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Entry: Q3ZJA7_9EUKA
LinkDB: Q3ZJA7_9EUKA
Original site: Q3ZJA7_9EUKA 
ID   Q3ZJA7_9EUKA            Unreviewed;       367 AA.
AC   Q3ZJA7;
DT   27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=Tubulin alpha chain {ECO:0000256|RuleBase:RU000352};
DE   Flags: Fragment;
OS   Monocercomonoides exilis.
OC   Eukaryota; Metamonada; Preaxostyla; Oxymonadida; Polymastigidae;
OC   Monocercomonoides.
OX   NCBI_TaxID=2049356 {ECO:0000313|EMBL:AAW22162.1};
RN   [1] {ECO:0000313|EMBL:AAW22162.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PA203 {ECO:0000313|EMBL:AAW22162.1};
RX   PubMed=16120804; DOI=10.1093/molbev/msi245;
RA   Hampl V., Horner D.S., Dyal P., Kulda J., Flegr J., Foster P.G.,
RA   Embley T.M.;
RT   "Inference of the phylogenetic position of oxymonads based on nine genes:
RT   support for metamonada and excavata.";
RL   Mol. Biol. Evol. 22:2508-2518(2005).
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; AY831438; AAW22161.1; -; Genomic_DNA.
DR   EMBL; AY831439; AAW22162.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3ZJA7; -.
DR   VEuPathDB; GiardiaDB:MONOS_4301; -.
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; 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 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          19..216
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   DOMAIN          218..363
FT                   /note="Tubulin/FtsZ 2-layer sandwich"
FT                   /evidence="ECO:0000259|SMART:SM00865"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAW22162.1"
FT   NON_TER         367
FT                   /evidence="ECO:0000313|EMBL:AAW22162.1"
SQ   SEQUENCE   367 AA;  40385 MW;  5E2DBD820CD56F7C CRC64;
     QPDGQMPSDK TIGGGDDAFN TFFSETGAGK HVPRAVFIDL EPTVADEVRS GTYRELFHPE
     QIISGKEDAA NNYARGHYTI GKEIVDLCLD RIRKLADQCT GLQGFLVFSS VGGGTGAGLG
     SLLLERLSVD YGRKSKLTFT IYPSPQISNA CVEPYNAVLS THSLLNHTEV CVMLDNEAIY
     DICRRSLDIE RPTYTNLNRL IAQVISSLTA SLRFDGALNV DLCEFQTNLV PYPRIHFMLS
     SYAPVVTPEK AYHENLSVAE ITNSAFEPAN MMAKCDPRHG KYMACCMMYR GDVVPKDVNA
     AVATIKTKRT IQFVDWCPTG FKCGINYQPP TVVPGGDLAK VQRAVCMISN STAIAEVFSR
     IDHKFDL
//
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