ID A0A2G2XH54_CAPBA Unreviewed; 451 AA.
AC A0A2G2XH54;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Tubulin alpha chain {ECO:0000256|RuleBase:RU000352};
GN ORFNames=CQW23_05319 {ECO:0000313|EMBL:PHT56833.1};
OS Capsicum baccatum (Peruvian pepper).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX NCBI_TaxID=33114 {ECO:0000313|EMBL:PHT56833.1, ECO:0000313|Proteomes:UP000224567};
RN [1] {ECO:0000313|EMBL:PHT56833.1, ECO:0000313|Proteomes:UP000224567}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. PBC81 {ECO:0000313|Proteomes:UP000224567};
RC TISSUE=Leaf {ECO:0000313|EMBL:PHT56833.1};
RX PubMed=29089032; DOI=10.1186/s13059-017-1341-9;
RA Kim S., Park J., Yeom S.I., Kim Y.M., Seo E., Kim K.T., Kim M.S., Lee J.M.,
RA Cheong K., Shin H.S., Kim S.B., Han K., Lee J., Park M., Lee H.A.,
RA Lee H.Y., Lee Y., Oh S., Lee J.H., Choi E., Choi E., Lee S.E., Jeon J.,
RA Kim H., Choi G., Song H., Lee J., Lee S.C., Kwon J.K., Lee H.Y., Koo N.,
RA Hong Y., Kim R.W., Kang W.H., Huh J.H., Kang B.C., Yang T.J., Lee Y.H.,
RA Bennetzen J.L., Choi D.;
RT "New reference genome sequences of hot pepper reveal the massive evolution
RT of plant disease-resistance genes by retroduplication.";
RL Genome Biol. 18:R210.1-R210.11(2017).
RN [2] {ECO:0000313|Proteomes:UP000224567}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. PBC81 {ECO:0000313|Proteomes:UP000224567};
RA Kim S., Park J., Yeom S.-I., Kim Y.-M., Seo E., Kim K.-T., Kim M.-S.,
RA Lee J.M., Cheong K., Shin H.-S., Kim S.-B., Han K., Lee J., Park M.,
RA Lee H.-A., Lee H.-Y., Lee Y., Oh S., Lee J.H., Choi E., Choi E., Lee S.E.,
RA Jeon J., Kim H., Choi G., Song H., Lee J., Lee S.-C., Kwon J.-K.,
RA Lee H.-Y., Koo N., Hong Y., Kim R.W., Kang W.-H., Huh J.H., Kang B.-C.,
RA Yang T.-J., Lee Y.-H., Bennetzen J.L., Choi D.;
RT "Multiple reference genome sequences of hot pepper reveal the massive
RT evolution of plant disease resistance genes by retroduplication.";
RL J. Anim. Genet. bioRxivorg:115410-115410(2017).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PHT56833.1}.
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DR EMBL; MLFT02000002; PHT56833.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G2XH54; -.
DR STRING; 33114.A0A2G2XH54; -.
DR Proteomes; UP000224567; Chromosome 2.
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:UP000224567}.
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; 49706 MW; 4CC840FC348CEF1F CRC64;
MRECISVHIG QAGIQVGNAC WELYCLEHGI QPDGQMPSDK TLGGGDDAFN TFFSETGSGK
HVPRAVFVDL EPTVIDEVRA GAYRQLFHPE QLISGKEDAA NNFARGHYTI GREIVDLCLD
RIRKLADNCT GLQGFLVFNA VGGGTGSGLG SLLLERLSVD YGKKSKLGFT VYPSPQVSTS
VVEPYNSVLS THSLLEHTDV AVLLDNEAIY DICRRSLDIE RPTYTNLNRL VSQVISSLTA
SLRFDGALNV DVNEFQTNLV PYPRIHFMLS SYAPVISAEK AHHEQHSVAE ITTTAFEPAS
MMAKCDPRRG KYMACCLMYR GDVVPKDVNA AVSIIKTKRS IQFVDWCPTG FKCGINYQTP
TVVPGGDLAK VQRAVCMISN STSVAEVFSR IDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
AREDLAALEK DYEEVGAEYG QGEEGSEGEE Y
//
