ID   TBB2_OOMCK              Reviewed;         423 AA.
AC   P50260;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Tubulin beta-2 chain;
DE   AltName: Full=Beta-2-tubulin;
DE   Flags: Fragment;
GN   Name=TUBB2;
OS   Oomycete-like sp. (strain MacKay2000).
OC   Eukaryota; Sar; Stramenopiles.
OX   NCBI_TaxID=129195;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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}.
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DR   EMBL; Z67992; CAA91940.1; -; mRNA.
DR   AlphaFoldDB; P50260; -.
DR   SMR; P50260; -.
DR   PRIDE; P50260; -.
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; 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.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding.
FT   CHAIN           <1..423
FT                   /note="Tubulin beta-2 chain"
FT                   /id="PRO_0000048376"
FT   REGION          394..423
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        403..423
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         115..121
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   423 AA;  47367 MW;  4EB030756DD3A45A CRC64;
     DEHGVDPTGT YHGDSDLQLE RINVYYNEAT GGRYVPRAIL MDLEPGTMDS VRAGPFGQLF
     RPDNFVFGQT GAGNNWAKGH YTEGAELIDS VLDVVRKEAE SCDCLQGFQI THSLGGGTGS
     GMGTLLISKI REEYPDRVML TFSVCPSPKV SDTVVEPYNA TLSVHQLVEN ADEVMVLDNE
     ALYDICFRTL KLTTPTYGDL NHLVCACMSG VTSCLRFPGQ LNSDLRKLAV NLIPFPRLHF
     FMIGFAPLTS RGSQQYRALT VPELTQQQFD AKNMMCAADP RHGRYLTASC MFRGRMSTKE
     VDEQMLNVQN KNSSYFVEWI PNNIKSSVCD IPPKGLKMSA CFIGNSTAIQ EMFKRIGEQF
     TAMFRRKAFL HWYTGEGMDE MEFTEAESNM NDLVSEYQQY QDATAEEEGE YDEDEDDEGG
     DYA