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Database: UniProt
Entry: F9GEV4_FUSOF
LinkDB: F9GEV4_FUSOF
Original site: F9GEV4_FUSOF 
ID   F9GEV4_FUSOF            Unreviewed;       115 AA.
AC   F9GEV4;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Tubulin/FtsZ GTPase domain-containing protein {ECO:0000259|Pfam:PF00091};
DE   Flags: Fragment;
GN   ORFNames=FOXB_17188 {ECO:0000313|EMBL:EGU72303.1};
OS   Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU72303.1};
RN   [1] {ECO:0000313|EMBL:EGU72303.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fo5176 {ECO:0000313|EMBL:EGU72303.1};
RX   PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA   Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT   "A highly conserved effector in Fusarium oxysporum is required for full
RT   virulence on Arabidopsis.";
RL   Mol. Plant Microbe Interact. 25:180-190(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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGU72303.1}.
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DR   EMBL; AFQF01006605; EGU72303.1; -; Genomic_DNA.
DR   AlphaFoldDB; F9GEV4; -.
DR   STRING; 660025.F9GEV4; -.
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..115
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|Pfam:PF00091"
FT   NON_TER         115
FT                   /evidence="ECO:0000313|EMBL:EGU72303.1"
SQ   SEQUENCE   115 AA;  12609 MW;  FFC50697B139CB8F CRC64;
     MREIVHLQAG QCGNQIGSAF WQTISGEHGL DSSGMYNGTS ELQLARMNVY FNETSSNKYV
     PRAVLVDLEP GTMDAVRSGP LSQLFRPDNF VFGHSSAGNN WAKGHYTEGA ELIDQ
//
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