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Database: UniProt
Entry: A0A8J1TSW4_OWEFU
LinkDB: A0A8J1TSW4_OWEFU
Original site: A0A8J1TSW4_OWEFU 
ID   A0A8J1TSW4_OWEFU        Unreviewed;      1380 AA.
AC   A0A8J1TSW4;
DT   25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 1.
DT   18-JUN-2025, entry version 16.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   ORFNames=OFUS_LOCUS14666 {ECO:0000313|EMBL:CAH1789278.1};
OS   Owenia fusiformis (Polychaete worm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC   Sedentaria; Canalipalpata; Sabellida; Oweniida; Oweniidae; Owenia.
OX   NCBI_TaxID=6347 {ECO:0000313|EMBL:CAH1789278.1, ECO:0000313|Proteomes:UP000749559};
RN   [1] {ECO:0000313|EMBL:CAH1789278.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Martin C.;
RL   Submitted (MAR-2022) 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:CAH1789278.1}.
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DR   EMBL; CAIIXF020000007; CAH1789278.1; -; Genomic_DNA.
DR   OrthoDB; 69641at2759; -.
DR   Proteomes; UP000749559; 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; cd20346; BRcat_RBR_ANKIB1; 1.
DR   CDD; cd20361; Rcat_RBR_ANKIB1; 1.
DR   FunFam; 1.20.120.1750:FF:000003; RBR-type E3 ubiquitin transferase; 1.
DR   FunFam; 1.25.40.20:FF:000040; 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; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR045840; Ariadne.
DR   InterPro; IPR031127; E3_UB_ligase_RBR.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR047564; Rcat_RBR_ANKIB1.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR003903; UIM_dom.
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; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF19422; Ariadne; 1.
DR   Pfam; PF01485; IBR; 1.
DR   Pfam; PF22191; IBR_1; 1.
DR   SMART; SM00248; ANK; 3.
DR   SMART; SM00647; IBR; 2.
DR   SMART; SM00726; UIM; 3.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS50330; UIM; 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:UP000749559};
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   REGION          773..810
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          883..925
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1007..1072
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1144..1176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1194..1267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1315..1380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        899..911
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1007..1022
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1023..1035
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1194..1211
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1224..1239
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1338..1355
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1364..1373
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1380 AA;  153864 MW;  DF76DC33D9D39710 CRC64;
     MGSASTKFRK HLQTGDEYAA LHLYNNSSDL RKGLDPNISY GDHYNHETPL HYAAKHGMKS
     LLRIFLNELQ GNPNKKNSRN ETSLHCVCMA MNGQNFSVQQ RRLECLMLIL QWKGATLKDG
     EVEKADLGGQ DEKQNTALHY AAASGLKKSV ELLVSQGAPL FTENEQKQTP CDCAEKNNHS
     NIALYLESKM VFSNESEDEQ QEETDDMNQL IDTMEDYCGL RAQDLQEAKD QLLVETSDML
     RVPLFTAEAL LRNHEWSREM LLEAWMGDPI ACCEKCGVTP PPNLFEDRPM AGPPQSVDHD
     LTTPTYASAP ADAVCDICAG LIGHSEEELV PMQCDHAFCR GCWNRYLTGK IQEGDTHNIG
     CPAYQCHKLV PVEVIETIVS RDMARRYLQF DIKAFVDSNP NIKWCPYPGC GRAVKLPEAE
     ASTPTTPKPR DLTETSHAVD CGNGHYFCWE CLGEAHEPVN CDSWKDWFTK ISEIKPEELD
     GTADTSESAA NCLWLVTNSK PCPQCKSPIQ KNEGCNHMKC SKCKSDFCWV CLEPWKKHSS
     ATGGYFRCNR YEVVKKVEEN TENLKSDAER NNKKAQEMNR FVHYYTRFKN HENSYKLEEP
     LITTAKEKMM VLAKAITDPD TANIETKFVE EGVVQLLKAR RVLKCSYAYG YFLEDTGYKK
     PIFEFMQTEL EECTESLSEM IARPYLRTPR AKIIQTAHTV QRKRHEFVQA IAKGLVPADN
     SPYRKRKTRF SIDLDDDLKK ALIESLKDLD PHNPWIKDPT GRHTNVAALL DWPEESDDSD
     TEVSPVPIAT STSNLSSSPP PPTNNNSGIC ARGGCMRQKA QNPRTGTLHD HCSLRCMRLD
     RIEKQELKKE GGVQPTREFV TDYQIDLLRA LEMSRLQFIR DDQTVAASGR RPDTPPGNSP
     VSSTQDIPSS SQKDDVTSPD ISDVVKSKHE GGVVKRAVLE NLEDFDREFN RALEMSREED
     NDLTMAIRLS LQDSGEDDLV AGRQRRVPSR EELPMISSVV AKVPNKSVED IHEASSHGDS
     RVRSTSVGSR SRSGTMGSEF ELLGATGGAA PRPPISPKVR FSDDETTEDQ GDCLFPQADI
     SKTIEHTLNS VNSSPFGLIK DINVSNIFVK DTDKTKNFEQ KYFLYNNKKE DGIFEPRLLD
     SSNASNAHEN DLGLPSVGNP RRGRSREEPS INPQFSSIVM KCPNSVSVLD TVSRSPSELG
     SSFSLDSTVS KSSKRETGRT GSFSSLQGSS RSGRSSLQSD ATARCQSDPL RHDNTALGPD
     HTGLGPAAPI DVWIKQTTEQ VNQQAQQTQQ QRVDDTLDTA LHNLTTLSNE LNYTQSRVRD
     TSSSQSSSQP DTVELAHMTS SGSEVTGDTR SWSSESNEHG QEQSNNSSGN STSKGDAVFV
//
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