ID A0A8S4R527_9NEOP Unreviewed; 1114 AA.
AC A0A8S4R527;
DT 12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT 12-OCT-2022, sequence version 1.
DT 02-APR-2025, entry version 10.
DE SubName: Full=Jg7184 protein {ECO:0000313|EMBL:CAH2231772.1};
GN Name=jg7184 {ECO:0000313|EMBL:CAH2231772.1};
GN ORFNames=PAEG_LOCUS10223 {ECO:0000313|EMBL:CAH2231772.1};
OS Pararge aegeria aegeria.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Nymphalidae; Satyrinae; Satyrini; Parargina; Pararge.
OX NCBI_TaxID=348720 {ECO:0000313|EMBL:CAH2231772.1, ECO:0000313|Proteomes:UP000838756};
RN [1] {ECO:0000313|EMBL:CAH2231772.1}
RP NUCLEOTIDE SEQUENCE.
RA Lindestad O.;
RL Submitted (MAR-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the RBR family. {ECO:0000256|ARBA:ARBA00008278}.
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:CAH2231772.1}.
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DR EMBL; CAKXAJ010024854; CAH2231772.1; -; Genomic_DNA.
DR OrthoDB; 9978677at2759; -.
DR Proteomes; UP000838756; Unassembled WGS sequence.
DR GO; GO:0071797; C:LUBAC complex; IEA:InterPro.
DR GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; IEA:TreeGrafter.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IEA:TreeGrafter.
DR GO; GO:1990450; F:linear polyubiquitin binding; IEA:TreeGrafter.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:TreeGrafter.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0097039; P:protein linear polyubiquitination; IEA:TreeGrafter.
DR CDD; cd19815; Bbox1_HOIP; 1.
DR CDD; cd20337; BRcat_RBR_HOIP; 1.
DR CDD; cd20351; Rcat_RBR_HOIP; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 1.
DR InterPro; IPR047543; Bbox1_RNF31-like.
DR InterPro; IPR047540; BRcat_RBR_RNF31-like.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR047542; Rcat_RBR_RNF31-like.
DR InterPro; IPR026254; RNF31-like.
DR InterPro; IPR041031; RNF31_C.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR16004:SF2; E3 UBIQUITIN-PROTEIN LIGASE LUBEL; 1.
DR PANTHER; PTHR16004; RING FINGER PROTEIN 31-RELATED; 1.
DR Pfam; PF18091; E3_UbLigase_RBR; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000838756};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 713..950
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..10
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..65
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..138
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..380
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..390
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..522
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..672
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1114 AA; 124508 MW; 22B5BF1CF65BC18D CRC64;
MLKNRGRDPR SAVPSTPTMA LRSNVHRAPM AKPEPDYEVV EFPSDQYVNA KLQPPPPPPP
RPPTGHPIDA DASCGLCGGG GARVRCTECG RRALCASCDD MYHRHPKRRH HQRQALSHAQ
LRDERPPLPP KAAPPVPPPR RHKIGGDRLS ASPLPPAIDR RSTMNPLMGI PKQMAAITNT
NHFVSQRPQM HHQRPSVPSV TSHMGSVPYL PNAVHHSNTP VTSHDQSNTL GHFSSWNRPR
GSLSGINVPQ NVVQAPQLEP WEVQENLSTQ SWGRPLRRGT SVMELGGGPT ACPGCAHCAS
NPWRYGSCAN LDHSWVGQSP WPQTCCVPHP AAHNPQMFPH LHPHPPQTPQ PYRRADSRAV
SRAASRAGSR AASPALSVRS RASRRSKHRT PSPVPLPSSD ADSESENESD SKESKIPSVN
TNNAKEMVED SLGPAPSPPN SSWQCEHCTF VNEPGTRVCA VCCRTPTTKA KIISTDGINN
GVARLRVTNK SSPSPTSNLI DDRRKKIDDK INKTARPSKE RTSTGCGPSP PRDGRPVLKS
SNRLATPTRE QNNERTAQTR IRHDIAVGPS PPKELPNKQQ AVSTSRNAAT VQSLIQDRVE
IQSFPKRETP LREPLTKHSV SVGPSPPRDS PLRVVATIRN VSPNFQKKYV GNSPPREPDR
PSSRSSRTNT GTSPPPQSIS TQTYEVPSNW DRAQSVSRSS RPRRRVLDEN RRERSHSRLS
LSSDTRESER SVRTSGGRWE WREPRDSSPS VQITERSIAD CVCPYCKEPE LENLPEDDWL
DYFAHMDILL KTLLETETHE LFQRKLRDRT LARDPNFRWC VECSSGFFVH PKHKRLRCPE
CKSVTCASCR RPWSTNHDDM TCEQYALWLE DNDPERSVAA VQQHLRENGL DCPRCHFKYS
LSRGGCMHFT CSQCKYEFCY GCGKPFMMGA RCGLSEYCSR LGLHAHHPRN CLFYLRDKEP
RELQTLLQMN NITYETKAAE GSTGRCPIQL QRETPTGLLD TICGSEVQQN QAGLCKNHYL
EYLSRLVRGR KVDPLPILGV DDLETLVRRA AIHYVEYLAG LARSLDPIPI MEVSELVAEL
RRRALPLPER GPWDTDPIYA GMCAEIVREK IPLD
//
