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Database: UniProt
Entry: Q0ZCS9_9PEZI
LinkDB: Q0ZCS9_9PEZI
Original site: Q0ZCS9_9PEZI 
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
//
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