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Database: UniProt
Entry: A0A0L1JFI2_ASPNO
LinkDB: A0A0L1JFI2_ASPNO
Original site: A0A0L1JFI2_ASPNO 
ID   A0A0L1JFI2_ASPNO        Unreviewed;       618 AA.
AC   A0A0L1JFI2;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   ORFNames=ANOM_001375 {ECO:0000313|EMBL:KNG90138.1};
OS   Aspergillus nomiae NRRL 13137.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG90138.1, ECO:0000313|Proteomes:UP000037505};
RN   [1] {ECO:0000313|EMBL:KNG90138.1, ECO:0000313|Proteomes:UP000037505}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG90138.1,
RC   ECO:0000313|Proteomes:UP000037505};
RA   Moore M.G., Shannon B.M., Brian M.M.;
RT   "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL   Submitted (JUN-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};
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:KNG90138.1}.
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DR   EMBL; JNOM01000018; KNG90138.1; -; Genomic_DNA.
DR   RefSeq; XP_015411061.1; XM_015546632.1.
DR   AlphaFoldDB; A0A0L1JFI2; -.
DR   STRING; 1509407.A0A0L1JFI2; -.
DR   GeneID; 26803179; -.
DR   OrthoDB; 3084186at2759; -.
DR   Proteomes; UP000037505; Unassembled WGS sequence.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR   CDD; cd20354; Rcat_RBR_RNF14; 1.
DR   CDD; cd23134; RING-HC_ITT1-like; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 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; IPR047548; Rcat_RBR_RNF14.
DR   InterPro; IPR006575; RWD-domain.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR11685:SF371; E3 UBIQUITIN-PROTEIN LIGASE RNF14; 1.
DR   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   Pfam; PF01485; IBR; 1.
DR   Pfam; PF05773; RWD; 1.
DR   SMART; SM00647; IBR; 2.
DR   SUPFAM; SSF57850; RING/U-box; 2.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS50908; RWD; 1.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037505};
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          13..170
FT                   /note="RWD"
FT                   /evidence="ECO:0000259|PROSITE:PS50908"
FT   DOMAIN          206..477
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          210..244
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          262..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          504..567
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        262..284
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   618 AA;  69464 MW;  29C8CB1370E28BF4 CRC64;
     MTDTELLDDE RSVELSSIAA IYPEIKLDPS FSFRATLDIP VNPSPPLRIC FEQYSETELP
     TVLTPPTSLD VSEISLGFAT KTVDGGTTAS SDEDVHVLSH LPPLCLEIEL PGGYPSEQSP
     IIKLSTDPAW LPSSIISKLL DDGKRLWEEC GRDLVVYTYI DHLQQLAEAA FGIDDIPDGE
     VRLPRELKIA LLDHNNKAER EAFEQETFEC GVCLEPKKGV NCHRLLLCSH VFCVPCLQDF
     YNTCITEGDV ESVRCLAPDC GKEDKSVRSQ EGQPKRRKKN DRSLSPSELL QIPLEQETVQ
     RYVFLKRKKK LEADKSTIYC PRQWCQGAAR SKRHPKPIDP MSDDLDPSDD EDVGLVFDPN
     GDEAQLPPMA DRVAVCEDCN YAFCCVCKKG WHGELVRCFP RREAELSAEE KATEEYLRLY
     TSACPTCDAP CQKRMGCNHM ICFKCDTHFC YLCSSWLSED NPYRHFNDGN SSCYNKLWDL
     EGGDGINPDG AEALHQIPNE LIDFDSSDDE DQPAWDFDDD DNHFRRQGHP PPPAPAPPRV
     NQRAGGPGRR EDGRNLNGLD AAGRAAAAER QAQARAIAEV RGRPDPEAIR RPGLQRFLEL
     VQNDREDEWD SDELDDDF
//
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