ID A0A1V9XYE5_9ACAR Unreviewed; 647 AA.
AC A0A1V9XYE5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Ubiquitin-protein ligase E3B-like {ECO:0000313|EMBL:OQR78480.1};
GN ORFNames=BIW11_00294 {ECO:0000313|EMBL:OQR78480.1};
OS Tropilaelaps mercedesae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Mesostigmata; Gamasina; Dermanyssoidea; Laelapidae;
OC Tropilaelaps.
OX NCBI_TaxID=418985 {ECO:0000313|EMBL:OQR78480.1, ECO:0000313|Proteomes:UP000192247};
RN [1] {ECO:0000313|EMBL:OQR78480.1, ECO:0000313|Proteomes:UP000192247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wuxi-XJTLU {ECO:0000313|EMBL:OQR78480.1};
RX PubMed=28327890; DOI=10.1093/gigascience/gix008;
RA Dong X., Armstrong S.D., Xia D., Makepeace B.L., Darby A.C., Kadowaki T.;
RT "Draft genome of the honey bee ectoparasitic mite, Tropilaelaps mercedesae,
RT is shaped by the parasitic life history.";
RL Gigascience 6:1-17(2017).
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:OQR78480.1}.
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DR EMBL; MNPL01002182; OQR78480.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9XYE5; -.
DR STRING; 418985.A0A1V9XYE5; -.
DR InParanoid; A0A1V9XYE5; -.
DR OrthoDB; 1126684at2759; -.
DR Proteomes; UP000192247; Unassembled WGS sequence.
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; IEA:InterPro.
DR GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
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; 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; 5.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 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:OQR78480.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000192247};
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 39..77
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REPEAT 426..468
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 512..552
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 132..189
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 647 AA; 72573 MW; 5A074B97DBAD4EBF CRC64;
MSASPAPRPN PKPRPLMRKR SLGVVPSSSE TSSDPTLDCP ICYSLIQDAY MTRCGHSFCH
DCVKRCIEKR PACPLCSCEL VDKDGKEQIF PNRLLNDLAL RAIKSEKRPR IGGAELGSRI
MQILAGEKDV SVNDVNQALD VLQTKKRQIE ATSREVQLTL LREFLDHSYK AKHEELNRIK
TDIALLEQDL SFLDSLSNTA VDWHFSDTNL PHSSHSSQST PIKSGLSVRV GDTTEDGAAT
SVQTVLSQRR FRMHAHFQCL EDCYFSARQI HREEDSMSPE PQQPADASED VDITVRMPRP
RAPRGLERFA ESLSKFTRYS QLRSLSTLNY ASDLLNSTSI VSSIEFDKDS EYFAIAGVTK
RIKMFEYSTV IRNDVDMHYP INEMTCSSKI SCISWSSYHK NMLGCSDYEG TVTLWDAYRS
QKVKTFQEHE KRCWSVDFNK VDTKILASGS DDTKVKLWAI NQEHSISSIE AKANVCCVRF
NPDSMYHLAM GSADHCVHYY DLRNCKTSLG VFKGHKKAVS YVKFLNAKEL VSASTDSQLK
LWKTDDPQCL RSFTGHVNEK NFVGLATDGD YIACGSENNS LYIYYKGLST QIQTWSFRTQ
GSGREDGTVP VAPGESNEFV SAVCWMTGSA VVVAANSQGT IKLLELV
//
