ID A0A0D2XCM2_FUSOF Unreviewed; 691 AA.
AC A0A0D2XCM2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 18-JUN-2025, entry version 54.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN Name=28943886 {ECO:0000313|EnsemblFungi:FOXG_01645P0};
OS Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660025 {ECO:0000313|EnsemblFungi:FOXG_01645P0, ECO:0000313|Proteomes:UP000002489};
RN [1] {ECO:0000313|Proteomes:UP000002489}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|Proteomes:UP000002489};
RX PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT "A highly conserved effector in Fusarium oxysporum is required for full
RT virulence on Arabidopsis.";
RL Mol. Plant Microbe Interact. 25:180-190(2012).
RN [2] {ECO:0000313|EnsemblFungi:FOXG_01645P0}
RP IDENTIFICATION.
RC STRAIN=4287 / CBS 123668 / FGSC 9935 / NRRL 34936
RC {ECO:0000313|EnsemblFungi:FOXG_01645P0};
RG EnsemblFungi;
RL Submitted (MAR-2025) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A0D2XCM2; -.
DR STRING; 426428.A0A0D2XCM2; -.
DR EnsemblFungi; FOXG_01645T0; FOXG_01645P0; FOXG_01645.
DR VEuPathDB; FungiDB:FOXG_01645; -.
DR Proteomes; UP000002489; 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; 3.30.40.10: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; IPR054694; Parkin-like_IBR.
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; PF22605; IBR_2; 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 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002489};
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 REGION 309..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..332
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..521
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..580
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..625
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..646
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 691 AA; 75263 MW; 741BCA926E18773A CRC64;
MDYSDDPRLI ELGSIEAIYP EIRRPDAKDP FTFEVDLPVE PAAPVTVTFP AASAPAHPGL
TTLGQATENA QPEVDSLEVS YLPPLRLRVR LPEGYPADAP PDIVVSTIPQ WLSRETIKRL
EDDGPRLWDE IGRDMVAFTY IDHIQRAAED VFGTISPGGT LQVDPEHKLA VLDHDIKAKK
AAFEKETFDC GVCLDPKKGS KCHRMLDCRH IFCIQCLQDF YNDAINEGNL STVRCLSPNC
AKKRAASKDT KKHKVAISPS ELLQIGLSEE MVKRYVTLKY KTELESDKNT IYCPRQWCNG
AARSKRHKKP KGLEFAETSD AESGKEEEEE EKEKEQEQGG VSAKSGKRKN KETFSKADLL
SICEDCGFAF CGQCYQSWHG EFVRCAPRRD KGELSEEEKA SLEYLQLHTS PCPTCNAPAQ
KTHGCNHMIC SRCDTHFCYL CSSWLDPVNP YQHYNQLAGG KVTSCYMRLW ELEGGDGDDV
GLGFVGGRGP VADAPAALDD IELMPLPEVI ESDDSDGEDE ANVQGNNRPL GGQGQGIEIA
REGPLVIRLV DNQARDGRRA IPPAAPDAPQ QLAGRGHNGP PRGPAGRGRG ARGAGRGGGA
VARGRGGGGG GGGGGGGGGA RGGGAVANRQ RVNQRQPQLP QQAQGQDENN QDGLDPAQEA
WVRRFVQMAL NDEEDLVDGD SDEDDGNWII R
//
