ID A0A165RIU0_9APHY Unreviewed; 396 AA.
AC A0A165RIU0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN ORFNames=DAEQUDRAFT_167136 {ECO:0000313|EMBL:KZT70807.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT70807.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT70807.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT70807.1,
RC ECO:0000313|Proteomes:UP000076727};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV429049; KZT70807.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165RIU0; -.
DR STRING; 1314783.A0A165RIU0; -.
DR OrthoDB; 4593171at2759; -.
DR Proteomes; UP000076727; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
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; PTHR35711:SF1; ECTODERMAL, ISOFORM F; 1.
DR PANTHER; PTHR35711; EXPRESSED PROTEIN; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000076727};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 83..158
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 183..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 11..80
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 213..250
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..396
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 396 AA; 45973 MW; 572E95188DFCB04A CRC64;
MPLTALDSTE FIRTKREIES LRKQLQQSKK TIHKQSKVID ELKMEAANSA KSQKEQAKDM
DKLKAQSKKS EELVANLEMN LSCQICMEIL ARPHGSVKSR LVLFPANSVD SLSPCGHVLC
QGCLQNWFRS APPGDDEMFD EDEPDALIYR RKTCPCCRTV VTSRPIPLFV VKSLTSVLEK
AKAHPCAPRL PTPPPDDDPW EGIFSDPESQ VDFRLMDEDE DEDENDSEDE DEDDEDDDYD
AEYDDWSYDD EDEDYHGSYV RQRWEPPTVH ATLEDYPFHD VDEHDLRMLR RGATLQMIDT
FEMSYTHEDG LCARVDGDNV VYLGWNIYLH PQDESGEAFI DWIMSDMHRR PRRWEADEER
NGPWTAWRLV PERDEQDYET TDSETWAADL AEDEDF
//