ID   TBB2_COLGL              Reviewed;         447 AA.
AC   P40904;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 2.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Tubulin beta-2 chain;
DE   AltName: Full=Beta-2-tubulin;
GN   Name=TUB2;
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], AND VARIANT LYS-198.
RC   STRAIN=Sp. aeschynomene / Isolate 3.1.3;
RX   PubMed=7993097; DOI=10.1128/aem.60.11.4155-4159.1994;
RA   Buhr T.L., Dickman M.B.;
RT   "Isolation, characterization, and expression of a second beta-tubulin-
RT   encoding gene from Colletotrichum gloeosporioides f. sp. aeschynomene.";
RL   Appl. Environ. Microbiol. 60:4155-4159(1994).
RN   [2]
RP   SEQUENCE REVISION TO 21-35.
RA   Buhr T.L.;
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
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; U14138; AAA62875.2; -; Genomic_DNA.
DR   AlphaFoldDB; P40904; -.
DR   SMR; P40904; -.
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..447
FT                   /note="Tubulin beta-2 chain"
FT                   /id="PRO_0000048402"
FT   REGION          426..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        427..447
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"
FT   VARIANT         198
FT                   /note="E -> K (in benomyl-resistant strain)"
FT                   /evidence="ECO:0000269|PubMed:7993097"
SQ   SEQUENCE   447 AA;  49847 MW;  C7937B515213F446 CRC64;
     MREIVHLQTG QCGNQIGAAF WQNISGEHGL DSNGVYNGTS ELQLERMSVY FNEASGNKYV
     PRAVLVDLEP GTMDAVRAGP FGQLFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDQVLDVV
     RREAEGCDCL QGFQITHSLG GGTGAGMGTL LISKIREEFP DRMMATFSVV PSPKVSDTVV
     EPYNATLSVH QLVENSDETF CIDNEALYDI CMRTLKLSNP SYGDLNHLVS AVMSGVTTCL
     RFPGQLNSDL RKLAVNMVPF PRLHFFMVGF APLTSRGAHS FRAVSVPELT QQMFDPKNMM
     AASDFRNGRY LTCSAIFRGK VAMKDVEDQM RNVQNKNSSY FVEWIPNNVQ TALCSIPPRG
     LKMSSTFVGN ATAIQELFKR VGEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
     EYQQYQDAGV DEEEEEYEEE APLEEEV