(data stored in SCRATCH zone)

SWISSPROT: Q75BT0_ASHGO

ID   Q75BT0_ASHGO            Unreviewed;      1149 AA.
AC   Q75BT0;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 137.
DE   RecName: Full=Protein kinase C {ECO:0000256|SAAS:SAAS01199224};
DE            EC=2.7.11.13 {ECO:0000256|SAAS:SAAS01199224};
GN   ORFNames=AGOS_ACR191C {ECO:0000313|EMBL:AAS51417.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS51417.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS51417.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13;
CC         Evidence={ECO:0000256|SAAS:SAAS01199216};
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:SAAS01199205};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. PKC subfamily. {ECO:0000256|SAAS:SAAS01199204}.
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DR   EMBL; AE016816; AAS51417.1; -; Genomic_DNA.
DR   RefSeq; NP_983593.1; NM_208946.2.
DR   STRING; 33169.AAS51417; -.
DR   EnsemblFungi; AAS51417; AAS51417; AGOS_ACR191C.
DR   GeneID; 4619725; -.
DR   KEGG; ago:AGOS_ACR191C; -.
DR   HOGENOM; HOG000176156; -.
DR   InParanoid; Q75BT0; -.
DR   KO; K02677; -.
DR   OMA; HLGPRIQ; -.
DR   Proteomes; UP000000591; Chromosome III.
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:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
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; 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; Q75BT0.
DR   SWISS-2DPAGE; Q75BT0.
KW   ATP-binding {ECO:0000256|SAAS:SAAS00593399};
KW   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000000591};
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          408..455
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          475..525
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          822..1081
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1082..1149
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          541..561
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          578..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          710..758
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          778..815
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          40..67
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          154..198
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        541..557
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        586..603
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        624..641
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        714..758
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1149 AA;  130439 MW;  4B9503FCB7A9D9C2 CRC64;
     MGAAMMNNVE QDILRKIERE RNIIQGASNL KKRTDNVMVI QKCNTNIREA QQNIQYLEDT
     LKKLHLESQA VAVSQVYPGY RQLSTMAPHE HRFSRLDLSK YDCPSLSQRI QYMLQQLEFK
     LRVERQYQEA NDKLTKLYQI DGDQRSSSAA QGGAQESKQR IQLLTKALKK YQALNVDMEQ
     LKEQADDALN SQQKFRRKQL TGEFTIGLTA IRDIDHIQSP LFSKNPETII TVKVDDVVRA
     KTKPTRTDRW HEEFTIHVDK GNELEITVYD RINDRIVPVA VMWLLLSDVA EEIRKKKVGQ
     VGSPTWLEAA SQLPDASDPY LNTSTAHLPL GGLPLATLDQ PPPESAPDTA HAQPITTSAW
     FVLEPAGQIM LTLGFSKSNQ NVRKDIPGGL RRHGAIVNRK DDVYEKHGHH FVQKSFYNIM
     CCAYCGDFLR YSGFQCQDCK FLCHKKCYNN VVTKCIAKTS TDGDPEEAKL NHHIPHRFEP
     VSNRGTKWCC HCGYILPWGK KNVRKCSECS IMCHTQCAHL VPDFCGMTME MANKILTTIQ
     DTKRNQQQRQ KSSPAGQMLE DASKMIPYNT TGSSIEARGG AAFSKRPTAS TETSPTSQLL
     AEDHSVQPYP DISNLPSATS SSEPQDKHSK RQTRLIYDDD DTTEDSAYYR FSEMTGQKEA
     QAESATLDPG SVYLLNDELL DDHPTTALMW QTMKEEEEQR WLLEQKKKEI SKQINQEAPS
     QWDPQQNPFN SDPSESITQR TLAAEAETSV QLSEAPKSLS SANYDNYVNC ASNLELPSEE
     MESIPQHPPA PLSPPKAQPV QPASGRHKRK TPKRRKVSLD DFILLKVLGK GNFGKVLLAR
     SKNTDRLCAI KVLKKDHIIQ NHDIESARAE KKVFLLATKA KHPFLTNLYC SFQTENRIYF
     AMEFIGGGDL MWHVQNQRLS VRRAKFYAAE VLLALKYFHD NGIIYRDLKL ENILLTLEGH
     IKIADYGLCK DEMWFGNRTS TFCGTPEFMA PEILREQAYT KAVDWWAFGV LLYQMLLCQS
     PFSGDDEDEV FNAILTDEPL YPIDMAGDIV QIFQGLLTKD PEKRLGAGSR DALEVMEEPF
     FRNINFDDIL NLRVEPPYIP TIKAADDTSY FEKEFTAAPP TLTPLPSILS SNLQEEFRGF
     SFMPDDLVL
//

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