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Database: UniProt
Entry: A0A2J6QLT6_9HELO
LinkDB: A0A2J6QLT6_9HELO
Original site: A0A2J6QLT6_9HELO 
ID   A0A2J6QLT6_9HELO        Unreviewed;      1127 AA.
AC   A0A2J6QLT6;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=DENN-domain-containing protein {ECO:0000313|EMBL:PMD27210.1};
GN   ORFNames=NA56DRAFT_227898 {ECO:0000313|EMBL:PMD27210.1};
OS   Hyaloscypha hepaticicola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Hyaloscyphaceae; Hyaloscypha.
OX   NCBI_TaxID=2082293 {ECO:0000313|EMBL:PMD27210.1, ECO:0000313|Proteomes:UP000235672};
RN   [1] {ECO:0000313|EMBL:PMD27210.1, ECO:0000313|Proteomes:UP000235672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 7357 {ECO:0000313|EMBL:PMD27210.1,
RC   ECO:0000313|Proteomes:UP000235672};
RG   DOE Joint Genome Institute;
RA   Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA   Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA   Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA   Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA   Martin F., Perotto S.;
RT   "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KZ613466; PMD27210.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J6QLT6; -.
DR   OrthoDB; 1331806at2759; -.
DR   Proteomes; UP000235672; 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; 3.30.60.20; -; 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; SM00109; C1; 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:UP000235672};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          252..1015
FT                   /note="UDENN"
FT                   /evidence="ECO:0000259|PROSITE:PS50211"
FT   DOMAIN          881..929
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   REGION          33..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          97..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          147..183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          738..781
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          794..819
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          391..418
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        97..114
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        750..781
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1127 AA;  124479 MW;  03EB2EEE3A890B40 CRC64;
     MASTSAPLAD YFWIAGIDSL SYSDPVSWPL NQKIVNGPPS PQVDATIDEG SEGETPVSAP
     SGTPRATAWH SRNNSWNRLS KSSNEVRTSI QGLDELDQTQ SNRSSVTIKA PTTNGNGGGL
     LGDFDFDKAL MKFANERENF LDDLSFSAGA PVQKPPPMTT PRTERFRTEE GNGNGAAGQV
     KRNPLRSVGG SIRRRISFKD MNSMKRQPSM IQRTSKLGFL HWNYKLAMMH SPSVRTSKRL
     SNYNSVIPQP EPLNADPEMH PLKRRFEPVL LDRYPPKSAT EELARRGKFP DYVPMFAFPN
     DINIVSADER PRSTWHGFAM TSEDNSKIYG ITVIVWMPLN QDAAANVERR CEQWRQAHMT
     HEERELAASL GERLASERAH LSQLLARLPS AASGSAAREA LEEQISAVEE KIGLMTDLLR
     PVRHGAAAKI DGLTDGETGL WTPRAYGILG RDPSLTSFWK EWLRAVVVPM TDGGVLRVPP
     SSPKVGRWQP LERYVVNLCT EALSPISSKT QVELAVRELR LFARKEAANE LPESRNTDLY
     ALFRALSIPN IVSLFEFALS ESRIILLSSH TAMLHLASKA LASLLYPLKW ASIFIPVLPA
     RLISALEAPC PYIVGIERRY DRIELPEDDY VLVDLDQDII EASGAPTSLP RQQRRKLIAL
     LQLAAPHHNK CGVPVGPPPY AIETFPYDAF SSENEAIFTQ NAPQGSLAKY VSQNSTTFGE
     PDPAAAKRPS VFNAFLQSKY DHSRVERPST SRSNRTSPPG SLSPVSGNFP ALPTTPISRN
     DSGFALTATL REKRSGHFDG SSRRSGSFGL ERQPTFRRPS MPFVNGHSAS LSTSALSIDS
     KSTYGYAPSA YAASTIAAST IMPNMLMQPV RNTDTTVWVE GHYFVLQSHD NSSVCSICDE
     KPDGDGTYKC TSCNTVSHGR CLGQVSLVCP SAFHSDRVRT AFVRCFASLF FTYRKYLNRP
     TREQKNSGQI YSFDMDGFMR SLPHEQQEYV AMLKQTQAFN EFIHERETTS SDNPSIQLFD
     SIILAKKSRG RTSFFSKSSN SASFLEDRSD HLWVSAAVPT PSAKFPGDYR TVVSRIPAQL
     DVSLMKEPRT IGGVPRVDMP GKRVGRKAVP SLLGGGGARG VPAIRLE
//
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