C2_TPCTV
ID C2_TPCTV Reviewed; 159 AA.
AC Q88889;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 29-SEP-2021, entry version 53.
DE RecName: Full=Protein C2;
DE AltName: Full=Protein L2;
GN ORFNames=C2, L2;
OS Tomato pseudo-curly top virus (TPCTV).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Topocuvirus.
OX NCBI_TaxID=49267;
OH NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OH NCBI_TaxID=4112; Solanum nigrum (Black nightshade).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8638404; DOI=10.1006/viro.1996.0264;
RA Briddon R.W., Bedford I.D., Tsai J.H., Markham P.G.;
RT "Analysis of the nucleotide sequence of the treehopper-transmitted
RT geminivirus, tomato pseudo-curly top virus, suggests a recombinant
RT origin.";
RL Virology 219:387-394(1996).
CC -!- FUNCTION: Acts as a suppressor of RNA-mediated gene silencing, also
CC known as post-transcriptional gene silencing (PTGS), a mechanism of
CC plant viral defense that limits the accumulation of viral RNAs.
CC Suppresses the host RNA silencing by inhibiting adenosine kinase 2
CC (ADK2), a kinase involved in a general methylation pathway. Also
CC suppresses the host basal defense by interacting with and inhibiting
CC SNF1 kinase, a key regulator of cell metabolism implicated in innate
CC antiviral defense. Determines pathogenicity (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Monomer. Suppress local silencing by interacting with and
CC inactivating host adenosine kinase 2 (ADK2) in the cytoplasm. Interacts
CC with and inhibits host SNF1 kinase (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250}.
CC -!- DOMAIN: The zinc finger is involved in PTGS suppression. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the geminiviridae transcriptional activator
CC protein 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; X84735; CAA59224.1; -; Genomic_DNA.
DR RefSeq; NP_620734.1; NC_003825.1.
DR GeneID; 944405; -.
DR KEGG; vg:944405; -.
DR Proteomes; UP000007068; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019028; C:viral capsid; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR InterPro; IPR000942; Gemini_AL2.
DR Pfam; PF01440; Gemini_AL2; 1.
PE 3: Inferred from homology;
KW Host cytoplasm; Host-virus interaction; Metal-binding; Reference proteome;
KW Suppressor of RNA silencing; Zinc; Zinc-finger.
FT CHAIN 1..159
FT /note="Protein C2"
FT /id="PRO_0000323706"
FT ZN_FING 65..81
FT /evidence="ECO:0000250"
FT REGION 102..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 43..60
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 112..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 159 AA; 17950 MW; DC0380A2D53ABAD1 CRC64;
MVLCDKGAHE LGNREIRKGF CERCLYPEYF DDEEAATTTP TIKKRPPKLT WAPKKKRRKA
IHLSCGCSYY GGIDCEDGFT HRGITHVHTV PDWLLLRRHQ EPNLLPPPEH NNNGDGEQNN
NITNQSQPQP AESVGSPDLL AELGGTFSIT SSEWRSIIR