ID   TBA_DICPU               Reviewed;         333 AA.
AC   A0AAL4;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Tubulin alpha chain;
DE   AltName: Full=Alpha-tubulin;
DE   Flags: Fragment;
GN   Name=tuba;
OS   Dictyostelium purpureum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=5786;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=WS321;
RX   PubMed=17068267; DOI=10.1126/science.1130670;
RA   Schaap P., Winckler T., Nelson M., Alvarez-Curto E., Elgie B., Hagiwara H.,
RA   Cavender J., Milano-Curto A., Rozen D.E., Dingermann T., Mutzel R.,
RA   Baldauf S.L.;
RT   "Molecular phylogeny and evolution of morphology in the social amoebas.";
RL   Science 314:661-663(2006).
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   -!- PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal
CC       and re-addition of a C-terminal tyrosine residue by the enzymes tubulin
CC       tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL),
CC       respectively. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR   EMBL; AM168456; CAJ44838.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0AAL4; -.
DR   SMR; A0AAL4; -.
DR   STRING; 5786.XP_003292600.1; -.
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..>333
FT                   /note="Tubulin alpha chain"
FT                   /id="PRO_0000312172"
FT   BINDING         50..56
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
FT   NON_TER         333
SQ   SEQUENCE   333 AA;  37009 MW;  B01B950DD1E802CF CRC64;
     LRGKEDAANN YARGHYTVGK ELIEVCADRI RKLADQCEGL QGFLVFHSVG GGTGSGFGSL
     LLQRLALEYG GKKSKLDFCV YPSPQVSTSV VEPYNSVLST HSLLEHTDVS FMLDNEAIYN
     ICKKSLDIEK PTYTNLNRLI AQVISSLTSS LRFPGPLNLD INDIQTNLVP FPRLHFVLCS
     YAPVISKEKS EHENITVDAI TNSVFSENNI MAKCQPHLGK YMACCLMYRG NIVPKEAQKA
     VQNIRNEKSK TVSFVDWSPT GFKCGINNSK PTTVLGENGD NMARTEKSVC MLSNTTAISQ
     VFSRINHKFD LMYIKRAFVH WYVGEGMEEG EGL