ID   POL_CAMVD               Reviewed;         674 AA.
AC   P03556;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 100.
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 D/H) (CaMV).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Caulimoviridae; Caulimovirus.
OX   NCBI_TaxID=10645;
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=7152260; DOI=10.1016/0378-1119(82)90013-0;
RA   Balazs E., Guilley H., Jonard G., Richards K.;
RT   "Nucleotide sequence of DNA from an altered-virulence isolate D/H of the
RT   cauliflower mosaic virus.";
RL   Gene 19:239-249(1982).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA46350.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M10376; AAA46350.1; ALT_INIT; Genomic_DNA.
DR   SMR; P03556; -.
DR   MEROPS; A03.001; -.
DR   Proteomes; UP000008439; 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..674
FT                   /note="Enzymatic polyprotein"
FT                   /id="PRO_0000222051"
FT   DOMAIN          267..447
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   REGION          40..130
FT                   /note="Protease"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        47
SQ   SEQUENCE   674 AA;  78164 MW;  E004E3222D349E29 CRC64;
     MDHLLQKTQI QNQTEQVMNI TNPNSIYIKG RLYFKGYKKI ELHCFVDTGA SLCIASKFVI
     PEEHWINAER PIMVKIADGS SITINKVCRD IDLIIAGEIF HIPTVYQQES GIDFIIGNNF
     CQLYEPFIQF TDRVIFTKDR TYPVHIAKLT RAVRVGTEGF LESMKKRSKT QQPEPVNIST
     NKIAILSEGR RLSEEKLFIT QQRMQKIEEL LEKVCSENPL DPNKTKQWMK ASIKLSDPSK
     AIKVKPMKYS PMDREEFDKQ IKELLDLKVI KPSKSPHMAP AFLVNNEAEK RRGKKRMVVN
     YKAMNKATVG DAYNPPNKDE LLTLIRGKKI FSSFDCKSGF WQVLLDQESR PLTAFTCPQG
     HYEWNVVPFG LKQAPSIFQR HMDEAFRVFR KFCCVYVDDI LVFSNNEEDH LLHVAMILQK
     CNQHGIILSK KKAQLFKKKI NFLGLEIDEG THKPQGHILE HINKFPDTLE DKKQLQRFLG
     ILTYASDYIP KLAQIRKPLQ AKLKENVPWK WTKEDTLYMQ KVKKNLQGFP PLHHPLPEEK
     LIIETDASDD YWGGMLKAIK INEGTNTELI CRYASGSFKA AEKNYHSNDK ETLAVINTIK
     KFSIYLTPVH FLIRTDNTHF KSFVNLNYKG DSKLGRNIRW QAWLSHYSFD VEHIKGTDNH
     FADFLSREFN RVNS