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Database: UniProt
Entry: A0A066XE96_COLSU
LinkDB: A0A066XE96_COLSU
Original site: A0A066XE96_COLSU 
ID   A0A066XE96_COLSU        Unreviewed;       820 AA.
AC   A0A066XE96;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=Calcium-independent protein kinase C {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CSUB01_03290 {ECO:0000313|EMBL:KDN67222.1};
OS   Colletotrichum sublineola (Sorghum anthracnose fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum graminicola species complex.
OX   NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN67222.1, ECO:0000313|Proteomes:UP000027238};
RN   [1] {ECO:0000313|Proteomes:UP000027238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX   PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA   Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT   "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT   of cultivated sorghum.";
RL   Genome Announc. 2:E0054014-E0054014(2014).
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:KDN67222.1}.
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DR   EMBL; JMSE01000831; KDN67222.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A066XE96; -.
DR   STRING; 1173701.A0A066XE96; -.
DR   eggNOG; KOG0694; Eukaryota.
DR   HOGENOM; CLU_000288_54_0_1; -.
DR   OMA; SHANCVH; -.
DR   OrthoDB; 21591at2759; -.
DR   Proteomes; UP000027238; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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   InterPro; IPR017892; Pkinase_C.
DR   Pfam; PF00130; C1_1; 2.
DR   Pfam; PF02185; HR1; 2.
DR   Pfam; PF00433; Pkinase_C; 1.
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; 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:UP000027238};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          1..67
FT                   /note="REM-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51860"
FT   DOMAIN          156..233
FT                   /note="REM-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51860"
FT   DOMAIN          469..517
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          537..587
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   REGION          64..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          364..419
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          609..643
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          657..801
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          7..64
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        382..396
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        609..636
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        657..702
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        735..801
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   820 AA;  90909 MW;  D2E90EE5E9387265 CRC64;
     MNDEDAIQNI LKKIEREKAL LNAANAMRAQ TNNEAVRSRL DSQMRDGRRN LQFFEEKLRE
     AQLRRGMDNM SLGSPTGDSR PLSGDMDDVP PPPPKDSGWE QRGGYGAGSA TSGGNVQYSQ
     IGGHADLMPP RHPYASPGPS SIPKSRPNFT KLDLIKYDTP YLGPRIQLML SQIQFKLNVE
     EQYLKGIEKM VQLYGMEGDR KSRADAAARR VESKQKILLL KQAMKRYEEL HIDMDTSDAQ
     DDDSINMPNL RKPLTGQLSI RVGQIKDVDH ASMSRFSRGP ETFIAVKVED NVVARTRVTR
     TDKWEAEYHT IDVDKANEIE LTVYDKPGEH AIPIAMLWVR ISDIAEEMRR KRIEAEINNS
     GWVSADRMGA PSQFPMNPPQ QQQSFGGPPP SPSPAQPGAQ GQQGPGGMPN PPIAQQPIDG
     WFNLEPAGQI QLSLGFLKQN NARRPVNLQG LGRVGAVRQR KEEVHEMYGH KFVQQQFYNI
     MRCALCGDFL KYSTGMQCED CKYTCHTKCY ASVVTKCISK SNAETDPDEE KINHRIPHRF
     QAFSNMTANW CCHCGYILPF GKKNCRKCAE CGLTAHAACV HLVPDFCGMS MAVANQILEG
     IKTTRMITKN KTSSSLSDRT LRKPTSPTST LGSPPHSGGQ AHYAVGSPEA TEAAKLMYQQ
     QQASPGQRPP HDRTTSNTAA AAAAATAAMS GTMASQPKPN PQDYGQYGGH PGYPPQAEQE
     DSYGGRKYNP ADYAAVNQQA ASYAQQSPVQ QQQRPVQQQQ QQPVPQQYQQ PPPQQTYQQQ
     PVASPKLQEP PQISPISSSG VLSQAMQEEF RGFSYTADFE
//
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