ID A0A165J515_XYLHT Unreviewed; 1108 AA.
AC A0A165J515;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=DDENN domain-containing protein {ECO:0000313|EMBL:KZF25739.1};
GN ORFNames=L228DRAFT_207426 {ECO:0000313|EMBL:KZF25739.1};
OS Xylona heveae (strain CBS 132557 / TC161).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Xylonomycetes;
OC Xylonales; Xylonaceae; Xylona.
OX NCBI_TaxID=1328760 {ECO:0000313|EMBL:KZF25739.1, ECO:0000313|Proteomes:UP000076632};
RN [1] {ECO:0000313|EMBL:KZF25739.1, ECO:0000313|Proteomes:UP000076632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC161 {ECO:0000313|EMBL:KZF25739.1,
RC ECO:0000313|Proteomes:UP000076632};
RX PubMed=26693682; DOI=10.1016/j.funbio.2015.10.002;
RA Gazis R., Kuo A., Riley R., LaButti K., Lipzen A., Lin J., Amirebrahimi M.,
RA Hesse C.N., Spatafora J.W., Henrissat B., Hainaut M., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The genome of Xylona heveae provides a window into fungal endophytism.";
RL Fungal Biol. 120:26-42(2016).
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DR EMBL; KV407455; KZF25739.1; -; Genomic_DNA.
DR RefSeq; XP_018191294.1; XM_018329718.1.
DR AlphaFoldDB; A0A165J515; -.
DR GeneID; 28894855; -.
DR InParanoid; A0A165J515; -.
DR OMA; RCEEWRK; -.
DR OrthoDB; 1331806at2759; -.
DR Proteomes; UP000076632; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00029; C1; 1.
DR Gene3D; 3.30.450.200; -; 1.
DR Gene3D; 3.40.50.11500; -; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR001194; cDENN_dom.
DR InterPro; IPR005112; dDENN_dom.
DR InterPro; IPR043153; DENN_C.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR037516; Tripartite_DENN.
DR InterPro; IPR005113; uDENN_dom.
DR PANTHER; PTHR12296:SF21; DENN DOMAIN-CONTAINING PROTEIN 3; 1.
DR PANTHER; PTHR12296; DENN DOMAIN-CONTAINING PROTEIN 4; 1.
DR Pfam; PF03455; dDENN; 1.
DR Pfam; PF02141; DENN; 1.
DR Pfam; PF03456; uDENN; 1.
DR SMART; SM00801; dDENN; 1.
DR SMART; SM00799; DENN; 1.
DR SMART; SM00800; uDENN; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR PROSITE; PS50211; DENN; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000076632};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 212..971
FT /note="UDENN"
FT /evidence="ECO:0000259|PROSITE:PS50211"
FT DOMAIN 839..886
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT REGION 33..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1052..1108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 297..324
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 33..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..743
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..806
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1108 AA; 122276 MW; 30F0E850A3CDB6EC CRC64;
MAPVASATQP SAPLADYFWI AGIDSDSLLQ VRANSGDRAS SNGAPAPPVA STIAEDSTLE
EEEPPSPRGR ANASSESRRS IQSTTSPDPK LTGSNRSSAT IKAPQLGGSG LSDADFDVAL
RKFASERESF LDDLSFSAGT VTTPRSKPRA KPPRIVGEDA STPKSGAESI KRRISFRDMN
SMKRAPSIAR QASIRTSKRL SNYNSVIPTP QPLNADSNMH PLKRKFEPVL LDRYPSHSVA
DEAKRRGPFP DYIPMFAFPN DINIVSSDDR PRSTWHGFAM TSGDNSRIYG ICVTIWLPLK
QEAAEELERQ CEEWRRDNMS DEERELASSL GERLAAERAK LSRLLTQLPT VPSGSAARES
LEEEIGQVEE KITLMTDLLR PVRHGAASKI DGLTDGDSGF WIPRAYGVLG RDANLTSFWK
EWLRAIVVPM TQGAVLRVPP TSPKAGMWQP LERYVVNLCT EALSPMTSKT QVEIAVRELR
LFARKEAVNE LPGSRNTDLY ALFRALSIQN IVILFEAALS ESRIIFLSSH TAMLHLACKA
LTSLLYPLVW AGVYIPILPA RLLQALEAPC PYIVGIERRY DNIELPDDDF LMVDLDHDQI
EATALPPPLP RQQRRKLVSL LQVAAPHHYR YGVPTGPPAY AVETYPFDAV STENSSIYTQ
NPAPSNLNKY VSQSSTSFGA PESQSSVRPP IFNAFLHARN NDYGRPSTST TIKGSAPPSP
KLSPTSSQFA QPPATAISRT DSGYGIQATL REKRSGHFDV ASRRSSSFGL DRKPTLRRPS
MPFGGHAVSH STSTLNDNQS TSHYAPSTYA PSTLAASTVM PNILMQPVRN TQTQTWVEGH
CLNWKPHDER SICSVCDERA EEGIYRCMGC NMFAHGRCSQ QICIVCPGAF YPDQVRAAFV
RCFASLFYTY RKSLHPATGE QRKNGQIYHF NMDGYLKSMP RENAEYLGML LQTQGFNEFI
HERECKRPND PSIVLFDEII LSKKNRGRSS LFSKSVTNFL CDTTDHIWRS AAATPPSSRF
PGDYRQVVSR IPAKLDPTLM KEPRVIQGVP RINNTKARRK PIPSMLGPSG DEDPVNLSHL
STHSLQNSLS PAAAATNVSK KSDSGRLG
//
