ID   TBB4_OOMCK              Reviewed;         451 AA.
AC   P50262;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Tubulin beta-4 chain;
DE   AltName: Full=Beta-4-tubulin;
GN   Name=TUBB4;
OS   Oomycete-like sp. (strain MacKay2000).
OC   Eukaryota; Sar; Stramenopiles.
OX   NCBI_TaxID=129195;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Mackay R.M., Gallant J.W.;
RT   "Expression of beta-tubulin genes in the sporophyte and gametophyte of the
RT   red alga Porphyra purpurea.";
RL   Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   REVISES SPECIES OF ORIGIN.
RX   PubMed=9783459; DOI=10.1111/j.1550-7408.1998.tb05117.x;
RA   Keeling P.J., Deane J.A., McFadden G.I.;
RT   "The phylogenetic position of alpha- and beta-tubulins from the
RT   Chlorarachnion host and Cercomonas (Cercozoa).";
RL   J. Eukaryot. Microbiol. 45:561-570(1998).
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}.
CC   -!- CAUTION: Was originally (Ref.1) thought to originate from Porphyra
CC       purpurea. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z67994; CAA91942.1; -; Genomic_DNA.
DR   AlphaFoldDB; P50262; -.
DR   SMR; P50262; -.
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..451
FT                   /note="Tubulin beta-4 chain"
FT                   /id="PRO_0000048378"
FT   REGION          417..451
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..451
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         140..146
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   451 AA;  50367 MW;  AD0EA63616116339 CRC64;
     MREIVHIQGG QCGDQIGAKF WEVISDEHGI DPTGTYNGDS DLQLERVNVY YNEATGGRYV
     PRAVLMDLEP GTMDSVRAGP YGQLFRPDNF VFGQTGAGNN WAKGHYTEGA ELIDSVLDVV
     RKEAEQCDCL QGFQVTHSLG GGTGSGMGTL LISKIREEYP DRVMMTFSVC PSPKVSDTVV
     EPYNATLSVH QLVENADEVM VLDNEALYDI CFRTLKLTTP TYGDLNHLVC VCMSGVTSSL
     RFPGQLNADL RKLAVNLIPF PRLHFFMLGF APLTSRGSQQ YRALTVPELT SQCFDAKNMM
     CAADPRHGRY LTASCMFRGR MSTKEVDEQM LNVQNKNSSY FVEWIPNNIK SSVCDIPPKG
     LKMSATFVGN STAIQEMFKR VGEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
     EYQQYQDATA EEEGEYDEDD GGYGDEDDGM M