ID   TBB_THAWE               Reviewed;         443 AA.
AC   Q9LKI8;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Tubulin beta chain;
DE   AltName: Full=Beta-tubulin;
OS   Thalassiosira weissflogii (Marine diatom).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC   Thalassiosiraceae; Conticribra.
OX   NCBI_TaxID=1577725;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Armbrust V.;
RT   "Structural features of nuclear genes in the centric diatom Thalassiosira
RT   weissflogii (Bacillariophyceae).";
RL   Submitted (JUN-2000) 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 (By similarity).
CC       {ECO:0000250}.
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR   EMBL; AF276908; AAF81906.1; -; mRNA.
DR   AlphaFoldDB; Q9LKI8; -.
DR   SMR; Q9LKI8; -.
DR   PRIDE; Q9LKI8; -.
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..443
FT                   /note="Tubulin beta chain"
FT                   /id="PRO_0000048317"
FT   BINDING         140..146
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   443 AA;  49520 MW;  3BFA1BE829753418 CRC64;
     MREIVHIQGG QCGNQIGAKF WEVMSDEHGV DPTGTYHGDS DLQLERINVY FNEATGGRYV
     PRAILMDLEP GTMDSVRAGP FGQLFRPDNF VFGQTGAGNN WAKGHYTEGA ELIDSVLDVV
     RKEAESCDCM QGFQLTHSMG GGTGAGMGTL LISKIREEYP DRVMSTYSVI PSPKVSDTVV
     EPYNATLSVH QLVENADQCF ALDNEALYDI CFRTLKLTTP TYGDLNHLIA AAVCGTTCCL
     RFPGQLNCDL RKLAVNMVPF PRLHFFMVGY APLTSRGSQQ YRALTVPELT QQCFDAKNMM
     CAADPRHGRY LTCAVLFRGR MSSKEVDEQM LNVVNKSSSY FVEWIPNNVK ASICDIPPKG
     LKMATTFVGN TTAVQETWKR VAEQFTVMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
     EYQQYQDATA DEEGEFDEDE MEG