ID   TBB_NAEPR               Reviewed;         451 AA.
AC   P34108; Q25564;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Tubulin beta chain;
DE   AltName: Full=Beta-tubulin;
OS   Naegleria pringsheimi (Amoeba).
OC   Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC   Vahlkampfiidae; Naegleria.
OX   NCBI_TaxID=234921;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NEG;
RX   PubMed=8289261; DOI=10.1016/s0022-2836(05)80045-2;
RA   Lai E.Y., Remillard S.P., Fulton C.;
RT   "A beta-tubulin gene of Naegleria encodes a carboxy-terminal tyrosine.
RT   Aromatic amino acids are conserved at carboxy termini.";
RL   J. Mol. Biol. 235:377-388(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ATCC 30961 / NB-1;
RA   Choi Y.-J., Park H.-L., Lee J.-H.;
RT   "Cloning and sequence determination of alpha-tubulin, beta-tubulin and
RT   flagellar calmodulin.";
RL   Misainmurhag Hoiji 33:40-45(1995).
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; Z13961; CAA78362.1; -; Genomic_DNA.
DR   EMBL; X81050; CAA56940.1; -; mRNA.
DR   PIR; S30514; S30514.
DR   AlphaFoldDB; P34108; -.
DR   SMR; P34108; -.
DR   PRIDE; P34108; -.
DR   KEGG; ngr:NAEGRDRAFT_55423; -.
DR   KEGG; ngr:NAEGRDRAFT_56391; -.
DR   KEGG; ngr:NAEGRDRAFT_83350; -.
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..451
FT                   /note="Tubulin beta chain"
FT                   /id="PRO_0000048302"
FT   REGION          426..451
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..451
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         140..146
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        184
FT                   /note="N -> H (in Ref. 2; CAA56940)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        380
FT                   /note="R -> S (in Ref. 2; CAA56940)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        442..444
FT                   /note="AEG -> EGA (in Ref. 2; CAA56940)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   451 AA;  50511 MW;  842777FC706EBDC1 CRC64;
     MREIVHIQAG QCGNQIGAKF WEVISDEHGV DPTGAYHGDS DLQLERINVY YNEATGGRYV
     PRAILMDLEP GTMDSVRAGP YGQIFRPDNF VFGQTGAGNN WAKGHYTEGA ELIDSVLDVV
     RKEAESCDCL QGFQIAHSLG GGTGSGMGTL LISKIREEYP DRMMMTFSVF PSPKVSDTVV
     EPYNATLSVH QLVENADEVM CIDNEALYDI CFRTLKLTTP TFGDLNHLVS IVMSGVTCCL
     RFPGQLNSDL RKLAVNLIPF PRLHFFLIGF APLTSRGSQQ YRALTVPELT QQMFDAKNMM
     AASDPRHGRY LTASAMFRGR MSTKEVDEQM LNVQNKNSSY FVEWIPNNIK SSVCDIPPRG
     LKMAATFIGN STAIQEMFKR VSEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
     EYQQYQDATA EEEGEFDENE GAEGEEQPAD Y