ID   POL_CAMVE               Reviewed;         679 AA.
AC   Q02964;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 90.
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 BBC) (CaMV).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Caulimoviridae; Caulimovirus.
OX   NCBI_TaxID=31556;
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=8428667; DOI=10.1016/0378-1119(93)90133-n;
RA   Chenault K.D., Melcher U.K.;
RT   "The complete nucleotide sequence of cauliflower mosaic virus isolate
RT   BBC.";
RL   Gene 123:255-257(1993).
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   ---------------------------------------------------------------------------
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; M90542; AAA62375.1; -; Genomic_DNA.
DR   SMR; Q02964; -.
DR   MEROPS; A03.001; -.
DR   Proteomes; UP000008440; 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..679
FT                   /note="Enzymatic polyprotein"
FT                   /id="PRO_0000222052"
FT   DOMAIN          272..452
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        45
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   679 AA;  78713 MW;  2D8031B62F1CB05A CRC64;
     MDHLLLKTQT QTEQVMNVTN PNSIYIKGRL YFKGYKKIEL HCFVDTGASL CIASKFVIPE
     EHWVNAERPI MVKIADGSSI TISKVCKDID LIIAREIFKI PTVYQQESGI DFIIGNNFCQ
     LYEPFIQFTD RVIFTKNKSY PVHIAKLTRA VRVGTEGFLE SMKKRSKTQQ PEPVNISTNK
     IENPLKEIAI LSEGRRLSEE KLFITQQRMQ KIEELLEKVC SENPLDPNKT KQWMKASIKL
     SDPSKAIKVK PMKYSPMDRE EFDKQIKELL DLKVIKPSKS PHMAPAFLVN NEAEKRRGKK
     RMVVNYKAMN KATIGDAYNL PNKDELLTLI RGKKIFSSFD CKSGFWQVLL DQESRPLTAF
     TCPQGHYEWN VVPFGLKQAP SIFQRHMDEA FRVFRKFCCV YVDDILVFSN NEEDHLLHVA
     MILQKCNQHG IILSKKKAQL FKKKINFLGL EIDEGTHKPQ GHILEHINKF PDTLEDKKQL
     QRFLGILTYA SDYIPKLAQI RKPLQAKLKE NVPWKWTKED TLYMQKVKKN LQGFPPLHHP
     LPEEKLIIET DASDDYWGGM LKAIKINEGT NTELICRYAS GSFKAAERNY HSNDKETLAV
     INTIKKFSIY LTPVHFLIRT DNTHFKSFVN LNYKGDSKLG RNIRWQAWLS HYSFDVEHIK
     GTDNHFADFL SREFNKVNS