ID A0A2T4GDJ7_FUSCU Unreviewed; 760 AA.
AC A0A2T4GDJ7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Protein kinase C-like protein {ECO:0000313|EMBL:PTD01648.1};
DE Flags: Fragment;
GN ORFNames=FCULG_00010079 {ECO:0000313|EMBL:PTD01648.1};
OS Fusarium culmorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=5516 {ECO:0000313|EMBL:PTD01648.1, ECO:0000313|Proteomes:UP000241587};
RN [1] {ECO:0000313|EMBL:PTD01648.1, ECO:0000313|Proteomes:UP000241587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PV {ECO:0000313|EMBL:PTD01648.1,
RC ECO:0000313|Proteomes:UP000241587};
RA Schmidt R.;
RT "Fusarium culmorum secondary metabolites in fungal-bacterial-plant
RT interactions.";
RL Submitted (FEB-2018) 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:PTD01648.1}.
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DR EMBL; PVEM01000028; PTD01648.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4GDJ7; -.
DR OMA; SHANCVH; -.
DR Proteomes; UP000241587; Unassembled WGS sequence.
DR GO; GO:0004697; F:diacylglycerol-dependent serine/threonine kinase activity; IEA:UniProtKB-EC.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; cd08689; C2_fungal_Pkc1p; 1.
DR CDD; cd11620; HR1_PKC-like_2_fungi; 1.
DR Gene3D; 3.30.60.20; -; 2.
DR Gene3D; 2.60.40.150; C2 domain; 1.
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; IPR037778; C2_fungal_PKC.
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 PANTHER; PTHR48125; LP07818P1; 1.
DR PANTHER; PTHR48125:SF10; RNA POLYMERASE II-ASSOCIATED FACTOR 1 HOMOLOG; 1.
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; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01207, ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000313|EMBL:PTD01648.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000241587};
KW Transferase {ECO:0000313|EMBL:PTD01648.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1..67
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 148..225
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 231..349
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 439..487
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 507..557
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT REGION 70..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 14..64
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 99..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..747
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 760
FT /evidence="ECO:0000313|EMBL:PTD01648.1"
SQ SEQUENCE 760 AA; 83650 MW; 7F3D01C0B80095E7 CRC64;
MNDDDAIHNI HKKIEREKAL INAANSMRAQ TNNEAVRSRL DSQMRDGRRN LQFFEEKLRD
IQLRRVNQGV GDMSLGGPAD DAGGPPAPPP KDASSNPAGD RGSYGSGSGQ YSQAGGGSDL
MPPVILMHRD LVDRVSLRHA PTLPNLIKYD TPHLGPRIQL MLSQIQFKLN VEEQYLKGIE
KMVQLYSMEG DRKSKADAAA RKVESKQKIL LLKQALKRYE ELHIDADVAD AQDDDSINAP
NLRKPLSGQL SIRMIAIKDV DHAATGRFTR GPETFIAVKV EDTVMARTKA SRNDRWEAEF
HTIEVDKANE IELTVYDKPG EHPMPIGMLW VRISDIVEEI RRKRIEAEMN SSGWVSADRM
GSTSAAPTQD DTGPFGAAGP QPQVQTGPIE EWFNLEPTGQ IQLQLTFNKS NNNSRPADLG
LGRKGAVRQR KEEVHEMYGH KFVQHQFYNI MRCALCGDFL KYSAGMQCED CKYTCHTKCY
SSVVTKCISK SNAETDPDEE KINHRIPHRF NPYSNMTANW CCHCGYILPF GKKNCRKCSE
CGLTAHAQCV HLVPDFCGMS MAVANQILDG IRTQKQRQAK VSSLSEKTLR HGKTSPTSTS
SPAPSYSSTT APSYQSGPVS PEATEAAKMM YSNPSTPRPA GPDRTSSSSQ AAAAASAAMS
GGPSAAQRQN SDFGRYSGGY DQPQEDPYAQ GGQYGAGQQR KYNPADYANV NPGYGGQQPA
AQAQRPVQQQ PAQQPPPQSP LPPVPQHQQQ QPQAAYQQPA
//
