ID V9VDE6_9ALVE Unreviewed; 384 AA.
AC V9VDE6;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Tubulin alpha chain {ECO:0000256|RuleBase:RU000352};
DE Flags: Fragment;
OS Colponema vietnamica.
OC Eukaryota; Sar; Alveolata; Colponemida; Colponemidia; Colponema.
OX NCBI_TaxID=1492817 {ECO:0000313|EMBL:AHC92569.1};
RN [1] {ECO:0000313|EMBL:AHC92569.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Colp-7 {ECO:0000313|EMBL:AHC92569.1};
RX PubMed=24316202; DOI=10.1016/j.cub.2013.10.062;
RA Janouskovec J., Tikhonenkov D.V., Mikhailov K.V., Simdyanov T.G.,
RA Aleoshin V.V., Mylnikov A.P., Keeling P.J.;
RT "Colponemids represent multiple ancient alveolate lineages.";
RL Curr. Biol. 23:2546-2552(2013).
RN [2] {ECO:0000313|EMBL:AHC92569.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Colp-7 {ECO:0000313|EMBL:AHC92569.1};
RX PubMed=24740116;
RA Tikhonenkov D.V., Janouskovec J., Mylnikov A.P., Mikhailov K.V.,
RA Simdyanov T.G., Aleoshin V.V., Keeling P.J.;
RT "Description of Colponema vietnamica sp.n. and Acavomonas peruviana n. gen.
RT n. sp., two new alveolate phyla (Colponemidia nom. nov. and Acavomonidia
RT nom. nov.) and their contributions to reconstructing the ancestral state of
RT alveolates and eukaryotes.";
RL PLoS ONE 9:E95467-E95467(2014).
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|ARBA:ARBA00011747,
CC 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; KF651094; AHC92569.1; -; Genomic_DNA.
DR AlphaFoldDB; V9VDE6; -.
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 21..218
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 220..365
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AHC92569.1"
FT NON_TER 384
FT /evidence="ECO:0000313|EMBL:AHC92569.1"
SQ SEQUENCE 384 AA; 42304 MW; 08D316F73068A224 CRC64;
GIQPDGQMPS DKTIGGGDDA FNTFFSETGA GKHVPRCVFL DLEPTVIDEV RTGTYRQLFH
PEQLISGKED AANNFARGHY TIGKEIVDLC LDRIRKLADN CTGLQGFLVF NAVGGGTGSG
LGSLLLERLS VDYGKKSKLG FTIYPSPQVS TAVVEPYNSV LSTHSLLEHT DVAVMLDNEA
IYDICRRQLG IERPTYTNLN RLIAQVISSL TASLRFDGAL NVDITEFQTN LVPYPRIHFM
LSSYAPIISA EKAYHEQLSV AEITNSAFEP ASMMAKCDPR HGKYMACCLM YRGDVVPKDV
NASVATIKTK RTIQFVDWCP TGFKCGINYQ PPTVVPGGDL AKVMRAVCMI SNSTTIAEVF
SRIDHKFDLM YAKRAFVHWY VGEG
//
