ID   A0A8C9Y582_SANLU        Unreviewed;       829 AA.
AC   A0A8C9Y582;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   28-JAN-2026, entry version 19.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS   Sander lucioperca (Pike-perch) (Perca lucioperca).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Percoidei; Percidae; Luciopercinae; Sander.
OX   NCBI_TaxID=283035 {ECO:0000313|Ensembl:ENSSLUP00000019920.1, ECO:0000313|Proteomes:UP000694568};
RN   [1] {ECO:0000313|Ensembl:ENSSLUP00000019920.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSSLUP00000019920.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2025) 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   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the ZNF598/HEL2 family.
CC       {ECO:0000256|ARBA:ARBA00035113}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; A0A8C9Y582; -.
DR   Ensembl; ENSSLUT00000020557.1; ENSSLUP00000019920.1; ENSSLUG00000009213.1.
DR   GeneTree; ENSGT00390000014178; -.
DR   Proteomes; UP000694568; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043022; F:ribosome binding; IEA:TreeGrafter.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:TreeGrafter.
DR   GO; GO:0072344; P:rescue of stalled ribosome; IEA:InterPro.
DR   CDD; cd16615; RING-HC_ZNF598; 1.
DR   InterPro; IPR057634; PAH_ZNF598/HEL2.
DR   InterPro; IPR041888; RING-HC_ZNF598/HEL2.
DR   InterPro; IPR044288; ZNF598/HEL2.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   InterPro; IPR059042; Znf_C2H2_ZNF598.
DR   InterPro; IPR001841; Znf_RING.
DR   PANTHER; PTHR22938:SF0; E3 UBIQUITIN-PROTEIN LIGASE ZNF598; 1.
DR   PANTHER; PTHR22938; ZINC FINGER PROTEIN 598; 1.
DR   Pfam; PF23202; PAH_ZNF598; 1.
DR   Pfam; PF25447; RING_ZNF598; 1.
DR   Pfam; PF23208; zf_C2H2_ZNF598; 1.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000694568};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          13..53
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          279..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          449..490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          507..607
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        453..465
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        466..479
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        543..563
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   829 AA;  93444 MW;  2D435864C50B25D9 CRC64;
     MASTTTKETE KHCVLCCQEV NIFALGKCDH PVCYRCSTKM RVLCDQKYCA VCREELDKVV
     FVKKLEAFSS LPYQQFPCEK KHNIYFCDEK IFAQYRHLLL PECLRCSEPK VFSKFEELEQ
     HMRKQHELFC CKLCTKHLKI FSHERKWYNR KELARHRLHG DPDDTSHRGH PLCKFCDDRY
     LDNDELLKHL RRDHYFCHFC DADGSQEYYS DYPYLSEHFR ESHYLCEEGR CATEQFTHAF
     RSEIDYKAHK AAAHSKNRAE ARQNRHIDLQ FNYAPRQQRR NEGTVTGEDY EEMRQTRGGR
     GRPHAGQKSW RYIRDEEDRE LAAAMRASMA KHRQEERGAM QERGAMQERG AMHERGAMHE
     RIAMHERGAM HERGAMHERG AMHERGPCHV PLTAAHAALK EDDFPSLSAV SVASPMTPAY
     SAQPKKNSSF QEEDFPALVS KIRPLKHAAG TKSAWSNHTA VTKPNTQPPP SSRPPPPPLS
     TSSSGGGVTQ QEFRSVPTMM DISSLLTVKG GKSKPSAVTT NPPNPTPNTP PTSKASKKKK
     TQKNTADPST SVSSVSGTTQ TVVANSVETA AQKENVPEKS WNKPPSSAAT APLMSGLANG
     HPEKSPPISK EAVAITLHPK PDPPLDQEEE FPALMTKNPP PGTALHNIHT IPSRAGPPKV
     SSSGYLVPED FHQRNLELIQ SIRKYLHNDE SKFNQFKNFS AQFRQSVISA VQYHSSCKDL
     LGDDFNRIFN ELLVLLPDTG KQQELLTAQA DCKALEKQSG TGGGKKNKNK KNAWQMPTAL
     ANAAAELDCQ VCPTCRQVLA PKDFNSHKTL HTGENEEFPS LQSISRIIS
//