ID   TBB1_ANEPH              Reviewed;         443 AA.
AC   P33630;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Tubulin beta-1 chain;
DE   AltName: Full=Beta-1-tubulin;
GN   Name=TUBB1;
OS   Anemia phyllitidis (Fern) (Osmunda phyllitidis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Polypodiopsida; Polypodiidae; Schizaeales; Anemiaceae; Anemia.
OX   NCBI_TaxID=12940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Moepps B., Maucher H.P., Bogenberger J.M., Schraudolf H.;
RT   "Characterization of the alpha and beta tubulin gene families from Anemia
RT   phyllitidis L.Sw.";
RL   Submitted (APR-1993) 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; X69185; CAA48929.1; -; mRNA.
DR   PIR; S32668; S32668.
DR   PRIDE; P33630; -.
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-1 chain"
FT                   /id="PRO_0000048329"
FT   REGION          419..443
FT                   /note="Disordered"
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   443 AA;  49741 MW;  BEEF97379C887E85 CRC64;
     MREILHVQGG QCGNQIGAKF WEVVCTEHGI DPTGTYRGDS ETQLERVNVY YNEASCGRYV
     PRAVLMDLEP GTMDSVRSGH YGQIFRPDNF VFGQSGAGNN WAKGXYTEGA ELIDSVLAVV
     RKEAENCDCL QGFQVCHSLG GGTGSGMGTL LISKIREEYP DRMMMTFSVF ASPKVSDTVV
     EPYNATLSVH QLVENADECM VLDNEALYDI XLRTLKLVTP TFGDLNHLIS ATMSGVTCCL
     RFPGQLNSDL RKLAVNLIPF PRLHFFMVGF APLTSRGSQQ YXSLTVPELT QQMWDAKNMM
     CAADPRHGRY LTASAMFRGK MSTKEVDEQM INVQNKNSSY FVEWIPNNVK SSVCDIPPVG
     LKMAVTFIGN STSIQEMFRR VSDQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
     EYQQYQDATA EREGEYEEDY DEA