ID D2JLP0_9HYPO Unreviewed; 339 AA.
AC D2JLP0;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Tubulin beta chain {ECO:0000256|RuleBase:RU000352};
DE Flags: Fragment;
GN Name=TUB2 {ECO:0000313|EMBL:ACZ56055.1};
GN Synonyms=beta-TUB {ECO:0000313|EMBL:QOP61441.1};
OS Fusarium incarnatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium incarnatum-equiseti species complex.
OX NCBI_TaxID=298378 {ECO:0000313|EMBL:ACZ56055.1};
RN [1] {ECO:0000313|EMBL:ACZ56055.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRRL 31160 {ECO:0000313|EMBL:ACZ56055.1};
RA Proctor R.H., McCormick S.P., Alexander N.J., Desajrdins A.E.;
RT "Evidence that a secondary metabolic biosynthetic gene cluster has grown by
RT gene relocation during evolution of the filamentous fungus Fusarium.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QOP61441.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JS9 {ECO:0000313|EMBL:QOP61441.1};
RA Wang L., Zhao K.H., Ge S.L., Liu L.M., Huang S.W.;
RT "First report of Fusarium incarnatum causing spikelet rot on rice in
RT China.";
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Tubulin is the major constituent of microtubules, a cylinder
CC consisting of laterally associated linear protofilaments composed of
CC alpha- and beta-tubulin heterodimers. Microtubules grow by the addition
CC of GTP-tubulin dimers to the microtubule end, where a stabilizing cap
CC forms. Below the cap, tubulin dimers are in GDP-bound state, owing to
CC GTPase activity of alpha-tubulin. {ECO:0000256|ARBA:ARBA00034296,
CC ECO:0000256|RuleBase:RU000352}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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 ECO:0000256|RuleBase:RU000352}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the tubulin family.
CC {ECO:0000256|ARBA:ARBA00009636, ECO:0000256|RuleBase:RU000352}.
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DR EMBL; GQ915444; ACZ56055.1; -; Genomic_DNA.
DR EMBL; MT895842; QOP61441.1; -; Genomic_DNA.
DR AlphaFoldDB; D2JLP0; -.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR CDD; cd02187; beta_tubulin; 1.
DR Gene3D; 3.30.1330.20; Tubulin/FtsZ, C-terminal domain; 1.
DR Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 1.
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; IPR017975; Tubulin_CS.
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 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; SSF55307; Tubulin C-terminal domain-like; 1.
DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR PROSITE; PS00227; TUBULIN; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000352};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU000352};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000352}.
FT DOMAIN 43..240
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 242..339
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACZ56055.1"
FT NON_TER 339
FT /evidence="ECO:0000313|EMBL:ACZ56055.1"
SQ SEQUENCE 339 AA; 37337 MW; E252CE313DDE4E25 CRC64;
VHLQTGQCGN QIGAAFWQTI SGEHGLDSNG VYNGTSELQL ERMSVYFNEA SGNKYVPRAV
LVDLEPGTMD AVRAGPFGQL FRPDNFVFGQ SGAGNNWAKG HYTEGAELVD NVLDVVRREA
EGCDCLQGFQ ITHSLGGGTG AGMGTLLISK IREEFPDRMM ATFSVVPSPK VSDTVVEPYN
ATLSVHQLVE NSDETFCIDN EALYDICMRT LKLSNPSYGD LNYLVSAVMS GVTTCLRFPG
QLNSDLRKLA VNMVPFPRLH FFMVGFAPLT SRGAHSFRAV SVPELTQQMF DPKNMMAASD
FRNGRYLTCS AIFRGRVAMK EVEDQMRNVQ NKNSSYFVE
//
