C2_BCTVC
ID C2_BCTVC Reviewed; 173 AA.
AC Q91J26; Q96634;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 29-SEP-2021, entry version 45.
DE RecName: Full=Protein C2;
DE AltName: Full=Protein L2;
GN ORFNames=C2, L2;
OS Beet curly top virus (strain California/Logan) (BCTV).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Curtovirus.
OX NCBI_TaxID=268960;
OH NCBI_TaxID=161934; Beta vulgaris (Sugar beet).
OH NCBI_TaxID=4071; Capsicum (peppers).
OH NCBI_TaxID=3650; Cucurbitaceae.
OH NCBI_TaxID=4005; Linum.
OH NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean).
OH NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OH NCBI_TaxID=4113; Solanum tuberosum (Potato).
OH NCBI_TaxID=3562; Spinacia oleracea (Spinach).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Infectious clone pBCT028;
RX PubMed=16453696; DOI=10.1002/j.1460-2075.1986.tb04424.x;
RA Stanley J., Markham P.G., Callis R.J., Pinner M.S.;
RT "The nucleotide sequence of an infectious clone of the geminivirus beet
RT curly top virus.";
RL EMBO J. 5:1761-1767(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Bisaro D.M., Hormuzdi S.G.;
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION.
RX PubMed=7856079; DOI=10.1006/viro.1995.1027;
RA Hormuzdi S.G., Bisaro D.M.;
RT "Genetic analysis of beet curly top virus: examination of the roles of L2
RT and L3 genes in viral pathogenesis.";
RL Virology 206:1044-1054(1995).
RN [4]
RP FUNCTION.
RX PubMed=11414806; DOI=10.1006/viro.2001.0950;
RA Sunter G., Sunter J.L., Bisaro D.M.;
RT "Plants expressing tomato golden mosaic virus AL2 or beet curly top virus
RT L2 transgenes show enhanced susceptibility to infection by DNA and RNA
RT viruses.";
RL Virology 285:59-70(2001).
RN [5]
RP FUNCTION, AND INTERACTION WITH ARABIDOPSIS THALIANA KIN11/SNF1.
RX PubMed=12671096; DOI=10.1105/tpc.009530;
RA Hao L., Wang H., Sunter G., Bisaro D.M.;
RT "Geminivirus AL2 and L2 proteins interact with and inactivate SNF1
RT kinase.";
RL Plant Cell 15:1034-1048(2003).
RN [6]
RP FUNCTION, AND INTERACTION WITH ARABIDOPSIS THALIANA ADK2.
RX PubMed=14615595; DOI=10.1105/tpc.015180;
RA Wang H., Hao L., Shung C.-Y., Sunter G., Bisaro D.M.;
RT "Adenosine kinase is inactivated by geminivirus AL2 and L2 proteins.";
RL Plant Cell 15:3020-3032(2003).
RN [7]
RP FUNCTION.
RX PubMed=15919897; DOI=10.1128/jvi.79.12.7410-7418.2005;
RA Wang H., Buckley K.J., Yang X., Buchmann R.C., Bisaro D.M.;
RT "Adenosine kinase inhibition and suppression of RNA silencing by
RT geminivirus AL2 and L2 proteins.";
RL J. Virol. 79:7410-7418(2005).
RN [8]
RP SUBUNIT, AND INTERACTION WITH ARABIDOPSIS THALIANA ADK2.
RX PubMed=17715241; DOI=10.1128/jvi.00617-07;
RA Yang X., Baliji S., Buchmann R.C., Wang H., Lindbo J.A., Sunter G.,
RA Bisaro D.M.;
RT "Functional modulation of the geminivirus AL2 transcription factor and
RT silencing suppressor by self-interaction.";
RL J. Virol. 81:11972-11981(2007).
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.
CC {ECO:0000269|PubMed:11414806, ECO:0000269|PubMed:12671096,
CC ECO:0000269|PubMed:14615595, ECO:0000269|PubMed:15919897,
CC ECO:0000269|PubMed:7856079}.
CC -!- SUBUNIT: Monomer. Interacting with and inactivating host adenosine
CC kinase 2 (ADK2) in the cytoplasm. Interacts with and inhibits host SNF1
CC kinase. {ECO:0000269|PubMed:12671096, ECO:0000269|PubMed:14615595,
CC ECO:0000269|PubMed:17715241}.
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}.
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DR EMBL; M24597; AAA42755.1; -; Genomic_DNA.
DR EMBL; AF379637; AAK59261.1; -; Genomic_DNA.
DR PIR; S28364; S28364.
DR Proteomes; UP000006542; 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 1: Evidence at protein level;
KW Host cytoplasm; Host-virus interaction; Metal-binding; Reference proteome;
KW Suppressor of RNA silencing; Zinc; Zinc-finger.
FT CHAIN 1..173
FT /note="Protein C2"
FT /id="PRO_0000323702"
FT ZN_FING 69..85
FT /evidence="ECO:0000250"
FT VARIANT 99
FT /note="G -> R (in strain: Infectious clone pBCT028)"
FT VARIANT 128
FT /note="P -> Q (in strain: Infectious clone pBCT028)"
FT VARIANT 147
FT /note="N -> D (in strain: Infectious clone pBCT028)"
FT VARIANT 150
FT /note="R -> W (in strain: Infectious clone pBCT028)"
SQ SEQUENCE 173 AA; 19888 MW; E9678B072FCF4398 CRC64;
MENHVSLKVV SPALYYAIQD LRAHTNNFLK NQKMKPLSPG HYIIQPSANS KVRSLITKQQ
HPRKVTLPCN CHFTIHHECN RGFSHRGTYY SPSGNKFRGI RECTESTVYE TPMVREIRAN
LSTEDTNPIQ LQPPESVESS QVLDRANDNR IEQDIDWTPF LEGLEKETRD ILG
