ID A0A8C3NPV3_GEOPR Unreviewed; 874 AA.
AC A0A8C3NPV3; A0A8U8CLC3;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2023, sequence version 2.
DT 28-JAN-2026, entry version 20.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS Geospiza parvula (Small tree-finch) (Camarhynchus parvulus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Thraupidae; Camarhynchus.
OX NCBI_TaxID=87175 {ECO:0000313|Ensembl:ENSCPVP00000022987.2, ECO:0000313|Proteomes:UP000694382};
RN [1] {ECO:0000313|Ensembl:ENSCPVP00000022987.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Enbody D E., Pettersson E M.;
RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCPVP00000022987.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSCPVP00000022987.2}
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; A0A8C3NPV3; -.
DR Ensembl; ENSCPVT00000023998.2; ENSCPVP00000022987.2; ENSCPVG00000016416.2.
DR Proteomes; UP000694382; Chromosome 14.
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.
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:UP000694382};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT REGION 299..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..319
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..343
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..582
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 874 AA; 97982 MW; 4C66510E76DF9E19 CRC64;
MVGRRSSPRS VVRAGRRGAE AAMAAMAGAG PGPAEGPCVL CCGELDVVAL GRCEHPICYR
CSVRMRALCG VRYCAVCREE LRQVVFGRKL PSFSSIALQQ LQHEKKYDIY FMDAEVYALY
RKLLQHECPL CPDAKPFNTF ADLEQHMRKQ HELFCCKLCV KHLKIFTYER KWYSRKDLFC
DERYLDNDEL LKHLRRDHYF CHFCDSEGAQ EYYSDYEYLR EHFREKHFLC EEGRCSSEQF
THAFRTEIDY KAHKSACHSK SRAEARQNRH IDLQFTYTPR HPRRTDGVVG GDDYEEVDRF
NRQGRASRLS SRGSQQNRRG SWRYKREEED RDVAAAVRAS VAAKRQEEKK RVEDKEEGSS
SRGRKEDLRD PDVLGSKRVP KRSGELWVCA VPWGSAASVT PVLSLPHSSA QPALVKLKDE
DFPSLSSSAA PTISSGMSLM YTATARKAAF QEEDFPALVS KVKPTNRTVT HITSAWNNGS
SKNVVKAMCS PCVNQPAKKP SLNTSKGNKK SNKLCESDDE DGSGGLTTQE IRSTPTMFDV
SSLLAASTSQ TFTKVGKKKK MGVEKQSPLS PRPPQEPPLP RPGPEKPPEA EQPCRAFPAA
HGPLVNGHTE KPSAACAAPK EPPGLKKPPV TNKCPLPQED FPALGSSGSA RMPPPPGFNS
VVLLKNPPPP PGLSVPVSKP PPGFAVIPSS TISEPVTTAL KEVTSGLFQH RPKSCHGSYL
IPENFQQRNI QLIQSIKEFL QSDESKFNKF KTHSGQFRQG LISAAQYYKS CRELLGENFK
KIFKELLVLL PDTAKQQELL SAHNDFRIKE KQSSNKPKKN KKNVWQTDSP ADLDCYICPT
CRQVLTQQDV VTHKALHLED EEFPSLQAIS RIIS
//
