ID A0A8H5K3K3_9HYPO Unreviewed; 582 AA.
AC A0A8H5K3K3;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 02-APR-2025, entry version 13.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=FNAPI_1232 {ECO:0000313|EMBL:KAF5566233.1};
OS Fusarium napiforme.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=42672 {ECO:0000313|EMBL:KAF5566233.1, ECO:0000313|Proteomes:UP000574317};
RN [1] {ECO:0000313|EMBL:KAF5566233.1, ECO:0000313|Proteomes:UP000574317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 25196 {ECO:0000313|EMBL:KAF5566233.1,
RC ECO:0000313|Proteomes:UP000574317};
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 (MAY-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:KAF5566233.1}.
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DR EMBL; JAAOAO010000045; KAF5566233.1; -; Genomic_DNA.
DR Proteomes; UP000574317; 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; cd20335; BRcat_RBR; 1.
DR Gene3D; 1.20.120.1750; -; 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; IPR044066; TRIAD_supradom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR PROSITE; PS51873; TRIAD; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000574317};
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 DOMAIN 310..555
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
SQ SEQUENCE 582 AA; 65949 MW; 2C1F8EBEAA10E2ED CRC64;
MSIDIQTCLN EKKAMADELD ELRAQSVGHP LGLLETTPRG IWISKLLSRS QSIQGNQNAL
QGYGLCNSEI ENAESDVKSP LDSILSADEV RGLFNSFEEC FDEQDLDSLS LIHCSVCHKM
RFEQANPNSS YPFVDEFSKC LRPPTTCTSS VCLVCYLGSV VRSIQGLPQT WWDTSGTTVL
LPCPCGACSG NIAFENRGAL KRLLGLANVK DAVDVLRIYD TAQHLVSVLD TLDPQPTLKA
RQVAKHLHQH LISNGIMKPL FGLQTSELHT LESVLPHDVN SQLVQIWELN GTDEVFRVPI
FTQLLRREQS PVECSICTEP IYDLISEALE TWNTICGDYG GDWKWKILPF PRKLGQRCSH
TVDFCTECLE SYIEAQLDQH GRTGCHLLTC PSFDCDRRLE YDEVKLYARQ ETFSKYDEYL
KLEALSNLPS FRWCLADNCS YGQIHDLIES NHVSCEECGY EMCFQHQVKW HIDLSCEEFD
SMQENGDPRF RETRDWVNAN TKQCPSCGVN TQKGPGCFHM TCTLCRYEFC WECLASWSDI
MPRSGRYNQS AHRDGCYFRS SSQEPTQVTG ERIPVSFLSS TI
//
