ID   TBA_ZYMTR               Reviewed;         450 AA.
AC   O94128;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Tubulin alpha chain;
OS   Zymoseptoria tritici (Speckled leaf blotch fungus) (Septoria tritici).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=1047171;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ST16;
RX   PubMed=9829778;
RX   DOI=10.1002/(sici)1097-0169(1998)41:3<247::aid-cm5>3.0.co;2-7;
RA   Rohel E.A., Payne A.C., Hall L., Barker H., Butters J., Holloman D.W.;
RT   "Isolation and characterization of alpha-tubulin genes from Septoria
RT   tritici and Rhynchosporium secalis, and comparative analysis of fungal
RT   alpha-tubulin sequences.";
RL   Cell Motil. Cytoskeleton 41:247-253(1998).
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; Y14509; CAA74849.1; -; Genomic_DNA.
DR   AlphaFoldDB; O94128; -.
DR   SMR; O94128; -.
DR   PRIDE; O94128; -.
DR   VEuPathDB; FungiDB:ZT3D1_G9572; -.
DR   VEuPathDB; FungiDB:ZTRI_10.67; -.
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..450
FT                   /note="Tubulin alpha chain"
FT                   /id="PRO_0000048194"
FT   BINDING         142..148
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   SITE            450
FT                   /note="Involved in polymerization"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   450 AA;  50008 MW;  A4441393B4A5C2CD CRC64;
     MREVISLNVG QAGCQIANSC WELYCLEHGI QPDGYLTEER KAAEDDDGFS TFFSETGNGK
     YVPRTIYADL EPNVVDEVRT GTYRSLFHPE LMITGKEDAS NNYARGHYTV GKELIDQVLD
     KVRHVADNCS GLQGFLVFHS FGGGTGSGFG ALLMERLSVD YGKKCKLEFC VYPAPQVATS
     VVEPYNSILT THTTLEHSDC SFMVDNEAIY DICRRNLGIE RPNYENLNRL IAQVVSSITA
     SLRFDGSLNV DLNEFQTNLV PYPRIHFPLV AYAPIVSAAK AAHEANSVQE ISMSCFEPNS
     QMVKCDPRNG KYMATCLLYR GDVVPKDVHQ AVATLKTKRT IQFVDWCPTG FKIGICYQPP
     QNVPNGDLAK VNRAVCMLSN TTAIAEAWSA LSHKFDLMYS KRAFVHWYVG EGMEEGEFSE
     AREDLAALER DYEEVAADSA EGDEGGEAEY