POL_CYLCV
ID POL_CYLCV Reviewed; 643 AA.
AC Q7TD08;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 74.
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 Cestrum yellow leaf curling virus (CmYLCV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Caulimoviridae; Soymovirus.
OX NCBI_TaxID=175814;
OH NCBI_TaxID=142762; Cestrum parqui.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=14645927; DOI=10.1099/vir.0.19405-0;
RA Stavolone L., Ragozzino A., Hohn T.;
RT "Characterization of Cestrum yellow leaf curling virus: a new member of the
RT family Caulimoviridae.";
RL J. Gen. Virol. 84:3459-3464(2003).
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; AF364175; AAP78924.1; -; Genomic_DNA.
DR RefSeq; NP_861410.1; NC_004324.3.
DR SMR; Q7TD08; -.
DR MEROPS; A03.001; -.
DR GeneID; 1732955; -.
DR KEGG; vg:1732955; -.
DR Proteomes; UP000007763; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; 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; 3.30.420.10; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
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; IPR036397; RNaseH_sf.
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; SSF50630; SSF50630; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS50878; RT_POL; 1.
PE 3: Inferred from homology;
KW Aspartyl protease; Endonuclease; Hydrolase; Magnesium; Metal-binding;
KW Multifunctional enzyme; Nuclease; Nucleotidyltransferase; Protease;
KW Reference proteome; RNA-binding; RNA-directed DNA polymerase; Transferase.
FT CHAIN 1..643
FT /note="Enzymatic polyprotein"
FT /id="PRO_0000317781"
FT DOMAIN 6..209
FT /note="Peptidase A3A"
FT DOMAIN 226..410
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT ACT_SITE 26
FT /note="For protease activity"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT BINDING 360
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT BINDING 361
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
SQ SEQUENCE 643 AA; 74082 MW; CD52FC1AEBCBE7D3 CRC64;
MKSKGNPNAT FITVKINDVF INAYVDTGAT ICLADPKIKL KWVKMEKPIK ISIADKSVQE
IWHRAEMVEI WIRNYKFVAA TVCQKSSGMD FVIGNNFLRL YQPFIQGLNY IKLRAPLDKD
INQPSKMIYI PVTTPSKILQ FAILEKLQDI LFELHVQENS KTPLELKVSS TLEEVCDENP
LDVKNTNTEL VKIELINPEK EVNVPNNIPY SLRDINEFSQ ECADLVRKGI IEESKSPHSA
PAFYVENHNE IKRKKRRMVI NYKALNKATI GNAHKLPRID SILTKVKGSN WFSTLDAKSG
YWQLRLHPQS KPLTAFSCPP QKHYQWNVLP FGLKQAPGIY QNFMDKNLEG LENFCLAYID
DILVFTNSSR EEHLSKLLVV LERCKEKGLI LSKKKAIIAR QTIDFLGLTL QENGEIKLQP
NVLEKLELFP DAIEDRKQLQ RFLGCLNYIA DKGFLKEIAK ETKNLYPKVS ITNPWHWSDL
DSKLVNQIKK KCKDLSPLYF PKPEDYLIIE TDASGDTWAG CLKAAELLFP KGTKNKVVER
LCKYTSGIFS SAEQKYTVHE KETLAALKTM RKWKAELLPK EFTLRTDSSY VTGFARHNLK
ANYNQGRLVR WQLEFLQYPA RVEYIKGEKN SLADTLTREW KQQ
