ID A0A6V7H0S3_9HYME Unreviewed; 914 AA.
AC A0A6V7H0S3;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 28-JAN-2026, entry version 17.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE Flags: Fragment;
GN ORFNames=MHI_LOCUS208556 {ECO:0000313|EMBL:CAD1470967.1};
OS Heterotrigona itama.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Heterotrigona.
OX NCBI_TaxID=395501 {ECO:0000313|EMBL:CAD1470967.1, ECO:0000313|Proteomes:UP000752696};
RN [1] {ECO:0000313|EMBL:CAD1470967.1}
RP NUCLEOTIDE SEQUENCE.
RA Nazaruddin N.;
RL Submitted (JUL-2020) 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:CAD1470967.1}.
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DR EMBL; CAJDYZ010004133; CAD1470967.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6V7H0S3; -.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP000752696; 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 PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_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:UP000752696};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00042}.
FT DOMAIN 22..62
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 870..897
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 289..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..592
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..729
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAD1470967.1"
FT NON_TER 914
FT /evidence="ECO:0000313|EMBL:CAD1470967.1"
SQ SEQUENCE 914 AA; 102558 MW; 7AF01C201330C16E CRC64;
SISEGDFTKR MSASNESTNN TCVVCYKNVD IYSIGMCEHP VCYECSTRMR VLCCQNECPI
CRQDLPKVVF TKEIKPFSHL HKGKLLDTRY NIYFDTSDIQ NKFYDLLANV CYICKERPVF
STFSSLKDHM RHHHELHYCD LCVENLKIFS HERRCYTRSD LAQHRRKGDI DDKSHKGHPL
CEFCDQRYMD NDELFRHLRR DHLYCHFCDA DGLHQYYSSY DYLRDHFRQE HFLCEEGMCA
EEKFTSVFRT DIDLKAHKAS VHSKQLSKAA AKQARTLELE FTLAPRGENR MNRRGMLGPS
TSRNSRDYSG RDYNLREYQQ TATSNFSNVF MPNNESTFAQ KPSVDVQSTE EFPTLGNTAP
IVPTLNQSKG RGNVTIRSTI RPQPLAVTDE NFPALGPESG NTSISKTVNF SVSSSNVSGS
SAQSHKNTTS NLSIQVNHEP NGTVTTKVSG PNIRIRPAQL SMESFPALGS AEPSTSNTNS
AHWKEVLQWT CSKPTSTSVP KAKKVASPPL IPSPPPIQSG EDFPTLSKSS KSKKQSTITV
VPSWGQTQSS NNSNNAKTIT DITKGKTKKK KVKQNCNNNT TNGNNGNSSK TNVSTVVVKK
ECETSINPSS MNNTDATQSI SQSMQNADIS NSENTSKNIN VQVLQKVEQN NKKEKKKHKN
VDNEAAVNTN IDNNTNGVQR KRTELKIDSL NSTNRNSRHL EDFPALSGSS SKPPGFTNPP
PGFGATTPPP PGFCIKYNSL DKINNSNGLT FTNSSGESYS ILPDNSKHNS AYNYVPPPEF
QKRNKCLVAK VNEVLTQDDQ IKEFRYISGL FRQGTCNAQD YYTHCREVMG LSAFENVFPE
LLVLLPDIEK QQELFKVHKK ESGNTIKGLE ICATCGQVLK NGSDFRTHMT SHTLENHFPA
LGKNNVLSQK NSWV
//
