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}.
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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
//