TBB_DOTSE
ID TBB_DOTSE Reviewed; 447 AA.
AC O42786;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Tubulin beta chain;
DE AltName: Full=Beta-tubulin;
GN Name=TUB1;
OS Dothistroma septosporum (Red band needle blight fungus) (Mycosphaerella
OS pini).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Dothistroma.
OX NCBI_TaxID=64363;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DP1;
RA Bidlake A., Monahan B.J., Bradshaw R.E.;
RT "The beta-tubulin gene, tub1, of Dothistroma pini (anamorphic form of
RT Mycosphaerella pini).";
RL Submitted (JAN-1998) 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; AF044975; AAC02112.1; -; Genomic_DNA.
DR AlphaFoldDB; O42786; -.
DR SMR; O42786; -.
DR PRIDE; O42786; -.
DR OMA; VCSVAPK; -.
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..447
FT /note="Tubulin beta chain"
FT /id="PRO_0000048421"
FT REGION 424..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..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"
SQ SEQUENCE 447 AA; 49777 MW; 74D4CBFDA94B206B CRC64;
MREIVHLQTG QCGNQIGAAF WQTISGEHGL DGSGVYNGTS DLQLERMNVY FNEASGNKYV
PRAVLVDLEP GTMDAVRAGP FGQLFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDQVLDVV
RREAEGCDCL QGFQITHSLG GGTGAGMGTL LISKIREEFP DRMMATFSVM PSPKVSDTVV
EPYNATLSVH QLVENSDETF CIDNEALYDI CMRTLKLNNP SYGDLNHLVS AVMSGVTTCL
RFPGQLNSDL RKLAVNMVPF PRLHFFMVGF APLTSRGAHS FRAVTVPELT QQIFDPKNMM
AASDFRNGRY LTCSAIYRGK VSMKEVEDQI RNVQNKNTAY FVEWIPNNVQ TALCSIPPRG
LKMSSTFVGN STSIQELFKR VGDQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
EYQQYQEASV SEGEEEYDEE APLEGEE