ID A0A423WPY7_9PEZI Unreviewed; 774 AA.
AC A0A423WPY7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Protein kinase C {ECO:0008006|Google:ProtNLM};
GN ORFNames=VSDG_00624 {ECO:0000313|EMBL:ROW05412.1};
OS Valsa sordida.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=252740 {ECO:0000313|EMBL:ROW05412.1, ECO:0000313|Proteomes:UP000284375};
RN [1] {ECO:0000313|EMBL:ROW05412.1, ECO:0000313|Proteomes:UP000284375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YSFL {ECO:0000313|EMBL:ROW05412.1,
RC ECO:0000313|Proteomes:UP000284375};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ROW05412.1}.
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DR EMBL; LJZO01000001; ROW05412.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423WPY7; -.
DR STRING; 252740.A0A423WPY7; -.
DR Proteomes; UP000284375; Unassembled WGS sequence.
DR GO; GO:0004697; F:diacylglycerol-dependent serine/threonine kinase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009272; P:fungal-type cell wall biogenesis; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd20822; C1_ScPKC1-like_rpt1; 1.
DR CDD; cd20823; C1_ScPKC1-like_rpt2; 1.
DR CDD; cd11620; HR1_PKC-like_2_fungi; 1.
DR Gene3D; 3.30.60.20; -; 2.
DR Gene3D; 1.10.287.160; HR1 repeat; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR036274; HR1_rpt_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR037312; PKC-like_HR1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF02185; HR1; 2.
DR SMART; SM00109; C1; 2.
DR SMART; SM00239; C2; 1.
DR SMART; SM00742; Hr1; 2.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR SUPFAM; SSF46585; HR1 repeat; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS51860; REM_1; 2.
DR PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01207, ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000284375};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1..67
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 150..227
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 234..352
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
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 REGION 29..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 204..234
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 67..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..408
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 774 AA; 85990 MW; B696281E37C5E004 CRC64;
MADEDKMMDI YKKIEREKAL IQAANLMRQQ TNNDNVRSKL DTQMREGKRN LEFFEEKLKE
LQLRRGMSSM SIASDGSASG SRSRGQQPDD DAPPAPPKDA SGFATSGGEP QYSQIGQHGD
LMPPRHPYAA PGPGSHPKTR PNYTKLDLIK YDTPYLGPRI QLMLSQIQFK LNVEEQYLKG
VEKMVQLYQM EGDKKSRADA AARKVESKQK ITLLKQALKR YEELHIDIDD SADNQDDDSI
NMPNMRKPLS GQLAIRVICV KDVDHAPTGR FSRSPDTFVA VKVEDTVVAR TRATRTDRWE
VEYHNIEVDK ANEIELTVYD KPGEHALPIG LLWVRISDIA EELRRKRIEA EINNSGWVSA
DRMASSKALP QFAANPQQSQ PQFGPPPTSP GYQSAQPTYP PPQQAPPQAV SQPIEGLFNL
EPTGQIQLSF NFIKQTSNTA KFDAGLGRKG AVRQRKEEIH EMYGHKFVQR QFYNIMRCAF
CGDFLKYSAG MQCEDCKYTC HTKCYTSVVT KCISKSNAET DPDEEKINHR IPHRFQTFSN
LTANWCCHCG YLLPFGKKNC RKCSECALTA HAQCVHLVPD FCGMSMITAT QILEGMRTQK
QRQSHKTSMS ERTLRSGMTS PGTSQSSTLY DRNSGASYSG TISPSAAEAA RKSYGQTSPE
TLGNRTSAST DAAAAATLAM TGAVGAQSPR AQQGGRPDYV GRQDSYPQED PYASQQFGAQ
TQQRPYNPAD YANVNQFSGQ PQASRSVSAA TALPTADCPA KGSARIYGPR DICY
//