POL_COYMV
ID POL_COYMV Reviewed; 1886 AA.
AC P19199; P19202;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Polyprotein P3;
DE Includes:
DE RecName: Full=Putative movement protein;
DE Short=MP;
DE Includes:
DE RecName: Full=Capsid protein;
DE AltName: Full=Coat protein;
DE Short=CP;
DE Includes:
DE RecName: Full=Protease;
DE Short=PR;
DE EC=3.4.23.-;
DE Includes:
DE RecName: Full=Reverse transcriptase;
DE Short=RT;
DE EC=2.7.7.49;
DE Includes:
DE RecName: Full=Ribonuclease H;
DE EC=3.1.26.4;
OS Commelina yellow mottle virus (CoYMV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Caulimoviridae; Badnavirus.
OX NCBI_TaxID=10653;
OH NCBI_TaxID=4743; Commelina.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1699203; DOI=10.1093/nar/18.18.5505;
RA Medberry S.L., Lockhart Olszewski N.E.;
RT "Properties of Commelina yellow mottle virus's complete DNA sequence,
RT genomic discontinuities and transcript suggest that it is a
RT pararetrovirus.";
RL Nucleic Acids Res. 18:5505-5513(1990).
CC -!- FUNCTION: Capsid protein self assembles to form a bacilliform capsid
CC about 90-900 nm in length. The capsid encapsulates the genomic dsDNA.
CC Following virus entry into host cell, provides nuclear import of the
CC viral genome. Virus particles do not enter the nucleus, but are
CC targeted to the nuclear membrane through the interaction with host
CC importins (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00408};
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 -!- PTM: Polyprotein P3 is presumably proteolytically cleaved into several
CC chains by viral protease. {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; X52938; CAA37110.1; -; Genomic_DNA.
DR PIR; S11480; S11480.
DR RefSeq; NP_039820.1; NC_001343.1.
DR SMR; P19199; -.
DR MEROPS; A03.004; -.
DR GeneID; 1489554; -.
DR KEGG; vg:1489554; -.
DR Proteomes; UP000002243; Genome.
DR GO; GO:0043657; C:host cell; IEA:GOC.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0046740; P:transport of virus in host, cell to cell; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-KW.
DR Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.30.70.270; -; 2.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR001995; Peptidase_A2_cat.
DR InterPro; IPR018061; Retropepsins.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR002156; RNaseH_domain.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR000477; RT_dom.
DR InterPro; IPR041577; RT_RNaseH_2.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF17919; RT_RNaseH_2; 1.
DR Pfam; PF00077; RVP; 1.
DR Pfam; PF00078; RVT_1; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS50879; RNASE_H_1; 1.
DR PROSITE; PS50878; RT_POL; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 3: Inferred from homology;
KW Aspartyl protease; Endonuclease; Hydrolase; Magnesium; Metal-binding;
KW Nuclease; Nucleotidyltransferase; Protease; Reference proteome;
KW RNA-directed DNA polymerase; Transferase; Transport;
KW Viral movement protein; Viral penetration into host nucleus;
KW Virus entry into host cell; Zinc; Zinc-finger.
FT CHAIN 1..1886
FT /note="Polyprotein P3"
FT /id="PRO_0000199569"
FT DOMAIN 1215..1292
FT /note="Peptidase A2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT DOMAIN 1425..1615
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT DOMAIN 1706..1841
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT ZN_FING 879..896
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1220
FT /note="For protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT BINDING 1715
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 1715
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 1758
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 1784
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 1833
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
SQ SEQUENCE 1886 AA; 215662 MW; 60E010C132FEDA91 CRC64;
MATRRLPAVT QTDGSRTATE SGVPEYEDQI RSYRNDQRRR HIWAGRGRRL LSIMPGVSSS
ERTLEMQMNP EVQLQRSMNH RAEAVPAEVL YRTFHGSVNH RVYSHRSEER MMVVNGSQVD
RSFIQESSFE VLSRTGIEFI HIGVMLVRIQ ILHRKFAGTM ALIVFRDTRW SDDRAVLAAM
EIDLSEGNQI VYVLPDIMMT IKSFYRHIQI CVMTKGYDGW QGEDNLLITR GLTGRLSNTS
NVGFAYDVKA MVEHLQSNGV KAIKGEKWDA KRFHNGQWNI EPSKVVVPMQ PTEMKAVSNY
DGTTSLRFSN YAAASTSKPP QYNEKDEEIN EDEQEINHSL NLILNDEEST DEDEEYYQYQ
RYAWSQVGDS TFYYDTDGVW EEIDRCNDLP EYVPSETSTP TIDESEAIID EFLEHAYEQR
CDSDESLQSG DPRKYEYPTP QSSPEHLDNE SRSRSSSASS TSMQDDVEEI VRLMKEMRMK
KQKKKKAQQA LSSQAQEEPI IEENIEENKQ AQEEPTQEEI PTHKENQPEE IQNEEIHVFE
EEPAFKHLAA QLSELVNMAE SSGQSGVGFQ PPVNAQPDVN MEGPAGYAPA TSQATWSNGV
NIPVKSANFR WKGPVGNFQL PSAQGKDGAM LVFGMNYSPE VFDRWASITR NYISSFNFND
GGDKIAWMED LLGETERKIF VSWRMRFKDE YQNLAKIANQ DGGTQAILSQ IRRIFLGEDP
VLGQNTVQNI AFRKLKQLVC PNYQSIRRYL MDYLTLAAET GLMWSETEGP AISEELFTKM
PAAIGERVAQ AYKIMDPTSA VNLPSRVYFT INYLTEQCKE ASYMRSLKAL DFCRDFPIEG
YYGRSGEKKK YTARKATKYT GKAHDNHIRV TKAKYQRKCK CYICGQEGHY ANQCRNKHKD
QQRVAILQSL DLKENEEVVS ADDKEEEDDE IFSVLGEEDY QEETIMVLEE DDIQQIIKEF
SKFGDLSRRN VGPNFPGPAE VQMGVLKPKS SWRRPIQATL EEINCHHNWT AISTGQLACR
SCKQFLAGVQ CHHCHAVYCF MCAEAYHDVQ AEKILSKDYS FSARGKKGKA VIIEEDEIEG
EFLISQLQQE NQRLQKQVER LQEELMKLHR EKDEALKHSE KASRVFSTIQ ESDEAELNLI
KEELRQFKEE TRMAIAQLKE AIIVQEEDTI EERCAMILEE KHTENIYSAT AKAEYNGLYN
VKVGIKPDNM EPYYINAIVD TGATACLIQI SAIPENYYED AKVTVNFRSV LGIGTSTQMI
KAGRILIGEQ YFRMPVTYVM NMGLSPGIQM IIGCSFIRSL EGGLRIEKDI ITFYKLVTSI
ETSRTTQVAN SIEELELSED EYLNIAASVE TPSFLDQEFA RKNKDLLKEM KEMKYIGENP
MEFWKNNKIK CKLNIINPDI KIMGRPIKHV TPGDEEAMTR QINLLLQMKV IRPSESKHRS
TAFIVRSGTE IDPITGKEKK GKERMVFNYK LLNENTESDQ YSLPGINTII SKVGRSKIYS
KFDLKSGFWQ VAMEEESVPW TAFLAGNKLY EWLVMPFGLK NAPAIFQRKM DNVFKGTEKF
IAVYIDDILV FSETAEQHSQ HLYTMLQLCK ENGLILSPTK MKIGTPEIDF LGASLGCTKI
KLQPHIISKI CDFSDEKLAT PEGMRSWLGI LSYARNYIQD IGKLVQPLRQ KMAPTGDKRM
NPETWKMVRQ IKEKVKNLPD LQLPPKDSFI IIETDGCMTG WGAVCKWKMS KHDPRSTERI
CAYASGSFNP IKSTIDAEIQ AAIHGLDKFK IYYLDKKELI IRSDCEAIIK FYNKTNENKP
SRVRWLTFSD FLTGLGITVT FEHIDGKHNG LADALSRMIN FIVEKNDESP YRFTSSVEDA
LKVCNDDHGR NLISAVINDI ITVLRR
