TBA2_EMENI
ID TBA2_EMENI Reviewed; 451 AA.
AC P24634; C8VBQ7; Q5AVW0;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Tubulin alpha-2 chain;
GN Name=tubB; ORFNames=AN7570;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1672037; DOI=10.1007/bf00282651;
RA Doshi P., Bossie C.A., Doonan J.H., May G.S., Morris N.R.;
RT "Two alpha-tubulin genes of Aspergillus nidulans encode divergent
RT proteins.";
RL Mol. Gen. Genet. 225:129-141(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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; AACD01000129; EAA62150.1; -; Genomic_DNA.
DR EMBL; BN001304; CBF79648.1; -; Genomic_DNA.
DR PIR; S13337; S13337.
DR RefSeq; XP_680839.1; XM_675747.1.
DR AlphaFoldDB; P24634; -.
DR SMR; P24634; -.
DR STRING; 162425.CADANIAP00000677; -.
DR PRIDE; P24634; -.
DR EnsemblFungi; CBF79648; CBF79648; ANIA_07570.
DR EnsemblFungi; EAA62150; EAA62150; AN7570.2.
DR GeneID; 2869740; -.
DR KEGG; ani:AN7570.2; -.
DR VEuPathDB; FungiDB:AN7570; -.
DR eggNOG; KOG1376; Eukaryota.
DR HOGENOM; CLU_015718_0_0_1; -.
DR InParanoid; P24634; -.
DR OMA; ICHLHIG; -.
DR OrthoDB; 514396at2759; -.
DR Proteomes; UP000000560; Chromosome IV.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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:0030437; P:ascospore formation; IMP:AspGD.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:AspGD.
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 3: Inferred from homology;
KW Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..451
FT /note="Tubulin alpha-2 chain"
FT /id="PRO_0000048166"
FT BINDING 144..150
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT SITE 451
FT /note="Involved in polymerization"
FT /evidence="ECO:0000250"
FT CONFLICT 60
FT /note="S -> C (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="I -> L (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="S -> L (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="V -> R (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="L -> Y (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="Q -> H (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="S -> T (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 376..378
FT /note="SVS -> AVC (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 451 AA; 50059 MW; F258F359284787F2 CRC64;
MRGEVCHIHI GQAGTQLGNS AWELYLLEHG LGADGRLDPE KGEDINAGGS FETFFTETGS
GKYVPRSIFV DLDPSPIDEI RTGPYRQLFH PEQLISGKED AANNYARGHY TVGKELVDTV
VDRVRRLSDN CSSLQGFLVF HSFGGGTGSG FGALLLERLS TEYGKKSKLE FAVYPSPRVS
TAVVEPYNAV LSTHSTIENS DCTFLVDNEA VYDICRRNLD IPRPSFEHLN RLIAQVVSSI
TSSLRFDGAL NVDLNEFQTN LVPFPRIHYP LISYAPVISS NRSSHESFKV QDLTLQCAEP
NNQMVVCDPR NGKYMAVALL YRGDCVPRDC TQAIASLKAK ASFNLVEWCP TGFKVGINYQ
KPARVPGSEL APVDRSVSML SNTTAISEAW SRLDHKFDLM YSKRAFVHWY VGEGMEEGEF
SEAREDLAAL EKDYEEVAGD SLDMEGEEAE Y
