TBA_GIBZE
ID TBA_GIBZE Reviewed; 449 AA.
AC Q5I2J3; A0A0E0RMY2; Q4IQ69; V6QUE5;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Tubulin alpha chain;
DE AltName: Full=Alpha-tubulin;
GN Name=TUB1; ORFNames=FGRRES_00639, FGSG_00639;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ZF43;
RX PubMed=15989278;
RA Chen C.-J., Li J., Qi Z.Q., Wang J.-X., Zhou M.-G.;
RT "Cloning of alpha-tubulin gene from Fusarium raminearum and analyzing its
RT relationship with carbendazim-resistance.";
RL Wei Sheng Wu Xue Bao 45:288-291(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
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; AY860418; AAW55660.1; -; Genomic_DNA.
DR EMBL; DS231663; ESU05846.1; -; Genomic_DNA.
DR EMBL; HG970332; CEF72607.1; -; Genomic_DNA.
DR RefSeq; XP_011316331.1; XM_011318029.1.
DR AlphaFoldDB; Q5I2J3; -.
DR SMR; Q5I2J3; -.
DR STRING; 5518.FGSG_00639P0; -.
DR PRIDE; Q5I2J3; -.
DR EnsemblFungi; ESU05846; ESU05846; FGSG_00639.
DR GeneID; 23548123; -.
DR KEGG; fgr:FGSG_00639; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G01613; -.
DR eggNOG; KOG1376; Eukaryota.
DR HOGENOM; CLU_015718_0_0_1; -.
DR InParanoid; Q5I2J3; -.
DR Proteomes; UP000070720; Chromosome 1.
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;
KW Reference proteome.
FT CHAIN 1..449
FT /note="Tubulin alpha chain"
FT /id="PRO_0000048173"
FT BINDING 142..148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT SITE 449
FT /note="Involved in polymerization"
FT /evidence="ECO:0000250"
FT CONFLICT 82
FT /note="A -> P (in Ref. 1; AAW55660)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 449 AA; 49971 MW; 0E87097487D0E58F CRC64;
MREVISINVG QAGCQIANSC WELYCLEHGI QPDGYLTEER KAQDPDQGFS TFFSETGNGK
HVPRAIYCDL EPNVVDEVRT GAYRNLFHPE MMITGKEDAS NNYARGHYTV GKELIDGVLD
KIRRVADNCA GLQGFLVFHS FGGGTGSGFG ALLMERLSVD YGKKSKLEFC VYPAPQTATS
VVEPYNSILT THTTLEHSDC SFMVDNEAIY DICRRNLGLE RPNYENLNRL IAQVVSSITA
SLRFDGSLNV DLNEFQTNLV PYPRIHFPLV AYSPVISAAK AAHEANSVQE MTMSCFEPNN
QMVKCDPRHG KYMATCLLYR GDVVPNDAHA AVATLKTKRT IQFVDWCPTG FKLGICYQAP
ENVPNGDLAK VSRAVCMLSN TTAIAEAWSS LSLKFDLMHS KRAFVHWYVG EGMEEGEFSE
AREDLAALER DYEEVATDSM GDEELEAEY
