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Database: UniProt
Entry: A0A8J2MAC3_9BILA
LinkDB: A0A8J2MAC3_9BILA
Original site: A0A8J2MAC3_9BILA 
ID   A0A8J2MAC3_9BILA        Unreviewed;       505 AA.
AC   A0A8J2MAC3;
DT   25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 1.
DT   18-JUN-2025, entry version 14.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   ORFNames=CJOHNSTONI_LOCUS7952 {ECO:0000313|EMBL:CAG9538223.1};
OS   Cercopithifilaria johnstoni.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Cercopithifilaria.
OX   NCBI_TaxID=2874296 {ECO:0000313|EMBL:CAG9538223.1, ECO:0000313|Proteomes:UP000746747};
RN   [1] {ECO:0000313|EMBL:CAG9538223.1}
RP   NUCLEOTIDE SEQUENCE.
RG   Pathogen Informatics;
RL   Submitted (SEP-2021) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC         EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
CC   -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC       {ECO:0000256|ARBA:ARBA00005884}.
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:CAG9538223.1}.
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DR   EMBL; CAKAEH010001636; CAG9538223.1; -; Genomic_DNA.
DR   OrthoDB; 10009520at2759; -.
DR   Proteomes; UP000746747; Unassembled WGS sequence.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR   CDD; cd20343; BRcat_RBR_HHARI-like; 1.
DR   CDD; cd20356; Rcat_RBR_HHARI-like; 1.
DR   FunFam; 1.20.120.1750:FF:000002; RBR-type E3 ubiquitin transferase; 1.
DR   FunFam; 3.30.40.10:FF:000019; RBR-type E3 ubiquitin transferase; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR045840; Ariadne.
DR   InterPro; IPR048962; ARIH1-like_UBL.
DR   InterPro; IPR031127; E3_UB_ligase_RBR.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   Pfam; PF19422; Ariadne; 1.
DR   Pfam; PF01485; IBR; 1.
DR   Pfam; PF22191; IBR_1; 1.
DR   Pfam; PF21235; UBA_ARI1; 1.
DR   SMART; SM00647; IBR; 2.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000746747};
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          135..342
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          139..184
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..51
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   505 AA;  58377 MW;  2594DEEA8891CDD5 CRC64;
     MSLGSDEAMD DDDAFSGGSE SDATSTYSDD DGIVVDPPVI KTERGGSHDS ESADFQVLDA
     EKVALEMNKI IEDVASVLRL SATICRLLLH HYKWNKESLL ERFYESTDMD SFFLDANIIS
     PFKVARRGDE GLADVVDTCA ICCNHTILTS LQCNHRFCYP CWDSYLTTKI MEEGKAHVAC
     PQHNCPIIVD DEKTLALVKS ENAKKRYRRL IINSFVECNR LLRWCPAADC GRVVEVGHLE
     ARPVKCNCGT VFCFACGHEW HEPVSCRLLK LWIKKCNDDS ETSNWISANT KECPKCQVTI
     EKDGGCNHMT CKNVACKMEF CWMCLGPWEP HGSSWYSCNR YDDTLAKQAR DAQERSRAAL
     QRYLHYYNRY MNHQQSLKLE HKLYSIVKSK MEVMQQANMS WIEVQFLRKA VDVLSECRRT
     LMYTYAFAFY LQKDNQSVIF EENQRDLEHA TEQLSEFLER DLDHENLVSL KQKVQDKYRY
     VEQRRTTLLK HCAEGVEHDF WRFTA
//
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