ID F8WPD5_9EUKA Unreviewed; 384 AA.
AC F8WPD5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Tubulin alpha chain {ECO:0000256|RuleBase:RU000352};
DE Flags: Fragment;
OS Dysnectes brevis.
OC Eukaryota; Metamonada; Carpediemonas-like organisms; Dysnectes.
OX NCBI_TaxID=391066 {ECO:0000313|EMBL:BAK52294.1};
RN [1] {ECO:0000313|EMBL:BAK52294.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NY0165 {ECO:0000313|EMBL:BAK52294.1};
RX PubMed=22364773; DOI=10.1016/j.protis.2011.12.007;
RA Takishita K., Kolisko M., Komatsuzaki H., Yabuki A., Inagaki Y.,
RA Cepicka I., Smejkalova P., Silberman J.D., Hashimoto T., Roger A.J.,
RA Simpson A.G.B.;
RT "Multigene phylogenies of diverse Carpediemonas-like organisms identify the
RT closest relatives of 'amitochondriate' diplomonads and retortamonads.";
RL Protist 163:344-355(2012).
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; AB600279; BAK52294.1; -; Genomic_DNA.
DR AlphaFoldDB; F8WPD5; -.
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; 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 27..224
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 226..371
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAK52294.1"
FT NON_TER 384
FT /evidence="ECO:0000313|EMBL:BAK52294.1"
SQ SEQUENCE 384 AA; 42858 MW; 536BD1FE76CFEA7C CRC64;
LYCLEHGIQH DGQMPSDKTI GGGDDAFNTF FSETGAGKYV PRAVFIDLEP TVIDEVRAGS
YRQLYHPEQL ISGKEDAANN YARGHYTIGK EIVDLVLDRV RKLADNCSGL QGFLIFHSFG
GGTGSGFGSL FMERLSVDYG RKSKLEFAIY PSPQIATAVV EPYNTILAAH SMLEHSDCAF
MVDNEAMYDI CRRNLDIERP THTNINRLIA QCVSSITASL RFDGALNVDL TEFQTNLVPY
PRIHFPLCSY APIVSSEKAY HEKLSVSELT NSVFEPANMM VKCDPRHGKY MACCMMYRGD
VVPKDVNSAI AVIKTKRTIQ FVDWCPTGFK VGINYQPPTV IPGGDLAKVQ RSCLMISNTT
AIAEVWSRMD HKFDLMYAKR AFVH
//
