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Database: UniProt
Entry: G3FK01_9HYPO
LinkDB: G3FK01_9HYPO
Original site: G3FK01_9HYPO 
ID   G3FK01_9HYPO            Unreviewed;       109 AA.
AC   G3FK01;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Beta-tubulin {ECO:0000313|EMBL:AEN92461.1};
DE   Flags: Fragment;
OS   Ilyonectria panacis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Ilyonectria.
OX   NCBI_TaxID=1079120 {ECO:0000313|EMBL:AEN92461.1};
RN   [1] {ECO:0000313|EMBL:AEN92461.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CDC-N-9a {ECO:0000313|EMBL:AEN92461.1};
RX   PubMed=22208602;
RA   Cabral A., Rego C., Nascimento T., Oliveira H., Groenewald J.Z.,
RA   Crous P.W.;
RT   "Multi-gene analysis and morphology reveal novel Ilyonectria species
RT   associated with black foot disease of grapevines.";
RL   Fungal Biol. 116:62-80(2012).
RN   [2] {ECO:0000313|EMBL:AEN92461.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CDC-N-9a {ECO:0000313|EMBL:AEN92461.1};
RA   Cabral A., Groenewald J.Z., Rego C., Oliveira H., Crous P.W.;
RT   "Cylindrocarpon root rot: multi-gene analysis reveals novel species within
RT   the Ilyonectria radicicola species complex.";
RL   Mycol. Prog. 11:655-688(2012).
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|ARBA:ARBA00011747}.
CC   -!- SIMILARITY: Belongs to the tubulin family.
CC       {ECO:0000256|ARBA:ARBA00009636}.
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DR   EMBL; JF735424; AEN92461.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3FK01; -.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR   GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR   Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 1.
DR   InterPro; IPR013838; Beta-tubulin_BS.
DR   InterPro; IPR002453; Beta_tubulin.
DR   InterPro; IPR000217; Tubulin.
DR   InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR   PANTHER; PTHR36527; OS01G0282866 PROTEIN; 1.
DR   PANTHER; PTHR36527:SF3; OS01G0282866 PROTEIN; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   PRINTS; PR01163; BETATUBULIN.
DR   PRINTS; PR01161; TUBULIN.
DR   SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR   PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          3..109
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|Pfam:PF00091"
FT   NON_TER         109
FT                   /evidence="ECO:0000313|EMBL:AEN92461.1"
SQ   SEQUENCE   109 AA;  11868 MW;  FBC6F5C80BB5B892 CRC64;
     MREIVHLQTG QCGNQIGAAF WQTISGEHGL DSNGVYNGTS ELQLERMSVY FNEASGNKYV
     PRAVLVDLEP GTMDAVRAGP FGQLFRPDNF VFGQSGAGNN WAKGHYTEG
//
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