ID A0A8J5TS60_FUSOX Unreviewed; 701 AA.
AC A0A8J5TS60;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 02-APR-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=ARI8 {ECO:0000313|EMBL:KAG7412550.1};
GN ORFNames=Forpe1208_v009092 {ECO:0000313|EMBL:KAG7412550.1};
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:KAG7412550.1, ECO:0000313|Proteomes:UP000694050};
RN [1] {ECO:0000313|EMBL:KAG7412550.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tf1208 {ECO:0000313|EMBL:KAG7412550.1};
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:KAG7412550.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JAELUQ010000006; KAG7412550.1; -; 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; cd20335; BRcat_RBR; 1.
DR CDD; cd22584; Rcat_RBR_unk; 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; 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; 2.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
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 212..414
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 216..261
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 160..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 413..511
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 608..646
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 170..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 701 AA; 78715 MW; 8A8D351ED09F084F CRC64;
MIAAALRQSP IIAVDMANST TSTPLTTTSF STGVNNGADT NTGATAPELS DLDYFIAVLQ
LPDGRTENQI EDDLVSKANA LGISSAPVAD KRITSSVESA STVYNARTFS MLSAGSTSTA
LTTHSSIFGP STPDLALSSA RQSKDLSFSQ YDRYLSVIDP HHNHSKTTRD SQTPDATAQS
IFSGKTKRSL FSVRSSFKLR WKKKASPQPL QVILTCASCR ADFKSSKSLH SISCGHTYCD
NCLRSLIHTA MSDESSMPPR CCAQPLPGFV MRDLLSRDAQ QEFLKAIIQY STPWQARIFC
SNPSCGGFIP PHQKLDLRYP STVTCRKCNT RVCIMCKHNA HPTGKDCPED WELDQVIKEG
GKPGWKRCYK CQNLVPLEEA STHMTCRCKA QFCYTCGGVW DANAGCPNDC DGEEEMDRRR
TEEQAQLAEY EDEKAAQEAA AAAASAERLE AEERTRNNAD FSNLAEMHRQ ELRRFLEFAE
QAREHMRARF VEQKKSTMKR HAELKESMKE KHARAVSQLE DRQVAAEMDL RNTLEASERS
VRIRLKHMEA YCDGLGRNSA NSSPGSDSQP HRVVTERDLR ELGQQYNIRD GMERSHQAKI
NVMRDRQAKR MEELIDRQEA EYESLLERNR QELVELDAQA VLEEETLAHT FTARKSKLVR
RWELAIEILR KELEDQDGVK YAPIPTPTWP EQTSQVLLSS E
//
