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Database: UniProt
Entry: M4ISH3_9PEZI
LinkDB: M4ISH3_9PEZI
Original site: M4ISH3_9PEZI 
ID   M4ISH3_9PEZI            Unreviewed;       136 AA.
AC   M4ISH3;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Beta-tubulin {ECO:0000313|EMBL:AGA18194.1};
DE   Flags: Fragment;
OS   Xylaria sp. 5327.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Xylariaceae; Xylaria.
OX   NCBI_TaxID=1235929 {ECO:0000313|EMBL:AGA18194.1};
RN   [1] {ECO:0000313|EMBL:AGA18194.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=5327 {ECO:0000313|EMBL:AGA18194.1};
RX   PubMed=23472167;
RA   Chen J., Zhang L.C., Xing Y.M., Wang Y.Q., Xing X.K., Zhang D.W.,
RA   Liang H.Q., Guo S.X.;
RT   "Diversity and taxonomy of endophytic xylariaceous fungi from medicinal
RT   plants of dendrobium (orchidaceae).";
RL   PLoS ONE 8:E58268-E58268(2013).
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; JX868519; AGA18194.1; -; Genomic_DNA.
DR   AlphaFoldDB; M4ISH3; -.
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:SF492; TUBULIN BETA-4 CHAIN; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   PRINTS; PR01163; BETATUBULIN.
DR   PRINTS; PR01161; TUBULIN.
DR   SMART; SM00864; Tubulin; 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          43..136
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AGA18194.1"
FT   NON_TER         136
FT                   /evidence="ECO:0000313|EMBL:AGA18194.1"
SQ   SEQUENCE   136 AA;  14718 MW;  DA6018193A6EFBC1 CRC64;
     VHLQTGQCGN QIGAAFWQQI SGEHGLDGNG VYNGTSDLQL ERMSVYFNEG ANNKYVPRAV
     LVDLEPGTMD AVRAGPFGQL FRPDNFVFGQ SGAGNNWAKG HYTEGAELVD NVLDVVRREA
     EGCDCLQGFQ ITHSLG
//
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