ID   TBB1_ECHMU              Reviewed;         448 AA.
AC   Q9NFZ7;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Tubulin beta-1 chain;
DE   AltName: Full=Beta-tubulin 1;
GN   Name=TUB-1;
OS   Echinococcus multilocularis (Fox tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus.
OX   NCBI_TaxID=6211;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=H-95;
RX   PubMed=10779606; DOI=10.1016/s0166-6851(00)00178-x;
RA   Brehm K., Kronthaler K., Jura H., Frosch M.;
RT   "Cloning and characterization of beta-tubulin genes from Echinococcus
RT   multilocularis.";
RL   Mol. Biochem. Parasitol. 107:297-302(2000).
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; AJ249548; CAB91640.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9NFZ7; -.
DR   SMR; Q9NFZ7; -.
DR   eggNOG; KOG1375; Eukaryota.
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..448
FT                   /note="Tubulin beta-1 chain"
FT                   /id="PRO_0000048290"
FT   REGION          428..448
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   448 AA;  50211 MW;  64C8A46E536FEEAF CRC64;
     MREIVHIQAG QCGNQIGSKF WEVISDEHGV DPTGSYHGDS DLQLERINVY YSEASGGKYV
     PRCVLVDLEP GTMDSVRAGP FGQLFRPDNF VFGQSGAGNN WAKGHYTEGA ELVESVLDVI
     RKECESCDCL QGFQMCHSLG GGTGSGMGTL LISKMREEFP DRIMNTFSVM PSPKVSDTVV
     EPYNATLSIH QLVENTDETF CIDNEALYDI CFRTLKLTNP TYGDLNHLVS ATMSGVTTCL
     RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRVLTVAELT QQMFDAKNMM
     AACDPRHGRY LTVAAMFRGR MSMKEVDDQM LNAQNKNSSY FVEWIPNNVK TAVCDIPPRG
     LKMSVTFMGN TTAIQEIFKR VSEQFTVMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
     EYQQYQEAGI GDDEEEDEEG VMGEEIDA