ID A0A034WAZ3_BACDO Unreviewed; 900 AA.
AC A0A034WAZ3;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 28-JAN-2026, entry version 45.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=ZN598 {ECO:0000313|EMBL:JAC50973.1};
GN Synonyms=LOC105222429 {ECO:0000313|RefSeq:XP_011198063.1};
OS Bactrocera dorsalis (Oriental fruit fly) (Dacus dorsalis).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC Tephritidae; Bactrocera; Bactrocera.
OX NCBI_TaxID=27457 {ECO:0000313|EMBL:JAC50973.1};
RN [1] {ECO:0000313|EMBL:JAC50973.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Punador {ECO:0000313|EMBL:JAC50973.1};
RX PubMed=25348373; DOI=10.1186/1471-2164-15-942;
RA Geib S.M., Calla B., Hall B., Hou S., Manoukis N.C.;
RT "Characterizing the developmental transcriptome of the oriental fruit fly,
RT Bactrocera dorsalis (Diptera: Tephritidae) through comparative genomic
RT analysis with Drosophila melanogaster utilizing modENCODE datasets.";
RL BMC Genomics 15:942-942(2014).
RN [2] {ECO:0000313|RefSeq:XP_011198063.1}
RP IDENTIFICATION.
RC STRAIN=Punador {ECO:0000313|RefSeq:XP_011198063.1};
RG RefSeq;
RL Submitted (APR-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 EMBL; GAKP01007979; JAC50973.1; -; Transcribed_RNA.
DR RefSeq; XP_011198063.1; XM_011199761.3.
DR AlphaFoldDB; A0A034WAZ3; -.
DR GeneID; 105222429; -.
DR KEGG; bdr:105222429; -.
DR OMA; FYCDICT; -.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP001652620; Chromosome 3.
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 Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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 InterPro; IPR013083; Znf_RING/FYVE/PHD.
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 SUPFAM; SSF57850; RING/U-box; 1.
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:UP001652620};
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 29..69
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..611
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..643
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..654
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..900
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 900 AA; 100823 MW; 68C986C213C8B59D CRC64;
MSTGEKSAND SGNNASKQPS SEETEHDACV LCCKEVEIYS IGECDHPICY ECSTRLRVLC
EQNECPICRQ VLSKVIFSFD KLPYRTLESK NRSGYYNKKY KIGFYTAKIQ QAYFNLLDHP
CPKCNVPPFR RFKDLEYHVR KEHDLHFCDL CTEHLKIFTF ERRCYTQAEL GLHRTKGDRD
NRSHRGHPLC EFCKKRYLDR DELFRHKRRE HYFCHFCDDE SNDFYRDYDA LANHFRERHF
LCEEGRCATE QFIGAFRTEI DYKAHFASVH GSTLNKQEAK KTRTVQLEIT LGRPARPGLP
DGGITNVRSR VPDDYNAPAE SSTSQAAQQR SITIDRSNEE DFPSLAGTSG GPSMPLVPAT
FTRLRSGASG LARTKENFPA LGAGGGGEHN EQRTHQAAPP ISTVLRKAPA VSKGAISRSS
GGNAASNGAT GMVLHVSNRP TSSVNHNSGA VSKKPHALDF PALPASGKSK KHPPRNPIDE
DMLPSGAHIP LSNVSAKHRP LVDDYVSVAN ASSFQKIQTV QKEELDAKNR KVSEQASAPK
LTSQDFPSLG LGSSSKSNHV QANNWAKGQK QSDKRQRELE NRKAKVAPAP LLSKENTNKQ
TVNTTNKKQT QPAATNNKIS TNATETSVNK KDKKSKDKKE KSNSDNSNQQ QKLNGKSKEK
NNNTNNNSLK RDQSSTSPTS SLDNDNDNDG MPQMRPPPGF AQSSANPQPP PGFQSTNVTV
NSIAKSPNNL TFTSSFGERY SIVRTHPYIQ PTDAVTRNQK LVSHFQDALK TPESMEEFRY
ISQKFREGVY KTQPYYEHCQ AALKDRFDGI FPELLALLPD INKQQELYLV HTQRLKTLSP
EQRQKTQKLD VCSICKQVLI SSDLQNHRKQ HELKENFPML GDGNSGSNMT KTATPANTRK
//
