ID J3LSB8_ORYBR Unreviewed; 451 AA.
AC J3LSB8;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Tubulin alpha chain {ECO:0000256|RuleBase:RU000352};
GN Name=102720966 {ECO:0000313|EnsemblPlants:OB03G39440.1};
OS Oryza brachyantha (malo sina).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4533 {ECO:0000313|EnsemblPlants:OB03G39440.1};
RN [1] {ECO:0000313|EnsemblPlants:OB03G39440.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 101232 {ECO:0000313|EnsemblPlants:OB03G39440.1};
RX PubMed=23481403;
RA Chen J., Huang Q., Gao D., Wang J., Lang Y., Liu T., Li B., Bai Z.,
RA Luis Goicoechea J., Liang C., Chen C., Zhang W., Sun S., Liao Y., Zhang X.,
RA Yang L., Song C., Wang M., Shi J., Liu G., Liu J., Zhou H., Zhou W., Yu Q.,
RA An N., Chen Y., Cai Q., Wang B., Liu B., Min J., Huang Y., Wu H., Li Z.,
RA Zhang Y., Yin Y., Song W., Jiang J., Jackson S.A., Wing R.A., Wang J.,
RA Chen M.;
RT "Whole-genome sequencing of Oryza brachyantha reveals mechanisms underlying
RT Oryza genome evolution.";
RL Nat. Commun. 4:1595-1595(2013).
RN [2] {ECO:0000313|EnsemblPlants:OB03G39440.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2013) to UniProtKB.
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|ARBA:ARBA00034296,
CC 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|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 RefSeq; XP_006650518.1; XM_006650455.2.
DR AlphaFoldDB; J3LSB8; -.
DR STRING; 4533.J3LSB8; -.
DR EnsemblPlants; OB03G39440.1; OB03G39440.1; OB03G39440.
DR GeneID; 102720966; -.
DR Gramene; OB03G39440.1; OB03G39440.1; OB03G39440.
DR KEGG; obr:102720966; -.
DR eggNOG; KOG1376; Eukaryota.
DR HOGENOM; CLU_015718_0_0_1; -.
DR OMA; RRMADQC; -.
DR OrthoDB; 1206011at2759; -.
DR Proteomes; UP000006038; Chromosome 3.
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:SF489; TUBULIN ALPHA-2 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 Acetylation {ECO:0000256|ARBA:ARBA00022990};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000006038}.
FT DOMAIN 49..246
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 248..393
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
SQ SEQUENCE 451 AA; 49703 MW; 65D0960768116F21 CRC64;
MRECISIHIG QAGIQVGNAC WELYCLEHGI QADGQMPSDK TVGGGDDAFN TFFSETGAGK
HVPRAVFVDL EPTVIDEVRT GGYRQLFHPE QLISGKEDAA NNFARGHYTI GKEIVDLCLD
RIRKLADNCT GLQGFLVFNA VGGGTGSGLG SLLLERLSVD YGKKSKLGFT VYPSPQVSTS
VVEPYNSVLS THSLLEHTDV AVLLDNEAIY DICRRSLDIE RPTYTNLNRL VSQVISSLTA
SLRFDGALNV DVNEFQTNLV PYPRIHFMLS SYAPVISAEK AYHEQLSVAE ITNSAFEPSS
MMAKCDPRHG KYMACCLMYR GDVVPKDVNA AVATIKTKRT IQFVDWCPTG FKCGINYQPP
SIVPGGDLAK VQRAVCMISN STSVVEVFSR IDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
AREDLAALEK DYEEVGAEFD EGEDGDEGDE Y
//
