ID I3J054_ORENI Unreviewed; 730 AA.
AC I3J054;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU367105};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU367105};
GN Name=LOC100690969 {ECO:0000313|Ensembl:ENSONIP00000002244.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000002244.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000002244.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR AlphaFoldDB; I3J054; -.
DR STRING; 8128.ENSONIP00000029603; -.
DR Ensembl; ENSONIT00000002244.2; ENSONIP00000002244.2; ENSONIG00000001793.2.
DR eggNOG; ENOG502QQ9M; Eukaryota.
DR GeneTree; ENSGT00940000157122; -.
DR HOGENOM; CLU_030422_4_0_1; -.
DR TreeFam; TF325526; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000005207; Linkage group LG3.
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; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12622; DELTEX-RELATED; 1.
DR PANTHER; PTHR12622:SF5; E3 UBIQUITIN-PROTEIN LIGASE DTX4; 1.
DR Pfam; PF18102; DTC; 1.
DR Pfam; PF02825; WWE; 2.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00678; WWE; 2.
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:UP000005207};
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..154
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 519..580
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 245..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..340
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 730 AA; 77657 MW; 636D890782CD5827 CRC64;
MLLASAVVVW EWLNEHGRWR PYSPAVCHHI EAVIRSDPRC GSVVLGQVDS RLSPYIIDLH
SMHQFRQDTG TLRPVRRSFY DPTSAPGQGW LWEWENDAGS WTAYDTEVGI AIQAARDRQQ
PWLDLAPLGF CYLIDFESMT QINGQTQRCR RIQRRSDLAY PLVSGPLPKS HHAWGPTSMP
GHGGLLGVDV SGVGMGIRMS SSGTGNGSAY PSGALPASAI TSLGQPCACQ QCMLLLSVKA
GTMSTAHTLG RRPPQTKPPS PKLSSLPIPG GSYSLTLPRP PTLSRSLSPH RTSMVGATGG
FTHSLSLLGS ATAGLSISST RPPPPPLPPP LPPPPPPSTT LSSSTTSTPH PSTSVSSLSI
SSTSTCTPSP SARVLGPVSS SGAAAAAACA APLPPRSSLA GLSRPALQRI AMAQSRALIA
SGVPTVPVKN LNGSSPVHPA LAGITGILMS AAGLPVCLTR PPKLVLHPPP VSKSDLKPVP
GLGHCCRKTT KKQARKGKTP EEVVKRYLQK VRNPPEEDCT ICMEALAGPS GYKGPGVGGI
SRAESVGRLA QCGHQYHLQC LVAMYNNGNK DGSLQCPTCK TIYGVKTGNQ PPGKMEYHVI
PHSLPGHPDC KTIRIIYNIP PGIQGPEHPN PGKPFTARGF PRHCYLPDSE KGRKVLRLLL
VAWDRRLIFS VGTSSTTGES DTVIWNEVHH KTEFGSNLTG HGYPDPGHLD NVLEELKAQG
ITEEECLPRD
//
