ID A0A0C2RZ18_AMAMK Unreviewed; 585 AA.
AC A0A0C2RZ18;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 18-JUN-2025, entry version 45.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=M378DRAFT_173495 {ECO:0000313|EMBL:KIL55610.1};
OS Amanita muscaria (strain Koide BX008).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pluteineae; Amanitaceae; Amanita.
OX NCBI_TaxID=946122 {ECO:0000313|EMBL:KIL55610.1, ECO:0000313|Proteomes:UP000054549};
RN [1] {ECO:0000313|EMBL:KIL55610.1, ECO:0000313|Proteomes:UP000054549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Koide BX008 {ECO:0000313|EMBL:KIL55610.1,
RC ECO:0000313|Proteomes:UP000054549};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (APR-2014) 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};
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DR EMBL; KN818494; KIL55610.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2RZ18; -.
DR FunCoup; A0A0C2RZ18; 475.
DR STRING; 946122.A0A0C2RZ18; -.
DR HOGENOM; CLU_009823_4_1_1; -.
DR InParanoid; A0A0C2RZ18; -.
DR OrthoDB; 10009520at2759; -.
DR Proteomes; UP000054549; Unassembled WGS sequence.
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; cd20356; Rcat_RBR_HHARI-like; 1.
DR CDD; cd16773; RING-HC_RBR_TRIAD1; 1.
DR FunFam; 1.20.120.1750:FF:000007; RBR-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045840; Ariadne.
DR InterPro; IPR048962; ARIH1-like_UBL.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF19422; Ariadne; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR Pfam; PF21235; UBA_ARI1; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054549};
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, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 152..410
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 156..200
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 585 AA; 66736 MW; BEBF7AAB5B897293 CRC64;
MFDATQEDDA SDHDIDMDAD ADDFKVAPKM KRKPYEIEYL SLSQGEVEKK MQEEVEYICN
ILGVEASTAS LLLRHLTWNR ERLIEQYMDN PSKVLVEAFV ILPSSQDYQS LGAGRSVSSR
RTTRSTATRI GTTYKPTHTT LKYTKYTPNP DEPFTCPICF DDSADIVTFS LDCGHTFCSK
CWNMFLASKI REEGEHAIRC MAEGCQLIAP DPFVRDILLS DGGAATPDPE PKKENAKIWA
RFQELLIRNF VDSNTDLKYC PYPGCTNTVS CQGAASRFSL TSVVPTVSCG ARGIPGSGSD
DVTTTKDGET SLCLAEKEHK FCFGCTIEDD HRPVVCAVAK MWVTKCSDDS ETANWIKSNT
KECPSCQSKI EKYGGCNHIT CQKCKHESCW VCMGPWSKHG TVWYSCNRYD DKSEVDARDA
RRASLERYLH YYNRWANHEQ SAKLSRDLYV KTEKKMEDMQ ITSSLTWIEV QFMKKAVEEV
EKCRMTLKWT YSMAYYLAKS NEKDLFEDNQ RDLEKAVEDL SELLETPVEP ENITSLRQRV
TDKTVYVQKR NEIVLEDSAN GFQEGRWRWN VTVEGFDEPD PSERV
//
