UB403_WSSVS
ID UB403_WSSVS Reviewed; 641 AA.
AC Q8VAK2; Q8VAJ4;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 11-NOV-2015, sequence version 2.
DT 29-SEP-2021, entry version 65.
DE RecName: Full=RING finger containing E3 ubiquitin-protein ligase WSV403;
DE EC=2.3.2.27 {ECO:0000269|PubMed:19087357};
DE AltName: Full=RING-type E3 ubiquitin transferase WSV403;
GN ORFNames=WSV403;
OS White spot syndrome virus (isolate Shrimp/China/Tongan/1996) (WSSV) (White
OS spot bacilliform virus).
OC Viruses; Naldaviricetes; Nimaviridae; Whispovirus.
OX NCBI_TaxID=654913;
OH NCBI_TaxID=6657; Crustacea.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11689662; DOI=10.1128/jvi.75.23.11811-11820.2001;
RA Yang F., He J., Lin X., Li Q., Pan D., Zhang X., Xu X.;
RT "Complete genome sequence of the shrimp white spot bacilliform virus.";
RL J. Virol. 75:11811-11820(2001).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19087357; DOI=10.1186/1743-422x-5-151;
RA He F., Kwang J.;
RT "Identification and characterization of a new E3 ubiquitin ligase in white
RT spot syndrome virus involved in virus latency.";
RL Virol. J. 5:151-151(2008).
RN [3]
RP SEQUENCE REVISION.
RA Yang F., He J., Lin X., Li Q., Pan D., Zhang X., Xu X.;
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable E3 ubiquitin-protein ligase which accepts ubiquitin
CC from an E2 ubiquitin-conjugating enzyme in the form of a thioester and
CC then directly transfers the ubiquitin to targeted substrates.
CC {ECO:0000269|PubMed:19087357}.
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:0000269|PubMed:19087357};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
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DR EMBL; AF332093; AAL33416.2; -; Genomic_DNA.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000000327; Genome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0039648; P:modulation by virus of host protein ubiquitination; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
PE 1: Evidence at protein level;
KW Host-virus interaction; Metal-binding;
KW Modulation of host ubiquitin pathway by viral E3 ligase;
KW Modulation of host ubiquitin pathway by virus; Reference proteome;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..641
FT /note="RING finger containing E3 ubiquitin-protein ligase
FT WSV403"
FT /id="PRO_0000397866"
FT ZN_FING 329..371
FT /note="RING-type; atypical"
SQ SEQUENCE 641 AA; 74155 MW; 6B3FF16D73087439 CRC64;
MVASTPCPGP GPVPTQELLS TNFLEAHKLV VELLLPSYSS DVVYCDSETY TKPIPIFGNK
SIVSTIGDYV LSNPNEDVSY QMVSSVLEKF PLLFHCTYKT NEEDKGIPLW KKLYNKRKFK
LLNSLLVHNN KNWTPVPAIP FDRENICDAS GRSVLMSEIM STSTFQTICK NNTHYLFDML
NMERGKQGGS FLHFFASRKN SFTNFENEEM DSHVLSNIAK FICNEKEKLD SFIPANGKIP
CPDKTNDEGY IPLEIAIMED NYPALLYLVC RYGASWANTY GDHNESLKAF AIRNDAKDCL
EIIEFISDHY SFNKNVTKEE FVKEKTVECV GCLYDIEDEK RCYKLPCGHF MHTFCLSNKC
SKANFRCVKC FQTFDDTIFR KCPPTIQWKM GINQTTNHKE MDLFNRAFDT YLDFICSYNV
KLDKKSKPKH KPENKKVEEE LAKRTAEIEE AMKKKEEELT KRTAEIEEAI KKKEEELAKR
TAEIEEAMKK KEEEELSKYN KIIEKGKRRL NEECVKLRDI STAAINMYKE KVRINGVLLK
DSDQELAEAK ERLRKILLLE EETKLDRFLF RPKRVEERIF LTKDDETLAF KLALEKKTED
IIAKKNNQKG SERRDGEYTI TSHIEKLPQS TALASVCVLN E
