ID A0A6P7YVT7_9AMPH Unreviewed; 878 AA.
AC A0A6P7YVT7;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 28-JAN-2026, entry version 23.
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_030067449.1};
OS Microcaecilia unicolor.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Gymnophiona; Siphonopidae; Microcaecilia.
OX NCBI_TaxID=1415580 {ECO:0000313|Proteomes:UP000515156, ECO:0000313|RefSeq:XP_030067449.1};
RN [1] {ECO:0000313|RefSeq:XP_030067449.1}
RP IDENTIFICATION.
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_030067449.1; XM_030211589.1.
DR AlphaFoldDB; A0A6P7YVT7; -.
DR FunCoup; A0A6P7YVT7; 1346.
DR GeneID; 115475671; -.
DR KEGG; muo:115475671; -.
DR CTD; 90850; -.
DR InParanoid; A0A6P7YVT7; -.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP000515156; Chromosome 8.
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; IPR056437; Znf-C2H2_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; PF23230; zf-C2H2_13; 1.
DR Pfam; PF23208; zf_C2H2_ZNF598; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
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:UP000515156};
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 10..50
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 249..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..336
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..516
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..589
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..637
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 878 AA; 99063 MW; 99DBED28FED59256 CRC64;
MAFRPPERSC VLCCQELEVF AVGKCDHYIC FRCSTKMRVL CEQRYCAVCR EELDKVAFVK
KLSPFSTIAT HQLQCEKKYG IYFADGKVFS LYRRLLQHEC SLCPETRPFH SFQDLEQHMR
KQHELFCCKL CVKYLKNFTY ERKWYSRKDL ARHRIHGDSD DTSHRGHPLC KFCDERYLDN
DELLKHLRRD HYFCHFCDSD GAQDYYSDYD YLREHFRETH FLCEEGRCVS EQFTHAFRTE
IDYKAHKTSF HSKNRAEARQ NRQIDLQFNY TPRHQRRNEG VVSREDFEEV DRYNRQQGRT
GRGGSRGGQN RRGSWRYKRE EEDREIAAAV RASVAARRQE ERKQGDNKED GNKPRRDDGR
DPEEGSSSKK MSRPPQDTSA AKEVVKPIGN AGTLSQEDSP AFGSMVAGPL PSSIESVSPK
LKEEDFPSLS TSVSSAVPTV STGLSVSYAS ARKSSAFQEE DFPALVSKHK PNKTVSTITS
AWANGSSKNM VKTASSNGIS PNPPMKKSSS SGSKVSQKSR KTPVSEEEDD EEGKSTLEIK
NTPTMFDISS LLTSSSAQTV AKLGKKKRMG SEKKSCSSSP PAPKEAASSS HKENVLEAER
TPSPQAVSIL SDKSNTVANG HTEKKGTDTS KSKEPPGLKK AVVVYQCPLP DEDFPALENH
TVSRTPPPGF TSAASLKSCH PPPGLSAHLS NPPPGFTTIP PKSTSSDSPH IPAKEPSPSM
GSYLVPENFQ QRNIHLIQSI KDFLQSDESR FNEFKTYSGK FRQGLISAAE YYRNCRDLLG
ENFKKVFNEL LVLLPDTAKQ QELLSAHNDF RIEEKQTSNR GKKNRNVWQT NSTPSELDFS
ICPSCKQVVA EKDAAAHKTL HVEDDEFPSL QAIRRIIS
//
