TBB1_EMENI
ID TBB1_EMENI Reviewed; 447 AA.
AC P10653; C8VT11; Q5BE48;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Tubulin beta-1 chain;
DE AltName: Full=Beta-1-tubulin;
GN Name=benA; Synonyms=rhiA; ORFNames=AN1182;
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=2959591; DOI=10.1016/0378-1119(87)90283-6;
RA May G.S., Tsang M.L.-S., Smith H., Fidel S., Morris N.R.;
RT "Aspergillus nidulans beta-tubulin genes are unusually divergent.";
RL Gene 55:231-243(1987).
RN [2]
RP SEQUENCE REVISION.
RA May G.S.;
RL Submitted (DEC-1987) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ANTIBIOTIC RESISTANCE TO RHIZOXIN.
RX PubMed=2274023; DOI=10.1007/bf00633814;
RA Takahashi M., Matsumoto S., Iwasaki S., Yahara I.;
RT "Molecular basis for determining the sensitivity of eucaryotes to the
RT antimitotic drug rhizoxin.";
RL Mol. Gen. Genet. 222:169-175(1990).
RN [4]
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 [5]
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 -!- MISCELLANEOUS: E.nidulans has two beta-tubulin genes: benA and tubC;
CC benA is expressed during vegetative growth.
CC -!- MISCELLANEOUS: Rhizoxin, an antibiotic that exhibits potent anti-
CC mitotic activity against most eukaryotic cells except for yeasts, binds
CC to beta tubulin.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; M17519; AAA33328.1; -; Genomic_DNA.
DR EMBL; AACD01000016; EAA66300.1; -; Genomic_DNA.
DR EMBL; BN001308; CBF87981.1; -; Genomic_DNA.
DR PIR; JQ0171; JQ0171.
DR RefSeq; XP_658786.1; XM_653694.1.
DR AlphaFoldDB; P10653; -.
DR SMR; P10653; -.
DR STRING; 162425.CADANIAP00001443; -.
DR PRIDE; P10653; -.
DR EnsemblFungi; CBF87981; CBF87981; ANIA_01182.
DR EnsemblFungi; EAA66300; EAA66300; AN1182.2.
DR GeneID; 2876958; -.
DR KEGG; ani:AN1182.2; -.
DR VEuPathDB; FungiDB:AN1182; -.
DR eggNOG; KOG1375; Eukaryota.
DR HOGENOM; CLU_015718_1_1_1; -.
DR InParanoid; P10653; -.
DR OMA; VCSVAPK; -.
DR OrthoDB; 962471at2759; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005881; C:cytoplasmic microtubule; IMP:AspGD.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005876; C:spindle microtubule; IDA:AspGD.
DR GO; GO:0045298; C:tubulin complex; ISO:AspGD.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; ISO:AspGD.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007019; P:microtubule depolymerization; IMP:AspGD.
DR GO; GO:0007017; P:microtubule-based process; ISO:AspGD.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:AspGD.
DR GO; GO:0051228; P:mitotic spindle disassembly; IMP:AspGD.
DR GO; GO:0030473; P:nuclear migration along microtubule; IMP:AspGD.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 1.10.287.600; -; 1.
DR Gene3D; 3.30.1330.20; -; 1.
DR Gene3D; 3.40.50.1440; -; 1.
DR InterPro; IPR013838; Beta-tubulin_BS.
DR InterPro; IPR002453; Beta_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; PR01163; BETATUBULIN.
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.
DR PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance; Cytoplasm; Cytoskeleton; GTP-binding; Microtubule;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..447
FT /note="Tubulin beta-1 chain"
FT /id="PRO_0000048406"
FT BINDING 140..146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT VARIANT 100
FT /note="N -> I (resistance to rhizoxin)"
FT CONFLICT 75
FT /note="A -> C (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="L -> W (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="T -> S (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 447 AA; 49852 MW; 83A81AA647B5CCE7 CRC64;
MREIVHLQTG QCGNQIGAAF WQTISGEHGL DGSGVYNGTS DLQLERMNVY FNEASGNKYV
PRAVLVDLEP GTMDAVRAGP FGELFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDNVVDVV
RREAEGCDCL QGFQITHSLG GGTGAGMGTL LISKIREEFP DRMMATFSVV PSPKVSDTVV
EPYNATLSVH QLVEHSDETF CIDNEALYDI CMRTLKLSNP SYGDLNHLVS AVMSGVTTCL
RFPGQLNSDL RKLAVNMVPF PRLHFFMVGF APLTSRGAYS FRAVSVPELT QQMFDPKNMM
AASDFRNGRY LTCSAIFRGK VSMKEVEDQM RNIQSKNQSY FVEWIPNNIQ TALCSIPPRG
LKMSSTFIGN STSIQELFKR VGDQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
EYQQYQDASI SEGEEEYAEE EIMEGEE
