ID   TBB_USTVI               Reviewed;         444 AA.
AC   Q8WZE0; Q8WZD2;
DT   28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Tubulin beta chain;
DE   AltName: Full=Beta-tubulin;
OS   Microbotryum violaceum (Anther smut fungus) (Ustilago violacea).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX   NCBI_TaxID=5272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=22000, A128, GC3, Nine, and TB1;
RA   Perlin M.H., Freeman A.B., Shi T.-L., Duong K.K., Hughes C.F.;
RT   "Gene phylogenies support co-evolution for Microbotryum violaceum and its
RT   host species.";
RL   Submitted (NOV-2000) 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; AF323121; AAL36612.1; -; mRNA.
DR   EMBL; AF323122; AAL36613.1; -; mRNA.
DR   EMBL; AF323123; AAL36614.1; -; mRNA.
DR   EMBL; AF323128; AAL36619.1; -; mRNA.
DR   EMBL; AF323130; AAL36621.1; -; mRNA.
DR   AlphaFoldDB; Q8WZE0; -.
DR   SMR; Q8WZE0; -.
DR   PRIDE; Q8WZE0; -.
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   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding.
FT   CHAIN           1..444
FT                   /note="Tubulin beta chain"
FT                   /id="PRO_0000048441"
FT   BINDING         140..146
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   VARIANT         33
FT                   /note="T -> S (in strain: 22000, A128 and Nine)"
FT   VARIANT         40
FT                   /note="S -> T (in strain: 22000, A128 and Nine)"
FT   VARIANT         54
FT                   /note="T -> A (in strain: 22000, A128 and Nine)"
FT   VARIANT         69
FT                   /note="K -> E (in strain: 22000, A128 and Nine)"
FT   VARIANT         439
FT                   /note="E -> A (in strain: 22000, A128 and Nine)"
SQ   SEQUENCE   444 AA;  49281 MW;  98CA19E3F140A676 CRC64;
     MREIVSLQAG QCGNQIGTKF WEVVSEEHGI DGTGQYTGTS DLQLERINVY YNETGTGKYV
     PRAVLVDLKP GTMDVIQGGP LGGLFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDQVLDVV
     RKEAEGTDCL QGFQLTHSLG GGTGSGMGTL LVSKIREEFP DRMMATFSVV PSPKVSDTVV
     EPYNAVLSVH QLVENSDETF CIDNEALYDI CFRTLKLSAP THGDLNGLVS IVMSGITTCL
     RFPGQLNSDL RKLAVNMVPF PRLHFFTVGF APLTARGSSQ YRAVTVAELT AQMFDAKNMM
     AASDPRHGRY LTVAAYFRGK VSMKEVEDQM VSIQQKNSQY FVEWIPNNVQ SAHCEVAPRG
     LKMSVTFIGN NTSIQELFKR VGDHFDVMFR RRAFLHWYTG EGMDEMEFSE ASANMHDLIA
     EYTQYQEAGV DDEEEVAYEE EPQE