(data stored in SCRATCH zone)

SWISSPROT: Q6FJ43_CANGA

ID   Q6FJ43_CANGA            Unreviewed;      1144 AA.
AC   Q6FJ43;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   08-MAY-2019, entry version 125.
DE   RecName: Full=Protein kinase C {ECO:0000256|SAAS:SAAS00929532};
DE            EC=2.7.11.13 {ECO:0000256|SAAS:SAAS00929532};
GN   OrderedLocusNames=CAGL0M09361g {ECO:0000313|CGD:CAL0136549,
GN   ECO:0000313|EMBL:CAG62729.1};
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593 {ECO:0000313|Proteomes:UP000002428};
RN   [1] {ECO:0000313|EMBL:CAG62729.1, 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.,
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-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC         EC=2.7.11.13; Evidence={ECO:0000256|SAAS:SAAS01126135};
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=2.7.11.13; Evidence={ECO:0000256|SAAS:SAAS01126142};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. PKC subfamily.
CC       {ECO:0000256|SAAS:SAAS00929254}.
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DR   EMBL; CR380959; CAG62729.1; -; Genomic_DNA.
DR   RefSeq; XP_449751.1; XM_449751.1.
DR   STRING; 5478.XP_449751.1; -.
DR   EnsemblFungi; CAG62729; CAG62729; CAGL0M09361g.
DR   GeneID; 2891315; -.
DR   KEGG; cgr:CAGL0M09361g; -.
DR   CGD; CAL0136549; CAGL0M09361g.
DR   EuPathDB; FungiDB:CAGL0M09361g; -.
DR   eggNOG; KOG0694; Eukaryota.
DR   eggNOG; ENOG410XNPH; LUCA.
DR   HOGENOM; HOG000176156; -.
DR   InParanoid; Q6FJ43; -.
DR   KO; K02677; -.
DR   OMA; HLGPRIQ; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR   GO; GO:0005856; C:cytoskeleton; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR   GO; GO:0030427; C:site of polarized growth; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004697; F:protein kinase C activity; IEA:UniProtKB-EC.
DR   GO; GO:0007015; P:actin filament organization; IEA:EnsemblFungi.
DR   GO; GO:0030242; P:autophagy of peroxisome; IEA:EnsemblFungi.
DR   GO; GO:0032186; P:cellular bud neck septin ring organization; IEA:EnsemblFungi.
DR   GO; GO:0009272; P:fungal-type cell wall biogenesis; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:EnsemblFungi.
DR   GO; GO:0010606; P:positive regulation of cytoplasmic mRNA processing body assembly; IEA:EnsemblFungi.
DR   GO; GO:0060237; P:regulation of fungal-type cell wall organization; IEA:EnsemblFungi.
DR   GO; GO:0060211; P:regulation of nuclear-transcribed mRNA poly(A) tail shortening; IEA:EnsemblFungi.
DR   CDD; cd00029; C1; 2.
DR   CDD; cd08689; C2_fungal_Pkc1p; 1.
DR   CDD; cd11620; HR1_PKC-like_2_fungi; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR037778; C2_fungal_PKC.
DR   InterPro; IPR011072; HR1_rho-bd.
DR   InterPro; IPR036274; HR1_rpt_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR037312; PKC-like_HR1.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00130; C1_1; 2.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF02185; HR1; 2.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   SMART; SM00109; C1; 2.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00742; Hr1; 2.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF46585; SSF46585; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE   3: Inferred from homology;
DR   PRODOM; Q6FJ43.
DR   SWISS-2DPAGE; Q6FJ43.
KW   ATP-binding {ECO:0000256|SAAS:SAAS00593399};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002428};
KW   Kinase {ECO:0000256|SAAS:SAAS00593820};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00253054};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00593601};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002428};
KW   Serine/threonine-protein kinase {ECO:0000256|SAAS:SAAS00593706};
KW   Transferase {ECO:0000256|SAAS:SAAS00592725};
KW   Zinc {ECO:0000256|SAAS:SAAS00253075};
KW   Zinc-finger {ECO:0000256|SAAS:SAAS00795753}.
FT   DOMAIN      422    469       Phorbol-ester/DAG-type.
FT                                {ECO:0000259|PROSITE:PS50081}.
FT   DOMAIN      489    539       Phorbol-ester/DAG-type.
FT                                {ECO:0000259|PROSITE:PS50081}.
FT   DOMAIN      817   1076       Protein kinase. {ECO:0000259|PROSITE:
FT                                PS50011}.
FT   DOMAIN     1077   1144       AGC-kinase C-terminal.
FT                                {ECO:0000259|PROSITE:PS51285}.
FT   COILED       36     63       {ECO:0000256|SAM:Coils}.
FT   COILED      132    152       {ECO:0000256|SAM:Coils}.
FT   COILED      685    719       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   1144 AA;  130708 MW;  FC084151D5059D68 CRC64;
     MLSQVEQDIR RKIAVEENII KGSSALKKKT DNVMVIQKCN TNIREARQNI EYLEETLKKL
     QLSQSQQGQT DSQQQQANDD STVTEIDRGQ GYRQLSTIAP EEHVFSRLDL VKYDCPSLAQ
     KIQYMLQQLE FKLQVERQYQ EANNKLTKLY QIDGDQRSSS AAEGGALESK NRVQLLKKAL
     KKYQAINVDL DQYYKHHNDE SLKDMQPKLR EKQLTGMLTI GITAIRDVDH IQSPLFARNP
     ETFITVKIDD VVKSRTKPSR NDRWNEEFSI EVDKGNEIEI TIYDRVNESV TPVAVMWLLL
     SDIAEEIRKK KVGKTNGQGW VRAASIKSQT VHNSQAVANR TYASDSRTTS LNNSNSDLNQ
     DMSLSPTQVT TNAWFVLEPA GQILLTLGFH KTSQHQRKNL VGGLHRHGAI INRKEEVYEQ
     HGHHFVQKSF YNIMCCAYCG DFLRYTGFQC QDCKFLCHKK CYGNVVTKCI SKASTETDPS
     EAKLNHHIPH RFEPVSNRGT KWCCHCGYIL PWGKQKVRKC TECGIMCHTQ CAHLVPDFCG
     MSMEMANKIL KTIEDTKRTQ EKKKRKPPQT NASALTSTST MIGSSVHDRL DSSPSKSMNA
     SIPSIPSPRK HPYAANQYHE KAEEHQMQNQ NRLNNYIEDN EAYLKFTSGV GVPGASQDVK
     AQNMNDAYVD QYGHEYQQDN NDSQLKASED ELELWKQHRE RMERELQQEQ QMQMSYDNNA
     EGQIDLYTKQ ASGDVNMLPA VDETVSSHNN PFRDMNHETF EQTQNYVANQ LQGDVTDIRS
     STEIITAAGN NVSPQKRSSG KHKKRGSKRP KVSLDNFVLL KVLGKGNFGK VILSRSKNTN
     RLCAIKVLKK DNIIQNHDIE SARAEKKVFL LATKTKHPFL TNLYCSFQTE NRIYFAMEFI
     GGGDLMWHVQ NQRLSVRRAK FYAAEVLLAL KFFHDNGVIY RDLKLENILL TPEGHIKIAD
     YGLCKDGMWY GNKTSTFCGT PEFMAPELLR EQDYTKAVDW WAFGVLLYQM LLCQSPFSGD
     DEDEVFNAIL TDEPLYPIDM AGDIVQIFQG LLTKDPEKRL GAGPRDALEI MEEPFFRNIN
     FDDLLNLRIK PPYIPEIKSA EDTSYFEQEF TSAPPSLTPL PSVLSTTQQE EFRGFSYMPE
     DLEL
//

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