TBB1_SUIBO
ID TBB1_SUIBO Reviewed; 446 AA.
AC Q6EVK8;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Tubulin beta-1 chain;
DE AltName: Full=Beta-1-tubulin;
GN Name=TUBB1;
OS Suillus bovinus (Jersey cow bolete) (Boletus bovinus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Suillineae; Suillaceae; Suillus.
OX NCBI_TaxID=48563;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SBH1;
RX PubMed=15770509; DOI=10.1007/s00294-005-0564-6;
RA Juuti J.T., Jokela S., Tarkka M.T., Paulin L., Lahdensalo J.;
RT "Two phylogenetically highly distinct beta-tubulin genes of the
RT basidiomycete Suillus bovinus.";
RL Curr. Genet. 47:253-263(2005).
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; AJ698040; CAG27308.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6EVK8; -.
DR SMR; Q6EVK8; -.
DR PRIDE; Q6EVK8; -.
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..446
FT /note="Tubulin beta-1 chain"
FT /id="PRO_0000048431"
FT BINDING 140..146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
SQ SEQUENCE 446 AA; 50033 MW; ADF826385ED3216E CRC64;
MREIVHIQTG QCGNQIGAKF WEVVSDEHGI ERDGLYKGTN DMQLERISVY YNEIGSNKYV
PRAVLVDLEP GTMDSVRSGP LGGLFRPDNF IFGQSGAGNN WAKGHYTEGA ELVDSVLDVV
RKEAEGTDCL QGFQITHSLG GGTGAGMGTL LMSKIREEYP DRMMCTYSVV PSPAVSDTVV
EPYNATLSVH QLVENSDETF CIDNEALYDI CFRTLKLSTP TYGDLNHLVS FVMSGITTCL
RFPGQLNSDL RKLAVNMVPF PRLHFFMTGF APLTARGSQQ YRAVTVPELT QQMFDAKNMM
AASDPRHGRY LTVAAVFRGK VSMKEVEEQM QNVQNKNSAY FVEWIPNNVL SAQCDIPPRG
VKMAVTFLGN STAIQELFKR VSDHFTAMFK RKAFLHWYTQ EGMDEMEFTE AESNMQDLIA
EYQQYQDATV EEEAEYEEEV PADEES
