ID A8DNK1_FUSME Unreviewed; 439 AA.
AC A8DNK1;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Tubulin alpha chain {ECO:0000256|RuleBase:RU000352};
DE Flags: Fragment;
OS Fusarium meridionale.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=282269 {ECO:0000313|EMBL:ABD97306.1};
RN [1] {ECO:0000313|EMBL:ABD97306.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRRL 28436 {ECO:0000313|EMBL:ABD97306.1}, NRRL 28721
RC {ECO:0000313|EMBL:ABD97307.1}, NRRL 28723
RC {ECO:0000313|EMBL:ABD97309.1}, and NRRL 29010
RC {ECO:0000313|EMBL:ABD97308.1};
RX PubMed=17451976; DOI=10.1016/j.fgb.2007.03.001;
RA Starkey D.E., Ward T.J., Aoki T., Gale L.R., Kistler H.C., Geiser D.M.,
RA Suga H., Toth B., Varga J., O'donnell K.;
RT "Global molecular surveillance reveals novel Fusarium head blight species
RT and trichothecene toxin diversity.";
RL Fungal Genet. Biol. 44:1191-1204(2007).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
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; DQ441554; ABD97306.1; -; Genomic_DNA.
DR EMBL; DQ441555; ABD97307.1; -; Genomic_DNA.
DR EMBL; DQ441556; ABD97308.1; -; Genomic_DNA.
DR EMBL; DQ441557; ABD97309.1; -; Genomic_DNA.
DR AlphaFoldDB; A8DNK1; -.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; cd02186; alpha_tubulin; 1.
DR Gene3D; 1.10.287.600; Helix hairpin bin; 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; IPR002452; Alpha_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; IPR023123; Tubulin_C.
DR InterPro; IPR017975; Tubulin_CS.
DR InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR PANTHER; PTHR11588; TUBULIN; 1.
DR PANTHER; PTHR11588:SF417; TUBULIN ALPHA-4 CHAIN; 1.
DR Pfam; PF00091; Tubulin; 1.
DR Pfam; PF03953; Tubulin_C; 1.
DR PRINTS; PR01162; ALPHATUBULIN.
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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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 47..244
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 246..391
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABD97306.1"
FT NON_TER 439
FT /evidence="ECO:0000313|EMBL:ABD97306.1"
SQ SEQUENCE 439 AA; 48705 MW; 2472CDCDCEFD414A CRC64;
EVISINVGQA GCQIANSCWE LYCLEHGIQP DGYLTEERKA QDPDQGFSTF FSETGNGKHV
PRAIYCDLEP NVVDEVRTGA YRNLFHPEMM ITGKEDASNN YARGHYTVGK ELIDGVLDKI
RRVADNCAGL QGFLVFHSFG GGTGSGFGAL LMERLSVDYG KKSKLEFCVY PAPQTATSVV
EPYNSILTTH TTLEHSDCSF MVDNEAIYDI CRRNLGLERP NYENLNRLIA QVVSSITASL
RFDGSLNVDL NEFQTNLVPY PRIHFPLVAY SPVISAAKAA HEANSVQEMT MSCFEPNNQM
VKCDPRHGKY MATCLLYRGD VVPNDAHAAV ATLKTKRTIQ FVDWCPTGFK LGICYQAPEN
VPNGDLAKVS RAVCMLSNTT AIAEAWSSLS LKFDLMHSKR AFVHWYVGEG MEEGEFSEAR
EDLAALERDY EEVATDSMG
//
