ID G1WZF6_ARTOA Unreviewed; 795 AA.
AC G1WZF6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGX53679.1};
GN ORFNames=AOL_s00006g7 {ECO:0000313|EMBL:EGX53679.1};
OS Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX53679.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX53679.1, ECO:0000313|Proteomes:UP000008784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC {ECO:0000313|Proteomes:UP000008784};
RX PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT provide insights into nematode-trap formation.";
RL PLoS Pathog. 7:E1002179-E1002179(2011).
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:EGX53679.1}.
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DR EMBL; ADOT01000009; EGX53679.1; -; Genomic_DNA.
DR RefSeq; XP_011117618.1; XM_011119316.1.
DR AlphaFoldDB; G1WZF6; -.
DR STRING; 756982.G1WZF6; -.
DR GeneID; 22889156; -.
DR eggNOG; KOG0694; Eukaryota.
DR HOGENOM; CLU_000288_54_0_1; -.
DR InParanoid; G1WZF6; -.
DR OMA; SHANCVH; -.
DR OrthoDB; 21591at2759; -.
DR Proteomes; UP000008784; 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: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 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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008784};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1..76
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 149..226
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 232..350
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 455..503
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 523..573
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT REGION 33..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..133
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..695
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 795 AA; 87736 MW; D3AA47CBB8D1AC33 CRC64;
MQAPTPGPGT AGDDVISSVR KKIEKERMLI TAARSMRQST DNASVQQRLD SSIRESQSNI
NYLEGVIRDL QNKRMQNISA GIDNISLNST NAYSESPPTP PPKNQRDSSH EPDPVYNAAP
GGGPRPPFAQ PGPGLHKSRP TYSKLDLIKY DSPHLGPRIT LMLSQLEFKL SVEKQYKEGI
EKMAKLYQME GDRRSRADAD SKRVESNQKI HLLKQALKRY EDLHVDVEGD AQGDDDSINA
PNIRRPLTGR LHIKILAVKD VDHAATSRFG RAPETFVTVK VEDVIRAKTK PSRNERWVDE
SNEIDVDKAN EIEITVYDRS GDHHLPIGMM WIRLSDIVEE LRRKRIEQDI SATGWVSAEN
MEASSHGNYS TPLSTPQSTA SSGAPHTATP GNIPHDPEEP KPVFIDAWFV LEPVGQIQLQ
LSFVKYNKNK RPFDVGLNRK GAVRKQKEEV HETYGHKFVQ QQFYNIMRCA LCGDFLKYSV
GYQCEDCKYT CHKKCYPKVV TKCISKSNAE TDPEEEKLNH RIPHRFEPTT NFGANWCCHC
GYMLPVGKKN ARKCTECQLT CHAQCAHLVP DFCGMSMEVA NRILSEIGKT KRNGVSGPGH
MADRTLRTSQ VPLVSPRPAS VGSETLVDSI SPENRVTPIQ TQAGQSPTLS VSSQPAVFDP
SGHDGKGAYN AAAKAYGPYS PIPPPPPPPP PQSRPQSTSI AAAAAAAALG GRPNTTGRQE
PGYRPVSQVP YNPSTMPNST PVYQPAQATV NPLDQQRMSI GYIPPSPTPT PASQPVDPDP
NIYTTISSNW NRGAE
//
