ID E9P5H6_BOTFU Unreviewed; 128 AA.
AC E9P5H6;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Beta-tubulin {ECO:0000313|EMBL:ADW78889.1};
DE Flags: Fragment;
GN Name=tub2 {ECO:0000313|EMBL:ADW78889.1};
OS Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=40559 {ECO:0000313|EMBL:ADW78889.1};
RN [1] {ECO:0000313|EMBL:ADW78889.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=8046 {ECO:0000313|EMBL:ADW78889.1};
RX PubMed=22130648; DOI=10.1016/j.micres.2011.10.006;
RA Fekete E., Fekete E., Irinyi L., Karaffa L., Arnyasi M., Asadollahi M.,
RA Sandor E.;
RT "Genetic diversity of a Botrytis cinerea cryptic species complex in
RT Hungary.";
RL Microbiol. Res. 167:283-291(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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HQ890458; ADW78889.1; -; Genomic_DNA.
DR AlphaFoldDB; E9P5H6; -.
DR SMR; E9P5H6; -.
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; IPR002453; Beta_tubulin.
DR InterPro; IPR000217; Tubulin.
DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR PANTHER; PTHR11588; TUBULIN; 1.
DR PANTHER; PTHR11588:SF492; TUBULIN BETA-4 CHAIN; 1.
DR Pfam; PF00091; Tubulin; 1.
DR PRINTS; PR01163; BETATUBULIN.
DR PRINTS; PR01161; TUBULIN.
DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 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 2..128
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|Pfam:PF00091"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADW78889.1"
FT NON_TER 128
FT /evidence="ECO:0000313|EMBL:ADW78889.1"
SQ SEQUENCE 128 AA; 13794 MW; 1C6D50D3BD739E45 CRC64;
VHLQTGQCGN QIGAAFWQTI SGEHGLDGSG VYNGTSDLQL ERMNVYFNEA SGNKYVPRAV
LVDLEPGTMD AVRAGPFGQL FRPDNFVFGQ SGAGNNWAKG HYTEGAELVD QVLDVVRREA
EGCDCLQG
//
