ID   TBB_ENCCU               Reviewed;         439 AA.
AC   Q8SS99; Q24827;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Tubulin beta chain;
DE   AltName: Full=Beta-tubulin;
GN   Name=TUB2; OrderedLocusNames=ECU03_0820i;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
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).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=16691553; DOI=10.1002/pmic.200500796;
RA   Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT   "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT   (microsporidia): a reference map for proteins expressed in late sporogonial
RT   stages.";
RL   Proteomics 6:3625-3635(2006).
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   -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC       {ECO:0000269|PubMed:16691553}.
CC   -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR   EMBL; AL590443; CAD26226.1; -; Genomic_DNA.
DR   EMBL; L31807; AAA79115.1; -; Genomic_DNA.
DR   RefSeq; NP_597591.1; NM_001040955.1.
DR   AlphaFoldDB; Q8SS99; -.
DR   SMR; Q8SS99; -.
DR   STRING; 284813.Q8SS99; -.
DR   PRIDE; Q8SS99; -.
DR   GeneID; 858753; -.
DR   KEGG; ecu:ECU03_0820i; -.
DR   VEuPathDB; MicrosporidiaDB:ECU03_0820i; -.
DR   HOGENOM; CLU_015718_1_1_1; -.
DR   InParanoid; Q8SS99; -.
DR   OMA; VCSVAPK; -.
DR   OrthoDB; 962471at2759; -.
DR   Proteomes; UP000000819; Chromosome III.
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   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..439
FT                   /note="Tubulin beta chain"
FT                   /id="PRO_0000048408"
FT   BINDING         140..146
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   439 AA;  49082 MW;  2DC56BAEB35CC6BB CRC64;
     MREIIHLQTG QCGNQVGCKF WETISGEHGI DQTGRYVGTS DNQLERINVY YNEASSKKYV
     PRAVLIDLEP GTMDAVRQGP FGELFRPDNF VFGQSGAGNN WAKGHYTEGA ELIDSVMDVV
     RKEAESSDCL QGFQITHSLG GGTGAGMGTL LLSKIREDFP DRMICTFSVV PSPKVSDTVV
     EPYNATLSIH QLVENADETF CIDNEALYDI CFRTLKLNNP GYGDLNHLVS LVMSGVTTCL
     RFPGQLNADL RKLAVNMIPF PRLHFFVAGF APLIAIGTQK FKTYSVSELT QQMFDSKNMM
     TACDPRKGRY LTVAAMFRGK ISMKDVDEQM SMVQSKNSSL FVEWIPSNVK TAVCDIAPTG
     LEMSATFVGN TTSIQELFKR ISDQFTVMFR RKAFLHWYTG EGMDEMEFSE AESNMNDLLS
     EYQQYQDATI EDAEEFLVN