ID B9RKM7_RICCO Unreviewed; 1268 AA.
AC B9RKM7;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
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_1051840 {ECO:0000313|EMBL:EEF48225.1};
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; EQ973784; EEF48225.1; -; Genomic_DNA.
DR AlphaFoldDB; B9RKM7; -.
DR STRING; 3988.B9RKM7; -.
DR eggNOG; KOG0167; Eukaryota.
DR InParanoid; B9RKM7; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008311; Unassembled WGS sequence.
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; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
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; IPR045210; RING-Ubox_PUB.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR47446; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR PANTHER; PTHR47446:SF2; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF04564; U-box; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00504; Ubox; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS51698; U_BOX; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008311};
KW WD repeat {ECO:0000256|PROSITE-ProRule:PRU00221}.
FT DOMAIN 413..488
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REPEAT 1013..1046
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
SQ SEQUENCE 1268 AA; 139790 MW; 6D56D145AB096946 CRC64;
MTTAATSSQI LHQISSFLSE ALSQPDLRRH LFSILRNGTS PSNKTTSVKP LNLALETLEK
ALSATNPFVQ SSSLRLAESL LLSYPETPFS SFLLSLLYSL TQQPTNASIS LLNIFYLDPL
LARSEIAPLI FQELFLVHLL PVLDWFNEQR SRISSASFSM NMSYDDRDED SACDVSIILP
SSKLLSKMSG GQALEFRELE GSYDDVLDEN CRVYAQYFKE ILKNNDENRV ITPPSLILKE
TGKVDKLNGS EDKMIKTEEL GLKNGRYNPI WADGERSVEF FSFGGSSRSK FPPSSNPRRV
SAKTLKNHYS RALTTSPAVI SDSELESSLD DNMVNSSSSE SEAELEVIVA NKNLVQFLTD
LTMLLFLVIN IFSLSCRLCI ATPLTFLNLS VTISSTDHVM GDIDNHPGAG KHTPPKDFVC
PITSHLLDDP VTLETGQTYE RRAIQEWISR GNSTCPITRQ ALHSNQLPKT NYVLKRLVAS
WREQNPEFAS NQSETAPQKT EPNFKSTIIS PVTSPNSVIS QSAIDSTMSE LRQAITDLCM
SEILSESEMA VLRIEQFWQE LNMDLDVQSM LSKPPVINGF VEILFNSLDP QVLKATVFLL
SELGSRDKGV VQTLTRVESD VECIVALFKN GLWEAVVLIY LLRPSTMSLL EMDLVESLLT
VIKKKEDMLK MCLKPKTAAV LLLGQILSSS EESIVISIVN AIVSTKVIES IAGCLEAECA
EERIAAVGIL SRCMQEHGKC RNTISAKAEL APVLDSFLSA TDGERFEIVL FFSELVKLNR
RTLSEQVLHI IKDEGPVSTM HSLVSFLQTA LQDQCPVVAG LLLQLDLLAE PRKMSIYREE
AIDTLISCLR KSEFTAAQIA AADTIVSLQG RFTASGKSLS RAILLKRAGL SKSYRNLTRM
EKLGNLSGEI EETSVCFQGL RDLTSYMRDI KKGLRELKKS SPLALEILKI LSEGHESSAE
LWNHEQLAQA DCTENGEVLS VTCFKDKIFS GHSDGTIKIW TGRGSVLHLI QEIKEHTKAV
TSLVVLQSGE RLYSGSLDRT ARVWSIGNEE LHCVQIHDMK DQVQSLVVAN SISCFIPQGA
GVKVHSWNGG SKLLNSNKYV KCLTLIQGKL YCGCHDSSIQ EIDLATGTLV TIQHGSRKLL
GKANPIHALQ VGNGLIYAAS SALDGAAVKI WNASNYGPAG SLPTTLEVRA IAVSSELIYL
GSKGGNVEIW DQKKLSIIET LQTGTEGARI LCMALDSNEE MLVIGTSDGR IQVKDFSLFL
HFPAIKQF
//