TBB_ENCIN
ID TBB_ENCIN Reviewed; 439 AA.
AC Q9GSR5;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Tubulin beta chain;
DE AltName: Full=Beta-tubulin;
GN Name=TUB2;
OS Encephalitozoon intestinalis (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=58839;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Bonafonte M.T., Mead J.R.;
RL Submitted (AUG-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; AF297876; AAG15252.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9GSR5; -.
DR SMR; Q9GSR5; -.
DR VEuPathDB; MicrosporidiaDB:Eint_030710; -.
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_0000048410"
FT BINDING 140..146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 439 AA; 49080 MW; C5EBFCB2E69F8862 CRC64;
MREIIHLQTG QCGNQVGCKF WETISGEHGI DQSGRYVGTS DNQLERVNVY YNEASSKKYV
PRAVLIDLEP GTMDAVRQGP FGELFRPDNF VFGQSGAGNN WAKGHYTEGA ELIDSVMDVV
RKEAESSDCL QGFQITHSLG GGTGAGMGTL LLSKIREDFP DRMICTFSVV PSPKVSDTVV
EPYNATLSIH QLVENADETF CIDNEALYDM CFRTLKLNNP GYGDLNHLVS LVMSGVTTCL
RFPGQLNAYL RKLAVNMIPF PRLHFFVVGF APLTAVGTQK FKTYSVSELT QQMFDSKNMM
TACDPKKGRY LTVAAMFRGK ISMKDVDEQM SMVQSKNSSL FVEWIPSNVK TAVCDIAPTG
LEMSATFVGN TTSIQELFKR ISDQFTVMFR RKAFLHWYTG EGMDEMEFSE AESNMNDLLS
EYQQYQDATV EDAEEFLVN
