ID Q29TM3_9FUNG Unreviewed; 387 AA.
AC Q29TM3;
DT 04-APR-2006, integrated into UniProtKB/TrEMBL.
DT 04-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Tubulin beta chain {ECO:0000256|RuleBase:RU000352};
DE Flags: Fragment;
GN Name=btub {ECO:0000313|EMBL:AAY40402.1};
OS Mycotypha africana.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mycotyphaceae; Mycotypha.
OX NCBI_TaxID=64632 {ECO:0000313|EMBL:AAY40402.1};
RN [1] {ECO:0000313|EMBL:AAY40402.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FSU296 {ECO:0000313|EMBL:AAY40402.1};
RX PubMed=18309361; DOI=10.1038/ismej.2008.19;
RA Schmitt I., Partida-Martinez L.P., Winkler R., Voigt K., Einax E., Dolz F.,
RA Telle S., Wostemeyer J., Hertweck C.;
RT "Evolution of host resistance in a toxin-producing bacterial-fungal
RT alliance.";
RL ISME J. 2:632-641(2008).
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|RuleBase:RU000352}.
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|RuleBase:RU000352}.
CC -!- SIMILARITY: Belongs to the tubulin family.
CC {ECO:0000256|ARBA:ARBA00009636, ECO:0000256|RuleBase:RU000352}.
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DR EMBL; AY944805; AAY40402.1; -; Genomic_DNA.
DR AlphaFoldDB; Q29TM3; -.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
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 CDD; cd02187; beta_tubulin; 1.
DR Gene3D; 1.10.287.600; Helix hairpin bin; 1.
DR Gene3D; 3.30.1330.20; Tubulin/FtsZ, C-terminal domain; 1.
DR Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 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; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR InterPro; IPR023123; Tubulin_C.
DR InterPro; IPR017975; Tubulin_CS.
DR InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR PANTHER; PTHR11588; TUBULIN; 1.
DR PANTHER; PTHR11588:SF429; TUBULIN BETA-1 CHAIN; 1.
DR Pfam; PF00091; Tubulin; 1.
DR Pfam; PF03953; Tubulin_C; 1.
DR PRINTS; PR01163; BETATUBULIN.
DR PRINTS; PR01161; TUBULIN.
DR SMART; SM00864; Tubulin; 1.
DR SMART; SM00865; Tubulin_C; 1.
DR SUPFAM; SSF55307; Tubulin C-terminal domain-like; 1.
DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR PROSITE; PS00227; TUBULIN; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000352};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU000352};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000352}.
FT DOMAIN 32..229
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 231..368
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAY40402.1"
FT NON_TER 387
FT /evidence="ECO:0000313|EMBL:AAY40402.1"
SQ SEQUENCE 387 AA; 43213 MW; 298A42AE34735EA8 CRC64;
IGQKFWEGIS QEHGIDSTGA YAGDNDLQLE RINVYYNEGS AGKYVPRAVL VDLEPATMDA
IRSSTYSKLY RPDNFIFGQS GAGNSWAKGY YTEGAELVEG VLDIIRKEAE HTDCLQGFQL
CHSLGGGTGS GLGSLLLSKI REEYPDRMLC TYSVVPSPKV SDTVVEPYNA VLTVHQLVEN
CDATFCIDNE ALYDICFRTL KLSNPNYGDL NQLVSAVMSG VSTSLRFPGQ LNSDLRKTFV
NMVPFPRLHF FMVGFAPLTA FNSQRYRNLS VPELTAQMFD ARNMMAASDP RHGRYLTVAT
IFRGRLSTKE VENQMLAVQQ KNSSYFVEWI PNSVKTSLCD IPPVGLKMSG TFIGNSTAIQ
ELFKRVNEQF TAMFRRKAFM HWYTGEG
//
