UniProt: A0A310SWQ6

Database: UniProt
Entry: A0A310SWQ6_9HYME

LinkDB:  A0A310SWQ6_9HYME 
Original site:  A0A310SWQ6_9HYME

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (16)   
   InterPro (8)   
   Pfam (4)   
   PROSITE (3)   
   SMART (1)   
All databases (24)   

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ID   A0A310SWQ6_9HYME        Unreviewed;       742 AA.
AC   A0A310SWQ6;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   28-JAN-2026, entry version 24.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=WN48_06999 {ECO:0000313|EMBL:OAD62261.1};
OS   Eufriesea mexicana.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Apidae; Eufriesea.
OX   NCBI_TaxID=516756 {ECO:0000313|EMBL:OAD62261.1, ECO:0000313|Proteomes:UP000250275};
RN   [1] {ECO:0000313|EMBL:OAD62261.1, ECO:0000313|Proteomes:UP000250275}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0111107269 {ECO:0000313|EMBL:OAD62261.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:OAD62261.1};
RA   Pan H., Kapheim K.;
RT   "The genome of Eufriesea mexicana.";
RL   Submitted (JUL-2015) 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; KQ759878; OAD62261.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A310SWQ6; -.
DR   OrthoDB; 3838338at2759; -.
DR   Proteomes; UP000250275; 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:UP000250275};
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          696..723
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   REGION          379..402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          463..509
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          523..549
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        379..398
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   742 AA;  83743 MW;  2743A0164D1D9AF2 CRC64;
     MSVSTESTNN NTCVVCYKNV DIYSIGMCEH PVCYECSTRM RVLCCQNECP ICRQDLPKVV
     FTKLIKPFRQ LHKGDLLDTR YNIYFDTPDI QNKFYDLLAN VCYICKEKSV FNNFNSLKDH
     MRYQHELHYC DLCVENLKIF SHERRCYTRS DLAQHRRKGD VDDKSHKGHP LCEFCDQRYM
     DNDELFRHLR RDHLYCHFCD ADGLHQYYSS YDYLRDHFRQ EHFLCEEGMC VEEKFTSVFR
     TDIDLKAHKA SVHSKQLSKA AAKQARTLEL EFTLAPRGEN RMNRRGMPGP SNTSNVFMSN
     NEPTFVQQPS VDVQSTEEFP TLGNTAPVVP TLNQNKGRGN VTIRSTIRPQ PLAVTDENFP
     ALGLESGSTS ISKTVNFSVS SSNASGSSAQ SQKSTTSNVS IQVNHEPNGT VTTKVSGPNI
     RIRPAQLSME SFPALGTVEP STSSNTNSAH WKEVLQWTCS KSASTSVPKP KKVASPPLVP
     SPPPIQSGED FPTLSKSSKS KKQSTITVVP SWGQPQIKKE CETPRNVSNT NSVDAVHSKP
     SGFTNPPPGF GTTPPPPGFC IKYNSMDKLN NSNGLTFTNS SGESYSILPD NSKHNSAYNY
     VPPPEFQKRN KCLVAKVNEV LMQHDQIEEF RYISGLFRQG TRNAQDYYTH CREVMGLSAF
     ENVFPELLVL LPDIEKQQEL FKIHKRESGN KLKGLEICAT CGQVLKNGSD FRTHMTSHTL
     ENHFPALGKN SAQPQKNSWV RK
//

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