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Database: UniProt
Entry: A0A834SKI1_9FABA
LinkDB: A0A834SKI1_9FABA
Original site: A0A834SKI1_9FABA 
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}.
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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
//
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