TBB_TRIRU
ID TBB_TRIRU Reviewed; 447 AA.
AC Q5UBX3;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Tubulin beta chain;
DE AltName: Full=Beta-tubulin;
OS Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=5551;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zomorodian K., Tarazooie B., Kordbacheh P., Rezaian M., Korramizadeh M.R.,
RA Rezaie S.;
RT "Molecular characterization of beta-tubulin gene from dermatophyte pathogen
RT Trichophyton rubrum.";
RL Submitted (SEP-2004) 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; AY763789; AAV33733.1; -; mRNA.
DR AlphaFoldDB; Q5UBX3; -.
DR SMR; Q5UBX3; -.
DR VEuPathDB; FungiDB:TERG_07904; -.
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..447
FT /note="Tubulin beta chain"
FT /id="PRO_0000048433"
FT BINDING 140..146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 447 AA; 49670 MW; 25E7A3AD41E01AD8 CRC64;
MREIVHLQTG QCGNQIGAAF WQTIAGEHGL DGSGHYTGSS DLQLERMNVY FNEASSKKYV
PRAVLVDLEP AALDAVRAGP FGQLFRPDNV VFGQSGAGNN WAKGHYTEGA NLVDQVIDVV
RREAEGCDCL QGFQITHSLG GGTGAGMGTL LISKIREEFP AGMMATFSVV PSPMVSDTVV
EPYNATLSIH QLVEHSDETF CIDNEALYNI CMRTLKLTNP SYGDLNHLVS AVMSGVSTSL
RFPGQLNSDL RKLAVNMVPF PRLHFFMVGF APLTSRNAYS FRAVSVPELT QQMFDPKNMM
AATDFRSGRY LTCSAIFRGK VSMKEVEDQM RNIQNKNSAY FVEWIPNNVQ TALCSIPPRG
LQMSSTFVGN STSIQELFKR VGDQFTAMFR KKAFLFWYTG EGMDEMEFTE AENNMNDLVS
EYQQYQDASV SDGEEEYLED EQLEGEE
