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Database: UniProt
Entry: D2X3B4_9MICR
LinkDB: D2X3B4_9MICR
Original site: D2X3B4_9MICR 
ID   D2X3B4_9MICR            Unreviewed;       261 AA.
AC   D2X3B4;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   22-FEB-2023, entry version 44.
DE   RecName: Full=Tubulin alpha chain {ECO:0000256|RuleBase:RU000352};
DE   Flags: Fragment;
GN   Name=tub1 {ECO:0000313|EMBL:ADB12569.1};
OS   Hamiltosporidium magnivora.
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Dubosqiidae;
OC   Hamiltosporidium.
OX   NCBI_TaxID=148818 {ECO:0000313|EMBL:ADB12569.1};
RN   [1] {ECO:0000313|EMBL:ADB12569.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FmT1-2 {ECO:0000313|EMBL:ADB12569.1};
RX   PubMed=20946698; DOI=10.1017/S0031182010001393;
RA   Haag K.L., Larsson J.I., Refardt D., Ebert D.;
RT   "Cytological and molecular description of Hamiltosporidium tvaerminnensis
RT   gen. et sp. nov., a microsporidian parasite of Daphnia magna, and
RT   establishment of Hamiltosporidium magnivora comb. nov.";
RL   Parasitology 138:447-462(2011).
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   -!- 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; GQ496301; ADB12569.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2X3B4; -.
DR   VEuPathDB; MicrosporidiaDB:CWI36_0518p0010; -.
DR   VEuPathDB; MicrosporidiaDB:CWI39_2156p0010; -.
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   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; IPR017975; Tubulin_CS.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR   PANTHER; PTHR11588; TUBULIN; 1.
DR   PANTHER; PTHR11588:SF239; 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   Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU000352};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000352}.
FT   DOMAIN          1..124
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   DOMAIN          126..261
FT                   /note="Tubulin/FtsZ 2-layer sandwich"
FT                   /evidence="ECO:0000259|SMART:SM00865"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADB12569.1"
FT   NON_TER         261
FT                   /evidence="ECO:0000313|EMBL:ADB12569.1"
SQ   SEQUENCE   261 AA;  28770 MW;  B02754F0A5FAE624 CRC64;
     VRKLADNCDG LQGFLIYHSF GGGTGSGFGA LVMDRLSTEF GKKCKLEFCV YPAPRVSTAV
     VEPYNSILTT HTTLDHSDCS FLVDNEAIYD MCRNLGIERP MYGDLNRIIA QVVSSVTASL
     RFPGSLNVDL TEFQTNLVPY PRIHFPLAAY SPMLSKEKAS HESLTVSEIA AACFEPQNQM
     VKCNPKNGKY MACCLLFRGD VKPKDANQAA TLIKNKRINQ FVEWCPTGFK IGINDRPPFI
     LEGSFMAPVK RACCSLSNTT A
//
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