ID   UB222_WSSVS             Reviewed;         844 AA.
AC   Q77J49;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=RING finger containing E3 ubiquitin-protein ligase WSV222;
DE            EC=2.3.2.27 {ECO:0000269|PubMed:16571805};
DE   AltName: Full=RING-type E3 ubiquitin transferase WSV222;
GN   ORFNames=WSV222;
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, CATALYTIC ACTIVITY, INTERACTION WITH HOST UBE2E1/UBCH6, AND
RP   INTERACTION WITH SHRIMP TUMOR SUPPRESSOR-LIKE PROTEIN.
RX   PubMed=16571805; DOI=10.1128/jvi.80.8.3884-3892.2006;
RA   He F., Fenner B.J., Godwin A.K., Kwang J.;
RT   "White spot syndrome virus open reading frame 222 encodes a viral E3 ligase
RT   and mediates degradation of a host tumor suppressor via ubiquitination.";
RL   J. Virol. 80:3884-3892(2006).
RN   [3]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=19264591; DOI=10.1099/vir.0.008912-0;
RA   He F., Syed S.M., Hameed A.S., Kwang J.;
RT   "Viral ubiquitin ligase WSSV222 is required for efficient white spot
RT   syndrome virus replication in shrimp.";
RL   J. Gen. Virol. 90:1483-1490(2009).
CC   -!- FUNCTION: Probable E3 ubiquitin-protein ligase which accepts ubiquitin
CC       from the E2 ubiquitin-conjugating enzyme UBE2E1/UBCH6 in the form of a
CC       thioester and then directly transfers the ubiquitin to targeted
CC       substrates. Mediates ubiquitination of host tumor-suppressor-like
CC       protein (TSL) targeting it for degradation. Might function as an anti-
CC       apoptosis protein by counteracting TSL-induced apoptosis.
CC       {ECO:0000269|PubMed:16571805}.
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:16571805};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with host UBE2E1/UBCH6 (Probable); this interaction
CC       results in WSV222 auto-ubiquitination. Interacts with host tumor
CC       suppressor-like protein. {ECO:0000269|PubMed:16571805}.
CC   -!- DISRUPTION PHENOTYPE: Reduction of host mortality.
CC       {ECO:0000269|PubMed:19264591}.
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; AF332093; AAL33226.1; -; Genomic_DNA.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000000327; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Host-virus interaction; Metal-binding;
KW   Modulation of host ubiquitin pathway by viral E3 ligase;
KW   Modulation of host ubiquitin pathway by virus; Nucleotide-binding;
KW   Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..844
FT                   /note="RING finger containing E3 ubiquitin-protein ligase
FT                   WSV222"
FT                   /id="PRO_0000410892"
FT   ZN_FING         308..359
FT                   /note="RING-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   BINDING         229..236
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   844 AA;  97040 MW;  DA298EE9EC4396AB CRC64;
     MFTHLTRAFR KMNNLVNRSF IDVHRVVAEL SYPEFEEDVK NPESSIYRTP ISLFQNKDIV
     TIVGDYILSP KTDSFQVLYP IKKVIEHFPV IFHCTHNNAP LWVHLLDERH HRLLQSLLTY
     EIVNAKYRGI VVIPYYRRPI NYQTGKSLLM SKLASVKVLD ILMRCGSYKF ISLMCMINKK
     NNTNFLHCCA SKWGEVGSKM MLHIAEMFFA NPTTSQHLSD ASSFPDAAAE DDKGKTPAHL
     AIQEDNADAL LFLISLYGAP WFQDNNSYMK SALELKSNKC VKVLSFAADK YEILPNINNN
     QLEPDTMCGV CATSVEEDEN EGKTTSLSWY QMNCKHYIHC ECLMGMCAAA GNVQCPMCRE
     DVGDEVLERC PPTIFRWLKL AERSEHNRVL FEAKKQEFYK QMEAMKPPRV VVPPRRTFLT
     PARRGERAIR IAREIATNAI AEATAQGDVN SYFPVLIDGS GEEYEEEGEE FFNSEEEALA
     FGRPFLEDEE EARQIQMRQF AELSRRGVSV NIINNDNPHR HISTVNIVQP VYGVEKSPAA
     SFIYNMLKND VFESIRSRDT RVGGERVPVM NLSNDKRALF HAASSMLCDF ATETNSQIVG
     LDFQAVYDPH HISNYIETFG SPLHAYPGAV TFLDGAQDYY AESIRYDNDI VSFSEMASEL
     HITEALDVFE GSLLSPLFKK IRTGKSYSNW NDHLRRRNYA RDIAEEFVRV CENSLASREH
     PPVHVHPFRD GAIPILIEYI VDFIHHCITW SMQVNALHCM RKYIEHENTN VHLLNLRPTD
     ERVEVLRVSQ LRWSRLFNEQ YNTRMSLSTK RLSLMKIFNH DLGVSKFGVY KLLDIIEMYC
     FTLI