ID A0A087SML7_AUXPR Unreviewed; 472 AA.
AC A0A087SML7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=E3 ubiquitin-protein ligase COP1 {ECO:0000313|EMBL:KFM26971.1};
GN ORFNames=F751_2057 {ECO:0000313|EMBL:KFM26971.1};
OS Auxenochlorella protothecoides (Green microalga) (Chlorella
OS protothecoides).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Auxenochlorella.
OX NCBI_TaxID=3075 {ECO:0000313|EMBL:KFM26971.1, ECO:0000313|Proteomes:UP000028924};
RN [1] {ECO:0000313|EMBL:KFM26971.1, ECO:0000313|Proteomes:UP000028924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0710 {ECO:0000313|EMBL:KFM26971.1,
RC ECO:0000313|Proteomes:UP000028924};
RX PubMed=25012212; DOI=10.1186/1471-2164-15-582;
RA Gao C., Wang Y., Shen Y., Yan D., He X., Dai J., Wu Q.;
RT "Oil accumulation mechanisms of the oleaginous microalga Chlorella
RT protothecoides revealed through its genome, transcriptomes, and
RT proteomes.";
RL BMC Genomics 15:582-582(2014).
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; KL662138; KFM26971.1; -; Genomic_DNA.
DR RefSeq; XP_011399927.1; XM_011401625.1.
DR AlphaFoldDB; A0A087SML7; -.
DR STRING; 3075.A0A087SML7; -.
DR GeneID; 23613448; -.
DR KEGG; apro:F751_2057; -.
DR eggNOG; KOG0297; Eukaryota.
DR OrthoDB; 21736at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000028924; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd16504; RING-HC_COP1; 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; 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; 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:SF1; E3 UBIQUITIN-PROTEIN LIGASE COP1; 1.
DR Pfam; PF04564; U-box; 1.
DR Pfam; PF00400; WD40; 3.
DR SMART; SM00184; RING; 1.
DR SMART; SM00504; Ubox; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000028924};
KW WD repeat {ECO:0000256|PROSITE-ProRule:PRU00221};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 23..61
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REPEAT 285..327
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 368..398
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 134..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 102..129
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 472 AA; 50332 MW; CA2A14AE1580CD5E CRC64;
MPAVHASSAG PGEDVASHAD FSCPVCREVM RSPCVTPCGH TFCHACILRH VQRDSTCPCC
RSYLTEARVW PNHLLAGVCK ALEVRGARTR LSPIARLKRL LEESKEAELD RVQDRLDCLE
TDIRAVARRV DPGCLPGTEL EDTGSSREEG EDSSNASGSG VSPRDPAPGP DPTQDLAGAP
LFTVAVIPRP PGARPNSIVS GLEYNSRGNL FACAGVSRRI SVYEHAAVLA PGSPAQQPPA
AELMARSKIS SLSWDPGSEH RVAASDYDGA MSLWDVEGLA LVHEFEAHVR RVWAVHYCAA
AQGLLATGSD DGLVKLWSTS LATMIDVGVN VCCVRWRPGS SHHVALGCSD HHAYLYDTRH
VARPLETLSG HSKPVSYVRW LDSGSLITAS TDSTLRRWGM LGADPGPGPS SYTGHTNEKN
FVGLCVEDGL IASGSETNEP FVSAVAWRPG AEHLLAANSA GAIQLMRVVG SD
//
