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Database: UniProt
Entry: A0A165PDY8_9APHY
LinkDB: A0A165PDY8_9APHY
Original site: A0A165PDY8_9APHY 
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}.
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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
//
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