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Database: UniProt
Entry: N1R6Q2_FUSC4
LinkDB: N1R6Q2_FUSC4
Original site: N1R6Q2_FUSC4 
ID   N1R6Q2_FUSC4            Unreviewed;       563 AA.
AC   N1R6Q2;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   SubName: Full=Protein kinase C-like protein {ECO:0000313|EMBL:EMT60504.1};
GN   ORFNames=FOC4_g10011775 {ECO:0000313|EMBL:EMT60504.1};
OS   Fusarium oxysporum f. sp. cubense (strain race 4) (Panama disease fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=2502994 {ECO:0000313|EMBL:EMT60504.1, ECO:0000313|Proteomes:UP000016929};
RN   [1] {ECO:0000313|Proteomes:UP000016929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RA   Fang X., Huang J.;
RT   "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT   banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000016929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RX   PubMed=24743270;
RA   Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA   Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA   Fang X., Peng M., Huang J.;
RT   "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT   oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL   PLoS ONE 9:E95543-E95543(2014).
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DR   EMBL; KB726997; EMT60504.1; -; Genomic_DNA.
DR   AlphaFoldDB; N1R6Q2; -.
DR   STRING; 1229665.N1R6Q2; -.
DR   HOGENOM; CLU_020491_0_0_1; -.
DR   Proteomes; UP000016929; 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: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; cd11620; HR1_PKC-like_2_fungi; 1.
DR   Gene3D; 3.30.60.20; -; 1.
DR   Gene3D; 1.10.287.160; HR1 repeat; 1.
DR   InterPro; IPR046349; C1-like_sf.
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; 1.
DR   Pfam; PF02185; HR1; 2.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00742; Hr1; 2.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR   SUPFAM; SSF46585; HR1 repeat; 1.
DR   PROSITE; PS51860; REM_1; 2.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01207, ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000313|EMBL:EMT60504.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016929};
KW   Transferase {ECO:0000313|EMBL:EMT60504.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          1..67
FT                   /note="REM-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51860"
FT   DOMAIN          146..223
FT                   /note="REM-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51860"
FT   DOMAIN          476..524
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   REGION          69..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          370..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          530..563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          14..64
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        370..395
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        530..544
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        546..563
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   563 AA;  62371 MW;  91650CC3B74E8F45 CRC64;
     MNDDDAIHSI HKKIEREKAL INAANSMRAQ TNNEAVRSRL DSQMRDGRRN LQFFEEKLRD
     IQMRRVNAGV GDMSLGGPSD DAGGPPAPPP KDSREDRGSY GSGSGQYAQS GAGSDLMPPR
     HPYAPGPGGS GIPKPRPNFT KLDLIKYDTP HLGPRIQLML SQIQFKLNVE EQYLKGIEKM
     VQLYGMEGDR KSKADAAARK VESKQKIILL KQALKRYEEL HIDADVADAQ DGKFTLQHFL
     LRHIDKRADD SINAPNLRKP LSGQLSIRML AIKDVDHLAT GRFTRGPETF IAVKVEDTVM
     ARTKASRNDR WEAEYHTIEV DKANEIELTV YDKPAEHAMP IAMLWVRISD IVEEMRRKRI
     EAEMNSSGWV SADRMGSSGG APSQFPMSPS SGSFGPGSPA GGGAQGTETG PFGTAGPQPQ
     VQTGPIEEWF NLEPTGQIQL QLAFNKTNAN SRPVDLGLGR KGAVRQRKEE VHEMYGHKFV
     QHQFYNIMRC ALCGDFLKYS AGMQCEDCKY TCHTKCYSSV VTKCISKSNA ETDPDEEKIN
     HRIPHRFNPS PPPPPPPASA SSI
//
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