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Database: UniProt
Entry: W6UGZ9_ECHGR
LinkDB: W6UGZ9_ECHGR
Original site: W6UGZ9_ECHGR 
ID   W6UGZ9_ECHGR            Unreviewed;       633 AA.
AC   W6UGZ9;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   ORFNames=EGR_04274 {ECO:0000313|EMBL:EUB60835.1};
OS   Echinococcus granulosus (Hydatid tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus;
OC   Echinococcus granulosus group.
OX   NCBI_TaxID=6210 {ECO:0000313|EMBL:EUB60835.1, ECO:0000313|Proteomes:UP000019149};
RN   [1] {ECO:0000313|EMBL:EUB60835.1, ECO:0000313|Proteomes:UP000019149}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24013640; DOI=10.1038/ng.2757;
RA   Zheng H., Zhang W., Zhang L., Zhang Z., Li J., Lu G., Zhu Y., Wang Y.,
RA   Huang Y., Liu J., Kang H., Chen J., Wang L., Chen A., Yu S., Gao Z.,
RA   Jin L., Gu W., Wang Z., Zhao L., Shi B., Wen H., Lin R., Jones M.K.,
RA   Brejova B., Vinar T., Zhao G., McManus D.P., Chen Z., Zhou Y., Wang S.;
RT   "The genome of the hydatid tapeworm Echinococcus granulosus.";
RL   Nat. Genet. 45:1168-1175(2013).
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   -!- 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:EUB60835.1}.
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DR   EMBL; APAU02000026; EUB60835.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6UGZ9; -.
DR   STRING; 6210.W6UGZ9; -.
DR   EnsemblMetazoa; XM_024493523.1; XP_024352031.1; GeneID_36339989.
DR   OMA; RRRICAM; -.
DR   OrthoDB; 2943236at2759; -.
DR   Proteomes; UP000019149; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR   CDD; cd20355; Rcat_RBR_RNF19; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
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   PANTHER; PTHR11685:SF427; RBR-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR   Pfam; PF01485; IBR; 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   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019149};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
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   TRANSMEM        461..494
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        515..543
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          79..449
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          83..130
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          303..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          584..633
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        314..328
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        584..617
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        618..633
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   633 AA;  69184 MW;  D3BA37E569A2B7B7 CRC64;
     MEVINNLLAG NQRKPRTDTS VISSSSGSIR YKWPHRRRRT KVQKSAEVES VPAAAAAISE
     VGSDTASVVL YPGLLRVPAD DSCVVCANDV DSLYALQKCG HRACLDCWRA FVASQVSSFA
     MAHITCIACN CRLSRALTLQ LLRPPHQSHS ETSFTQNAYV AFSAGQQASA AKLYQRYEDF
     LLHQYLIHDK RTRWCPRGCG YAVLASHKFR ACPRIECSNS DCPNAAFCYK CRGPWSTDGC
     DHICHKPNTA ASTSVGGGTE GTNNLIDNHR SLLSRLQQLF RLSGAVAAPM DAAVVVTVAG
     GGAQPKTEAD TSGDSKEGSG SQVRRLSERR FSTPAIPVQA ADAIGVNTDD EDDNGPVDQD
     ILEAEEKTNP YLKYYRSDVD ISKVELELPD NLNGQVKACP RCKTLLLKLD DGSCNHMSCF
     ICGCEFCWLC LREVRDTHFL SPTGCTFWGR KRWPFRRRIC AMLLAAFGTP FILAIVTALA
     MPGIAIGFPA YLVYKVGQNV KGRKWKRLLL KTLSFFGGLL VSPIIAGLVA LFGIPLVLIY
     VYIFMPITLF SELKVRLSTD STNAPDVDPE VGFKINWDRV GESASTSSST VTASVDTSAP
     DDSPKTTKAS KHAQARSTKS LEVLHERAAE FDP
//
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