ID Q0ZCS9_9PEZI Unreviewed; 83 AA.
AC Q0ZCS9;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE SubName: Full=Beta-tubulin {ECO:0000313|EMBL:ABG37629.1};
DE Flags: Fragment;
OS Pestalotiopsis besseyi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Sporocadaceae; Pestalotiopsis.
OX NCBI_TaxID=290097 {ECO:0000313|EMBL:ABG37629.1};
RN [1] {ECO:0000313|EMBL:ABG37629.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PSHI2003Endo1009 {ECO:0000313|EMBL:ABG37629.1};
RA Liu A.R., Xu T., Guo L.D.;
RT "Phylogenetic relationships of Pestalotiopsis and allied genera inferred
RT from ribosomal DNA and beta-tubulin gene sequences and morphological
RT characters.";
RL Submitted (MAY-2006) 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|ARBA:ARBA00034296}.
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}.
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DR EMBL; DQ534050; ABG37629.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0ZCS9; -.
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; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 1.
DR InterPro; IPR002453; Beta_tubulin.
DR InterPro; IPR000217; Tubulin.
DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR InterPro; 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.
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 9..83
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|Pfam:PF00091"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABG37629.1"
FT NON_TER 83
FT /evidence="ECO:0000313|EMBL:ABG37629.1"
SQ SEQUENCE 83 AA; 8939 MW; 6F696C2F15A29676 CRC64;
QTISGEHGLD SNGVYNGTSE LQLERMSVYF NEASGNKYVP RAVLVDLEPG TMDAVRAGPF
GQLFRPDNFV FGQSGAGNNW AKG
//