ID A0A833W9R9_9HYME Unreviewed; 908 AA.
AC A0A833W9R9;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, 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=E2986_02068 {ECO:0000313|EMBL:KAF3428997.1};
OS Frieseomelitta varia.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Frieseomelitta.
OX NCBI_TaxID=561572 {ECO:0000313|EMBL:KAF3428997.1, ECO:0000313|Proteomes:UP000655588};
RN [1] {ECO:0000313|EMBL:KAF3428997.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USP_RPSP 00005682 {ECO:0000313|EMBL:KAF3428997.1};
RC TISSUE=Whole individual {ECO:0000313|EMBL:KAF3428997.1};
RA Freitas F.C.P., Lourenco A.P., Nunes F.M.F., Paschoal A.R., Abreu F.C.P.,
RA Barbin F.O., Bataglia L., Cardoso-Junior C.A.M., Cervoni M.S., Silva S.R.,
RA Dalarmi F., Del Lama M.A., Depintor T.S., Ferreira K.M., Goria P.S.,
RA Jaskot M.C., Lago D.C., Luna-Lucena D., Moda L.M., Nascimento L.,
RA Pedrino M., Rabico F.O., Sanches F.C., Santos D.E., Santos C.G., Vieira J.,
RA Lopes T.F., Barchuk A.R., Hartfelder K., Simoes Z.L.P., Bitondi M.M.G.,
RA Pinheiro D.G.;
RT "The nuclear and mitochondrial genomes of Frieseomelitta varia - a highly
RT eusocial stingless bee (Meliponini) with a permanently sterile worker
RT caste.";
RL Submitted (NOV-2019) 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:KAF3428997.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; WNWW01000189; KAF3428997.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A833W9R9; -.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP000655588; 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:UP000655588};
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 12..52
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 862..889
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 279..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..421
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..553
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..584
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..670
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..722
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 908 AA; 102106 MW; 7CF3670F6FDA53F5 CRC64;
MSASNESTNN TCVVCYKNVD IYSIGMCEHP VCYECSTRMR VLCCQNECPI CRQDLPKVVF
TKEIKPFRHL HKGNLLDTRY 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 SAQSQKSTTS
NLSIQVNHEP NGTVTTKVSG PNIRIRPAQL SMESFPALGS AEPSTSSNTN SAHWKEVLQW
TCSKSASTSI PKAKKVASPP LIPSPPPIQS GEDFPTLSKS SKSKKQSTIT VVPSWGQTQS
SNNSNNAKTT TDMTKGKTKK KKVKQNCNNN TANGNNGNNS KTNVSTVVVK KEYETLRSPP
SMNNTDAAQS TSQSMQNADI SNSENISKNM NVQVLKTVEQ NNKKEKKKHK NVDNETTVNT
DIDNNTTNAV QRKRTELKID SLNSTNRNAR HLEDFPALSG SSSTPPGFTN PPPGFGATTP
PPPGFCIKYN SLDKINNSNG LTFTNSSGES YSILPDNSKH NSAYNYVPPP EFQKRNKCLV
AKVNEVLLQD DQIKEFRYIS GLFRQGTCNA QDYYMHCREV MGLSAFENVF LELLVLLPDI
EKQQELFKVH KKESGNTIKG LEICATCGQV LKNGSDFRTH MTSHTLENHF PVLGKNNVLP
QKNSWVRK
//
