ID   TBA1_NEUCR              Reviewed;         454 AA.
AC   P38668; Q7RVS0;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 3.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Tubulin alpha-A chain;
GN   Name=tba-1; ORFNames=NCU09132;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=74-ORS-6a / FGSC 4200;
RX   PubMed=9163903; DOI=10.1111/j.1574-6968.1997.tb10346.x;
RA   Monnat J., Ortega Perez R., Turian G.;
RT   "Molecular cloning and expression studies of two divergent alpha-tubulin
RT   genes in Neurospora crassa.";
RL   FEMS Microbiol. Lett. 150:33-41(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; X79403; CAA55940.1; -; mRNA.
DR   EMBL; CM002236; EAA29668.2; -; Genomic_DNA.
DR   PIR; S45050; S45050.
DR   RefSeq; XP_958904.2; XM_953811.3.
DR   AlphaFoldDB; P38668; -.
DR   SMR; P38668; -.
DR   STRING; 5141.EFNCRP00000006439; -.
DR   PRIDE; P38668; -.
DR   EnsemblFungi; EAA29668; EAA29668; NCU09132.
DR   GeneID; 3875052; -.
DR   KEGG; ncr:NCU09132; -.
DR   VEuPathDB; FungiDB:NCU09132; -.
DR   HOGENOM; CLU_015718_1_1_1; -.
DR   InParanoid; P38668; -.
DR   OMA; ICHLHIG; -.
DR   Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005819; C:spindle; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0000280; P:nuclear division; IBA:GO_Central.
DR   GO; GO:0098863; P:nuclear migration by microtubule mediated pushing forces; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..454
FT                   /note="Tubulin alpha-A chain"
FT                   /id="PRO_0000048199"
FT   BINDING         142..148
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   SITE            453
FT                   /note="Involved in polymerization"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        210..213
FT                   /note="VYDI -> GMT (in Ref. 1; CAA55940)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        432
FT                   /note="A -> R (in Ref. 1; CAA55940)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   454 AA;  50256 MW;  8DDE60E6146A5816 CRC64;
     MRGEVVHIHL GQAGTQLGNS AWELYLLEHG LTQDGRKDPD STVAGEGGSY DTFFTESSNG
     KYVPRSLFVD LDPSPIDEIR TGPYRQLFHP ELLISGKEDA ANNYARGHYT VGKEMAENVL
     DRIRKITDNC HSLQGFLVFH SFGGGTGSGF GALVLERLAQ DYAKKCKLEF SVYPAPRVAT
     AVVEPYNAVL ATHSTLEHSD VTFLVDNEAV YDICRRNLDI PRPSYEHLNR LIAQVVSSIT
     SSLRFDGALN VDLNEFQTNL VPFPRVHYPL ISYAPVISAT KSAHESFKTS ELTLQCFEPN
     NQMVVCDPRN GKYMAVALLY RGDVVPRDTS AAVAALKAKS SFNLVEWCPT GFKIGINHQK
     PMSVPTASPA DGGLASVDRS VSMLSNTTAI AEAWSRLDHK FDLMYSKRAF VHWYVGEGME
     EGEFSEARED LASLEKDYEE VAGDYNDVDV DAEY