ID   TBA_CANAX               Reviewed;         448 AA.
AC   P87066;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Tubulin alpha chain;
GN   Name=TUB1;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10231 / CBS 6431 / CIP 48.72 / DSM 1386 / NBRC 1594;
RX   PubMed=9099874; DOI=10.1016/s0378-1119(96)00737-8;
RA   Daly S., Yacoub A., Dundon W., Mastromei G., Islam K., Lorenzetti R.;
RT   "Isolation and characterization of a gene encoding alpha-tubulin from
RT   Candida albicans.";
RL   Gene 187:151-158(1997).
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; U38534; AAB53194.1; -; Genomic_DNA.
DR   AlphaFoldDB; P87066; -.
DR   SMR; P87066; -.
DR   ChEMBL; CHEMBL3988634; -.
DR   CGD; CAL0000195890; TUB1.
DR   VEuPathDB; FungiDB:CAWG_02186; -.
DR   VEuPathDB; FungiDB:CR_09120C_A; -.
DR   PhylomeDB; P87066; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005828; C:kinetochore microtubule; IDA:CGD.
DR   GO; GO:0005874; C:microtubule; IDA:CGD.
DR   GO; GO:0005819; C:spindle; IDA:CGD.
DR   GO; GO:0045298; C:tubulin complex; IGI:CGD.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IGI:CGD.
DR   GO; GO:0007017; P:microtubule-based process; IMP:CGD.
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..448
FT                   /note="Tubulin alpha chain"
FT                   /id="PRO_0000048146"
FT   BINDING         143..149
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   SITE            448
FT                   /note="Involved in polymerization"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   448 AA;  49968 MW;  345D45B737ECF3A1 CRC64;
     MREVISINVG QAGCQIGNAC WELYSQEHGI RPDGYLQEGL DRPKGGEEGF STFFSETGSG
     KYVPRALYVD LEPNVIDEVR TGVYKDLFHP EQLIAGKEDA ANNYARGHYT VGREILDDIL
     DRVRRMSDQC DGLQGFLFTH SLGGGTGSGL GSLLLEQLSL DYGKKSKLEF AVYPAPQVST
     SVVEPYNTVL TTHTTLEHAD CTFMVDNEAI YDMCRRNLDI ARPNFSSLNN LIAQVVSSVT
     ASLRFDGSLN VDLNEFQTNL VPYPRIHFPL VSYAPVFSKS RATHEANSVS EITQSCFEPG
     NQMVKCDPRT GKYMATCLLY RGDVVTRDVQ NAVAQVKSKK TVQLVDWCPT GFKIGICYQP
     PTAIKGSELA SASRAVCMLS NTTAIAEAWR RIDRKFDLMY SKRAFVHWYV GEGMEEGEFT
     EAREDLAALE RDYIEVGTDS FPEEEEEY