ID A0A1Q0Y6Y2_9PLEO Unreviewed; 133 AA. AC A0A1Q0Y6Y2; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 14-DEC-2022, entry version 15. DE SubName: Full=Beta-tubulin {ECO:0000313|EMBL:AQK47989.1}; DE Flags: Fragment; OS Alternaria sp. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes; OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria. OX NCBI_TaxID=1715220 {ECO:0000313|EMBL:AQK47989.1}; RN [1] {ECO:0000313|EMBL:AQK47989.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=P1267 {ECO:0000313|EMBL:AQK47989.1}; RX PubMed=28667772; RA Glynou K., Ali T., Haghi Kia S., Thines M., Macia-Vicente J.G.; RT "Genotypic diversity in root-endophytic fungi reflects efficient dispersal RT and environmental adaptation."; RL Mol. Ecol. 26:4618-4630(2017). 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 -!- SIMILARITY: Belongs to the tubulin family. CC {ECO:0000256|ARBA:ARBA00009636}. 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; KX361834; AQK47989.1; -; Genomic_DNA. DR AlphaFoldDB; A0A1Q0Y6Y2; -. DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. 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; 3.30.1330.20; -; 1. DR Gene3D; 3.40.50.1440; -; 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; IPR036525; Tubulin/FtsZ_GTPase_sf. DR InterPro; IPR003008; Tubulin_FtsZ_GTPase. DR PANTHER; PTHR11588; TUBULIN; 1. DR Pfam; PF00091; Tubulin; 1. DR PRINTS; PR01163; BETATUBULIN. DR PRINTS; PR01161; TUBULIN. DR SUPFAM; SSF55307; Tubulin C-terminal domain-like; 1. DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1. PE 3: Inferred from homology; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134}; KW Microtubule {ECO:0000256|ARBA:ARBA00022701}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}. FT DOMAIN 2..54 FT /note="Tubulin" FT /evidence="ECO:0000259|Pfam:PF00091" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AQK47989.1" FT NON_TER 133 FT /evidence="ECO:0000313|EMBL:AQK47989.1" SQ SEQUENCE 133 AA; 14826 MW; 1BCE04FB67084A38 CRC64; EFPDRMMATY SVVPSPKVSD TVVEPYNATL SIHQLVENSD ETFCIDNEAL YDICMRTLKL NNPSYGDLNH LVSAVMSGVT TCLRFPGQLN SDLRKLAVNM VPFPRLHFFM VGFAPLTSRG AHSFRAVTVP ELT //