ID   TBB_ACHKL               Reviewed;         444 AA.
AC   P20802;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Tubulin beta chain;
DE   AltName: Full=Beta-tubulin;
OS   Achlya klebsiana.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Achlya.
OX   NCBI_TaxID=4767;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2394720; DOI=10.1016/s0021-9258(18)77248-7;
RA   Cameron L.E., Hutsul J.-A., Thorlacius L., Lejohn H.B.;
RT   "Cloning and analysis of beta-tubulin gene from a protoctist.";
RL   J. Biol. Chem. 265:15245-15252(1990).
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   -!- DEVELOPMENTAL STAGE: Sporangium formation.
CC   -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR   EMBL; J05597; AAA63161.1; -; Genomic_DNA.
DR   PIR; A35885; A35885.
DR   AlphaFoldDB; P20802; -.
DR   SMR; P20802; -.
DR   PRIDE; P20802; -.
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..444
FT                   /note="Tubulin beta chain"
FT                   /id="PRO_0000048390"
FT   REGION          424..444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        426..444
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         139..145
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   444 AA;  49851 MW;  7B3BF25B29626B5E CRC64;
     MRELVHIQGG QCGNQIGAKF WEVISDEHGV DPTGSYHGDS DLQLERINVY YNEATGTYVP
     RAILMDLEPG TMDSVRAGPY GQLFRPDNFV FGQTGAGNNW AKGHYTEGAE LIDSVLDVVR
     KEAESCDCLQ GFQITHSLGG GTGSGMGTLL ISKIREEYPD RIMCTYSVCP SPKVSDTVVE
     PYNATLSVHQ LVENADEVMC LDNEALYDIC FRTLKLTNPT YGDLNHLVCA AMSGITTLLR
     FPGQLNSVLK LAVNLIPFPR LHFFMIGFAP LTSRGSQQYR ALTVPELTQQ QFDAKNMMCA
     ADPRHGRYLT AACMFRGRMS TKEVDEQMLN VQNKNSSYFV EWIPNNIKAS VCDIPPKGLK
     MSTTFIGNST AIQEMFKRVS EQFTAMFRRK AFLHWYTGEG MDEMEFTEAE SNMNDLVSEY
     QQYQDATAEE EGEFDEDEEM DEMM