ID A0A8C3CYV3_CAIMO Unreviewed; 856 AA.
AC A0A8C3CYV3;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 18.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS Cairina moschata (Muscovy duck).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Cairina.
OX NCBI_TaxID=8855 {ECO:0000313|Ensembl:ENSCMMP00000027730.1, ECO:0000313|Proteomes:UP000694556};
RN [1] {ECO:0000313|Ensembl:ENSCMMP00000027730.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Vignal A., Thebault N., Warren W.C.;
RT "Common duck and Muscovy duck high density SNP chip.";
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCMMP00000027730.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSCMMP00000027730.1}
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; A0A8C3CYV3; -.
DR Ensembl; ENSCMMT00000030254.1; ENSCMMP00000027730.1; ENSCMMG00000016950.1.
DR Proteomes; UP000694556; Chromosome 15.
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:UP000694556};
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 22..62
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 283..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..348
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 856 AA; 96406 MW; E1047430D0EA281B CRC64;
MAASGPGPAS ASGSGCGAEG PCVLCCGELD VVALGRCDHP ICYRCSVRMR ALCGVRYCAV
CREELRQVVF GRKLTSFSTI ALSQLQHEKK YDIYFMDAEV YALYRKLLQH ECFLCPDLKP
FNTFADLEQH MRKQHELFCC KLCVKHLKIF TYERKWYTRK DLARHRIHGD PDDTSHRGHP
LCKFCDERYL DNDELLKHLR RDHYFCHFCD SDGAQEYYSD YEYLREHFRE KHFLCEEGRC
STEQFTHAFR TEIDYKAHKT ACHSKNRAEA RQNRQIDLQF TYAPRHQRRT EGVIGGEDYE
EVDRYNRQGR SGRLGGRGSQ QNRRGSWRYK REEEDRDVAA AVRASVAAKR QEEKKRVEDK
EDSSSRGKKE DLRDSEGSSS KHVPKSSNET PGYSAQLAAV KLKEEDFPSL SSSAAPTISS
GMSLTYTATA KKTAFQEEDF PALVSKMRPN SKTITNITSA WNNGSSKNVV KAIGSPCVNQ
IAKKTSSLNS TKGSKKSNKL CQSDDEDNGS GLTTQEIRNT PTMFDVSSLL AASTSQTFTK
VSKKKRMGVE KQRPSSPHQF QETAFPKSSI EKLPEAEQTP NASSALHAPD RFTTVMNGHS
EKSLAICSTP KEPPGLKKPT VTNQCPLPQE DFPALGSSGS VRMPPPPGFN TVVLLKSPPP
PPGLSVPVSK PPPGFAVIPA TNISEPVTTS LKEPKSCHGS YLIPENFQQR NIQLIQSIKE
FLQSDESKFN KFKTHSGQFR QGLISAAQYY KSCRELLGDN FKKIFNELLV LLPDTVKQQE
LLSAHNDFRI KEKQSSNKSK KNKKHVWQTD SNSDLDCCIC PTCKQVLTQQ DIVTHKALHI
EDEEFPSLQA ISRIIS
//
