(data stored in ACNUC8465 zone)

SWISSPROT: Q6FPH3_CANGA

ID   Q6FPH3_CANGA            Unreviewed;       467 AA.
AC   Q6FPH3;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 113.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN   Name=MKK1 {ECO:0000313|CGD:CAL0133234};
GN   OrderedLocusNames=CAGL0J03828g {ECO:0000313|CGD:CAL0133234,
GN   ECO:0000313|EMBL:CAG60820.1};
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593 {ECO:0000313|Proteomes:UP000002428};
RN   [1] {ECO:0000313|EMBL:CAG60820.1, ECO:0000313|Proteomes:UP000002428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC   {ECO:0000313|Proteomes:UP000002428};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., 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   -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC       {ECO:0000256|RuleBase:RU000304}.
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DR   EMBL; CR380956; CAG60820.1; -; Genomic_DNA.
DR   RefSeq; XP_447871.1; XM_447871.1.
DR   STRING; 5478.XP_447871.1; -.
DR   EnsemblFungi; CAG60820; CAG60820; CAGL0J03828g.
DR   GeneID; 2889658; -.
DR   KEGG; cgr:CAGL0J03828g; -.
DR   CGD; CAL0133234; MKK1.
DR   EuPathDB; FungiDB:CAGL0J03828g; -.
DR   eggNOG; KOG0581; Eukaryota.
DR   eggNOG; ENOG410XQ5A; LUCA.
DR   HOGENOM; HOG000234206; -.
DR   InParanoid; Q6FPH3; -.
DR   KO; K08294; -.
DR   OMA; PSPRQMI; -.
DR   Proteomes; UP000002428; Chromosome J.
DR   GO; GO:0005935; C:cellular bud neck; IEA:EnsemblFungi.
DR   GO; GO:0005934; C:cellular bud tip; IEA:EnsemblFungi.
DR   GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR   GO; GO:0000935; C:division septum; IEA:EnsemblFungi.
DR   GO; GO:0043332; C:mating projection tip; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004708; F:MAP kinase kinase activity; IEA:EnsemblFungi.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030242; P:autophagy of peroxisome; IEA:EnsemblFungi.
DR   GO; GO:0000196; P:cell wall integrity MAPK cascade; IEA:EnsemblFungi.
DR   GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IEA:EnsemblFungi.
DR   GO; GO:0060237; P:regulation of fungal-type cell wall organization; IEA:EnsemblFungi.
DR   InterPro; IPR011009; Kinase-like_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   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
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; Q6FPH3.
DR   SWISS-2DPAGE; Q6FPH3.
KW   ATP-binding {ECO:0000256|RuleBase:RU000304};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|RuleBase:RU000304};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000304};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002428};
KW   Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304};
KW   Transferase {ECO:0000256|RuleBase:RU000304}.
FT   DOMAIN          180..447
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          163..183
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..17
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..56
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..107
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   467 AA;  51828 MW;  C3D188323077A7E3 CRC64;
     MASLFRPPES TRQNARSPRL KLPPLSNVSL AVPGESPTGK LSATSSRGSS ATSANMKRPM
     PPPLPKLDVP LSAASSTEGL VRKMKQLSVE DESPQSGSSR GVERDDTTAV NQSVDSFFSN
     LISVYDQSSS AITSPKIDEP EDSAVKDALA TRVPRSLTQG KDIDELSEEV WHSKNLLAEI
     ETQGVLGEGA GGSVAKCKLR TGKKVFALKT INILNGDPEF QKQLLRELQF NKSFKSEYIV
     RYFGMFTDEQ NSSIYIAMEY MGGKSLEAIY KELLSRGGRI SEKVLGKISE AVLRGLSYLH
     EKKVIHRDIK PQNILLNEDG QVKLCDFGVS GEAVNSLATT FTGTSYYMAP ERIQGQPYSV
     TCDVWSLGLT ILEVAQGHFP FGPDKMATTI APIELLTLIL TFTPHLDDEP DKNIKWSRAF
     KSFIEYCLRK EARARPSPRQ MIQHPWIQGQ MKKQVDMRKF ITKCWQK
//

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