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Database: UniProt
Entry: A0A132BDN3_MOLSC
LinkDB: A0A132BDN3_MOLSC
Original site: A0A132BDN3_MOLSC 
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
//
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