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Database: UniProt
Entry: A0A8J2HNU4_COTCN
LinkDB: A0A8J2HNU4_COTCN
Original site: A0A8J2HNU4_COTCN 
ID   A0A8J2HNU4_COTCN        Unreviewed;      1707 AA.
AC   A0A8J2HNU4;
DT   25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 1.
DT   02-APR-2025, entry version 12.
DE   SubName: Full=Similar to LUBEL: E3 ubiquitin-protein ligase lubel (Drosophila melanogaster) {ECO:0000313|EMBL:CAG5106856.1};
GN   ORFNames=HICCMSTLAB_LOCUS12469 {ECO:0000313|EMBL:CAG5106856.1};
OS   Cotesia congregata (Parasitoid wasp) (Apanteles congregatus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Ichneumonoidea; Braconidae;
OC   Microgastrinae; Cotesia.
OX   NCBI_TaxID=51543 {ECO:0000313|EMBL:CAG5106856.1, ECO:0000313|Proteomes:UP000786811};
RN   [1] {ECO:0000313|EMBL:CAG5106856.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Chebbi M.A.C M.;
RL   Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases.
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:CAG5106856.1}.
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DR   EMBL; CAJNRD030001124; CAG5106856.1; -; Genomic_DNA.
DR   OrthoDB; 9978677at2759; -.
DR   Proteomes; UP000786811; 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; cd20337; BRcat_RBR_HOIP; 1.
DR   CDD; cd20351; Rcat_RBR_HOIP; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
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; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
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; 2.
DR   Pfam; PF01485; IBR; 1.
DR   Pfam; PF22191; IBR_1; 1.
DR   SMART; SM00647; IBR; 1.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000786811};
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, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          1286..1522
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          1290..1339
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          77..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          126..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          887..923
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          983..1060
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1090..1125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1206..1234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..110
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..152
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        896..916
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        997..1049
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1105..1121
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1707 AA;  192095 MW;  7E96732AAA205977 CRC64;
     MRIWGPPAGV ENDEAAPRKD AANEAGVAGL SELVGGAMDL DALKQVIPSL DNLAELQAGC
     KQDSTRTKPT DQLLKNVQEA DDKNIGNNSN DLSNSFKDSD KPCTSPSSKT DLNKLESGKI
     LLQENGDIGN KIESAEQKSD EKDIEQTEEI KNQSDSSAKN LAVENLLLAT KLSEQVPIEE
     FSAKLEPKVV SNDKIDEILN VPIETPQVST QASEIVDKEV VKEENKLEVN LPVKISSEEV
     VKIEQEVIEE KPIKEDVKLS IDASSESKKL LETEETVVET NSPVKEEIIV GSVSEVDKSD
     ILNITKNKDE EVFDKAVRIS ESEIKFESQE KLNQATPTVL SAPPSRMTAL KSLKNRLTSM
     ISKFPSMKLS YEKPESMGIN QVNYKESMDS SLYSHPNLII NNINQHASNG INNHNNTDKL
     NDDIISLDCA STQNHLKTFI SSATITPTNK EVVQKINGIN KYNETINSAS SSDDQAVLKN
     NTKEYESSVF FQNTLSNPES RDIKRSTMYI EPLMVSKDKK NEDYVKNNVE VVATVDVEVN
     EENHKLKDQD LKIKMTETEN NYKNLQIYQE VDNVMEYNNF EKIDSNENNM EVDIVNESGD
     KDDLFVDASS SPETFELKIT EAPLLIVNDA APVENPAVVR GSLTINLSQF SDMKELTTEM
     LQFASQEILE NESTGPLSPL EAELPEIFSA SSKIETSIEI NESAVKTDSV QTNYFIPKPK
     GRSKSPVKRS FVLRKLPARK CFVGTKRSFN FGGVPKDTAL TRAKECADKI AAKSLMSSRS
     VNQVKKAEVV DVNRKGECDK KQELVSQTEK VEREKKMNLS SQKIDKNFIN KPTPKSKLPS
     RIPIFQKKPW VAGQTISVAS QKIIEVNVLK PTNSSFNVPR RTIPVLQPLV GPPADNKNQN
     GGNQSNEVSK NVNGKVQSEK ENKNCISKLR DDGKLLTNNE TAQSKNSSKN IIRGLTFIKD
     ENDTSGIDKS KINESVNPEI DFKDEFNKYS SEASVDVSDD EEEVDDDDEE EEEFEEIEEI
     EIEDEESSEE ISDEEEIEEK EEELSDSETT DTNTKSSVIM RRINSTEELT NAELMLKKTL
     DNIKAEISDS EYEEISSNSQ KSEGSDEAEL SEANDLPEDP IELSTTKNDV DVESTIVLTL
     PKRKSTEIEG EENAVTQSTS KTIRLKDSKV LKVRVTEPEV VVHKKKESRK RFSIVAEYVQ
     QFEGDSLNHE RRNSKTKQQE SLKITRDQSP VNERERTARR LLAEGRVSSY DEAEIAASLI
     GLKFQDDEAI HAAQECTSVE SAIAFLQQEC ELCTGRFAVS QMISMLKCIH RCCNDCAKNY
     FTIQISDRNI MDAVCPFCKE PDLKDATEDE VLEYFSILDI QLKSLLDPPI HELFQRKLRD
     RTLMQDPNFK WCAQCSSGFY ANPNQKRLIC PDCRSVTCAF CRKPWEKQHE GITCEQFEEW
     KNENDPDNQA IGLAKHLADN GIDCPKCKFR YSLSRGGCMH FTCNQCKYEF CCGCGKAFMM
     GAKCTVSPYC AKLGLHSHHP RNCLFYLRDK EPAQLQSLLK GHGIEFNTEN SSGDRKCKVQ
     LQKETPTGVI DAVCNSDVVE NHAGLCRIHY IEYLVRKIRL SKLEPLSLFS IDDLETCIKR
     AGLNLPANWY RRDPEDYRRD LAEHYVEYLA GLVLKSKLDP VTIFDLNETK QELRRRGKVP
     PIKAQEMSEQ DYLRTCIQVV QKEIPLE
//
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