ID A0A1S3RLY3_SALSA Unreviewed; 625 AA.
AC A0A1S3RLY3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU367105};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU367105};
GN Name=LOC106603780 {ECO:0000313|RefSeq:XP_014053341.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014053341.1};
RN [1] {ECO:0000313|RefSeq:XP_014053341.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014053341.1};
RG RefSeq;
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 RefSeq; XP_014053341.1; XM_014197866.1.
DR AlphaFoldDB; A0A1S3RLY3; -.
DR STRING; 8030.ENSSSAP00000059978; -.
DR PaxDb; 8030-ENSSSAP00000059978; -.
DR KEGG; sasa:106603780; -.
DR OMA; DAPEEDC; -.
DR OrthoDB; 5487971at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000087266; Chromosome ssa04.
DR Bgee; ENSSSAG00000055664; Expressed in semen and 15 other cell types or tissues.
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:SF21; E3 UBIQUITIN-PROTEIN LIGASE DTX2-RELATED; 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:UP000087266};
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 24..112
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 113..189
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 401..463
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 625 AA; 66803 MW; D7DFDF2683DCCAD7 CRC64;
MATASSSCVG INGSRNGPTN STPTLVTPGQ SQPMVVVWEW QDDLGFWRPY SGQVSGYIEQ
YFSSPRGHRG GGPGSTSISL GQSDPSLSPY LIDIPSLNQF RQDTGKTRSV RRQLFAQSSG
LGSGVYWEWA NDEGGWTPYE TRTSILLEHS YLARQATADM ASHGYNYIVD LTALAQVNKA
TGFRRQVRRQ GNFPYPLASG ASVIHSGPAC SCHQCLSHSC TGPMPSRSRH SFSSGQLSRP
SFQGPSRAAG AHPTSVYSPY PRRPLSVGGM AWGGPWPPTP SASQFPGPPL SYPTSANGLS
VPAIPLQRNG STSVSSALAG MASILMSAVG LGVRFTSAPL PHPSSAPPPP SSTSRHAGSK
THSSSSVRTA KRQHRTAPAQ KPEDVIHRYM EEVASAQDED CIICMDRLSC PSDYAVASEG
AQSIPPGAVG KFTKCGHTLH MLCMLAMYNN GTKDGSLQCP SCKTIYGEKT GTQPKGKMEI
YSIAQSLPGH PACGTIQIIY SIPPGIQGPE HPNPGQPYTC RGFPRFCFLP DNDKGRKVLE
LLKVAWTRRL IFTVGTSSTT GEPDTVVWNE IHHKTEMMSN VSGHGYPDPN YLENVLSELS
SQGVTDDCLV KQEGPSQGGA SNSGL
//
