ID A0A9N9RL70_9DIPT Unreviewed; 892 AA.
AC A0A9N9RL70;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 11.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=CHIRRI_LOCUS3249 {ECO:0000313|EMBL:CAG9800300.1};
OS Chironomus riparius.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC Chironominae; Chironomus.
OX NCBI_TaxID=315576 {ECO:0000313|EMBL:CAG9800300.1, ECO:0000313|Proteomes:UP001153620};
RN [1] {ECO:0000313|EMBL:CAG9800300.1}
RP NUCLEOTIDE SEQUENCE.
RA King R.;
RL Submitted (JAN-2022) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAG9800300.1}
RP NUCLEOTIDE SEQUENCE.
RG ENA_rothamsted_submissions;
RG culmorum;
RA King R.;
RL Submitted (OCT-2022) to the EMBL/GenBank/DDBJ databases.
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; OU895877; CAG9800300.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9N9RL70; -.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP001153620; Chromosome 1.
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; IPR056437; Znf-C2H2_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; PF23230; zf-C2H2_13; 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:UP001153620};
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 57..97
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 318..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..449
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..658
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..706
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 892 AA; 101873 MW; 743F1C2D1866D626 CRC64;
MFRGTTVVDK TTRTPFKKIE NLHKFFIFRE IKQEIMSDLS ENVEQNNMQQ AENENTCVVC
FKKTFIFSIG SCNHPVCYEC SARMRCLCLQ NECPICRQDL PRVIFTKTID LFLTLDKTTR
SGLFEKKFRI VFADLEIQKA FYHLLEHRCP RCEDSNLFVD FYKLKEHVRK VHEQFYCEIC
TENLKVFSSE RRCYTRQEIA QHRRVGDPDN KSHKGHPRCD YCELRYLDKD ELFRHLRREH
YFCHLCDADG INLFYGTVRE MRDHFKAEHF LCEEEDCLEE EFTAVYRTEI DLRAHKATVH
SKNMSRMEVK HARTLDLDIS YGPRGRGGGN ENNNNRHPRI RTNDTQREFD INPEQQIVQM
PPIQIDTKNE DHFPSLGVPS NASNASNGPV QLANSVRHVY YGQQGLARTK ENFPALGGLG
NERNSSQPKQ NNGNKQNSSS KQSAPSASSL FKANKPSSAP QQNYQQKPQS STSNPHPKNI
YKKDSIADFP SLGPSSSKNS FFTESPKYSS SQSIDRKPTT SVASKSSVPA TISKKNLFND
YPTISSAASK KRDLLMEDLI LPSNNNIDKG MIAAKHKGLM NDYVSIASQM TKVSLVKQKE
ESIVENQQFV PTLSSENNFP TLGSSDSASK PIQWITVNSK SNNNNQKQQP QQNVGNKNSF
NPKKQQQKNE VPQKNQKTNG TKKVNDENKK TSNDKKIAKD NTDKENRTML ESKLGSSVKS
PPPGFQQIQP ITARYHPVPD ASKRNQGLVD EFQKVLKTNE SMQEFRLLSQ MFRDGSYFAR
SYYESCKGVL GEKFDTIFPE LLALLPDIDR QQKLYRIHLE ESLTDVDITD DTPTITKKKN
KKSQKTLEVC ATCQQVLLSK DLSLHVQSHS LENSFPTLSK KISSSKAAGG KK
//
