POL_SOCMV
ID POL_SOCMV Reviewed; 692 AA.
AC P15629;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 102.
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 Soybean chlorotic mottle virus.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Caulimoviridae; Soymovirus.
OX NCBI_TaxID=10651;
OH NCBI_TaxID=3847; Glycine max (Soybean) (Glycine hispida).
OH NCBI_TaxID=35936; Lablab purpureus (Hyacinth bean) (Dolichos lablab).
OH NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean).
OH NCBI_TaxID=3917; Vigna unguiculata (Cowpea).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2602148; DOI=10.1093/nar/17.23.9993;
RA Hasegawa A., Verver J., Shimada A., Saito M., Goldbach R., van Kammen A.,
RA Miki K., Kameya-Iwaki M., Hibi T.;
RT "The complete sequence of soybean chlorotic mottle virus DNA and the
RT identification of a novel promoter.";
RL Nucleic Acids Res. 17:9993-10013(1989).
RN [2]
RP SEQUENCE REVISION.
RA Hibi T.;
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
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; X15828; CAC16945.1; -; Genomic_DNA.
DR PIR; JS0375; JS0375.
DR RefSeq; NP_068729.1; NC_001739.2.
DR SMR; P15629; -.
DR MEROPS; A03.001; -.
DR PRIDE; P15629; -.
DR GeneID; 912254; -.
DR KEGG; vg:912254; -.
DR Proteomes; UP000001065; 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; -; 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; 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; Nuclease;
KW Nucleotidyltransferase; Protease; Reference proteome;
KW RNA-directed DNA polymerase; Transferase.
FT CHAIN 1..692
FT /note="Enzymatic polyprotein"
FT /id="PRO_0000222057"
FT DOMAIN 227..411
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT ACT_SITE 36
FT /note="For protease activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 692 AA; 80374 MW; 232795255EF93BBE CRC64;
MNTEIVQKHR VLTKGNPNVT FIKVSIGKRN FLAYIDTGAT LCFGKRKISN NWEILKQPKE
IIIADKSKHY IREAISNVFL KIENKEFLIP IIYLHDSGLD LIIGNNFLKL YQPFIQRLET
IELRWKNLNN PKESQMISTK ILTKNEVLKL SFEKIHICLE KYLFFKTIEE QLEEVCSEHP
LDETKNKNGL LIEIRLKDPL QEINVTNRIP YTIRDVQEFK EECEDLLKKG LIRESQSPHS
APAFYVENHN EIKRGKRRMV INYKKMNEAT IGDSYKLPRK DFILEKIKGS LWFSSLDAKS
GYYQLRLHEN TKPLTAFSCP PQKHYEWNVL SFGLKQAPSI YQRFMDQSLK GLEHICLAYI
DDILIFTKGS KEQHVNDVRI VLQRIKEKGI IISKKKSKLI QQEIEYLGLK IQGNGEIDLS
PHTQEKILQF PDELEDRKQI QRFLGCINYI ANEGFFKNLA LERKHLQKKI SVKNPWKWDT
IDTKMVQSIK GKIQSLPKLY NASIQDFLIV ETDASQHSWS GCLRALPKGK QKIGLDEFGI
PTADLCTGSS SASSDNSPAE IDKCHSASKQ DTHVASKIKK LENELLLCKY VSGTFTDTET
RYPIAELEVL AGVKVLEKWR IDLLQTRFLL RTDSKYFAGF CRYNIKTDYR NGRLIRWQLR
LQAYQPYVEL IKSENNPFAD TLTREWSKPS SS
