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Database: UniProt
Entry: A0A8J2I5U6_9PLEO
LinkDB: A0A8J2I5U6_9PLEO
Original site: A0A8J2I5U6_9PLEO 
ID   A0A8J2I5U6_9PLEO        Unreviewed;       445 AA.
AC   A0A8J2I5U6;
DT   25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 1.
DT   02-APR-2025, entry version 15.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   ORFNames=ALTATR162_LOCUS3186 {ECO:0000313|EMBL:CAG5153458.1};
OS   Alternaria atra.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC   Alternaria sect. Ulocladioides.
OX   NCBI_TaxID=119953 {ECO:0000313|EMBL:CAG5153458.1, ECO:0000313|Proteomes:UP000676310};
RN   [1] {ECO:0000313|EMBL:CAG5153458.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CS162 {ECO:0000313|EMBL:CAG5153458.1};
RA   Stam R.;
RL   Submitted (MAY-2021) 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   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SIMILARITY: Belongs to the RBR family. RNF14 subfamily.
CC       {ECO:0000256|ARBA:ARBA00044508}.
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:CAG5153458.1}.
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DR   EMBL; CAJRGZ010000016; CAG5153458.1; -; Genomic_DNA.
DR   RefSeq; XP_043166727.1; XM_043310792.1.
DR   GeneID; 67014714; -.
DR   OrthoDB; 1431934at2759; -.
DR   Proteomes; UP000676310; 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; cd20354; Rcat_RBR_RNF14; 1.
DR   CDD; cd23134; RING-HC_ITT1-like; 1.
DR   CDD; cd23820; RWD_RNF14; 1.
DR   FunFam; 3.10.110.10:FF:000112; RBR-type E3 ubiquitin transferase; 1.
DR   FunFam; 3.30.40.10:FF:000416; RBR-type E3 ubiquitin transferase; 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_dom.
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; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   Pfam; PF01485; IBR; 1.
DR   Pfam; PF22191; IBR_1; 1.
DR   Pfam; PF05773; RWD; 1.
DR   SMART; SM00647; IBR; 1.
DR   SMART; SM00591; RWD; 1.
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   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000676310};
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          7..126
FT                   /note="RWD"
FT                   /evidence="ECO:0000259|PROSITE:PS50908"
FT   DOMAIN          157..423
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          161..195
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          280..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..292
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        297..309
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   445 AA;  50506 MW;  77FA7F6B1B1D8FAD CRC64;
     MEDERAEELS TLQSIYPELV INDSDPYSAT LELLVAPTKP LPITFEPQQD VERLPYLPPL
     RLEIILPAEY PEHIPPVVKL STSPSWLRQD LQATLTAEAK TLWDEYGGGS ILFAYISSIQ
     EQAENAFGLQ ELTLPSSMRK VLVDYSRRMK KELFDKDTFD CEVCLEPKKG SSCYRMARCS
     HVFCINCLQD YYNNCIKEGD VNNVKCMSTE CGSSGKKKDR LLSPKELLSI PIARDQVERY
     AKIKRKKKIE SDPNIVFCPR TWCQGAMRTD KYPKITDVTQ MDDSDSEADD EAPTQQRDTD
     VETGPEKRGI GVRGMDRLQV CEDCTLAFCV VCLASWHGDF VRCEPRDATQ LTEEDQASLN
     FISKNTTPCP YCSVPCQKSM GCNHMTCAQC KSHFCYLCSA WLNPDHPYAH FNDPKNKNCF
     MRLMDGAEGD MGNGAHEWTF KLYPS
//
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