ID A0A3G2S6T3_9BASI Unreviewed; 1264 AA. AC A0A3G2S6T3; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 07-OCT-2020, entry version 10. DE SubName: Full=Protein kinase C-like protein {ECO:0000313|EMBL:AYO43019.1}; DE EC=2.7.11.13 {ECO:0000313|EMBL:AYO43019.1}; GN Name=pkcA {ECO:0000313|EMBL:AYO43019.1}; GN ORFNames=DNF11_2069 {ECO:0000313|EMBL:AYO43019.1}; OS Malassezia restricta CBS 7877. OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina; OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia. OX NCBI_TaxID=425264 {ECO:0000313|EMBL:AYO43019.1, ECO:0000313|Proteomes:UP000269793}; RN [1] {ECO:0000313|EMBL:AYO43019.1, ECO:0000313|Proteomes:UP000269793} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS 7877 {ECO:0000313|EMBL:AYO43019.1, RC ECO:0000313|Proteomes:UP000269793}; RA Morand S.C., Bertignac M., Iltis A., Kolder I., Pirovano W., Jourdain R., RA Clavaud C.; RT "Complete genome sequence of Malassezia restricta CBS 7877."; RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases. 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|ARBA:ARBA00000946}; 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|ARBA:ARBA00000569}; CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS19 family. CC {ECO:0000256|ARBA:ARBA00010014}. 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; CP033150; AYO43019.1; -; Genomic_DNA. DR Proteomes; UP000269793; Chromosome iii. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004698; F:calcium-dependent protein kinase C activity; IEA:UniProtKB-EC. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0009272; P:fungal-type cell wall biogenesis; IEA:InterPro. DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:InterPro. DR CDD; cd00029; C1; 2. DR CDD; cd11620; HR1_PKC-like_2_fungi; 1. DR Gene3D; 1.10.10.2700; -; 1. DR InterPro; IPR000961; AGC-kinase_C. DR InterPro; IPR000008; C2_dom. 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; IPR001266; Ribosomal_S19e. DR InterPro; IPR018277; Ribosomal_S19e_CS. DR InterPro; IPR038111; Ribosomal_S19e_sf. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR InterPro; IPR036390; WH_DNA-bd_sf. DR Pfam; PF00130; C1_1; 2. DR Pfam; PF02185; HR1; 1. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF00433; Pkinase_C; 1. DR Pfam; PF01090; Ribosomal_S19e; 1. DR SMART; SM00109; C1; 2. DR SMART; SM00239; C2; 1. DR SMART; SM00742; Hr1; 2. DR SMART; SM01413; Ribosomal_S19e; 1. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF46585; SSF46585; 2. DR SUPFAM; SSF46785; SSF46785; 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; PS00628; RIBOSOMAL_S19E; 1. DR PROSITE; PS00479; ZF_DAG_PE_1; 1. DR PROSITE; PS50081; ZF_DAG_PE_2; 2. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AYO43019.1}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022771}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Reference proteome {ECO:0000313|Proteomes:UP000269793}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274}; KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980}; KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AYO43019.1}; KW Zinc {ECO:0000256|ARBA:ARBA00022771}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}. FT DOMAIN 464..512 FT /note="Phorbol-ester/DAG-type" FT /evidence="ECO:0000259|PROSITE:PS50081" FT DOMAIN 532..582 FT /note="Phorbol-ester/DAG-type" FT /evidence="ECO:0000259|PROSITE:PS50081" FT DOMAIN 786..1045 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 1046..1116 FT /note="AGC-kinase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51285" FT REGION 78..99 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 247..269 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 605..685 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 697..774 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1239..1264 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 46..66 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 605..669 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 697..717 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 730..759 FT /note="Pro-rich" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1243..1264 FT /note="Acidic" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1264 AA; 142063 MW; 26A303713FEB3D32 CRC64; MPDSVPTKIA DLESRIQKQH RIIEGFQNLR SATPNQDVIK QADSNIRDAQ RTIHYLQDSL MSLQRRASID AINTERKPSL SGTIPATPTT SAHLDSLNDP TMSPSQVVDE YAQTTFDAPS FAPFPIDSSA AYRSGSYSMD HGISPLNDMN LLSREPTAAR RNYSPLDLMR YDTPLTSAKV QRMLNQLEYK LQLERQFKQG YDKIARLYEA EGDRRSQDDA ASRRSESAGK LVLIQQALNR YQQLDMRDAE EVQQENPYAA RRARKPQSGT LSISIKRAKE IDHAAISNST RLMRESYVAI KVEETERVQT PSSRTDTWNV KYELPLENTN EVELVIFDQV GSSVPVPVGL LWLRISDIIE QLRRIKTGQV LPDNAQSSPA AGGGEWVTAE RMASLHSSNT MNQTVMQQAK ETGMEGWFTV EPTGAIYLRL DFTKQNVTKR PYDTGLGRHG AMRKRPEEVS VVNGHKFVPR QFYQVIRCAL CGELLLNAAG SQCQDCNYTC HKKCAQKVVT KCISKTSDLS ARDEVELKHR IPHRFEPFTN LGTNWCCHCG SMLPLGRRVG RKCSECDITC HADCMHLVPD FCGMSMEMAN QMLSNIATIK KNRFSSSLPD SAAPKRSSVL STDTLRPSAQ QASMGQLTPG MQQLMVTPSS SRPSVSMQGS TQHSPARSPL PSPQQSPKPS PVHPIRQNLA SMRQPSIDSN GVALTSPPSS LQPMSQPFKD SARIPPKSVN RVPVPTPSPS HASPLPPRPS LPQVAVVPPQ LPSGPEQASS LEFPPSSMRN VTLDDFNFLA VLGKGNFGKV MLAEEKQTGV LYAIKVLKKE FIIENDEIDS TRSEKRVFLT VARERHPFLL NLHSCFQTET RVYFVMEYVG GGDLMLHIQR QQFNLHRAKF YAAEVLLALE YFHKHGIIYR DLKLDNIMLT LDGHVKIADY GLCKENMWYG NTTSTFCGTP EFMAPEILLE QRYGRAVDWW AFGILLYEML LGQAPFRGDD EDEIFDAILE DDPLYPIQMP RDSVSLLQRL LTRDPSRRLG AGPNDADDVK AHPFFRDVNW DDLINKRVPP PFCPTLRHAS DTEWFDTEFT REKPTLTPVH SIFSPEDQAE FRDFSCVKDV DAAQFINAYA QHLKRSGKIE MPTWVDIVKT GAFKEQAPYD PDWWYVRAAT LARHVYLHKS VGVGALCKLH GGPKNRGFRP SHHSRASASV QRKVLQSLEA IGVVEISSKG GRIISQDGMR DLDRIAVAVL ESQREDEEDE DEDEDEDEDE EDDE //