ID A0AAD9EPV2_DISEL Unreviewed; 461 AA.
AC A0AAD9EPV2;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 8.
DE SubName: Full=E3 ubiquitin-protein ligase ZNF598 {ECO:0000313|EMBL:KAK1876993.1};
GN ORFNames=KUDE01_002312 {ECO:0000313|EMBL:KAK1876993.1};
OS Dissostichus eleginoides (Patagonian toothfish) (Dissostichus amissus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Notothenioidei; Nototheniidae; Dissostichus.
OX NCBI_TaxID=100907 {ECO:0000313|EMBL:KAK1876993.1, ECO:0000313|Proteomes:UP001228049};
RN [1] {ECO:0000313|EMBL:KAK1876993.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DE {ECO:0000313|EMBL:KAK1876993.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAK1876993.1};
RA Park H.;
RT "Chromosome-level genome of Chaenocephalus aceratus.";
RL Submitted (APR-2023) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAK1876993.1}.
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DR EMBL; JASDAP010000027; KAK1876993.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AAD9EPV2; -.
DR Proteomes; UP001228049; Unassembled WGS sequence.
DR GO; GO:0043022; F:ribosome binding; IEA:TreeGrafter.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:TreeGrafter.
DR GO; GO:0072344; P:rescue of stalled ribosome; IEA:InterPro.
DR InterPro; IPR057634; PAH_ZNF598/HEL2.
DR InterPro; IPR044288; ZNF598/HEL2.
DR InterPro; IPR059042; Znf_C2H2_ZNF598.
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; PF23208; zf_C2H2_ZNF598; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP001228049}.
FT DOMAIN 303..379
FT /note="ZNF598/HEL2 PAH"
FT /evidence="ECO:0000259|Pfam:PF23202"
FT DOMAIN 417..451
FT /note="ZNF598 C2H2 zinc finger"
FT /evidence="ECO:0000259|Pfam:PF23208"
FT REGION 54..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..249
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 461 AA; 49128 MW; 0C94DA3EA5423D26 CRC64;
MKSDNPGDGE DDFPALGGGA ALTIVKPAPA TLSTPRAALK EDDFPSLSAV AVSSPMTPAY
SAQPKKSSSF QEEDFPALVS KIRPLRNAAG TKSAWSSHAA KMKVGVKSAS SRSPPSSDDE
KGGVKQQQVF RSVPTMSDIS SLLTVKGGNS KAPTKENVPE KIRNKPPPSN AAVTATMTSV
LSNGHQEKSP PVSKKEAVAV TPHPKVDLPL DQEEDFPALM TKNPPPGFKS SFKSSFPMKT
SAPAPASSAM PPPPPGLGLS ATKPPPGFTG IPLNSNVVEP APTEVNPPTK VQSSGYMVPE
DFHERNLQLI ASIKKYLYND ESKFNQFKNL SAQFRQSVIS AVQYHSSCKE LLGDDFHRIF
NELLVLLPDT GKQQELLAVQ GDCRALERQA VAGGGGKKNK NKKNAWQTPS SAANVAAELD
CQVCPTCRQV LAPKDFNSHK TLHTGEAEEF PSLQSISRII S
//
