ID A0A8C3PR58_9CHAR Unreviewed; 879 AA.
AC A0A8C3PR58;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS Calidris pygmaea (Spoon-billed sandpiper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Charadriiformes; Scolopacidae;
OC Calidris.
OX NCBI_TaxID=425635 {ECO:0000313|Ensembl:ENSCPGP00000020996.1, ECO:0000313|Proteomes:UP000694419};
RN [1] {ECO:0000313|Ensembl:ENSCPGP00000020996.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCPGP00000020996.1}
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; A0A8C3PR58; -.
DR Ensembl; ENSCPGT00000022997.1; ENSCPGP00000020996.1; ENSCPGG00000014659.1.
DR Proteomes; UP000694419; 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:UP000694419};
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 21..61
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 306..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..347
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..601
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 879 AA; 98356 MW; FCF3EF58812A300E CRC64;
MAASASSASG AAAAGPADGS CVLCCGELEV VALGRCDHPI CYRCSVRMRA LCGVRYCAVC
REELGQVVFG RKLTSFSTIA LNQLQHEKKY DIYFMDGEVY ALYRKLLQHE CPLCPDAKPF
NTFADLEQHM RKQHELFCCK LCVKHLKIFT YERKWYSRKD LARHRIHGDP DDTSHRGHPL
CKFCDERYLD NDELLKHLRR DHYFCHFCDS DGAQEYYSDY EYLREHFREK HFLCEEGRCS
TEQFTHAFRT EIDYKAHKTA FHSKNRAEAR QNRQIDLQFN YAPRHQRRNE GVIGGEDYEE
VDRYNRQGRA GRLGGRGSQQ NRRGSWRYKR EEEDRDVAAA VRASVAAKRQ EEKKRVEDKD
DSSSSRGKKE DLRDSDVLSS KRLPRSSNDV TEAAANGALS QDDFPAIGSA VGPLQGSAQL
AAVKLKEEDF PSLSSSPAPT ISSGISLTYT ATAKKTAFQE EDFPALVSKM RPNNKTVTNI
TSAWNNGSSK NVVKAISNPC VNQIAKKPSS LNSTKVSKKS NKLSQSDDED GGSGLTTQEI
RNTPTMFDVS SLLAASTSQT FTKVSKKKKM GVEKQRPSSP HLSQETSLPR SSTEKLPEAE
RTSNASSALH APDRSTTVMN GHSEKSLAIC STPKEPPGLK KPTVTNKCPL PQEDFPALGS
SGSARMPPPP GFNTVVLLKS PPPPPGLSVP VSKPPPGFAV IPSTNISEPV TTSLKEPKSS
HGSYLIPENF QQRNIQLIQS IKEFLQSDES KFNKFKTHSG QFRQGLISAA QYYKSCRELL
GDNFKKIFNE LLVLLPDTVK QQELLSAHND FRIKEKQSSN KSKKNKKNVW QTDSNSDLDC
YICPTCKQVL TQQDVVTHKA LHIEDEEFPS LQAISRIIS
//
