ID A0A165PDY8_9APHY Unreviewed; 527 AA.
AC A0A165PDY8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=RING-CH-type domain-containing protein {ECO:0000259|PROSITE:PS51292};
GN ORFNames=DAEQUDRAFT_728363 {ECO:0000313|EMBL:KZT68088.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT68088.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT68088.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT68088.1,
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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; KV429070; KZT68088.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165PDY8; -.
DR STRING; 1314783.A0A165PDY8; -.
DR OrthoDB; 2730627at2759; -.
DR Proteomes; UP000076727; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46283:SF2; AT07234P-RELATED; 1.
DR PANTHER; PTHR46283; E3 UBIQUITIN-PROTEIN LIGASE MARCH5; 1.
DR SMART; SM00744; RINGv; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51292; ZF_RING_CH; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000076727};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 121..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 24..96
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 527 AA; 58456 MW; 6DC2AB842E37C530 CRC64;
MTGIAGTTMQ ATPTTQSQSR IPTVDDLRVK LCFICREEEQ YNSPEDPPRA WTHPCTCTLV
AHEACLLQWI KAAQDDPTRA LNALKCPQCG ASYQLESDNP HPKILRLLDN ANALLSIAGK
VFVIGGLATV VVSFGFGVYL VLTSYGAHAL RSMVGEEMYN ILLTDEPSNW PWHAFINLPM
IPVSLVLSRS AYFSSFPLLP LIISWPSSHP VTSAAARIGG TGWRLLSGPR DDLPYGPVFG
WPPSPMMASL LFPLIGRIYR EQYSKVMHAI LGKKPSERGP VRDIVWDFGG EGPVPFRARI
GLAVDPAERQ RRQQQRREQR EQQEQQEGQE GQEGQEQEHQ PNAQAPAQDA EGQDQQGNAQ
TIRITNASIG RAIGGALFMP TIASFMGSVL YRLAKYSPTL RTILAIRPPL VGRRRIQLLG
PWLDSQGFTR MSLLKKVGMS LHVALNLVCG GTRVWYESDP VWWRNSLGLG IFIVARDCIE
LLYLYLAKRD FETRRVKSRP FEGVDLSQLD LIHPPTSDAS NGLVPAA
//