ID A0A8H5G1X9_9AGAR Unreviewed; 1153 AA.
AC A0A8H5G1X9;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 02-APR-2025, entry version 14.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS51873};
GN ORFNames=D9756_006828 {ECO:0000313|EMBL:KAF5356819.1};
OS Leucoagaricus leucothites.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX NCBI_TaxID=201217 {ECO:0000313|EMBL:KAF5356819.1, ECO:0000313|Proteomes:UP000559027};
RN [1] {ECO:0000313|EMBL:KAF5356819.1, ECO:0000313|Proteomes:UP000559027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 146.42 {ECO:0000313|EMBL:KAF5356819.1,
RC ECO:0000313|Proteomes:UP000559027};
RX PubMed=32382073; DOI=10.1038/s41396-020-0667-6;
RA Floudas D., Bentzer J., Ahren D., Johansson T., Persson P., Tunlid A.;
RT "Uncovering the hidden diversity of litter-decomposition mechanisms in
RT mushroom-forming fungi.";
RL ISME J. 14:2046-2059(2020).
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAF5356819.1}.
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DR EMBL; JAACJO010000006; KAF5356819.1; -; Genomic_DNA.
DR OrthoDB; 10009520at2759; -.
DR Proteomes; UP000559027; Unassembled WGS sequence.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR CDD; cd20339; BRcat_RBR_RNF216; 1.
DR CDD; cd20353; Rcat_RBR_RNF216; 1.
DR CDD; cd16630; RING-HC_RBR_RNF216; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR InterPro; IPR047545; BRcat_RBR_RNF216.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR051628; LUBAC_E3_Ligases.
DR InterPro; IPR047546; Rcat_RBR_RNF216.
DR InterPro; IPR047544; RING-HC_RBR_RNF216.
DR InterPro; IPR044066; TRIAD_supradom.
DR PANTHER; PTHR22770:SF47; E3 UBIQUITIN-PROTEIN LIGASE RNF216; 1.
DR PANTHER; PTHR22770; UBIQUITIN CONJUGATING ENZYME 7 INTERACTING PROTEIN-RELATED; 1.
DR Pfam; PF01485; IBR; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR PROSITE; PS51873; TRIAD; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000559027};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 507..721
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 929..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 986..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1125..1153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1022..1080
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 23..35
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..261
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..505
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..840
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..903
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1018
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1153 AA; 128114 MW; 2144D60A10136171 CRC64;
MHDADIIELS SGASSPPPVP IRTPKRGMAR NKGKGKMKEV DVIELTDDSD DSDFEVEILR
SPPPKRGPRV TRTGFPGSSQ RKLKGKQPLV VDDVSDDDIV AAPEPRFLAG PSRVNGDLRP
RELKEQLSLN EENVLVASTS SVSGRKDQPR AYSLEESDIG AEVTQVTDMS WTVDRAGTHD
FDAPDLAPGG SNMTNGAKNM DVDPQLPPQS PSPTVSSTRA ASGPSTVPIP SPSNTTSAPA
NNAVSLNTIP PPVPVPPPPL LESPEEMASR YVAQVLEIVP DVDPEHCASL VEDHKHLGEG
AVERILHILL EDPGYPRIKK GNGLDKGKRK ADGPGEDRER PNKKQKGSLK GKAADEDDGL
WLNVERPFIG GIDYHDLALN TLQQDYPFIP KPYLRDRLSS HKGFYAPTFF FLRKLNHQLQ
NGEVARDDCP YQPRKTAYRL PRGGKQRAMV DGEFERELAW VKKTVDIEEG RAIADQNSGG
GDHDEKDSDT ESEEANEAES DGEDEANGIE CGCCFSKYRF EKMIQCPDAH LFCLSCLRSY
ASTLLGSHNP NITCMSQAVC TATFPASQLV RVLPRKTYAL YERLVQAKEI DAAGLEGLEE
CPFCEWKCVM EVGFEGEKLF RCENDIGGCG VVSCRKCKKL DHLPKSCEEV EQDKKLDARH
LVEEAMTKAL MRNCPKCQKA FIKESGCNKM TCPNCHALSC YVCRQIITGY EHFNQSRNPS
AASSSSKPKK CVLWDKDLDA FHANEVKLAA DQAMAEARML HPEVSSSDLK VDLPSTTKAK
NLQGLPLPGL VPLMNMNAMG PGGIRRVANL RRGRRSPPPI VQRRAARRND GHDGVAREVR
FLPVVRPPPP QMPHVHVHVH QHQHEQRRPA QPQPPQQNIP QLRHRPHPVL QHPPQQPQQP
PLPGQGVEGP AAQRRYHEVV AQAMMGQYHP HGAPQHIPQQ PQRPPLPGQG VEGPAAQRQY
HEAIAEAMMG QCRPIDRGVE VGGRILRARP GRPGDAGDNR PPQAMGMGMA NNGAGVPAPN
ALDRLRELNE QQVKQLLQER LQRHQEQQEQ LRQQQILLRQ RQLEQQRQQQ EVQRRLLVEQ
HRVREQQRQR ERQRAWEAHE LGLALPQEWL VPPALGVRQV LDRVEIGGRG PPDPDPEYQA
QAVGQKRKRG HDD
//
