ID A0A068AX91_AMAPH Unreviewed; 81 AA. AC A0A068AX91; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 24-JAN-2024, entry version 22. DE RecName: Full=Tubulin beta chain {ECO:0000256|RuleBase:RU000352}; DE Flags: Fragment; OS Amanita phalloides (Death cap). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes; OC Agaricomycetidae; Agaricales; Pluteineae; Amanitaceae; Amanita. OX NCBI_TaxID=67723 {ECO:0000313|EMBL:AIC65831.1}; RN [1] {ECO:0000313|EMBL:AIC65831.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=24950598; RA Cai Q., Tulloss R.E., Tang L.P., Tolgor B., Zhang P., Chen Z.H., Yang Z.L.; RT "Multi-locus phylogeny of lethal amanitas: Implications for species RT diversity and historical biogeography."; RL BMC Evol. Biol. 14:143-143(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|ARBA:ARBA00011747, CC 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; KJ466523; AIC65831.1; -; Genomic_DNA. DR AlphaFoldDB; A0A068AX91; -. 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; IPR002453; Beta_tubulin. 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:SF429; TUBULIN BETA-1 CHAIN-RELATED; 1. DR Pfam; PF00091; Tubulin; 1. DR PRINTS; PR01163; BETATUBULIN. DR PRINTS; PR01161; TUBULIN. 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}. FT DOMAIN 1..80 FT /note="Tubulin/FtsZ GTPase" FT /evidence="ECO:0000259|Pfam:PF00091" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AIC65831.1" FT NON_TER 81 FT /evidence="ECO:0000313|EMBL:AIC65831.1" SQ SEQUENCE 81 AA; 8703 MW; AF1153D58B609499 CRC64; WAKGHYTEGA ELVDAVLDVV RKEAEGTDCL QGFQITHSLG GGTGAGMGTL LISKIREEYP DRMMCTYSVV PSPKVSDTVV E //