ID A0A8J5P2F6_FUSOX Unreviewed; 529 AA.
AC A0A8J5P2F6;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 18-JUN-2025, entry version 14.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN Name=dbl4 {ECO:0000313|EMBL:KAG7419341.1};
GN ORFNames=Forpe1208_v002623 {ECO:0000313|EMBL:KAG7419341.1};
OS Fusarium oxysporum f. sp. rapae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=485398 {ECO:0000313|EMBL:KAG7419341.1, ECO:0000313|Proteomes:UP000694050};
RN [1] {ECO:0000313|EMBL:KAG7419341.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tf1208 {ECO:0000313|EMBL:KAG7419341.1};
RA Asai S.;
RT "First draft genome resource for Brassicaceae pathogens Fusarium oxysporum
RT f. sp. raphani and Fusarium oxysporum f. sp. rapae.";
RL Submitted (APR-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 -!- 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:KAG7419341.1}.
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DR EMBL; JAELUQ010000002; KAG7419341.1; -; Genomic_DNA.
DR Proteomes; UP000694050; 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; cd20346; BRcat_RBR_ANKIB1; 1.
DR CDD; cd20356; Rcat_RBR_HHARI-like; 1.
DR CDD; cd16625; RING-HC_RBR_HEL2-like; 1.
DR FunFam; 1.20.120.1750:FF:000007; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 3.30.40.10:FF:000019; RBR-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045840; Ariadne.
DR InterPro; IPR048962; ARIH1-like_UBL.
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 InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF19422; Ariadne; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR Pfam; PF21235; UBA_ARI1; 1.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00184; RING; 2.
DR SUPFAM; SSF57850; RING/U-box; 3.
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:UP000694050};
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 137..351
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 141..189
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..42
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 529 AA; 60695 MW; 3722B23ACC938AD9 CRC64;
MDSEEEYMSA LSSDDEIMQD ESGDEISAGE DFDDEEFDEP DPDFGLIKDA EKKKKSAHVV
SYKVYEPSDI QRQQDDMISE VNMILDMQKE DAAILLRHFR WNKERLLEDY MDRPEKVLEA
AGLSSNTSSP PKLEVIPGFT CDICCEDEEG LESFAMKCGH RYCVDCYRHY LTQKIREEGE
AARIQCPSDG CGRILDSASL DVLVTPALAD RYQELLNRTY VEDKDNFKWC PAPDCPNALE
CGVKKKDLGK IVPTVECRCG YRFCFGCPNP DHQPAPCELV KKWLKKCADD SETANWISAN
TKECPKCNST IEKNGGCNHM TCRKCKYEFC WMCMGLWSEH GTSWYNCNRY EEKSGSEARD
AQAKSRTSLE RYLHYYNRYA NHEQSAKLDK DIAQKTEKKM VQLQTASGMS WIEVQYLNSA
SQALQTCRQT LKWTYAFAFY LARNNLTEIF EDNQKDLEMA VENLSEMFEK PTAELSDPKL
KVDIMDKTSY CNKRRVILLE DTAENLAIGK WIFNSDLLAA TTSAPVNRR
//
