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Database: UniProt
Entry: B9T326_RICCO
LinkDB: B9T326_RICCO
Original site: B9T326_RICCO 
ID   B9T326_RICCO            Unreviewed;       218 AA.
AC   B9T326;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   SubName: Full=Ubiquitin-protein ligase, putative {ECO:0000313|EMBL:EEF29748.1};
GN   ORFNames=RCOM_0327010 {ECO:0000313|EMBL:EEF29748.1};
OS   Ricinus communis (Castor bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC   Ricinus.
OX   NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN   [1] {ECO:0000313|Proteomes:UP000008311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX   PubMed=20729833; DOI=10.1038/nbt.1674;
RA   Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA   Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA   Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA   Rabinowicz P.D.;
RT   "Draft genome sequence of the oilseed species Ricinus communis.";
RL   Nat. Biotechnol. 28:951-956(2010).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and
CC       subsequent proteasomal degradation of target proteins. E3 ubiquitin
CC       ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the
CC       form of a thioester and then directly transfers the ubiquitin to
CC       targeted substrates. It probably triggers the ubiquitin-mediated
CC       degradation of different substrates. {ECO:0000256|ARBA:ARBA00024004}.
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DR   EMBL; EQ974398; EEF29748.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9T326; -.
DR   STRING; 3988.B9T326; -.
DR   eggNOG; KOG3002; Eukaryota.
DR   InParanoid; B9T326; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000008311; Unassembled WGS sequence.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR044286; SINL_plant.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR013010; Znf_SIAH.
DR   PANTHER; PTHR46632; E3 UBIQUITIN-PROTEIN LIGASE SINA-LIKE 4; 1.
DR   PANTHER; PTHR46632:SF13; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR   Pfam; PF21361; Sina_ZnF; 1.
DR   SUPFAM; SSF49599; TRAF domain-like; 1.
DR   PROSITE; PS51081; ZF_SIAH; 1.
PE   4: Predicted;
KW   Ligase {ECO:0000313|EMBL:EEF29748.1};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00455};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008311};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00455};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00455}.
FT   DOMAIN          36..92
FT                   /note="SIAH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51081"
SQ   SEQUENCE   218 AA;  24320 MW;  C7622D3A591ED292 CRC64;
     MAFSYVFTWL LPMTDAPNLL TSSSIVFSEI VVVSEPVRTL CRNNEYGCNR ILDNNDDHEE
     TCSFSPCACP LLHCNFIGSS EQLSLHFSGK HWDTGRRFRY NSPLSVSLGM NEQFLVLQAE
     EDGILFLLSK STESIGNTTT ITCIGPSSSK EKFLYDIIAG RGVSSLRLKS STEYFPGRVE
     GFPPMDFLLI PFCFVSSSGQ LELELCIWNS TELDTDCS
//
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