ID J6EHE2_SACK1 Unreviewed; 457 AA.
AC J6EHE2;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Tubulin beta chain {ECO:0000256|RuleBase:RU000352};
GN Name=YFL037W {ECO:0000313|EMBL:EJT43404.1};
GN Synonyms=SKDI06G0280 {ECO:0000313|EMBL:CAI4060831.1};
GN ORFNames=SKDI_06G0280 {ECO:0000313|EMBL:CAI4060831.1}, SKUD_169502
GN {ECO:0000313|EMBL:EJT43404.1};
OS Saccharomyces kudriavzevii (strain ATCC MYA-4449 / AS 2.2408 / CBS 8840 /
OS NBRC 1802 / NCYC 2889) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=226230 {ECO:0000313|EMBL:EJT43404.1, ECO:0000313|Proteomes:UP000002753};
RN [1] {ECO:0000313|EMBL:EJT43404.1, ECO:0000313|Proteomes:UP000002753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4449 / AS 2.2408 / CBS 8840 / NBRC 1802 / NCYC 2889
RC {ECO:0000313|Proteomes:UP000002753}, and IFO 1802
RC {ECO:0000313|EMBL:EJT43404.1};
RX PubMed=12775844; DOI=10.1126/science.1084337;
RA Cliften P.F., Sudarsanam P., Desikan A., Fulton L., Fulton B., Majors J.,
RA Waterston R., Cohen B.A., Johnston M.;
RT "Finding functional features in Saccharomyces genomes by phylogenetic
RT footprinting.";
RL Science 301:71-76(2003).
RN [2] {ECO:0000313|EMBL:EJT43404.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFO 1802 {ECO:0000313|EMBL:EJT43404.1};
RA Cliften P.F., Johnston M.;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000002753}
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4449 / AS 2.2408 / CBS 8840 / NBRC 1802 / NCYC 2889
RC {ECO:0000313|Proteomes:UP000002753};
RX PubMed=22384314; DOI=10.1534/g3.111.000273;
RA Scannell D.R., Zill O.A., Rokas A., Payen C., Dunham M.J., Eisen M.B.,
RA Rine J., Johnston M., Hittinger C.T.;
RT "The awesome power of yeast evolutionary genetics: New genome sequences and
RT strain resources for the Saccharomyces sensu stricto genus.";
RL G3 (Bethesda) 1:11-25(2011).
RN [4] {ECO:0000313|EMBL:EJT43404.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFO 1802 {ECO:0000313|EMBL:EJT43404.1};
RA Cliften P., Hittinger C.T., Wang B., Sudarsanam P., Desikan A., Fulton L.,
RA Fulton B., Majors J., Waterston R., Cohen B.A., Johnston M.;
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:CAI4060831.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFO1802 {ECO:0000313|EMBL:CAI4060831.1};
RA Byrne P K.;
RL Submitted (OCT-2022) 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 -!- 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; OX365901; CAI4060831.1; -; Genomic_DNA.
DR EMBL; AACI03000828; EJT43404.1; -; Genomic_DNA.
DR AlphaFoldDB; J6EHE2; -.
DR STRING; 226230.J6EHE2; -.
DR HOGENOM; CLU_015718_1_1_1; -.
DR Proteomes; UP000002753; Unassembled WGS sequence.
DR Proteomes; UP001162087; Chromosome 6.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002753}.
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 REGION 423..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 457 AA; 50939 MW; EE3EC12187C5EEB8 CRC64;
MREIIHISTG QCGNQIGAAF WETICGEHGL DFNGTYHGHD DIQKERLNVY FNEASSGKWV
PRSINVDLEP GTIDAVRNSA IGNLFRPDNY IFGQSSAGNV WAKGHYTEGA ELVDSVMDVI
RREAEGCDSL QGFQITHSLG GGTGSGMGTL LISKIREEFP DRMMATFSVL PSPKTSDTVV
EPYNATLSVH QLVEHSDETF CIDNEALYDI CQRTLKLNQP SYGDLNNLVS SVMSGVTTSL
RYPGQLNSDL RKLAVNLVPF PRLHFFMVGY APLTAIGSQS FRSLTVPELT QQMFDSKNMM
AAADPRNGRY LTVAAFFRGK VSVKEVEDEM HKVQSKNSDY FVEWIPNNVQ TAVCSVAPQG
LDMAATFIAN STSIQELFKR VGDQFSAMFK RKAFLHWYTS EGMDELEFSE AESNMNDLVS
EYQQYQEATV EDDEEVDENG DFGAPQNQDE PITENFE
//
