ID A7Y254_9PEZI Unreviewed; 166 AA.
AC A7Y254;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Tubulin beta chain {ECO:0000256|RuleBase:RU000352};
DE Flags: Fragment;
OS Colletotrichum cereale.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=343994 {ECO:0000313|EMBL:ABU97069.1};
RN [1] {ECO:0000313|EMBL:ABU97069.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AHCC10.43 {ECO:0000313|EMBL:ABU97069.1}, ANCG17.18
RC {ECO:0000313|EMBL:ABU97071.1}, ANCG17.30
RC {ECO:0000313|EMBL:ABU97072.1}, CLGC5.12 {ECO:0000313|EMBL:ABU97073.1},
RC CLGC5.13 {ECO:0000313|EMBL:ABU97074.1}, EGGC21
RC {ECO:0000313|EMBL:ABU97077.1}, EGGC22 {ECO:0000313|EMBL:ABU97078.1},
RC FUGC11.4 {ECO:0000313|EMBL:ABU97080.1}, FUGC2.2
RC {ECO:0000313|EMBL:ABU97079.1}, SHGC26 {ECO:0000313|EMBL:ABU97083.1},
RC and SHGC28 {ECO:0000313|EMBL:ABU97084.1};
RA Wong F.P., de la Cerda K.A., Hernandez-Martinez R., Midland S.L.;
RT "Detection and characterization of benzimidazole resistance in California
RT populations of Colletotrichum cereale.";
RL Submitted (AUG-2007) 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; EU116274; ABU97069.1; -; Genomic_DNA.
DR EMBL; EU116276; ABU97071.1; -; Genomic_DNA.
DR EMBL; EU116277; ABU97072.1; -; Genomic_DNA.
DR EMBL; EU116278; ABU97073.1; -; Genomic_DNA.
DR EMBL; EU116279; ABU97074.1; -; Genomic_DNA.
DR EMBL; EU116282; ABU97077.1; -; Genomic_DNA.
DR EMBL; EU116283; ABU97078.1; -; Genomic_DNA.
DR EMBL; EU116284; ABU97079.1; -; Genomic_DNA.
DR EMBL; EU116285; ABU97080.1; -; Genomic_DNA.
DR EMBL; EU116288; ABU97083.1; -; Genomic_DNA.
DR EMBL; EU116289; ABU97084.1; -; Genomic_DNA.
DR AlphaFoldDB; A7Y254; -.
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 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 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 1..107
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABU97069.1"
FT NON_TER 166
FT /evidence="ECO:0000313|EMBL:ABU97069.1"
SQ SEQUENCE 166 AA; 18135 MW; 379CF8064392C7E1 CRC64;
SLGGGTGAGM GTLLISKIRE EFPDRMMATF SVVPSPKVSD TVVEPYNATL SVHQLVENSD
KTFCIDNEAL YDICMRTLKL SNPSYGDLNH LVSAVMSGVT TCLRFPGQLN SDLRKLAVNM
VPFPRLHFFM VGFAPLTSRG AHSFRAVSVP ELTQQMFDPK NMMAAS
//
