GenomeNet

Database: UniProt
Entry: A0A1Y3BUD3_EURMA
LinkDB: A0A1Y3BUD3_EURMA
Original site: A0A1Y3BUD3_EURMA 
ID   A0A1Y3BUD3_EURMA        Unreviewed;       217 AA.
AC   A0A1Y3BUD3;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Tubulin beta chain {ECO:0000256|RuleBase:RU000352};
DE   Flags: Fragment;
GN   ORFNames=BLA29_005036 {ECO:0000313|EMBL:OTF83393.1};
OS   Euroglyphus maynei (Mayne's house dust mite).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Analgoidea;
OC   Pyroglyphidae; Pyroglyphinae; Euroglyphus.
OX   NCBI_TaxID=6958 {ECO:0000313|EMBL:OTF83393.1, ECO:0000313|Proteomes:UP000194236};
RN   [1] {ECO:0000313|EMBL:OTF83393.1, ECO:0000313|Proteomes:UP000194236}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Arlian Lab {ECO:0000313|EMBL:OTF83393.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:OTF83393.1};
RA   Arlian L.G., Morgan M.S., Rider S.D.;
RT   "Genome Survey of Euroglyphus maynei.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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   -!- 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   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
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:OTF83393.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; MUJZ01003880; OTF83393.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y3BUD3; -.
DR   OrthoDB; 3087223at2759; -.
DR   Proteomes; UP000194236; Unassembled WGS sequence.
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   Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 1.
DR   InterPro; IPR013838; Beta-tubulin_BS.
DR   InterPro; IPR002453; Beta_tubulin.
DR   InterPro; IPR008280; Tub_FtsZ_C.
DR   InterPro; IPR000217; Tubulin.
DR   InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR   InterPro; IPR017975; Tubulin_CS.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR   PANTHER; PTHR11588; TUBULIN; 1.
DR   PANTHER; PTHR11588:SF280; TUBULIN BETA CHAIN; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   PRINTS; PR01163; BETATUBULIN.
DR   PRINTS; PR01161; TUBULIN.
DR   SMART; SM00864; Tubulin; 1.
DR   SUPFAM; SSF55307; Tubulin C-terminal domain-like; 1.
DR   SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR   PROSITE; PS00227; TUBULIN; 1.
DR   PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000194236}.
FT   DOMAIN          47..208
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   COILED          189..216
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   NON_TER         217
FT                   /evidence="ECO:0000313|EMBL:OTF83393.1"
SQ   SEQUENCE   217 AA;  24227 MW;  0030941351EAEC5E CRC64;
     MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGAYHGDS PLQLERINVY YNEASGGKYV
     PRAILLDLEP GTMDSVRSGV FGTLFRPDNF IFGQSGAGNN WAKGHYTEGA ELVDTVLDVV
     RKEAEGCDCL QGFQLAHSLG GGTGSGMGTL LISKIREEYP DRIMNTFTMF RRKAFLHWYT
     GEGMDEMEFT EAESNMNDLV NEYQQYQEAT AEDEELF
//
DBGET integrated database retrieval system