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Database: UniProt
Entry: A0A0E0CG70_9ORYZ
LinkDB: A0A0E0CG70_9ORYZ
Original site: A0A0E0CG70_9ORYZ 
ID   A0A0E0CG70_9ORYZ        Unreviewed;       459 AA.
AC   A0A0E0CG70;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Tubulin beta chain {ECO:0000256|RuleBase:RU000352};
OS   Oryza meridionalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=40149 {ECO:0000313|EnsemblPlants:OMERI02G05960.1};
RN   [1] {ECO:0000313|EnsemblPlants:OMERI02G05960.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI02G05960.1};
RA   Wing R.A., Panaud O., Henry R.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OMERI02G05960.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) 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   -!- 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|RuleBase:RU000352}.
CC   -!- SIMILARITY: Belongs to the tubulin family.
CC       {ECO:0000256|ARBA:ARBA00009636, ECO:0000256|RuleBase:RU000352}.
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DR   STRING; 40149.A0A0E0CG70; -.
DR   EnsemblPlants; OMERI02G05960.1; OMERI02G05960.1; OMERI02G05960.
DR   Gramene; OMERI02G05960.1; OMERI02G05960.1; OMERI02G05960.
DR   eggNOG; KOG1375; Eukaryota.
DR   HOGENOM; CLU_015718_1_1_1; -.
DR   Proteomes; UP000008021; Chromosome 2.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR   GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR   CDD; cd02187; beta_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; IPR002453; Beta_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:SF516; TUBULIN BETA-7 CHAIN; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   Pfam; PF03953; Tubulin_C; 1.
DR   PRINTS; PR01163; BETATUBULIN.
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   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:UP000008021}.
FT   DOMAIN          59..256
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   DOMAIN          258..395
FT                   /note="Tubulin/FtsZ 2-layer sandwich"
FT                   /evidence="ECO:0000259|SMART:SM00865"
FT   REGION          432..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..459
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   459 AA;  51345 MW;  B8EE796C0D42BFC0 CRC64;
     MREPDRGQVL GGDLRRAXIQ GGQCGNQIGA KFWEVICDEH GIDHTGKYSG DSDLQLERIN
     VYYNEASGGR FVPRAVLMDL EPGTMDSVRS GPFGQIFRPD NFVFGQSGAG NNWAKGHYTE
     GAELIDSVLD VVRKEAENCD CLQGFQVCHS LGGGTGSGMG TLLISKIREE YPDRMMLTFS
     VFPSPKVSDT VVEPYNATLS VHQLVENADE CMVLDNEALY DICFRTLKLA TPTFGDLNHL
     ISATMSGVTC CLRFPGQLNS DLRKLAVNLI PFPRLHFFMV GFAPLTSRGS QQYRALTVPE
     LTQQMWDAKN MMCAADPRHG RYLTASAMFR GKMSTKEVDE QMLNVQNKNS SYFVEWIPNN
     VKSSVCDIPP NGLKMASTFI GNSTSIQEMF RRVSEQFTAM FRRKAFLHWY TGEGMDEMEF
     TEAESNMNDL VAEYQQYQDA TADDEEEDYG DEEEDEVAA
//
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