ID   A0AAY4D709_9TELE        Unreviewed;       557 AA.
AC   A0AAY4D709;
DT   05-FEB-2025, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2025, sequence version 1.
DT   28-JAN-2026, entry version 5.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=ZNF598 {ECO:0000313|Ensembl:ENSDCDP00010041188.1};
OS   Denticeps clupeoides (denticle herring).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Clupei; Clupeiformes;
OC   Denticipitoidei; Denticipitidae; Denticeps.
OX   NCBI_TaxID=299321 {ECO:0000313|Ensembl:ENSDCDP00010041188.1, ECO:0000313|Proteomes:UP000694580};
RN   [1] {ECO:0000313|Ensembl:ENSDCDP00010041188.1, ECO:0000313|Proteomes:UP000694580}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Wellcome Sanger Institute Data Sharing;
RL   Submitted (JUN-2020) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSDCDP00010041188.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSDCDP00010041188.1}
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}.
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DR   AlphaFoldDB; A0AAY4D709; -.
DR   Ensembl; ENSDCDT00010051134.1; ENSDCDP00010041188.1; ENSDCDG00010026184.1.
DR   GeneTree; ENSGT00390000014178; -.
DR   Proteomes; UP000694580; Chromosome 7.
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:UP000694580};
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          339..369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        339..365
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   557 AA;  65079 MW;  DC0DBDF5EAD46248 CRC64;
     MESTSARETE RVCVLCCQDI DIFALGKCDH PVCYRCSTKM RVLCEQRYCA VCRVELDKVI
     FVKTLRPFAS IACEQLQCER KHDIYFSDGK IYAQFRRILL PECPRCPEQK VFSKFEELEQ
     HMRKQHELFC CKLCVKHLKI FSHERKWYNR KDLARHRTQG DPDDTSHRGH PLCKFCDDRY
     LDNDELLKHL RRDHYFCHFC DADGAQEYYS DYQYLREHFR DSHYLCEEGR CSTEQFTHAF
     RTEIDYKAHK AAAHSKNRAE ARQNRQIDLQ FTYAPRQQRR YEGLVGGEDF EEFDRLNRRP
     GRGRAPGTQQ NMRKSWRYNR EEEDRDVAAA LQASLAFRRQ EEKGVAQERN ISKPREAPDP
     EETRSGRIAA KPPSDLLSVC CCVNSFSINR SVQPLGTFLA PENFQQRNMD LIQSIKNFLL
     NDESKFNEFK TYSGQFRQGV ISAAQYHRSC QELLGDNFSR VFNELLVLLP DTQKQQELLT
     AHGDSKALEK QQGTAKAKKN KKKVWQTVSG SLGSELDCQV CPTCRQVLAM KDFNYHKALH
     IGDDDFPSLQ SISKVIS
//