMSGLT
     TGFRFPGQLN ADLRKLAVNL VPFPRLHFFT VGFAPLTTAA AYQNLGVAEL TQQMFDPKNV
     MSASDFRNGR FLTCSAIYRG KVSTKQIEEQ IRGVQAKNSA YFVEWIPNNV QTAHCSIPPV
     GMNASSTFIG NSTAIQDIFR RVGDQFSVMF RRKAFLHWYT GEGMDEMEFT EAESNMNDLV
     SEYQQYQDAG MDDDEAEEAY EEEEPVEE