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Database: UniProt
Entry: Q86ZZ7_9FUNG
LinkDB: Q86ZZ7_9FUNG
Original site: Q86ZZ7_9FUNG 
ID   Q86ZZ7_9FUNG            Unreviewed;       389 AA.
AC   Q86ZZ7;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   24-JAN-2024, entry version 83.
DE   RecName: Full=Tubulin alpha chain {ECO:0000256|RuleBase:RU000352};
DE   Flags: Fragment;
GN   Name=atub {ECO:0000313|EMBL:AAN35132.1};
OS   Capniomyces stellatus.
OC   Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC   Harpellomycetes; Harpellales; Legeriomycetaceae; Capniomyces.
OX   NCBI_TaxID=4885 {ECO:0000313|EMBL:AAN35132.1};
RN   [1] {ECO:0000313|EMBL:AAN35132.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MIS-10-108 {ECO:0000313|EMBL:AAN35132.1};
RX   PubMed=12684019; DOI=10.1016/S1087-1845(02)00537-6;
RA   Keeling P.J.;
RT   "Congruent evidence from alpha-tubulin and beta-tubulin gene phylogenies
RT   for a zygomycete origin of microsporidia.";
RL   Fungal Genet. Biol. 38:298-309(2003).
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|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|RuleBase:RU000352}.
CC   -!- SIMILARITY: Belongs to the tubulin family.
CC       {ECO:0000256|ARBA:ARBA00009636, ECO:0000256|RuleBase:RU000352}.
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DR   EMBL; AY138774; AAN35132.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q86ZZ7; -.
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: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:SF417; AT04270P-RELATED; 1.
DR   PANTHER; PTHR11588; TUBULIN; 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   Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU000352};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000352}.
FT   DOMAIN          26..223
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   DOMAIN          225..370
FT                   /note="Tubulin/FtsZ 2-layer sandwich"
FT                   /evidence="ECO:0000259|SMART:SM00865"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAN35132.1"
FT   NON_TER         389
FT                   /evidence="ECO:0000313|EMBL:AAN35132.1"
SQ   SEQUENCE   389 AA;  43302 MW;  FE35922EF3C7A452 CRC64;
     ELYCLEHGIK PDGTVEGVNQ RRDDSSSTFF SETSSGKRVP RTVFVDLEPT VIDEVRNGEY
     RQLYHPDQLI TGKEDAANNY ARGHYTIGKE IIDNVLDCIR KLADNCTGLQ GFLVFHSFGG
     GTGSGFGALL LERLSVDYGK KSKLEFSVYP APQISNAVVE PYNSILTTHT TLEHSDCSFM
     VDNEAIYDIC RRNLDIERPS FDNLNRLIAQ IVSSITASLR FEGSLNVDLN EFQTNLVPYP
     RIHFPLVTYA PIISANKASH ESLSVSEITM ACFEPSNQMV KCDPRRGKYM SCCLLYRGDV
     IPKDVNAAVA NIKTKRTIQF VDWCPTGFKL GINAQPPACV PGGDLAKVSR AVCMLSNTTA
     IAEAWARLDH KFDLMYAKRA FVHWYVGEG
//
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