ID A0A8H4NFF8_9HYPO Unreviewed; 545 AA.
AC A0A8H4NFF8;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-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 ORFNames=FACUT_10662 {ECO:0000313|EMBL:KAF4423030.1};
OS Fusarium acutatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=78861 {ECO:0000313|EMBL:KAF4423030.1, ECO:0000313|Proteomes:UP000536711};
RN [1] {ECO:0000313|EMBL:KAF4423030.1, ECO:0000313|Proteomes:UP000536711}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13308 {ECO:0000313|EMBL:KAF4423030.1,
RC ECO:0000313|Proteomes:UP000536711};
RA Kim H.-S., Busman M., Brown D.W., Divon H., Uhlig S., Proctor R.H.;
RT "Identification and distribution of gene clusters putatively required for
RT synthesis of sphingolipid metabolism inhibitors in phylogenetically diverse
RT species of the filamentous fungus Fusarium.";
RL Submitted (JAN-2020) 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:KAF4423030.1}.
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DR EMBL; JAADJF010000340; KAF4423030.1; -; Genomic_DNA.
DR OrthoDB; 10009520at2759; -.
DR Proteomes; UP000536711; 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:UP000536711};
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 161..375
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 165..213
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 545 AA; 62306 MW; ABA8E973E42512C1 CRC64;
MDSEEEYMSA LSSDDEIMQD ESGDEISAGE GVFPNILRDP PCSTTLDTND IDMTDFDDEE
FDEPDPDFGL IKDAEKKKKS AHVVSYKVYE PSDIQRQQDD MISEVNMILD MQKEDAAILL
RHFRWNKERL LEDYMDRPEK VLEAAGLSSN TSSPPKLEVI PGFACDICCE DEEGLESFAM
KCGHRYCVDC YRHYLTQKIR EEGEAARIQC PSDGCGRILD SASLDVLVTP ALADRYQELL
NRTYVEDKDN FKWCPAPDCP NALECGVKKK DLGKIVPTVE CRCGYRFCFG CPNPDHQPAP
CELVKKWLKK CADDSETANW ISANTKECPK CNSTIEKNGG CNHMTCRKCK YEFCWMCMGL
WSEHGTSWYN CNRYEEKSGS EARDAQAKSR TSLERYLHYY NRYANHEQSA KLDKDIAQKT
EKKMVQLQTA SGMSWIEVQY LNSASQALQT CRQTLKWTYA FAFYLARNNL TEIFEDNQKD
LEMAVENLSE MFEKPTAELS DPKLKVDIMD KTSYCNKRRV ILLEDTAENL AIGITTPTPP
SIPFI
//
