ID A0A8N5ETN5_GEOFO Unreviewed; 850 AA.
AC A0A8N5ETN5;
DT 03-AUG-2022, integrated into UniProtKB/TrEMBL.
DT 03-AUG-2022, sequence version 1.
DT 28-JAN-2026, entry version 18.
DE SubName: Full=E3 ubiquitin-protein ligase ZNF598 {ECO:0000313|RefSeq:XP_030916930.1};
GN Name=ZNF598 {ECO:0000313|RefSeq:XP_030916930.1};
OS Geospiza fortis (Medium ground-finch).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Thraupidae; Geospiza.
OX NCBI_TaxID=48883 {ECO:0000313|Proteomes:UP000504602, ECO:0000313|RefSeq:XP_030916930.1};
RN [1] {ECO:0000313|RefSeq:XP_030916930.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
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DR RefSeq; XP_030916930.1; XM_031061070.1.
DR AlphaFoldDB; A0A8N5ETN5; -.
DR GeneID; 102039193; -.
DR CTD; 90850; -.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP000504602; Unplaced.
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; IPR013087; Znf_C2H2_type.
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; PF25447; RING_ZNF598; 1.
DR Pfam; PF23208; zf_C2H2_ZNF598; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000504602}.
FT DOMAIN 158..179
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS00028"
FT REGION 256..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..300
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..324
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..567
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 850 AA; 95910 MW; 2E21BCB339204736 CRC64;
MDKIIQKFFE EKTATRHQDL KKRIIASSDF EEPRKLIYKL KGEVVFGRKL PSFSSIALQQ
LQHEKKYDIY FMDAEVYALY RKLLQHECPL CPDAKPFNTF ADLEQHMRKQ HELFCCKLCV
KHLKIFTYER KWYSRKDLAR HRIHGDPDDT SHRGHPLCKF CDERYLDNDE LLKHLRRDHY
FCHFCDSEGA QEYYSDYEYL REHFREKHFL CEEGRCSSEQ FTHAFRTEID YKAHKSACHS
KSRAEARQNR HIDLQFTYTP RHPRRTDGVV GGDDYEEVDR FNRQGRASRL SSRGSQQNRR
GSWRYKREEE DRDVAAAVRA SVAAKRQEEK KRVEDKEEGS SSRGRKEDLR DPDVLGSKRV
PKSSNDVTEA AANGVLSQED FPAIGSAAGP LQGSAQPALV KLKDEDFPSL SSSAAPTISS
GMSLMYTATA RKAAFQEEDF PALVSKVKPT NRTVTHITSA WNNGSSKNVV KAMCSPCVNQ
PAKKPSLNTS KGNKKSNKLC ESDDEDGSGG LTTQEIRSTP TMFDVSSLLA ASTSQTFTKV
GKKKKMGVEK QSPLSPRPPQ EPPLPRPGPE KPPEAEQPCR AFPAAHGPLV NGHTEKPSAA
CAAPKEPPGL KKPPVTNKCP LPQEDFPALG SSGSARMPPP PGFNSVVLLK NPPPPPGLSV
PVSKPPPGFA VIPSSTISEP VTTALKEPKS CHGSYLIPEN FQQRNIQLIQ SIKEFLQSDE
SKFNKFKTHS GQFRQGLISA AQYYKSCREL LGENFKKIFK ELLVLLPDTA KQQELLSAHN
DFRIKEKQSS NKPKKNKKNV WQTDSPADLD CYICPTCRQV LTQQDVVTHK ALHLEDEEFP
SLQAISRIIS
//
