ID   B9T1B5_RICCO            Unreviewed;       753 AA.
AC   B9T1B5;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=RCOM_0499500 {ECO:0000313|EMBL:EEF30352.1};
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
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DR   EMBL; EQ974332; EEF30352.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9T1B5; -.
DR   STRING; 3988.B9T1B5; -.
DR   eggNOG; KOG0167; Eukaryota.
DR   InParanoid; B9T1B5; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000008311; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd16664; RING-Ubox_PUB; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   InterPro; IPR045210; RING-Ubox_PUB.
DR   InterPro; IPR003613; Ubox_domain.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR23315; U BOX DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR23315:SF278; U-BOX DOMAIN-CONTAINING PROTEIN 3; 1.
DR   Pfam; PF00514; Arm; 3.
DR   Pfam; PF04564; U-box; 1.
DR   SMART; SM00185; ARM; 5.
DR   SMART; SM00504; Ubox; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50176; ARM_REPEAT; 3.
DR   PROSITE; PS51698; U_BOX; 1.
PE   4: Predicted;
KW   Ligase {ECO:0000313|EMBL:EEF30352.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008311};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          235..309
FT                   /note="U-box"
FT                   /evidence="ECO:0000259|PROSITE:PS51698"
FT   REPEAT          508..550
FT                   /note="ARM"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT   REPEAT          590..632
FT                   /note="ARM"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT   REPEAT          631..672
FT                   /note="ARM"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT   REGION          424..443
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   753 AA;  82636 MW;  CEA09F66284D68FA CRC64;
     MDMTPVRCLV NSISRFILLV SCQTRKPAPI QKDYGNMVTV LKHLKPVLDE IIDCKLSSDQ
     ILYKECEELD LAVNGARDFM ENWCPKMSKL CSVQQSEALY MKIRISSVKI CHLLSRLLRS
     SPSTSSLTSI QHCMQELQSL KQEMMTEHIE EAVRNKRDEV VPCSDPLVKI IQSLSLTSGQ
     EILKESVAVE KERMNIQVNK AKGDLDQINQ IVDLISDIRN CLLKIERVDP KSGVLIPSYF
     RCPLSLELML DPVIVASGQT YERASIQKWL EHGLTICPKT RKTLAHSNLI PNYTVKAMIS
     NWCEENHIRP SSNSKQDDLI SASVPADALQ CSDSLHYSLH NSNSISKSSL EGGNGFEKQR
     VVFLSKLSRE EPNGYQVQKI ESFERPSHEL SYNHSRSEST SSAISSIEYV PPIANEVSMV
     SRKHEKVSDS IPKTKADGEG NANHKLNRTR AVPFLDSGFD DLTTTSHVEC LIEGLKSQSN
     ELQATAAEEL RLLAKNKMEN RIIIGRSGAI TPLLSLLYSG VKQTQEHAVT ALLNLSINEE
     VKSMIAEAGA LEPLIHVLKS GNDGAKENSA AALFSLSVLE EYKAKIGCSG AVKALVDLLA
     SGTLRGKKDA ATALFNLSIL HENKARIVQA GAVKYLVELM DPATGMVDKS VALLANLSTI
     GEGRLAIARA GGIPSLVEIV ESGSQRGKEN AASVLLQLCL NSPKFCTFVL QEGAVPPLVA
     LSQSGTLRAK EKAQQLLSHF RNQREGSMGK GKS
//