ID A0A8V5G798_MELUD Unreviewed; 851 AA.
AC A0A8V5G798;
DT 14-DEC-2022, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 1.
DT 28-JAN-2026, entry version 15.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=LOC101878782 {ECO:0000313|Ensembl:ENSMUNP00000028410.1};
OS Melopsittacus undulatus (Budgerigar) (Psittacus undulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Psittaciformes; Psittaculidae; Melopsittacus.
OX NCBI_TaxID=13146 {ECO:0000313|Ensembl:ENSMUNP00000028410.1, ECO:0000313|Proteomes:UP000694405};
RN [1] {ECO:0000313|Ensembl:ENSMUNP00000028410.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Gedman G., Mountcastle J., Haase B., Formenti G., Wright T., Apodaca J.,
RA Pelan S., Chow W., Rhie A., Howe K., Fedrigo O., Jarvis E.D.;
RT "Melopsittacus undulatus (budgerigar) genome, bMelUnd1, maternal haplotype
RT with Z.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMUNP00000028410.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSMUNP00000028410.1}
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; A0A8V5G798; -.
DR Ensembl; ENSMUNT00000029880.1; ENSMUNP00000028410.1; ENSMUNG00000013963.2.
DR Proteomes; UP000694405; 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; 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:UP000694405};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT REGION 283..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..352
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..408
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 851 AA; 95633 MW; 7571D940440643F5 CRC64;
RATPRGGPRR TGAAMAASAG PADGPCVLCC GELDVVALGR CDHPICYRCS VRMRALCGVR
YCAVCREELA QVVFGRKLTS FSTIALNQLQ HEKKYDIYFT DGDVYALYRK LLQHKCSLCP
DVKPFNTFAD LEQHMRKQHE LFCCKLCVKH LKIFTYERKW YSRKDLARHR IHGDPDDTSH
RGHPLCKFCD ERYLDNDELL KHLRRDHYFC HFCDSDGAQE YYSDYEYLRE HFREKHFLCE
EGRCSTEQFT HAFRTEIDYK AHKTACHSKN RAEARQNRQI DLQFNYAPRH QRRNEGVVSG
EDYEEVDRYN RQARSARLGG RGSQQNRRGS WRYKREEEDR DIAAAVRASV AAKRQEERKR
VEDKEDSSSR GRKEDVRDSE VSSQPAVVKL KEEDFPSLSS SAAPTISSGM SLTYTTTAKK
AAFQEEDFPA LVSKMRPNNK TVTNITSAWN NGSSKSVVKA ISNPCVNQTA KKPSSSLNST
KGSKKSNKLP QSDDEDSGSG LTTQEIRNTP TMVDVSSLLA ASTSQTFTKV SKKKKVGVEK
QSPSSPRLSQ DTAFPKASTE KLPEAEQTSS ASSSALPNPD RPTAVVNGHS EKPLVVCSTP
KEPPGLKKPT VTNKCPLPQE DFPALGSSGS ARMPPPPGFN TVVLLKNPPP PPGLSVPVSK
PPPGFAVIPS TNITDPVTTD TSGLPNSRPK PRHGSYLIPE NFQQRNIQLI QSIKEFLQSD
ESKFNKFKTH SGQFRQGLIS AAQYYRSCRE LLGENFRKIF KELLVLLPDT AKQQELLSAH
NDFRLKEKQS SSKPKKNKRN VWQTDSNSEL DCSICPTCQQ VLTPQDVGTH KALHMEDEEF
PSLQAISRII S
//
