ID A1X5R1_HERER Unreviewed; 389 AA.
AC A1X5R1;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Tubulin beta chain {ECO:0000256|RuleBase:RU000352};
DE Flags: Fragment;
OS Hericium erinaceus (Lion's mane mushroom) (Hydnum erinaceus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Hericiaceae; Hericium.
OX NCBI_TaxID=91752 {ECO:0000313|EMBL:ABC59638.1};
RN [1] {ECO:0000313|EMBL:ABC59638.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=68609 {ECO:0000313|EMBL:ABC59643.1}, ATCC 56457
RC {ECO:0000313|EMBL:ABC59669.1}, CBS 204.74
RC {ECO:0000313|EMBL:ABC59673.1}, CBS 260.74
RC {ECO:0000313|EMBL:ABC59671.1}, CBS 485.95
RC {ECO:0000313|EMBL:ABC59667.1}, IUM 00416
RC {ECO:0000313|EMBL:ABC59646.1}, KFRI 509 {ECO:0000313|EMBL:ABC59654.1},
RC KFRI 658 {ECO:0000313|EMBL:ABC59647.1}, KME 38010
RC {ECO:0000313|EMBL:ABC59658.1}, KME 38011
RC {ECO:0000313|EMBL:ABC59659.1}, KME 38015
RC {ECO:0000313|EMBL:ABC59660.1}, KME 38016
RC {ECO:0000313|EMBL:ABC59661.1}, KUMC 1001
RC {ECO:0000313|EMBL:ABC59638.1}, KUMC 1002
RC {ECO:0000313|EMBL:ABC59639.1}, KUMC 1008
RC {ECO:0000313|EMBL:ABC59642.1}, KUMC e1 {ECO:0000313|EMBL:ABC59668.1},
RC KUMC e2 {ECO:0000313|EMBL:ABC59664.1}, NIAST 48001
RC {ECO:0000313|EMBL:ABC59648.1}, NIAST 48002
RC {ECO:0000313|EMBL:ABC59649.1}, and NIAST 48006
RC {ECO:0000313|EMBL:ABC59644.1};
RA Ko H.G., Kim S.H., Park H.G., Park W.M.;
RT "Molecular identification of medicinal mushroom Hericium erinaceum by
RT phylogenetic analysis of the beta-tubulin.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFJ44227.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CB1 {ECO:0000313|EMBL:AFJ44227.1};
RA Chi Y.J., Yin L.W.;
RT "Cloning and characterization of two novel manganese peroxidase genes from
RT ligninolytic basidiomycete Hericium erinaceum CB1.";
RL Submitted (FEB-2012) 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|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|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; DQ266904; ABC59638.1; -; Genomic_DNA.
DR EMBL; DQ266905; ABC59639.1; -; Genomic_DNA.
DR EMBL; DQ266908; ABC59642.1; -; Genomic_DNA.
DR EMBL; DQ266909; ABC59643.1; -; Genomic_DNA.
DR EMBL; DQ266910; ABC59644.1; -; Genomic_DNA.
DR EMBL; DQ266912; ABC59646.1; -; Genomic_DNA.
DR EMBL; DQ266913; ABC59647.1; -; Genomic_DNA.
DR EMBL; DQ266914; ABC59648.1; -; Genomic_DNA.
DR EMBL; DQ266915; ABC59649.1; -; Genomic_DNA.
DR EMBL; DQ266921; ABC59654.1; -; Genomic_DNA.
DR EMBL; DQ266925; ABC59658.1; -; Genomic_DNA.
DR EMBL; DQ266926; ABC59659.1; -; Genomic_DNA.
DR EMBL; DQ266927; ABC59660.1; -; Genomic_DNA.
DR EMBL; DQ266928; ABC59661.1; -; Genomic_DNA.
DR EMBL; DQ266931; ABC59664.1; -; Genomic_DNA.
DR EMBL; DQ266934; ABC59667.1; -; Genomic_DNA.
DR EMBL; DQ266935; ABC59668.1; -; Genomic_DNA.
DR EMBL; DQ266936; ABC59669.1; -; Genomic_DNA.
DR EMBL; DQ266938; ABC59671.1; -; Genomic_DNA.
DR EMBL; DQ266940; ABC59673.1; -; Genomic_DNA.
DR EMBL; JQ675730; AFJ44227.1; -; Genomic_DNA.
DR AlphaFoldDB; A1X5R1; -.
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; 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; 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 389
FT /evidence="ECO:0000313|EMBL:ABC59638.1"
SQ SEQUENCE 389 AA; 43265 MW; 0ADB53D3FA516BE5 CRC64;
MREIVHLQTG QCGNQIGVKF WEVISDEHGI ERDGLYKGTN DLQLERISVY YNETGANKYV
PRAVLIDLEP GTMDAVRAGP LGGLFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV
RKEAEGTEAL QGFQITHSLG GGTGAGMGTL LISKIREEYP DRMMCTFSVV PSPKVSDTVV
EPYNATLSVH QLVENSDETF CIDNEALYDI HFRTLKLSTP TYGDLNHLVS IVMSGITTCL
RFPGQLNSDL RKLAVNMVPF PRLHFFLTGF APLTARGSQQ YRAVTVPELT QQMFDAKNMM
AASDPRHGRY LTVAAIFRGR VSMKEVEEQM QNVQNKNSAY FVEWIPNNVL TAQCDIPPRG
LKMSVTFLGN STAIQELFRR VSDQFTAMF
//
