ID   POL_FMVD                Reviewed;         666 AA.
AC   P09523;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 87.
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   Figwort mosaic virus (strain DxS) (FMV).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Caulimoviridae; Caulimovirus.
OX   NCBI_TaxID=10650;
OH   NCBI_TaxID=46031; Scrophularia californica (California bee plant).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3671088; DOI=10.1093/nar/15.20.8451;
RA   Richins R.D., Scholthof H.B., Shepherd R.J.;
RT   "Sequence of figwort mosaic virus DNA (caulimovirus group).";
RL   Nucleic Acids Res. 15:8451-8466(1987).
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; X06166; CAA29527.1; -; Genomic_DNA.
DR   PIR; S01283; S01283.
DR   RefSeq; NP_619548.1; NC_003554.1.
DR   SMR; P09523; -.
DR   MEROPS; A03.001; -.
DR   GeneID; 940156; -.
DR   KEGG; vg:940156; -.
DR   Proteomes; UP000008622; 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; Reference proteome;
KW   RNA-directed DNA polymerase; Transferase.
FT   CHAIN           1..666
FT                   /note="Enzymatic polyprotein"
FT                   /id="PRO_0000222056"
FT   DOMAIN          215..445
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   ACT_SITE        54
SQ   SEQUENCE   666 AA;  77081 MW;  E65BC57D8FD2CA0F CRC64;
     MTSSSLFREG ELGHFCLNKQ EMLHLNVTNP NSIYIEGKLS FEGYKSFNIH CYVDTGASLC
     IASRYIIPEE LWENSPKDIQ VKIANQELIK ITKVCKNLKV KFAGKSFEIP TVYQQETGID
     FLIGNNFCRL YNPFIQWEDR IAFHLKNEMV LIKKVTKAFS VSNPSFLENM KKDSKTEQIP
     GTNISKNIIN PEERYFLITE KYQKIEQLLD KVCSENPIDP IKSKQWMKAS IKLIDPLKVI
     RVKPMSYSPQ DREGFAKQIK ELLDLGLIIP SKSQHMSPAF LVENEAERRR GKKRMVVNYK
     AINQATIGDS HNLPNMQELL TLLRGKSIFS SFDCKSGFWQ VVLDEESQKL TAFTCPQGHF
     QWKVVPFGLK QAPSIFQRHM QTALNGADKF CMVYVDDIIV FSNSELDHYN HVYAVLKIVE
     KYGIILSKKK ANLFKEKINF LGLEIDKGTH CPQNHILENI HKFPDRLEDK KHLQRFLGVL
     TYAETYIPKL AEIRKPLQVK LKKDVTWNWT QSDSDYVKKI KKNLGSFPKL YLPKPEDHLI
     IETDASDSFW GGVLKARALD GVELICRYSS GSFKQAEKNY HSNDKELLAV KQVITKFSAY
     LTPVRFTVRT DNKNFTYFLR INLKGDSKQG RLVRWQNWFS KYQFDVEHLE GVKNVLADCL
     TRDFNA