(data stored in SCRATCH zone)

SWISSPROT: Q6BLX3_DEBHA

ID   Q6BLX3_DEBHA            Unreviewed;       650 AA.
AC   Q6BLX3;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   08-MAY-2019, entry version 110.
DE   RecName: Full=Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU361162};
DE            EC=2.7.11.21 {ECO:0000256|RuleBase:RU361162};
GN   OrderedLocusNames=DEHA2F09966g {ECO:0000313|EMBL:CAG89139.1};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG89139.1, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG89139.1, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968
RC   {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.21; Evidence={ECO:0000256|RuleBase:RU361162};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC       protein kinase family. CDC5/Polo subfamily.
CC       {ECO:0000256|RuleBase:RU361162}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CR382138; CAG89139.1; -; Genomic_DNA.
DR   RefSeq; XP_460798.1; XM_460798.1.
DR   STRING; 4959.XP_460798.1; -.
DR   EnsemblFungi; CAG89139; CAG89139; DEHA2F09966g.
DR   GeneID; 2904210; -.
DR   KEGG; dha:DEHA2F09966g; -.
DR   HOGENOM; HOG000248546; -.
DR   InParanoid; Q6BLX3; -.
DR   KO; K06660; -.
DR   OMA; FEVDTWS; -.
DR   OrthoDB; 507604at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0005935; C:cellular bud neck; IEA:EnsemblFungi.
DR   GO; GO:1990023; C:mitotic spindle midzone; IEA:EnsemblFungi.
DR   GO; GO:0097431; C:mitotic spindle pole; IEA:EnsemblFungi.
DR   GO; GO:0044732; C:mitotic spindle pole body; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019237; F:centromeric DNA binding; IEA:EnsemblFungi.
DR   GO; GO:0051219; F:phosphoprotein binding; IEA:EnsemblFungi.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:EnsemblFungi.
DR   GO; GO:0051455; P:attachment of spindle microtubules to kinetochore involved in homologous chromosome segregation; IEA:EnsemblFungi.
DR   GO; GO:0031670; P:cellular response to nutrient; IEA:EnsemblFungi.
DR   GO; GO:0010458; P:exit from mitosis; IEA:EnsemblFungi.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:EnsemblFungi.
DR   GO; GO:1990813; P:meiotic centromeric cohesion protection; IEA:EnsemblFungi.
DR   GO; GO:1902425; P:positive regulation of attachment of mitotic spindle microtubules to kinetochore; IEA:EnsemblFungi.
DR   GO; GO:0045793; P:positive regulation of cell size; IEA:EnsemblFungi.
DR   GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IEA:EnsemblFungi.
DR   GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IEA:EnsemblFungi.
DR   GO; GO:0010696; P:positive regulation of mitotic spindle pole body separation; IEA:EnsemblFungi.
DR   GO; GO:0046827; P:positive regulation of protein export from nucleus; IEA:EnsemblFungi.
DR   GO; GO:0110083; P:positive regulation of protein localization to cell division site involved in mitotic actomyosin contractile ring assembly; IEA:EnsemblFungi.
DR   GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IEA:EnsemblFungi.
DR   GO; GO:0031031; P:positive regulation of septation initiation signaling; IEA:EnsemblFungi.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR   GO; GO:1903353; P:regulation of nucleus organization; IEA:EnsemblFungi.
DR   GO; GO:1902542; P:regulation of protein localization to mitotic spindle pole body; IEA:EnsemblFungi.
DR   GO; GO:0000712; P:resolution of meiotic recombination intermediates; IEA:EnsemblFungi.
DR   GO; GO:0090306; P:spindle assembly involved in meiosis; IEA:EnsemblFungi.
DR   GO; GO:0070194; P:synaptonemal complex disassembly; IEA:EnsemblFungi.
DR   CDD; cd13118; POLO_box_1; 1.
DR   CDD; cd13117; POLO_box_2; 1.
DR   Gene3D; 3.30.1120.30; -; 2.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR033701; POLO_box_1.
DR   InterPro; IPR033695; POLO_box_2.
DR   InterPro; IPR000959; POLO_box_dom.
DR   InterPro; IPR036947; POLO_box_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00659; POLO_box; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50078; POLO_BOX; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6BLX3.
DR   SWISS-2DPAGE; Q6BLX3.
KW   ATP-binding {ECO:0000256|RuleBase:RU361162};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000599};
KW   Kinase {ECO:0000256|RuleBase:RU361162};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU361162};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599};
KW   Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU361162};
KW   Transferase {ECO:0000256|RuleBase:RU361162}.
FT   DOMAIN       68    323       Protein kinase. {ECO:0000259|PROSITE:
FT                                PS50011}.
FT   DOMAIN      471    538       POLO box. {ECO:0000259|PROSITE:PS50078}.
FT   DOMAIN      567    640       POLO box. {ECO:0000259|PROSITE:PS50078}.
SQ   SEQUENCE   650 AA;  74611 MW;  8EA981467D41E097 CRC64;
     MSSVRTQPLQ PLNNGQLNSR ANNITPIKPV RHNKENQEEV KTKKKKEKLS ALCKTPPSIV
     RTRNGRDYRR GTFLGEGGFA RCFQMKDSSG KIYAAKTVAK ASIKNEKTKT KLLSEIKIHK
     SLKHSNIVNF IDCFEDDVNV YILLEICPNQ SLMELLKTRK RVSEPEVRYF MVQMVGAIKY
     LHSRRVIHRD LKLGNVFFDP DMNLKIGDFG LASILPSLES RKYTICGTPN YIAPEVLGGK
     NVGHSFEVDI WALGIMLYAL LVGKPPFQAK DVQVIYERIK KTEYSFPVDK PISEEAKVLI
     KDLLSLNPLH RPNINEILNY DWFKGSFPDK THEISLNGTP EGIDNISKAQ SAINFTNTKA
     SCGIYTPKTK NPVEILRSDL HSEQPRAMLP KSLSPGDTRN KYQEVDPAQL GKPRRVNFNS
     TYSTTIKRLN QICFETYQNM RRLEYSKHDR IDTMELPSCE NPTLISKWVD YSNKYGFSYQ
     LTNDDIGVLF NDENTFLKLH SSGRFLELIY HEGEGWTCIE NSSSHPPSQV KRQLEIVDFF
     AKYMNSNLSK VSENEERKET VFLRRYTRTS EYIMFEMTNG NFQFNFKDHH KVCISKSGLA
     ITHISPNRIT QTHPLIFILK HGDFPSTEVP NCLEKIAIIK EAIKRKAFKE
//

If you have problems or comments...

PBIL Back to PBIL home page