ID A0A132BDN3_MOLSC Unreviewed; 496 AA.
AC A0A132BDN3;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 02-APR-2025, entry version 42.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=LY89DRAFT_689742 {ECO:0000313|EMBL:KUJ10530.1};
OS Mollisia scopiformis (Conifer needle endophyte fungus) (Phialocephala
OS scopiformis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Mollisiaceae; Mollisia.
OX NCBI_TaxID=149040 {ECO:0000313|EMBL:KUJ10530.1, ECO:0000313|Proteomes:UP000070700};
RN [1] {ECO:0000313|EMBL:KUJ10530.1, ECO:0000313|Proteomes:UP000070700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 120377 {ECO:0000313|EMBL:KUJ10530.1,
RC ECO:0000313|Proteomes:UP000070700};
RG DOE Joint Genome Institute;
RA Walker A.K., Frasz S.L., Seifert K.A., Miller J.D., Mondo S.J., Labutti K.,
RA Lipzen A., Dockter R., Kennedy M., Grigoriev I.V., Spatafora J.W.;
RT "Full genome of DAOMC 229536 Phialocephala scopiformis, a fungal endophyte
RT of spruce producing the potent anti-insectan compound rugulosin.";
RL Submitted (OCT-2015) 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; KQ947429; KUJ10530.1; -; Genomic_DNA.
DR RefSeq; XP_018064885.1; XM_018215963.1.
DR AlphaFoldDB; A0A132BDN3; -.
DR STRING; 149040.A0A132BDN3; -.
DR GeneID; 28825689; -.
DR KEGG; psco:LY89DRAFT_689742; -.
DR InParanoid; A0A132BDN3; -.
DR OrthoDB; 1431934at2759; -.
DR Proteomes; UP000070700; 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; cd20335; BRcat_RBR; 1.
DR CDD; cd22584; Rcat_RBR_unk; 1.
DR Gene3D; 1.20.120.1750; -; 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; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 3.
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:UP000070700};
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 191..413
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 195..251
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 115..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..144
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..169
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 496 AA; 55758 MW; 484BD91BD4BDD904 CRC64;
MASNDGQRLL VLGLSYRQHH TLHMQQVLRA YDRLPANPMD RVVLYTALFD LAKDLDEDET
RNIENWLKNG GAFPAPTPKV PEVGPGGAGT TGATDEVDHD DWPEYNPVDF ETAQEVSNDA
EMTEDEDEDE GEQEEVAEEL YDIDDPTRQI DDPGEEFSDP SEDDIDDLDA NFGPRLRRHA
ISGLPKKLSA DAIECHICAE SYELADFPPS TQITSSCDHK YNERTCVYCL QQTIAGAVSE
GQLNRIVCPF CPAPLSREEV KRYATREIFS RYDYLVMRAN PDLVMCLGLD CGSGQVHTGE
DPMMICQACS FKTCAVHKLP WHEGQTCEEF DMDDSQIERL EEAEATAKLL ATEQAQICPN
CHQGVSRIDG CDHMTCRCGM EWCYQCGVTF ENIKRLGESA HGASCMYNPR RVQMRSGQKQ
AVQGSLTALV HGGPVSDTLE KARGARNERI RTEMRPKVAE AAERRQREME QQKKEERGGA
PEKKRKLNLQ PAWEEK
//