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Database: UniProt
Entry: K7XE67_PHYRM
LinkDB: K7XE67_PHYRM
Original site: K7XE67_PHYRM 
ID   K7XE67_PHYRM            Unreviewed;       302 AA.
AC   K7XE67;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   22-FEB-2023, entry version 48.
DE   RecName: Full=Tubulin beta chain {ECO:0000256|RuleBase:RU000352};
DE   Flags: Fragment;
OS   Phytophthora ramorum (Sudden oak death agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=164328 {ECO:0000313|EMBL:AFX60894.1};
RN   [1] {ECO:0000313|EMBL:AFX60894.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=P1349 {ECO:0000313|EMBL:AFX60890.1}, P1376
RC   {ECO:0000313|EMBL:AFX60888.1}, P1403 {ECO:0000313|EMBL:AFX60889.1},
RC   P1577 {ECO:0000313|EMBL:AFX60887.1}, P2054
RC   {ECO:0000313|EMBL:AFX60891.1}, P2057 {ECO:0000313|EMBL:AFX60892.1},
RC   P2460 {ECO:0000313|EMBL:AFX60893.1}, P2461
RC   {ECO:0000313|EMBL:AFX60894.1}, and P2462
RC   {ECO:0000313|EMBL:AFX60895.1};
RX   PubMed=23153808;
RA   Van Poucke K., Franceschini S., Webber J.F., Vercauteren A., Turner J.A.,
RA   McCracken A.R., Heungens K., Brasier C.M.;
RT   "Discovery of a fourth evolutionary lineage of Phytophthora ramorum: EU2.";
RL   Fungal Biol. 116:1178-1191(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   -!- 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; JQ837656; AFX60887.1; -; Genomic_DNA.
DR   EMBL; JQ837657; AFX60888.1; -; Genomic_DNA.
DR   EMBL; JQ837658; AFX60889.1; -; Genomic_DNA.
DR   EMBL; JQ837659; AFX60890.1; -; Genomic_DNA.
DR   EMBL; JQ837660; AFX60891.1; -; Genomic_DNA.
DR   EMBL; JQ837661; AFX60892.1; -; Genomic_DNA.
DR   EMBL; JQ837662; AFX60893.1; -; Genomic_DNA.
DR   EMBL; JQ837663; AFX60894.1; -; Genomic_DNA.
DR   EMBL; JQ837664; AFX60895.1; -; Genomic_DNA.
DR   AlphaFoldDB; K7XE67; -.
DR   VEuPathDB; FungiDB:PSURA_72114; -.
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; 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:SF429; TUBULIN BETA-1 CHAIN-RELATED; 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          2..169
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   DOMAIN          171..301
FT                   /note="Tubulin/FtsZ 2-layer sandwich"
FT                   /evidence="ECO:0000259|SMART:SM00865"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AFX60894.1"
FT   NON_TER         302
FT                   /evidence="ECO:0000313|EMBL:AFX60894.1"
SQ   SEQUENCE   302 AA;  33467 MW;  F615632F5FDEFF44 CRC64;
     VRAGPYGQLF RPDNFVFGQT GAGNNWAKGH YTEGAELIDS VLDVVRKEAE SCDCLQGFQI
     THSLGGGTGS GMGTLLISKI REEYPDRIMC TYSVCPSPKV SDTVVEPYNA TLSVHQLVEN
     ADEVMCLDNE ALYDICFRTL KLTTPTYGDL NHLVCAAMSG ITTCLRFPGQ LNSDLRKLAV
     NLIPFPRLHF FMIGFAPLTS RGSQQYRALT VPELTQQQFD AKNMMCAADP RHGRYLTAAC
     MFRGRMSTKE VDEQMLNVQN KNSSYFVEWI PNNIKASVCD IPPKGLKMST TFIGNSTAIQ
     EM
//
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