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Database: UniProt
Entry: A0A0D2ACB4_EXOME
LinkDB: A0A0D2ACB4_EXOME
Original site: A0A0D2ACB4_EXOME 
ID   A0A0D2ACB4_EXOME        Unreviewed;       587 AA.
AC   A0A0D2ACB4;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   18-JUN-2025, entry version 38.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   ORFNames=PV10_00412 {ECO:0000313|EMBL:KIV96563.1};
OS   Exophiala mesophila (Black yeast-like fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=212818 {ECO:0000313|EMBL:KIV96563.1, ECO:0000313|Proteomes:UP000054302};
RN   [1] {ECO:0000313|EMBL:KIV96563.1, ECO:0000313|Proteomes:UP000054302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 40295 {ECO:0000313|EMBL:KIV96563.1,
RC   ECO:0000313|Proteomes:UP000054302};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala mesophila CBS40295.";
RL   Submitted (JAN-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; KN847520; KIV96563.1; -; Genomic_DNA.
DR   RefSeq; XP_016228137.1; XM_016364488.1.
DR   AlphaFoldDB; A0A0D2ACB4; -.
DR   STRING; 212818.A0A0D2ACB4; -.
DR   GeneID; 27318257; -.
DR   VEuPathDB; FungiDB:PV10_00412; -.
DR   OrthoDB; 10254945at2759; -.
DR   Proteomes; UP000054302; 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; 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; 2.
DR   SUPFAM; SSF57850; RING/U-box; 2.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054302};
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          260..460
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   REGION          1..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          557..587
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..29
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..86
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        112..124
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..146
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..237
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        567..587
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   587 AA;  67286 MW;  46846EEA14D3F144 CRC64;
     MAEDKVRKRK SSHRRPAELK NSRSHDTLNH ENPPSGTTAT ADRSPDIHAL RQARLDYQSK
     TPEERKRGMK YEYVKTTREL ISEDTGKTVN TKSSRHRRRP KDDLHPITSS RPTEHDRPVK
     RRDDSDDEYG YEYVYEPARE RHDHSKSSPH ATSSRRKHRR TSSLDSTKPP NRRHIPERRR
     TAPLEPMALR NVTDEDDSQA SDAPPLLREQ HTKPTVKRRA TTPATTRTRA KPSAAPTITR
     RKTSNILGGF FGSSAPAPPR MVSCLTCGDD EIPLHRSAKL PCDHRMCHTC LKRVFTMSVS
     DAAHMPPRCC TEEAIDLKHV DKLFDNDFKI LWNRKFNEYK TRNRIYCPSR RCGAWIKPKY
     IIRDHGRKVG RCKHCGTRVC GTCSQKMHTS RECPKDPETA RFAEVAKKEG WQKCYNCSAT
     VELKEGCNHM TCRCNAEFCM VCGLKWKSCD CPWFSYEAVD AGLEDPLRLQ QEVDRRRGQV
     VRDEEIARAM QRLAMFDNIR AERVDLMNGN FMQQAREALT ANYAHAGRLL NQIMMQRDVN
     SAATHGAGPD DVIAIPDSAA EDDVGHRPAR RLTARARRRR TSRGADE
//
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