ID   TBB_ENCHE               Reviewed;         439 AA.
AC   Q24829; Q24828;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Tubulin beta chain;
DE   AltName: Full=Beta-tubulin;
GN   Name=TUB2;
OS   Encephalitozoon hellem (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=27973;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8813701; DOI=10.1016/s0166-6851(96)02628-x;
RA   Li J., Katiyar S.K., Hamelin A., Visvesvara G.S., Edlind T.D.;
RT   "Tubulin genes from AIDS-associated microsporidia and implications for
RT   phylogeny and benzimidazole sensitivity.";
RL   Mol. Biochem. Parasitol. 78:289-295(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 108-259.
RX   PubMed=7804238;
RA   Edlind T.D., Visvesvara G., Li J., Katiyar S.K.;
RT   "Cryptosporidium and microsporidial beta-tubulin sequences: predictions of
RT   benzimidazole sensitivity and phylogeny.";
RL   J. Eukaryot. Microbiol. 41:38S-38S(1994).
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; L47271; AAB12034.1; -; Genomic_DNA.
DR   EMBL; L31808; AAA79116.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q24829; -.
DR   SMR; Q24829; -.
DR   VEuPathDB; MicrosporidiaDB:EHEL_030720; -.
DR   VEuPathDB; MicrosporidiaDB:KMI_07g11830; -.
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..439
FT                   /note="Tubulin beta chain"
FT                   /id="PRO_0000048409"
FT   BINDING         140..146
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   439 AA;  48985 MW;  051AAB7F445A291D CRC64;
     MREIIHLQTG QCGNQVGCKF WETISGEHGI DQTGKYVGTS DNQLERVNVY YNEASSKKYV
     PRAVLIDLEP GTMDAVRQGP FGDLFRPDNF VFGQSGAGNN WAKGHYTEGA ELIDSVMDVV
     RKEAESSDCL QGFQITHSLG GGTGAGMGTL LLSKIREDFP DRMICTFSVV PSPKVSDTVV
     EPYNATLSIH QLVENADETF CIDNEALYDI CFRTLKMSNP GYGDLNHLVS LVMSGVTTCL
     RFPGQLNADL RKLAVNMIPF PRLHFFVVGS APLIAIGTQK FKTYSVSELT QQMFDSKNMM
     TACDPRKGRY LTVAAMFRGK ISMKDVDEQM SMVQSKNSTL FVEWIPSNVK TAVCDIAPTG
     LEMSATFVGN TTSIQELFKR ISDQFTVMFR RKAFLHWYTG EGMDEMEFSE AESNMNDLLS
     EYQQYQDATV EDAEEFLVN