ID A0A2J6SP18_9HELO Unreviewed; 724 AA.
AC A0A2J6SP18;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN ORFNames=K444DRAFT_543308 {ECO:0000313|EMBL:PMD52514.1};
OS Hyaloscypha bicolor E.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha; Hyaloscypha bicolor.
OX NCBI_TaxID=1095630 {ECO:0000313|EMBL:PMD52514.1, ECO:0000313|Proteomes:UP000235371};
RN [1] {ECO:0000313|EMBL:PMD52514.1, ECO:0000313|Proteomes:UP000235371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E {ECO:0000313|EMBL:PMD52514.1,
RC ECO:0000313|Proteomes:UP000235371};
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 (APR-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ613903; PMD52514.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6SP18; -.
DR STRING; 1095630.A0A2J6SP18; -.
DR InParanoid; A0A2J6SP18; -.
DR OrthoDB; 125113at2759; -.
DR Proteomes; UP000235371; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16536; RING-HC_RNF10; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR039739; MAG2/RNF10.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR12983; RING FINGER 10 FAMILY MEMBER; 1.
DR PANTHER; PTHR12983:SF9; RING FINGER PROTEIN 10; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000235371};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 185..235
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 724 AA; 81123 MW; 83E06A21F39694C7 CRC64;
MNSASSNTST AGGKSVNVSS SHSPLHQQQS QVVSPTFESR RSAGHSVPAH STPSPRNNQG
NRRQHKNSRK PRLADEDAMA ESGVMRNANS RRGQTSITHL MNFTLPPRPQ DHRNTLGRGT
RRGNIYGIGS GHHSSDKARY IHANYRFIVK PNGDYKAQAI NADQHLDWND VLQILASSVS
QESSCPICLS HPVAPRMAKC GHIFCLPCLI RYMHSTDDTN SIPEKKARWK KCPICWDTVY
ISDTRPVRWY TGQEGVPPRE GDDVVLRLVM REPGSTLALP RDGAEVPSKS EDIPWYFAAE
VMDYARIMKG SEEYMMEQYD SEIKEIQHQE NEDELMFGEE PEWTRKAVNA VNEAKERIKG
IGDPPAAAKQ PTERKPKRPP IQFTTTEEDV PEIYFVQHAS KSGLNLPNGF STHGTPEVIS
DQLTDDSTTS QPSPATEPKP IPPRPRSVHP RSNHNEAHHP DSPYYFYQAL LHYYLAPLDI
RILKSAFGNF ASFPSTLLPR VERVSTGHIM DDELRKRTKY LSHLPYGCEV GFLECNWTDV
VSPEVLKPFK DEIEKRRKRN RDKETREERD RLRAEKAEDD ARWATARRKR PSIPSESFSG
DDFHPLVPSS LEANNASPPW PDRQGSVFAS LASPSTSPSA PRTVWGTTLI TPPSPDVHPQ
QPEHDGDDGW LQSWEQELLA ENELIAQVAA TSLNGQSSAA TPGQGKKKKA KKITLMSTTA
RRAA
//
