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Database: UniProt
Entry: E9ABD9_9EURO
LinkDB: E9ABD9_9EURO
Original site: E9ABD9_9EURO 
ID   E9ABD9_9EURO            Unreviewed;       436 AA.
AC   E9ABD9;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=Tubulin beta chain {ECO:0000256|RuleBase:RU000352};
DE   Flags: Fragment;
GN   Name=benA {ECO:0000313|EMBL:CBY93731.1};
OS   Aspergillus tabacinus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1220209 {ECO:0000313|EMBL:CBY93731.1};
RN   [1] {ECO:0000313|EMBL:CBY93731.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCF 3690 {ECO:0000313|EMBL:CBY93731.1};
RX   PubMed=22458252; DOI=10.3109/13693786.2012.667578;
RA   Hubka V., Kubatova A., Mallatova N., Sedlacek P., Melichar J.,
RA   Skorepova M., Mencl K., Lyskova P., Sramkova B., Chudickova M., Hamal P.,
RA   Kolarik M.;
RT   "Rare and new etiological agents revealed among 178 clinical Aspergillus
RT   strains obtained from Czech patients and characterized by molecular
RT   sequencing.";
RL   Med. Mycol. 50:601-610(2012).
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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       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; FR775337; CBY93731.1; -; Genomic_DNA.
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; IPR013838; Beta-tubulin_BS.
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:SF492; TUBULIN BETA-4 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.
DR   PROSITE; PS00228; TUBULIN_B_AUTOREG; 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          47..244
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   DOMAIN          246..383
FT                   /note="Tubulin/FtsZ 2-layer sandwich"
FT                   /evidence="ECO:0000259|SMART:SM00865"
FT   NON_TER         436
FT                   /evidence="ECO:0000313|EMBL:CBY93731.1"
SQ   SEQUENCE   436 AA;  48575 MW;  2D456C7304A364D8 CRC64;
     MREIVHLQTG QCGNQIGAAF WQTISGEHGL DGSGVYNGTS DLQLERMNVY FNEASGNKYV
     PRAVLVDLEP GTMDAVRAGP FGQLFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDNVVNVV
     RREAEACDCL QGFQITHSLG GGTGAGMGTL LISKIREEFP DRMMATFSVV PSPKVSDTGV
     EPYNATLSVH QLVEHSDETF CIDNEALYDI CMRTLKLSNP SYGDLNHLVS AVMSGVTTCL
     RFPGQLNSDL RKLAVNMVPF PRLHFFMVGF APLTSRGAYS FRAVSVPELT QQMFDPKNMM
     AASDFRNGRY LTXXXXXRGR VSMKEVEDQM RNIQSKNQSY FVEWIPNNIQ TALCSIPPRG
     LKMSSTFIGN STSIQELFKR VGDQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
     EYQQYQDASI SEGEEE
//
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