ID B9T7A8_RICCO Unreviewed; 677 AA.
AC B9T7A8;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 80.
DE SubName: Full=Ubiquitin ligase protein cop1, putative {ECO:0000313|EMBL:EEF28255.1};
DE EC=1.3.1.74 {ECO:0000313|EMBL:EEF28255.1};
GN ORFNames=RCOM_0002700 {ECO:0000313|EMBL:EEF28255.1};
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).
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DR EMBL; EQ974729; EEF28255.1; -; Genomic_DNA.
DR RefSeq; XP_002534127.1; XM_002534081.2.
DR AlphaFoldDB; B9T7A8; -.
DR STRING; 3988.B9T7A8; -.
DR GeneID; 8266405; -.
DR KEGG; rcu:8266405; -.
DR eggNOG; KOG0297; Eukaryota.
DR InParanoid; B9T7A8; -.
DR OrthoDB; 21736at2759; -.
DR Proteomes; UP000008311; Unassembled WGS sequence.
DR GO; GO:0032440; F:2-alkenal reductase [NAD(P)+] activity; IEA:UniProtKB-EC.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd16504; RING-HC_COP1; 1.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR042755; COP1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR44080; E3 UBIQUITIN-PROTEIN LIGASE COP1; 1.
DR PANTHER; PTHR44080:SF7; E3 UBIQUITIN-PROTEIN LIGASE COP1; 1.
DR Pfam; PF00400; WD40; 4.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Ligase {ECO:0000313|EMBL:EEF28255.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:EEF28255.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008311};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 53..91
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REPEAT 461..493
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 547..587
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 257..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 139..203
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 677 AA; 76510 MW; 74E201F751A63B8D CRC64;
MEEVSTGAIV PAVKLEPRPS SSSVAVAAAV SSEPAAAAEE EAGLSELEKD FLCPICMQII
KDAFLTACGH SFCYMCIITH LRNKSDCPCC THYLTTNQLF PNFLLQKLLK KASARQTSKT
ASPVEHFRHA LQQGCEISIK ELDTLMSMLS EKKRKMEQEE AERNMQILLD FLHYLRKQKV
DELNEVRTDL QFIKEDIEAV EKHRIELYHA RDRYSMKLRM LGDDPNARKP WSPTIEKSNG
GVISNAFNVR GGMITGNLPT KKMDGKAQVS SHGLQRKDSL SGSDSQFNHS GLSVVRKKRV
HAQFNDLQEC YLQKRRQMAN QLHNQQDKDK NVMHREGYST GLLDFQSVLS TFTQYSRLRV
IAELRHGDIF HSANIVSSIE FDRDDELFAT AGVSRRIKVF DFSTVLNDPA DVHCPVEEMS
TRSKLSCLSW NKYAKNQIAS SDYEGIVTVW DVTTRQSVME YEEHEKRAWS VDFSRTEPSM
LVSGSDDCKV KVWCTNQEAS VLNIDMKANI CCVKYNPGSS NYIAVGSADH HIHYYDLRNV
SHPLHVFSGH RKAVSYVKFL SNSELASAST DSTLRLWDVK ENLPVRTFRG HTNEKNFVGL
SVNRDYIACG SETNEVYVYH KEISRPVTWH RFGSPEMDDA DEDAGSYFIS AVCWKSDSPT
MLTANSQGTI KVLVLAA
//