POL_CSVMV
ID POL_CSVMV Reviewed; 652 AA.
AC Q89703;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Putative enzymatic polyprotein;
DE Includes:
DE RecName: Full=Protease;
DE Short=PR;
DE EC=3.4.23.-;
DE Includes:
DE RecName: Full=Reverse transcriptase;
DE Short=RT;
DE EC=2.7.7.49;
DE Includes:
DE RecName: Full=Ribonuclease H;
DE EC=3.1.26.4;
GN ORFNames=ORF 3;
OS Cassava vein mosaic virus (CsVMV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Caulimoviridae; Cavemovirus.
OX NCBI_TaxID=38062;
OH NCBI_TaxID=3983; Manihot esculenta (Cassava) (Jatropha manihot).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9645200; DOI=10.1007/s007050050344;
RA de Kochko A., Verdaguer B., Taylor N., Carcamo R., Beachy R.N., Fauquet C.;
RT "Cassava vein mosaic virus (CsVMV), type species for a new genus of plant
RT double stranded DNA viruses?";
RL Arch. Virol. 143:945-962(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kochko de A., Verdaguer B., Beachy R.N., Fauquet C.;
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7730813; DOI=10.1099/0022-1317-76-5-1271;
RA Calvert L.A., Ospina M.D., Shepherd R.J.;
RT "Characterization of cassava vein mosaic virus: a distinct plant
RT pararetrovirus.";
RL J. Gen. Virol. 76:1271-1278(1995).
CC -!- FUNCTION: Encodes for at least two polypeptides: protease (PR) and
CC reverse transcriptase (RT). The protease processes the polyprotein in
CC cis. Reverse transcriptase is multifunctional enzyme that converts the
CC viral RNA genome into dsDNA in viral cytoplasmic capsids. This enzyme
CC displays a DNA polymerase activity that can copy either DNA or RNA
CC templates, and a ribonuclease H (RNase H) activity that cleaves the RNA
CC strand of RNA-DNA heteroduplexes in a partially processive 3'- to 5'-
CC endonucleasic mode. Neo-synthesized pregenomic RNA (pgRNA) are
CC encapsidated, and reverse-transcribed inside the nucleocapsid. Partial
CC (+)DNA is synthesized from the (-)DNA template and generates the
CC relaxed circular DNA (RC-DNA) genome. After budding and infection, the
CC RC-DNA migrates in the nucleus, and is converted into a plasmid-like
CC covalently closed circular DNA (cccDNA) (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00405};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
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DR EMBL; U20341; AAA79873.1; -; Genomic_DNA.
DR EMBL; U59751; AAB03327.1; -; Genomic_DNA.
DR RefSeq; NP_056848.1; NC_001648.1.
DR SMR; Q89703; -.
DR MEROPS; A03.005; -.
DR GeneID; 1403416; -.
DR KEGG; vg:1403416; -.
DR Proteomes; UP000002244; Genome.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.70.10; -; 1.
DR Gene3D; 3.30.70.270; -; 2.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR000588; Pept_A3A.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR000477; RT_dom.
DR InterPro; IPR041373; RT_RNaseH.
DR Pfam; PF02160; Peptidase_A3; 1.
DR Pfam; PF17917; RT_RNaseH; 1.
DR Pfam; PF00078; RVT_1; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS50878; RT_POL; 1.
PE 3: Inferred from homology;
KW Aspartyl protease; DNA recombination; DNA-binding;
KW DNA-directed DNA polymerase; Endonuclease; Hydrolase; Magnesium;
KW Metal-binding; Multifunctional enzyme; Nuclease; Nucleotidyltransferase;
KW Protease; Reference proteome; RNA-binding; RNA-directed DNA polymerase;
KW Transferase.
FT CHAIN 1..652
FT /note="Putative enzymatic polyprotein"
FT /id="PRO_0000397901"
FT DOMAIN 21..99
FT /note="Peptidase A2"
FT DOMAIN 231..413
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT ACT_SITE 26
FT /evidence="ECO:0000250"
FT BINDING 301
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT BINDING 364
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT BINDING 365
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
SQ SEQUENCE 652 AA; 77054 MW; 564AAF8FDE925F9C CRC64;
MNKITYMTIK ISIPKYMSRI YHGLFDTGAN ICICKKKVLP DELWHKTENL VLRGFNDEKH
VAEYRADNIT IMIAKEKFII PYIYAMDEMS PDIIIGATFY NKYSPIELDI GKGIIKFTKN
NEKYPNYLVK YPKKRKLVPW TKGNPSVTET MENIGINQIE SRNPIEEEIN QILGTDIYGE
NPLEKWEKHK TLAKIELKNE TDNIYKPPML YQETDLPEFK MHIEEMIKEG FIEEKTNFED
KKYSSPAFIV NKHSEQKRGK TRMVIDYKDL NKKAKVVKYP IPNKDTLIHR SIQARYYSKF
DCKSGFYHIK LEEDSKKYTA FTVPQGYYQW KVLPFGYHNS PSIFQQFMDR IFRPYYDFII
VYIDDILVFS KTIEEHKIHI AKFRDITLAN GLIISKKKTE LCKEKIDFLG VQIEQGGIEL
QPHIINKILE KHTKIKNKTE LQSILGLLNQ IRHFIPHLAQ ILLPIQKKLK IKDEEIWTWT
KEDEEKIKLI QDYSKNLVIK MKYPINKEDM NWIIEVDASN NAYGSCLKYK PKNSKIEYLC
RYNSGTFKEN EQKYDINRKE LIAVYQGLQS YSLFTCEGNK LVRTDNSQVY YWIKNDTNKK
SIEFRNIKYL LAKIAVYNFE IQLIDGKTNI IADYLSRYNS SDTDGRYDEA NT
