ID   TBB_TRYCR               Reviewed;         442 AA.
AC   P08562; Q27915;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Tubulin beta chain;
DE   AltName: Full=Beta-tubulin;
OS   Trypanosoma cruzi.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX   NCBI_TaxID=5693;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DM28;
RA   Amorim M.I., Traub-Cseko Y.M.;
RL   Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 203-299.
RC   STRAIN=Stock EP;
RX   PubMed=3276517; DOI=10.1111/j.1432-1033.1988.tb13788.x;
RA   Maingon R., Gerke R., Rodriguez M., Urbina J., Hoenicka J., Negri S.,
RA   Aguirre T., Nehlin J., Knapp T., Crampton J.;
RT   "The tubulin genes of Trypanosoma cruzi.";
RL   Eur. J. Biochem. 171:285-291(1988).
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   ---------------------------------------------------------------------------
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; M97956; AAA91956.1; -; Genomic_DNA.
DR   EMBL; M96849; AAA91958.1; -; Genomic_DNA.
DR   EMBL; X07145; CAA30150.1; -; Genomic_DNA.
DR   PIR; S00269; S00269.
DR   AlphaFoldDB; P08562; -.
DR   SMR; P08562; -.
DR   PRIDE; P08562; -.
DR   ABCD; P08562; 1 sequenced antibody.
DR   VEuPathDB; TriTrypDB:BCY84_04025; -.
DR   VEuPathDB; TriTrypDB:C3747_133g40; -.
DR   VEuPathDB; TriTrypDB:C4B63_333g16; -.
DR   VEuPathDB; TriTrypDB:Tc_MARK_6063; -.
DR   VEuPathDB; TriTrypDB:TcBrA4_0038090; -.
DR   VEuPathDB; TriTrypDB:TcCL_ESM07655; -.
DR   VEuPathDB; TriTrypDB:TcCLB.411235.9; -.
DR   VEuPathDB; TriTrypDB:TcCLB.506563.40; -.
DR   VEuPathDB; TriTrypDB:TcCLB.509695.120; -.
DR   VEuPathDB; TriTrypDB:TCDM_13503; -.
DR   VEuPathDB; TriTrypDB:TcG_07744; -.
DR   VEuPathDB; TriTrypDB:TCSYLVIO_007352; -.
DR   VEuPathDB; TriTrypDB:TcYC6_0022480; -.
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..442
FT                   /note="Tubulin beta chain"
FT                   /id="PRO_0000048320"
FT   BINDING         140..146
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        219..223
FT                   /note="TPTFG -> APNVR (in Ref. 2; CAA30150)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        265..269
FT                   /note="FFMMG -> LIMTC (in Ref. 2; CAA30150)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        274..278
FT                   /note="SSRGS -> TSPAR (in Ref. 2; CAA30150)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        288..289
FT                   /note="DV -> EL (in Ref. 2; CAA30150)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        295..299
FT                   /note="DAKNM -> ECQNL (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   442 AA;  49573 MW;  0E089C2F7ABED8E8 CRC64;
     MREIVCVQAG QCGNQIGSKF WEVISDEHGV DPTGTYQGDS DLQLERINVY FDEATGGRYV
     PRAVLIDLEP GTMDSVRAGP YGQIFRPDNF IFGQSGAGNN WAKGHYTEGA ELIDSVLDVC
     RKEAESCDCL QGFQICHSLG GGTGSGMGTL LISKLREEYP DRIMMTFSII PSPKVSDTVV
     EPYNTTLSVH QLVENSDESM CIDNEALYDI CFRTLKLTTP TFGDLNHLVS AVVSGVTCCL
     RFPGQLNSDL RKLAVNLVPF PRLHFFMMGF APLSSRGSQQ YRGLSVPDVT QQMFDAKNMM
     QAADPAHGRY LTASALFRGR MSTKEVDEQM LNVQNKNSSY FIEWIPNNIK SSICDIPPKG
     LKMAVTFVGN NTCIQEMFRR VGEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
     EYQQYQDATI EEEGEFDEEE QY