ID A0A2T4GE02_FUSCU Unreviewed; 962 AA.
AC A0A2T4GE02;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 02-APR-2025, entry version 24.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=FCULG_00010586 {ECO:0000313|EMBL:PTD01670.1};
OS Fusarium culmorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=5516 {ECO:0000313|EMBL:PTD01670.1, ECO:0000313|Proteomes:UP000241587};
RN [1] {ECO:0000313|EMBL:PTD01670.1, ECO:0000313|Proteomes:UP000241587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PV {ECO:0000313|EMBL:PTD01670.1,
RC ECO:0000313|Proteomes:UP000241587};
RA Schmidt R.;
RT "Fusarium culmorum secondary metabolites in fungal-bacterial-plant
RT interactions.";
RL Submitted (FEB-2018) 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:PTD01670.1}.
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DR EMBL; PVEM01000028; PTD01670.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4GE02; -.
DR OrthoDB; 10009520at2759; -.
DR Proteomes; UP000241587; 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; cd22584; Rcat_RBR_unk; 2.
DR Gene3D; 1.20.120.1750; -; 2.
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; 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; 2.
DR SMART; SM00647; IBR; 4.
DR SMART; SM00184; RING; 4.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 2.
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:UP000241587};
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 58..268
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 349..543
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 496..534
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 941..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..25
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 962 AA; 106872 MW; 17D96DEDED5761E3 CRC64;
MDRNPIPRQA RRPKMTRSAR VPGKRPRSEF ETHHIQENDP APTIPSSPSV RRATRLIRTK
ECLACGEDFP QSLMIFAPCS HLFCKPCADN LVSLAMRDEA YFPARCCDTM IPVTLSNGFS
NEVVTQYNAK AVEFAIPSLG RVYCSSELCS TFIPPTQIDS GIGHCKHCLT DTCIACKAKA
HKGVCGHKEE DVQGVLRLAQ NTGWKRCSKC GHVIEKSMGC DHMVCLCGHR FCYVCGKDAG
KCACDEVPVD VPMPPHAANP PCNNHRWGRI LQPENCEDCG KAVQGYNIFI CRGCAHIACL
ASDCTSAMSI GHENDSVASE STVSSDLPPL IRANSSHNYP VKDRNPYRAV ETCGGCMNDF
PEDETAVMAC THELCRLCFS LIIERSLDGS SAFPPRCCDI LFTRDYVYPH ISGETRRRFE
EKQVIYETLD RTYCSNVECQ TFIPPWTIKS DIGCCPSCPQ RTCAICKNPE HTGRCVVDKS
KNKLLALAKK KGWKPCPRCG QLINKTSGCE HVMCPCGHDF CFRCEEDFAG HICPREALCT
GICIDLLVDA GRCLLRGLFM PVRWTRRRSR YQAQNDVMDV SANLATSLAR AAEADAALIQ
ELRLEDQIAR DRMIAEAIQD GRRPTVETGY QYPLDDETFN ILRQFNALAI ESDNGEEERN
PATDGTQNGQ EAQQIQLTVH TNEIQDTVID LEDGTQRFNP EEDLLGTTTE DKSANEPQET
DSPGTERDHA QNSSTVVDES AAPAQPTDIV MEQCVSCQDD FPKAFEAPCF HRWCQTCLVI
RIEASLRDES LFPPSCCEPL PIEVGDFVTQ EMVDSCQKKT VELSTVDRTY CSHATCSTFI
PHQSIEGDLG RCSACEKQTY VLCKRASHEG TCPEDNASQD VLRLGEREGW RRCKRCKHLI
DLRIGCFHIS EYIFQQPLSL TNIAQLALAV INFATSVEPV GKPAHAPNGK KTDSSMPLAS
VL
//
