ID A0A3S1BAW2_ELYCH Unreviewed; 552 AA.
AC A0A3S1BAW2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU367105};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU367105};
GN ORFNames=EGW08_013080 {ECO:0000313|EMBL:RUS79172.1};
OS Elysia chlorotica (Eastern emerald elysia) (Sea slug).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Sacoglossa; Placobranchoidea;
OC Plakobranchidae; Elysia.
OX NCBI_TaxID=188477 {ECO:0000313|EMBL:RUS79172.1, ECO:0000313|Proteomes:UP000271974};
RN [1] {ECO:0000313|EMBL:RUS79172.1, ECO:0000313|Proteomes:UP000271974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC2010 {ECO:0000313|EMBL:RUS79172.1};
RC TISSUE=Whole organism of an adult {ECO:0000313|EMBL:RUS79172.1};
RA Cai H., Li Q., Fang X., Li J., Curtis N.E., Altenburger A., Shibata T.,
RA Feng M., Maeda T., Schwartz J.A., Shigenobu S., Lundholm N., Nishiyama T.,
RA Yang H., Hasebe M., Li S., Pierce S.K., Wang J.;
RT "A draft genome assembly of the solar-powered sea slug Elysia chlorotica.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900,
CC ECO:0000256|RuleBase:RU367105};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU367105}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU367105}.
CC -!- SIMILARITY: Belongs to the Deltex family.
CC {ECO:0000256|ARBA:ARBA00009413, ECO:0000256|RuleBase:RU367105}.
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:RUS79172.1}.
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DR EMBL; RQTK01000467; RUS79172.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S1BAW2; -.
DR STRING; 188477.A0A3S1BAW2; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000271974; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR CDD; cd09633; Deltex_C; 1.
DR Gene3D; 3.30.390.130; -; 1.
DR Gene3D; 3.30.720.50; -; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR039396; Deltex_C.
DR InterPro; IPR039399; Deltex_C_sf.
DR InterPro; IPR039398; Deltex_fam.
DR InterPro; IPR004170; WWE-dom.
DR InterPro; IPR018123; WWE-dom_subgr.
DR InterPro; IPR037197; WWE_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12622; DELTEX-RELATED; 1.
DR PANTHER; PTHR12622:SF4; PROTEIN DELTEX; 1.
DR Pfam; PF18102; DTC; 1.
DR Pfam; PF02825; WWE; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00678; WWE; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF117839; WWE domain; 2.
DR PROSITE; PS50918; WWE; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU367105};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367105};
KW Notch signaling pathway {ECO:0000256|ARBA:ARBA00022976};
KW Reference proteome {ECO:0000313|Proteomes:UP000271974};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367105};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367105};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 1..77
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 78..165
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 347..404
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 156..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 552 AA; 61004 MW; B445101845DEFD7F CRC64;
MSVIVWGRNN DYRLLTPYPP EVSNSIEEIF AANKTTFKNL GRIQLGSFSP DYANYSIDTA
LMKQCQTDSG RRFAVKRSTM ESYSALAKGY IWEFEGDTPN HWFSYDVTTM LYLEEAYTKL
MKRKSKSRKA QHVVDMSRSF MPYVIDVEKM QQTRSGIGTV RNVRRQPLTQ PYKTGTLDSP
SDDDQGSLSD DLAQNIPTVT RSSLKRRNVA SNGATAQPTA ASVAASVGQQ SSAPASTQVQ
QPPATGAAAT AVKQAPAAAA TKKSLSKKRQ GSGSSRKKDK AAAKEREALP TEKNIKINTK
KGKKARPAEE VLQQYTTVIR VDDKNHREDD NDMDADEGTE ERENHDCCIC CDKLSGPSGY
GEGLACADVV VQLKRCAHKF HRFCLLEMYK STHKNESLQC PSCKLIYGEK TGTCPAGVMR
WDILSGSSVA GYEGYDTISV SYDIRSGVQG PEHPKPGQAF YTQGFPRVGY LPDTDKGRKV
CTFFFVFISS NLLMFTVGTS YTTGSSDVVT WNEIHHKTEL YGNYSGHGYP DASYLDNVIL
ELADHGVTED CL
//