ID A0A3B4Y2P7_SERLL Unreviewed; 749 AA.
AC A0A3B4Y2P7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU367105};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU367105};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000025110.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000025110.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A3B4Y2P7; -.
DR STRING; 1841481.ENSSLDP00000025110; -.
DR Ensembl; ENSSLDT00000025896.1; ENSSLDP00000025110.1; ENSSLDG00000019546.1.
DR GeneTree; ENSGT00940000157122; -.
DR OrthoDB; 5487971at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000261360; Unplaced.
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 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 2..84
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 85..161
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 538..599
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 239..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..351
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 749 AA; 79820 MW; BA608C584203714A CRC64;
MASGNNMLLA SAVVVWEWMN EHGRWRPYSP AVSHQIEAAI RSSDPRGGSV VLGQVDSRLS
PYIIDLQSMH QFRQDTGTIR PVRRSFYDPA SAPGQGWQWE WENDAGTWTP YDMEVAIAIE
SAHNRQQPCL DLTPLGFCYF IDYQNMTQVN RQSQRCRRIQ RRADMAYPLV SGPLPVPKGG
GVGASGGLTG ALLGVGVSGA SMGIGSVYPN GGLLATGLGQ PCSCQQCMLV LSVKTNTGRA
GGGAAGLQTL GRRSLTMQRP KNSASKPLSP SKSATLGRGQ PQNSSYYQTL PHGLAISKNT
ASPRRNAQLF AQSLAALTTC TSSLGISSSS VRPPPPSLPP PQPPSSNPNL NPPSIPAKHS
SSSAGESVPT GTLITPASNV TTPPSPVPSP SPMVMKPQRM VSSTATVCHA PLPQRSSLAG
LSRPALQRIA MAQSRALIAS GVPTVPVKNL SGSSPVHPAL AGITGILMSA AALPVCLTRP
PKLVLHPPPV SKSDIKPVPG FGHCCRKTTK KQARKGKTPE EVVKKYLQKV KSPPEEDCTI
CMEPLGGPSG YKGPGVGPVS RADSVGRLAQ CGHQYHFQCL VAMYNNGNKD GSLQCPTCKT
IYGVKTGNQP AGKMEYHVIP HSLPGHPDCK TIRIIYNIPP GIQGPEHPNP GKPFTARGFP
RHCYLPDSEK GRKVLRLLLV AWDRRLIFSV GTSSTTGESD TVIWNEVHHK TEFGSNLTGH
GFPDPGHLDN VLEELRAQGI TEDDGLMEK
//
