ID   TBA1_ENTHI              Reviewed;         455 AA.
AC   P31017;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Tubulin alpha-1 chain;
GN   Name=TUB1;
OS   Entamoeba histolytica.
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=5759;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 30459 / HM-1:IMSS;
RX   PubMed=8076825; DOI=10.1016/0378-1119(94)90299-2;
RA   Sanchez M.A., Peattie D.A., Wirth D., Orozco E.;
RT   "Cloning, genomic organization and transcription of the Entamoeba
RT   histolytica alpha-tubulin-encoding gene.";
RL   Gene 146:239-244(1994).
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; L07898; AAA57315.1; -; Genomic_DNA.
DR   AlphaFoldDB; P31017; -.
DR   SMR; P31017; -.
DR   STRING; 5759.rna_EHI_005950-1; -.
DR   PRIDE; P31017; -.
DR   VEuPathDB; AmoebaDB:EHI5A_136790; -.
DR   VEuPathDB; AmoebaDB:EHI5A_163770; -.
DR   VEuPathDB; AmoebaDB:EHI7A_112330; -.
DR   VEuPathDB; AmoebaDB:EHI8A_121620; -.
DR   VEuPathDB; AmoebaDB:EHI_005950; -.
DR   VEuPathDB; AmoebaDB:KM1_191480; -.
DR   eggNOG; KOG1376; 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; IPR002452; Alpha_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; PR01162; ALPHATUBULIN.
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.
PE   3: Inferred from homology;
KW   Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding.
FT   CHAIN           1..455
FT                   /note="Tubulin alpha-1 chain"
FT                   /id="PRO_0000048169"
FT   BINDING         147..153
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   455 AA;  50275 MW;  9A204A83B70C1AD0 CRC64;
     MREVITINIG QAGCQLGNKC WELFCLEHGI QPDGTAIANS NEKRSVITGG IDTAYNAFFQ
     ELQNGRHVPR AIFVDTEPTV IDEIKTGEYC GLYHPEHLIC GKEDASSNFA KGKTGYEPLL
     NQTMDAIRKA TENCTGLQGF FIYNSVGGGT GSGFTAALCE KLADKYTKKT KLNTVIWPSP
     KLSSGVVEPY NAVLNTHAMM KFVNCTFMVD NESIYKICQK QLGVHSPSYF HLNQLIAQAM
     SSITASLRFE GTLNVDLNEF PTNLVPFPRD HFAMMSYAPI VTPEKAIRQT LSVQELTSSL
     FDPNSLMIQC DDINKGKFMS CCMMYRGDVS SREVNLAVSG IKKQNTVPFV GWCPCSFKCG
     INSQPATAVP GSSYASTARS ACMIANHTAM CQVFQKVNQN FDLMFGKRAF VHHYVGEGME
     ENEFTDARQD LYELEVDYAN LALDNTIEGE SMTAQ