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Database: UniProt
Entry: H9MH51_9PEZI
LinkDB: H9MH51_9PEZI
Original site: H9MH51_9PEZI 
ID   H9MH51_9PEZI            Unreviewed;        99 AA.
AC   H9MH51;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 2.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Beta-tubulin {ECO:0000313|EMBL:AEY82880.2};
DE   Flags: Fragment;
OS   Neofusicoccum parvum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Neofusicoccum.
OX   NCBI_TaxID=310453 {ECO:0000313|EMBL:AEY82880.2};
RN   [1] {ECO:0000313|EMBL:AEY82880.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CDZ1-1s1 {ECO:0000313|EMBL:AEY82880.2};
RA   Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V.,
RA   Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M., Henderson B.A.,
RA   Jones I.B., McGettigan J.A., Micheletti S.J., Nasrallah M.E., Ortiz D.,
RA   Piller C.R., Privatt S.R., Schneider S.L., Sharp S., Smith T.C.,
RA   Stanton J.D., Ullery H.E., Wilson R.J., Serrano M.G., Buck G., Lee V.,
RA   Wang Y., Carvalho R., Voegtly L., Shi R., Duckworth R., Johnson A.,
RA   Loviza R., Walstead R., Shah Z., Kiflezghi M., Wade K., Ball S.L.,
RA   Bradley K.W., Asai D.J., Bowman C.A., Russell D.A., Pope W.H.,
RA   Jacobs-Sera D., Hendrix R.W., Hatfull G.F.;
RL   Submitted (AUG-2015) 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; HQ840417; AEY82880.2; -; Genomic_DNA.
DR   AlphaFoldDB; H9MH51; -.
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          2..98
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|Pfam:PF00091"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AEY82880.2"
FT   NON_TER         99
FT                   /evidence="ECO:0000313|EMBL:AEY82880.2"
SQ   SEQUENCE   99 AA;  10625 MW;  3429BF298EB92F3C CRC64;
     IGNQIGAAFW QTISGEHGLD GSGVYNGTSD LQLERMNVYS NEASNNKYVP RAVLVDLEPG
     TMDAVRAGPF GQLFRPDNFV FGQSGAGNNW AKGHYTEGS
//
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