ID A0A0K9PJ88_ZOSMR Unreviewed; 678 AA.
AC A0A0K9PJ88;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Constitutively photomorphogenic 1 {ECO:0000313|EMBL:KMZ69034.1};
GN ORFNames=ZOSMA_223G00310 {ECO:0000313|EMBL:KMZ69034.1};
OS Zostera marina (Eelgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ69034.1, ECO:0000313|Proteomes:UP000036987};
RN [1] {ECO:0000313|Proteomes:UP000036987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX PubMed=26814964; DOI=10.1038/nature16548;
RA Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA Van de Peer Y.;
RT "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT the sea.";
RL Nature 530:331-335(2016).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KMZ69034.1}.
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DR EMBL; LFYR01000794; KMZ69034.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K9PJ88; -.
DR STRING; 29655.A0A0K9PJ88; -.
DR OMA; EEIVSAX; -.
DR OrthoDB; 21736at2759; -.
DR Proteomes; UP000036987; Unassembled WGS sequence.
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 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; IPR020472; G-protein_beta_WD-40_rep.
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:SF1; E3 UBIQUITIN-PROTEIN LIGASE COP1; 1.
DR Pfam; PF00400; WD40; 2.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR PRINTS; PR00320; GPROTEINBRPT.
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; 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:UP000036987};
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 55..92
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REPEAT 461..503
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 15..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 184..214
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 678 AA; 76860 MW; 318AF128493C72EF CRC64;
MTDASGVVPS VMKIESRGEG VSRCEAPDTE GGRIGNGNGS GSEEIVTLED RDFFCPICLA
TIKDAFLTLC GHSFCYMCII THLNSKNDCP CCGHYLTANQ IFPNFLLEKL IKKTCASQIS
KTASSSENFH LALQACEMSV KELDSLLYLL AEKKRKTEEE ESETNMQILI DFFQCLRKEK
FEELSEVQKD LQYIKEDLNA LNNHRIELNH ARERQSVKSC MLEDDLFSKI PIETHENPVV
YNVHDVNDVM SSERYQGIKK IEKKSQWTSH VLPRKEYFDS DTAKYSPIKS ELLAARKCRI
HQEFDELQEC YLQRRRLGVS HANKKPERNT SAKCRAGYHP GLEDFQSVLT AFTRYSRFRV
IAQLRQSDIC QTANIVSSIE FDRDDEFFAT AGVSKCIKVF EFSTVVNEPV DVHPPIVDIP
TRSKLSCLSW NKYSKNIIAS SDYEGIVNVW DVNTKQNIME YEEHEKRAWS VDFSQTNPSM
LVSGSDDFKV KVWCMNQETS VLNIVMKANI CCVKYNPGSS NYVAVGSADR HIHYYDLRNI
STPLHVFKGH LKAVSYVKFL SNNELASAST DSTLRLWDVQ DNCLVRTFEG HRNDKNFVGL
TVNNDYIACG SETNEVVAYH KAVSKPAAVH KFSSSDLNDT DVDDANSYFI SAVCWKTYHQ
TMLAANSLGT IKVIVLAT
//
