(data stored in SCRATCH zone)

SWISSPROT: Q75BP6_ASHGO

ID   Q75BP6_ASHGO            Unreviewed;       449 AA.
AC   Q75BP6;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 118.
DE   RecName: Full=Tubulin beta chain {ECO:0000256|RuleBase:RU000352};
GN   ORFNames=AGOS_ACR225C {ECO:0000313|EMBL:AAS51451.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS51451.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS51451.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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       {ECO:0000256|RuleBase:RU000352, ECO:0000256|SAAS:SAAS00031082}.
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. {ECO:0000256|RuleBase:RU000352}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|SAAS:SAAS00361597}.
CC   -!- SIMILARITY: Belongs to the tubulin family.
CC       {ECO:0000256|RuleBase:RU000352, ECO:0000256|SAAS:SAAS00576975}.
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DR   EMBL; AE016816; AAS51451.1; -; Genomic_DNA.
DR   RefSeq; NP_983627.1; NM_208980.1.
DR   STRING; 33169.AAS51451; -.
DR   EnsemblFungi; AAS51451; AAS51451; AGOS_ACR225C.
DR   GeneID; 4619626; -.
DR   KEGG; ago:AGOS_ACR225C; -.
DR   HOGENOM; HOG000165714; -.
DR   InParanoid; Q75BP6; -.
DR   KO; K07375; -.
DR   OMA; EVGANKY; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IEA:EnsemblFungi.
DR   GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR   GO; GO:0005876; C:spindle microtubule; IEA:EnsemblFungi.
DR   GO; GO:0045298; C:tubulin complex; IEA:EnsemblFungi.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:EnsemblFungi.
DR   GO; GO:0071963; P:establishment or maintenance of cell polarity regulating cell shape; IEA:EnsemblFungi.
DR   GO; GO:0048312; P:intracellular distribution of mitochondria; IEA:EnsemblFungi.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0007017; P:microtubule-based process; IBA:GO_Central.
DR   GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0090307; P:mitotic spindle assembly; IEA:EnsemblFungi.
DR   GO; GO:1903087; P:mitotic spindle pole body duplication; IEA:EnsemblFungi.
DR   GO; GO:0098863; P:nuclear migration by microtubule mediated pushing forces; IEA:EnsemblFungi.
DR   GO; GO:0090316; P:positive regulation of intracellular protein transport; IEA:EnsemblFungi.
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; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR   InterPro; IPR037103; Tubulin/FtsZ_C_sf.
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;
DR   PRODOM; Q75BP6.
DR   SWISS-2DPAGE; Q75BP6.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00045372};
KW   Cytoskeleton {ECO:0000256|SAAS:SAAS00439051};
KW   GTP-binding {ECO:0000256|RuleBase:RU000352, ECO:0000256|SAAS:SAAS00977278};
KW   Microtubule {ECO:0000256|RuleBase:RU000352, ECO:0000256|SAAS:SAAS00576796};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000352,
KW   ECO:0000256|SAAS:SAAS00977287};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591}.
FT   DOMAIN          47..244
FT                   /note="Tubulin"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   DOMAIN          246..383
FT                   /note="Tubulin_C"
FT                   /evidence="ECO:0000259|SMART:SM00865"
FT   REGION          429..449
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          408..428
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   449 AA;  50156 MW;  A62D7AF009CC53CC CRC64;
     MREIIHLSTG QCGNQIGAAF WETICGEHGL DFNGTYSGTD ELQRARLNVY FNEASSGKWV
     PRSVNVDLEP GTIDTVRNSN IGNLFRPDNY IFGQSSAGNV WAKGHYTEGA ELVDSVMDVI
     RREAEGCDSL QGFQITHSLG GGTGSGMGTL LISKIREEFP DRMMATFSVV PSPKTSDTVV
     EPYNATLSVH QLVEHSDETF CIDNEALYDI CQRTLKLPQP SYSDLNNLVS SVMSGVTTSL
     RYPGQLNSDL RKLAVNLVPF PRLHFFMVGY APLTSIGAQS FRALTVPELT QQMFDARNMM
     AASDPRNGRY LTVAAFFRGK VSVKEVEDEM HKVQTRNSSY FVEWIPNNVQ TAVCSVPPQG
     LDMSATFIGN STSIQELFKR VGDQFGAMFK RKAFLHWYTS EGMDEMEFSE AESNMNDLVS
     EYQQYQEATV EDDEELNYGD EQPMVENFE
//

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