ID   TBAN_GUITH              Reviewed;         448 AA.
AC   Q9SCC8; Q9ZTL4;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Tubulin alpha chain, nucleomorph;
DE   AltName: Full=Nucleomorph alpha-tubulin;
GN   Name=tubA; Synonyms=atubNM;
OS   Guillardia theta (Cryptophyte) (Cryptomonas phi).
OG   Nucleomorph.
OC   Eukaryota; Cryptophyceae; Pyrenomonadales; Geminigeraceae; Guillardia.
OX   NCBI_TaxID=55529;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11323671; DOI=10.1038/35074092;
RA   Douglas S.E., Zauner S., Fraunholz M., Beaton M., Penny S.L., Deng L.-T.,
RA   Wu X., Reith M.E., Cavalier-Smith T., Maier U.-G.;
RT   "The highly reduced genome of an enslaved algal nucleus.";
RL   Nature 410:1091-1096(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-412.
RX   PubMed=10486984; DOI=10.1093/oxfordjournals.molbev.a026221;
RA   Keeling P.J., Deane J.A., Hink-Schauer C., Douglas S.E., Maier U.-G.,
RA   McFadden G.I.;
RT   "The secondary endosymbiont of the cryptomonad Guillardia theta contains
RT   alpha-, beta-, and gamma-tubulin genes.";
RL   Mol. Biol. Evol. 16:1308-1313(1999).
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   -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR   EMBL; AJ010592; CAB40411.1; -; Genomic_DNA.
DR   EMBL; AF050093; AAD02572.1; -; Genomic_DNA.
DR   PIR; F90104; F90104.
DR   RefSeq; XP_001713198.1; XM_001713146.1.
DR   AlphaFoldDB; Q9SCC8; -.
DR   SMR; Q9SCC8; -.
DR   PRIDE; Q9SCC8; -.
DR   GeneID; 857555; -.
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   GTP-binding; Microtubule; Nucleotide-binding.
FT   CHAIN           1..448
FT                   /note="Tubulin alpha chain, nucleomorph"
FT                   /id="PRO_0000233348"
FT   BINDING         142..148
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   448 AA;  49803 MW;  D6C68139CC084F3A CRC64;
     MREVLSIHIG QAGIQVGNAC WELYCLEHGI NPDGSIIQDF NKKKNDDAFS TFFSETSTGK
     RVPRCVFLDL ESGVIDEVKN GRYKNLYHPE QLICGNEDAA NNYARGHYTI GKEIIEIALD
     RIRKLVENCS GLQGFLIFNS VGGGTGSGLG SLLLERLSLD YGKKSKLGFT VYPSPQVSTA
     VVEPYNSVLA THSLLEHTDV AVVLDNEAIY EICQRSLNIE RPTYTNLNRL IAQVISSITA
     SLRFDGALNV DITEFQTNLV PYPRIHFMLS SLAPVISLEM ANHEQYSTAE ITNAAFEPNS
     MMAKCDPRRG KYMACCLMFR GDVAPKDVNG SVAAIKTKKT IQFVDWCPTG FKCGINYQPP
     TVVPDGDLAK VDRAVCMISN STAISEVFSR INKKFDLMYS KRAFVHWYVG EGMEEGEFNE
     AREDMAALEK DYEEVGSESQ DLISNSFF