ID A0A8J2RB43_9CRUS Unreviewed; 854 AA.
AC A0A8J2RB43;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-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 ORFNames=DGAL_LOCUS335 {ECO:0000313|EMBL:CAH0098286.1};
OS Daphnia galeata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=27404 {ECO:0000313|EMBL:CAH0098286.1, ECO:0000313|Proteomes:UP000789390};
RN [1] {ECO:0000313|EMBL:CAH0098286.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=M5 {ECO:0000313|EMBL:CAH0098286.1};
RA Schell T.;
RL Submitted (NOV-2021) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CAH0098286.1}.
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DR EMBL; CAKKLH010000001; CAH0098286.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8J2RB43; -.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP000789390; Unassembled WGS sequence.
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:UP000789390};
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 20..60
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 280..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..470
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 854 AA; 96169 MW; 38C5E739B13B23C5 CRC64;
MTSPFKKREK AIETTEIACC PVCFKDVEIF SIGICDHPIC HECSTRMRVL CKEDACPICR
QELTKVFFVK DPKPYQLLAL NLYPMDKITK IHFENASLQD VFEQLLVHIC YTCPLKPTFQ
NLQILKDHLR KEHELFFCDL CVENLKIFSQ ERKAYTRQEL ALHRRKGDPD NTSHRGHPLC
NFCDQRYVDA DELFRHLRRD HYFCHFCDAD GLNQYYCNYE DLRKHFRGAH FLCEEGECKE
EKFTRVFRTE IDIRAHKAQT HSQTLGKAAI KQARTLELEF TLAPRPGENK GRSGRRVTSR
ASDKQDSNSQ NVSEQQTSRP FGVSSAVSAD IGNPEEFPSL STGSGSVMKS RTNGSDSLAQ
KLAKNNRFTV KNTVGAHDEF PSLVAEGLPF DHQEISLPGE KKTSGAKRSV RSRLGGQDAN
NDDFISGTPI ARVSRVSTSQ NIHVQPSRDL RLENFPSLSS TSQLSEQQAL KPGWIKKNLP
KPANISSDKS VSHRNSLSSV EQYPLLVPSS SHDSGDTSVW ATSKDKIHNV VAVPCVVPNI
ESSSKHPDIR LKKKKNPSKV TNKTQTESLA FSGEIKKKVS ENQIGELKRH TVEIPKTSRN
GRTKFDMSNS QMESTTCIAS KVNIIDSQIN VKPIESNGAR PKTKVKPINL SSSEFPALGN
SSPAISFFDN NHHGLPLARD EKVAPTKITF TSSSGQDFPL PLNNNTNRVF LQPPDFSIRN
QQLIATVMDL LCNQRKKIEK FRTISTQFRS GQLDSKEYYM NCLAVMGEDC FSALFPELIC
LLPDISKQQQ LLRVHRSEIR VKGGLVATEP YVICATCGQV LSPSDLKHHL ANHNLETHFP
SLGTTLDDVP WNKR
//
