ID   TBB1_COLGR              Reviewed;         445 AA.
AC   P22013;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, 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   Colletotrichum graminicola (Maize anthracnose fungus) (Glomerella
OS   graminicola).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum graminicola species complex.
OX   NCBI_TaxID=31870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2323570; DOI=10.1016/0378-1119(90)90275-v;
RA   Panaccione D.G., Hanau R.M.;
RT   "Characterization of two divergent beta-tubulin genes from Colletotrichum
RT   graminicola.";
RL   Gene 86:163-170(1990).
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; M34491; AAA33045.1; -; Genomic_DNA.
DR   PIR; JQ0422; JQ0422.
DR   AlphaFoldDB; P22013; -.
DR   SMR; P22013; -.
DR   PRIDE; P22013; -.
DR   VEuPathDB; FungiDB:GLRG_01057; -.
DR   OMA; QSCTILE; -.
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..445
FT                   /note="Tubulin beta-1 chain"
FT                   /id="PRO_0000048403"
FT   REGION          422..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..445
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"
SQ   SEQUENCE   445 AA;  49709 MW;  ADFE3AA0850B6C9B CRC64;
     MREIIHLQTG QCGNQVGTAF WQTIHGEHGL DQDGVFRGSD EQQSERLSVY FTEAAKQKYV
     PRAVLVDLEP ATMDAIRSGP LGDFFRPDNM VYGQSGAGNN WAKGHYTEGA ELVDQVLDVV
     RREAEACDSL QGFQITHSLG GGTGSGMGTL LIAKVREEFP DRMMATFSVL PSAKVSEVVV
     EPYNATLSIH QLVENSDETF CIDNEALYDI CRRTLKQAHP SYGHLNHLVS RVMSGLTTGF
     RFPGQLNADL RKLAVNLVPF PRLHFFTVGF APLTSSASFS NLGIAELTQQ MFDPKNVMLA
     SDFRDGRFLT CSTMFRGKVS MKQVEEQIQA IKNKNSANFV EWIPNNIQTA HCSVPPKGLD
     VSSTFIGNST AIQNSFRRVG DQFSLMFRRK AFLHWYTGEG MDEMEFTEAE SNMNDLVSEY
     QQYQDAGMDD EYGEEYEDEA PAEEE