ID   VP2_CAVCI               Reviewed;         216 AA.
AC   P69485; P54091; Q99151;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=Dual specificity protein phosphatase VP2;
DE            EC=3.1.3.16;
DE            EC=3.1.3.48;
GN   Name=VP2;
OS   Chicken anemia virus (isolate USA CIA-1) (CAV).
OC   Viruses; Anelloviridae; Gyrovirus.
OX   NCBI_TaxID=73478;
OH   NCBI_TaxID=9031; Gallus gallus (Chicken).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8971016; DOI=10.1128/jvi.70.12.8872-8878.1996;
RA   Renshaw R.W., Soine C., Weinkle T., O'Connell P.H., Ohashi K., Watson S.,
RA   Lucio B., Harrington S., Schat K.A.;
RT   "A hypervariable region in VP1 of chicken infectious anemia virus mediates
RT   rate of spread and cell tropism in tissue culture.";
RL   J. Virol. 70:8872-8878(1996).
RN   [2]
RP   SEQUENCE REVISION TO 24.
RA   Renshaw R.W.;
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May act as a scaffold protein in virion assembly. May also
CC       play a role in intracellular signaling during viral replication (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620; EC=3.1.3.48;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC   -!- INDUCTION: VP1 and VP2 are detected 12 hours post infection, while VP3
CC       only after 24 hours.
CC   -!- SIMILARITY: Belongs to the gyrovirus protein VP2 family. {ECO:0000305}.
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; L14767; AAD09422.1; -; Genomic_DNA.
DR   PIR; A39926; A39926.
DR   Proteomes; UP000008444; Genome.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR004118; HEV_TT_virus_Orf2/Gyrovir_Vp2.
DR   Pfam; PF02957; TT_ORF2; 1.
PE   2: Evidence at transcript level;
KW   Early protein; Hydrolase; Protein phosphatase.
FT   CHAIN           1..216
FT                   /note="Dual specificity protein phosphatase VP2"
FT                   /id="PRO_0000223005"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          165..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        95
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   216 AA;  24139 MW;  F82B69EF88BDDE52 CRC64;
     MHGNGGQPAA GGSESALSRE GQPGPSGAAQ GQVISNERSP RRYSTRTING VQATNKFTAV
     GNPSLQRDPD WYRWNYNHSI AVWLRECSRS HAKICNCGQF RKHWFQECAG LEDRSTQASL
     EEAILRPLRV QGKRAKRKLD YHYSQPTPNR KKVYKTVRWQ DELADREADF TPSEEDGGTT
     SSDFDEDINF DIGGDSGIVD ELLGRPFTTP APVRIV