GenomeNet

Database: UniProt
Entry: X2FD10_9EUGL
LinkDB: X2FD10_9EUGL
Original site: X2FD10_9EUGL 
ID   X2FD10_9EUGL            Unreviewed;       381 AA.
AC   X2FD10;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Tubulin beta chain {ECO:0000256|RuleBase:RU000352};
DE   Flags: Fragment;
GN   Name=tubB {ECO:0000313|EMBL:AHM94117.1};
OS   Colacium vesiculosum.
OC   Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Euglenophyceae;
OC   Euglenales; Colacium.
OX   NCBI_TaxID=102910 {ECO:0000313|EMBL:AHM94117.1};
RN   [1] {ECO:0000313|EMBL:AHM94117.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=UW-Lazienki {ECO:0000313|EMBL:AHM94117.1};
RX   PubMed=24296662; DOI=10.1093/molbev/mst227;
RA   Milanowski R., Karnkowska A., Ishikawa T., Zakrys B.;
RT   "Distribution of Conventional and Nonconventional Introns in Tubulin (? and
RT   ?) Genes of Euglenids.";
RL   Mol. Biol. Evol. 31:584-593(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   -!- 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}.
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; KC907674; AHM94117.1; -; Genomic_DNA.
DR   AlphaFoldDB; X2FD10; -.
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:0046872; F:metal ion binding; 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; 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:SF429; TUBULIN BETA-1 CHAIN-RELATED; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU000352};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000352}.
FT   DOMAIN          32..229
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   DOMAIN          231..368
FT                   /note="Tubulin/FtsZ 2-layer sandwich"
FT                   /evidence="ECO:0000259|SMART:SM00865"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AHM94117.1"
FT   NON_TER         381
FT                   /evidence="ECO:0000313|EMBL:AHM94117.1"
SQ   SEQUENCE   381 AA;  42569 MW;  F93D93628F80FE54 CRC64;
     IGSKFWEVIS DEHGVDPTGT YQGDSDLQLE RINVYYNEAT GGRYVPRAIL MDLEPGTMDS
     VRAGPYGQIF RPDNFVFGQT GAGNNWAKEH YTEGAELIDS VLDVVRKEAE SCDCLQGFQI
     AHSLGGGTGS GMGTLLISKI REEYPDRMMM TFSVIPSPKV SDTVVEPYNT TLSVHQLVEN
     ADEVMCIDNE ALYDICFRTL KLTTPTFGDL NHLVSAVMSG VTCCLRFPGQ LNSDLRKLAV
     NLIPFPRLHF FLVGFAPLTS RGSQQYRALT VPELTQQMFD AKNMMAASDP RHGRYLTASA
     MFRGRMSTKE VDEQILNVQN KNSSYFVEWI PNNIKSSVCD IPPKGLKMSA TFIGNNTAIQ
     EMFKRVSEQF TAMFRRKAFL H
//
DBGET integrated database retrieval system