ID   POL_CERV                Reviewed;         659 AA.
AC   P05400;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   03-AUG-2022, entry version 98.
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   Carnation etched ring virus (CERV).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Caulimoviridae; Caulimovirus.
OX   NCBI_TaxID=10640;
OH   NCBI_TaxID=3570; Dianthus caryophyllus (Carnation) (Clove pink).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16453731; DOI=10.1002/j.1460-2075.1986.tb04614.x;
RA   Hull R., Sadler J., Longstaff M.;
RT   "The sequence of carnation etched ring virus DNA: comparison with
RT   cauliflower mosaic virus and retroviruses.";
RL   EMBO J. 5:3083-3090(1986).
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; X04658; CAA28360.1; -; Genomic_DNA.
DR   PIR; S00854; S00854.
DR   RefSeq; NP_612577.1; NC_003498.1.
DR   SMR; P05400; -.
DR   MEROPS; A03.001; -.
DR   GeneID; 935429; -.
DR   KEGG; vg:935429; -.
DR   Proteomes; UP000008446; 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; 3.30.70.270; -; 2.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR000588; Pept_A3A.
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..659
FT                   /note="Enzymatic polyprotein"
FT                   /id="PRO_0000222055"
FT   DOMAIN          252..436
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   REGION          1..180
FT                   /note="Protease"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        34
SQ   SEQUENCE   659 AA;  76517 MW;  25CC30475E38B3C6 CRC64;
     MSLRNRTNPN SIYVKGILKF PGYQTNLDLH CYVDTGSSLC MASKYVIPEE YWQTAEKPLN
     IKIANGKIIQ LTKVCSKLPI RLGGERFLIP TLFQQESGID LLLGNNFCQL YSPFIQYTDR
     IYFHLNKQSV IIGKITKAYQ YGVKGFLESM KKKSKVNRPE PINITSNQHL FLEEGGNHVD
     EMLYEIQISK FSAIEEMLER VSSENPIDPE KSKQWMTATI ELIDPKTVVK VKPMSYSPSD
     REEFDRQIKE LLELKVIKPS KSTHMSPAFL VENEAERRRG KKRMVVNYKA MNKATKGDAH
     NLPNKDELLT LVRGKKIYSS FDCKSGLWQV LLDKESQLLT AFTCPQGHYQ WNVVPFGLKQ
     APSIFPKTYA NSHSNQYSKY CCVYVDDILV FSNTGRKEHY IHVLNILRRC EKLGIILSKK
     KAQLFKEKIN FLGLEIDQGT HCPQNHILEH IHKFPDRIED KKQLQRFLGI LTYASDYIPK
     LASIRKPLQS KLKEDSTWTW NDTDSQYMAK IKKNLKSFPK LYHPEPNDKL VIETDASEEF
     WGGILKAIHN SHEYICRYAS GSFKAAERNY HSNEKELLAV IRVIKKFSIY LTPSRFLIRT
     DNKNFTHFVN INLKGDRKQG RLVRWQMWLS QYDFDVEHIA GTKNVFADFL QENTLTNYV