ID A0A834SKI1_9FABA Unreviewed; 587 AA.
AC A0A834SKI1;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 18-JUN-2025, entry version 16.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=G2W53_037523 {ECO:0000313|EMBL:KAF7805362.1};
OS Senna tora.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Caesalpinioideae; Cassia clade; Senna.
OX NCBI_TaxID=362788 {ECO:0000313|EMBL:KAF7805362.1, ECO:0000313|Proteomes:UP000634136};
RN [1] {ECO:0000313|EMBL:KAF7805362.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7805362.1};
RA Kang S.-H., Pandey R.P., Lee C.-M., Sim J.-S., Jeong J.-T., Choi B.-S.,
RA Jung M., Ginzburg D., Zhao K., Won S.Y., Oh T.-J., Yu Y., Kim N.-H.,
RA Lee O.R., Lee T.-H., Bashyal P., Kim T.-S., Lee W.-H., Kawkins C.,
RA Kim C.-K., Kim J.S., Ahn B.O., Rhee S.Y., Sohng J.K.;
RT "Genome-Enabled Discovery of Anthraquinone Biosynthesis in Senna tora.";
RL Submitted (SEP-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Might act as an E3 ubiquitin-protein ligase, or as part of E3
CC complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating
CC enzymes and then transfers it to substrates.
CC {ECO:0000256|ARBA:ARBA00003976}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC {ECO:0000256|ARBA:ARBA00005884}.
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:KAF7805362.1}.
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; JAAIUW010000012; KAF7805362.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A834SKI1; -.
DR OrthoDB; 10009520at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000634136; Chromosome 12.
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:UniProtKB-UniPathway.
DR CDD; cd20346; BRcat_RBR_ANKIB1; 1.
DR CDD; cd22583; Rcat_RBR_ARI7-like; 1.
DR FunFam; 1.20.120.1750:FF:000005; 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 Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 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; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
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; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 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:UP000634136};
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:PRU00322}.
FT DOMAIN 135..348
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 139..183
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 559..587
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..49
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..541
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 587 AA; 67021 MW; 2662F6EC85527461 CRC64;
MDSEDDMHDA NDIESLDDDF YSGETEDAPL DYYSDYDDEA DDYFEDADES DKIKSRRPEQ
NFTILRESDI EQRQEDDITR VSTVLYISRV DASILLRHYN WNVSQVHEAW FADEERVRKT
VGLLDKPVVE FPNARELTCG ICFENYPCSR IESAACGHPY CISCWEGYIG TSINDGPGCL
MLRCPDPSCG AAVGQNMISL LASDEDKKKY SRYLLRSYIE DNKKTKWCPA PGCEYAVTFD
AGNGNYDVSC LCSYCFCWNC TEEAHRPVDC GTVAKWILKN SAESENMNWI LANSKPCPKC
KRPIEKNQGC MHMTCTPPCK FEFCWLCLGA WSDHGERTGG FYACNRYEAA KQEGVYDESE
RRREMAKNSL ERYTHYYERW ASNQSSRQKA LADLHQMQTV HIEKLSDTQC QPESQLKFIT
EAWLQIVECR RVLKWTYAYG YYLPEHEHAK KQFFEYLQGE AESGLERLHQ CAEKELQQYL
SADGPSKEFN DFRTKLAGLT SVTRNYFENL VRALENGLSD VDSNGAASSK ATSSKNGAGS
SKGRGGRGKG TSRINKMTDD SSWSCEHCTY ANGASVNTCQ MCRQQRR
//