ID A0A6J2HVN7_9PASS Unreviewed; 872 AA.
AC A0A6J2HVN7;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 28-JAN-2026, entry version 24.
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|RefSeq:XP_027591895.2};
OS Pipra filicauda (Wire-tailed manakin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Pipridae; Pipra.
OX NCBI_TaxID=649802 {ECO:0000313|Proteomes:UP000504627, ECO:0000313|RefSeq:XP_027591895.2};
RN [1] {ECO:0000313|RefSeq:XP_027591895.2}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_027591895.2};
RG RefSeq;
RL Submitted (AUG-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 RefSeq; XP_027591895.2; XM_027736094.2.
DR AlphaFoldDB; A0A6J2HVN7; -.
DR GeneID; 113995713; -.
DR CTD; 90850; -.
DR Proteomes; UP000504627; 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:UP000504627};
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 16..56
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 278..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..342
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 872 AA; 97525 MW; BD13B00D9F67A25F CRC64;
MAAMAGAGPG PAEGPCVLCC GELDVLALGR CEHPICYRCS VRMRALCGVR YCAVCREELR
QVVFGRKLPS FSSIALHQLQ HEKKYDIYFM DGEVYALYRK LLQHECSLCP DAKPFNTFAD
LEQHMRKQHE LFCCKLCVKH LKIFTSERKW YSRKDLARHR IHGDPDDTSH RGHPLCKFCD
ERYLDNDELL KHLRRDHYFC HFCDSDGAQE YYSDYEYLRE HFREKHFLCE EGRCSTEQFT
HAFRTEIDYK AHKTACHSKS RAEARQNRHI DLQFTYTPRH PRRNEGVVGA EDYEEVDRYN
RQGRTGRLNG RGSQQNRRGS WRYKREEEDR DVAAAVRASV AAKRQEEKKR VEDKEDGGSS
RGKKEDLRDP DVLGSKRVPK APNDVAAAAN GALSQDDFPA IGSPAGPLQG SAQPALVKLK
EEDFPSLSSS AAPTISSGMS LTYTATAKKA AFQEEDFPAL VSKMKPNNKT VTNITSAWNN
GSSKNVVKAI TNPCVSQPAK KPSLNTSKGS KKSNKLCESD DEDGGGGLTT QEIRNTPTMF
DVSSLLAAST SQTFTKVGKK KKVGVEKQRP SSPRPSPDTA FPRPCAEKPP EAEQPSRVFP
APHGPDRPTA VMNGHSEKSS AVCGTPKEPP GLKKPTVTNK CPLPQEDFPA LGSSGSARMP
PPPGFNSVVL LKNPPPPPGL SVPVSKPPPG FAVIPSTNIS EPVTTALKEP KPCHGSYLIP
ENFQQRNIQL IQSIKEFLQS DESKFNKFKT HSGQFRQGVI SAAQYYKSCR ELLGENFKKI
FKELLVLLPD TVKQQELLSA HNDFRVKEKQ SSNRPKKNKK NVWQVDSPVD LDCYICPTCK
QVLTQQDVVT HKALHIEDEE FPSLQAISRI IS
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