ID A0A6J3JWU5_9HYME Unreviewed; 910 AA.
AC A0A6J3JWU5;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=LOC117231221 {ECO:0000313|RefSeq:XP_033345322.1};
OS Bombus vosnesenskii.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Bombus; Pyrobombus.
OX NCBI_TaxID=207650 {ECO:0000313|Proteomes:UP000504631, ECO:0000313|RefSeq:XP_033345322.1};
RN [1] {ECO:0000313|RefSeq:XP_033345322.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_033345322.1};
RG RefSeq;
RL Submitted (AUG-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 RefSeq; XP_033345322.1; XM_033489431.1.
DR AlphaFoldDB; A0A6J3JWU5; -.
DR GeneID; 117231221; -.
DR KEGG; bvk:117231221; -.
DR Proteomes; UP000504631; Unplaced.
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:UP000504631};
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 13..53
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 864..891
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 281..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..500
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..554
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..576
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..725
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 910 AA; 102282 MW; AF4FC8008CE3A3FB CRC64;
MSANNESMNN NTCVVCYKNV DIYSIGMCEH PVCYECSTRM RVLCCQNECP ICRQDLPKVV
FTKEIKPFNQ LHKGNLLDTR YNIYFDTLDI QSKFYDLLAN VCYICKERPV FSTFNSLKDH
MRHQHELHYC DLCVENLKIF SHERRCYTRS DLAQHRRKGD IDDKSHKGHP LCEFCDQRYM
DNDELFRHLR RDHLYCHFCD ADGLHQYYSS YDYLRDHFRQ EHFLCEEGMC AEEKFTSVFR
TDIDLKAHKA SVHSKQLSKA AAKQARMLEL EFTLAPRGEN RMNRRGMLGP STSRNSRDYS
GRDYNLREYQ QTVTPNTSNV FMSNNEPAFV QQPSVDVQST EEFPTLGNTA PIVPTLNQSK
GRGNVTIRST IRPQPLAVTD ENFPALGPES GSTSISKTVN FSVSSSNASG LSTQSQKSTT
SNVSIQVNHE PNGTVTTKVS GPNIRIRPAQ FSMESFPALG SAEPSTSSNT NLAHWKEVLQ
WTCSKSASTS APKPKKVASP PLIPSPPPIQ SGEDFPTLSK SSKSKKQSTI TVVPSWSQAQ
SSNNSNNAKT TTDITKGKTK KKKVKQNCNN NTANGNDGSS SKTNVSTAVV KKECETPTSS
PITNKTHAGQ SSSQSILKYA DITNSENTSK NINVQPLKEI EQINKKEKKK HKNADNEAVV
NTDIDNNATN GVQRKRTELK IDSLNSTNRN TRHLEDFPAL SGSSSKPPGF TNPPPGFGTT
TPPPPGFCIK YNSMDKINNS NGLTFTNSSG ESYSILPDNS KHDSAYNYVH PPEFQKRNKC
LVAKVNEVLM QHDQIEEFRY ISGLFRQGTC NAQDYYMHCR EVMGLSAFEN VFSELLVLLP
DIEKQQELFK VHQKESGNKI KGLEICATCG QVLKNGSDFR THMTSHTLEN HFPALGKNNV
LPQKNSWVRK
//
