ID   POL_CAMVN               Reviewed;         680 AA.
AC   Q00962;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Enzymatic polyprotein;
DE   Includes:
DE     RecName: Full=Aspartic protease;
DE              EC=3.4.23.-;
DE   Includes:
DE     RecName: Full=Endonuclease;
DE   Includes:
DE     RecName: Full=Reverse transcriptase;
DE              EC=2.7.7.49;
GN   ORFNames=ORF V;
OS   Cauliflower mosaic virus (strain NY8153) (CaMV).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Caulimoviridae; Caulimovirus.
OX   NCBI_TaxID=31557;
OH   NCBI_TaxID=3702; Arabidopsis thaliana (Mouse-ear cress).
OH   NCBI_TaxID=3705; Brassica.
OH   NCBI_TaxID=3725; Raphanus.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16653000; DOI=10.1104/pp.100.1.542;
RA   Chenault K.D., Steffens D.L., Melcher U.K.;
RT   "Nucleotide sequence of cauliflower mosaic virus isolate NY8153.";
RL   Plant Physiol. 100:542-545(1992).
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   -!- DOMAIN: The polymerase/reverse transcriptase (RT) and ribonuclease H
CC       (RH) domains are structured in five subdomains: finger, palm, thumb,
CC       connection and RNase H. Within the palm subdomain, the 'primer grip'
CC       region is thought to be involved in the positioning of the primer
CC       terminus for accommodating the incoming nucleotide. The RH domain
CC       stabilizes the association of RT with primer-template (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the caulimoviridae enzymatic polyprotein family.
CC       {ECO:0000305}.
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DR   EMBL; M90541; AAA46358.1; -; Genomic_DNA.
DR   SMR; Q00962; -.
DR   MEROPS; A03.001; -.
DR   Proteomes; UP000008441; Genome.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0003964; F:RNA-directed DNA polymerase activity; 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   PRINTS; PR00731; CAULIMOPTASE.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS50878; RT_POL; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease; Endonuclease; Hydrolase; Nuclease;
KW   Nucleotidyltransferase; Protease; RNA-directed DNA polymerase; Transferase.
FT   CHAIN           1..680
FT                   /note="Enzymatic polyprotein"
FT                   /id="PRO_0000222053"
FT   DOMAIN          273..453
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   REGION          41..131
FT                   /note="Protease"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        46
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   680 AA;  78665 MW;  FCE02E09647C2221 CRC64;
     MMNHLLLKTQ TQTEQVMNVT NPNSIYIKGR LYFKGYKKIE LHCFVDTGAS LCIASKFVIP
     EEHWVNAERP IMVKIADGSS ITISKVCKDI DLIIVGVIFK IPTVYQQESG IDFIIGNNFC
     QLYEPFIQFT DRVIFTKNKS YPVHIAKLTR AVRVGTEGFL ESMKKRSKTQ QPEPVNISTN
     KIENPLEEIA ILSEGRRLSE EKLFITQQRM QKTEELLEKV CSENPLDPNK TKQWMKASIK
     LSDPSKAIKV KPMKYSPMDR EEFDKQIKEL LDLKVIKPSK SPHMAPAFLV NNEAENGRGN
     KRMVVNYKAM NKATVGDAYN LPNKDELLTL IRGKKIFSSF DCKSGFWQVL LDQESRPLTA
     FTCPQGHYEW NVVPFGLKQA PSIFQRHMDE AFRVFRKFCC VYVDDIVVFS NNEEDHLLHV
     AMILQKCNQH GIILSKKKAQ LFKKKINFLG LEIDEGTHKP QGHILEHINK FPDTLEDKKQ
     LQRFLGILTY ASDYIPNLAQ MRQPLQAKLK ENVPWKWTKE DTLYMQKVKK NLQGFPPLHH
     PLPEEKLIIE TDASDDYWGG MLKAIKINEG TNTELICRYR SGSFKAAERN YHSNDKETLA
     VINTIKKFSI YLTPVHFLIR TDNTHFKSFV NLNYKGDSKL GRNIRWQAWL SHYSFDVEHI
     KGTDNHFADF LSREFNKVNS