ID   TBB_LEIME               Reviewed;         445 AA.
AC   P21148;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Tubulin beta chain;
DE   AltName: Full=Beta-tubulin;
OS   Leishmania mexicana.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5665;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3185616; DOI=10.1016/0166-6851(88)90149-1;
RA   Fong D., Lee B.;
RT   "Beta tubulin gene of the parasitic protozoan Leishmania mexicana.";
RL   Mol. Biochem. Parasitol. 31:97-106(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}.
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DR   EMBL; M23441; AAA29276.1; -; Genomic_DNA.
DR   PIR; A54515; A54515.
DR   AlphaFoldDB; P21148; -.
DR   SMR; P21148; -.
DR   PRIDE; P21148; -.
DR   VEuPathDB; TriTrypDB:LmxM.32.0794; -.
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..445
FT                   /note="Tubulin beta chain"
FT                   /id="PRO_0000048299"
FT   BINDING         140..146
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   445 AA;  50052 MW;  9BE2309619E948FE CRC64;
     MREIVSCQAG QCGNQIGSKF WEVIADEHGV DPTGSYQGDS DLQLERINVY FDESAGGRYV
     PRAVLMDLEP GTMDSVRAGP YGQLFRPDNF IFGQSGAGNN WAKGHYTEGA ELIDSVLDVC
     RKEAESCDCL QGFQLSHSLG GGTGSGMGTL LISKLREEYP DRIMMTFSVI PSPRVSDTVV
     EPYNTTLSVH QLVENSDESM CIDNEALYDI CFRTLKLTTP TFGDLNHLVA AVMSGVTCCL
     RFPGQLNSDL RNRLAVNLVP FPRLHFFMMG FAPLTSRGSQ EYRQGLSVAD VTQQMFDAKN
     MMQAADPRHG RYLTASALFR GRMSTKEVDE QMLNVQNKNS SYFIEWIPNN IKSSICDIPP
     KGLKMSVTFI GNNTCIQEMF RRVGEQFTGM FRRKRFLHWY TGEGMDEMEF TEAESNMNDL
     VSEYQQYQDA TVEEEGEFDE EEEAY