ID A0A8H6W0A6_9AGAR Unreviewed; 959 AA.
AC A0A8H6W0A6;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 02-APR-2025, entry version 12.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=MIND_01007100 {ECO:0000313|EMBL:KAF7294699.1};
OS Mycena indigotica.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Mycenaceae; Mycena.
OX NCBI_TaxID=2126181 {ECO:0000313|EMBL:KAF7294699.1, ECO:0000313|Proteomes:UP000636479};
RN [1] {ECO:0000313|EMBL:KAF7294699.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=171206Taipei {ECO:0000313|EMBL:KAF7294699.1};
RA Tsai I.J.;
RT "Mycena genomes resolve the evolution of fungal bioluminescence.";
RL Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
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:KAF7294699.1}.
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DR EMBL; JACAZF010000009; KAF7294699.1; -; Genomic_DNA.
DR RefSeq; XP_037216062.1; XM_037366668.1.
DR GeneID; 59349184; -.
DR OrthoDB; 1431934at2759; -.
DR Proteomes; UP000636479; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd20335; BRcat_RBR; 1.
DR CDD; cd16449; RING-HC; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.1370.210; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR041367; Znf-CCCH_4.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR Pfam; PF15227; zf-C3HC4_4; 1.
DR Pfam; PF18044; zf-CCCH_4; 1.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00356; ZnF_C3H1; 2.
DR SUPFAM; SSF90229; CCCH zinc finger; 1.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50103; ZF_C3H1; 2.
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, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000636479};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KAF7294699.1};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 1..25
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 33..60
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 610..820
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 614..653
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT ZN_FING 1..25
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 33..60
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 67..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 889..944
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 959 AA; 108054 MW; 2E35FD9F0EF106D0 CRC64;
MAPCKLFLRG HCRFGDRCKY SHNEETNTQP RLKRGERPCF AWRDGDCPKG DKCFFAHDPQ
IREERLRQEQ ARQEADRRAE QARQRLEAER EAAQRAREVR QQIQRRETAR QEAAHTIQRI
VLGSSLVTYA AGIAIHDIIC GSESCRIRIR QLPLDARSDE ILALFTQQGI DRKRLFIVGQ
KPVDGHLEAT LVTTAEEGGA VAIGLEGIDF RQEHLQFDVS ETANGMGISA TKDSDTLTVA
CWAPSNAVIA TFPSQEIARA KVHSLNRQVC GGRRVKVEMN QLTPGYRGSM FGDVQCSIKI
TGLPLVLSHE TLVQFVGSDQ LRYLKPISYD PVHGFGLLQQ HIRTVAARDL ISMDATQLEG
DVDGNIIVKF RFSSWEAAKR VDEELSGKKF TYLGNRILRT RLPTPHQYIL SITTQQYNAQ
RHQWDALAGS DVSSKQAASV VIQNGVRVRI RVVGGDKQAV GSLKVRVESL AGGEALPREL
WHRSLRWGSG TQFLNSVFRA TGAYARADWK ACVVKVFGET AARERAREMV KAEIDRLNAS
ECSILLKQKS IRFFVDRGLA ALKEALGEDN ATLVIVGGAK IVVRGGDNAR QIVDRLIAES
LEETTTRNVD GVLCPICYDE ISHPVSLGCD HTYCMNCLSH YISSAADTFP LTCLANDATC
NTPIPLPTIE RFLSPALLQQ LFETAYIRYI EQHPNEFKYC KTPDCTQVYR RQTTPATVTC
PSCFLKVCRA CDEEGHEGMS CDEWKLQGDP GEQERRNQEW AAENGVKRCP VCSVWIEKTE
GCNHMTCKCG AHLCWLCVRQ FPEGEIYNHL NSAHGGAFDV PAALRPQPQL AAIPRPVENQ
REMVEQRARE AARAANRLPQ NNPGPFARAA PRVQYPYGYG PVDPAVAARQ HARLREDQAE
REAAQLEQEE RQRRIAMQER IAIQERWHQQ IEEQRRRRQQ AMAEEAARRE QNRNWCIVM
//
