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Database: UniProt
Entry: Q8QME5_9POTV
LinkDB: Q8QME5_9POTV
Original site: Q8QME5_9POTV 
ID   Q8QME5_9POTV            Unreviewed;       475 AA.
AC   Q8QME5;
DT   01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2002, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
DE   Flags: Fragment;
OS   Colombian datura virus.
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC   Patatavirales; Potyviridae; Potyvirus.
OX   NCBI_TaxID=91613 {ECO:0000313|EMBL:CAD26690.1};
RN   [1] {ECO:0000313|EMBL:CAD26690.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Godollo {ECO:0000313|EMBL:CAD26690.1};
RA   Salamon P., Palkovics L.;
RT   "Colombian datura virus is a new pathogen in Hungary (In Hungarian).";
RL   Kertesz. Szolesz. 51:13-13(2002).
RN   [2] {ECO:0000313|EMBL:CAD26690.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Godollo {ECO:0000313|EMBL:CAD26690.1};
RA   Salamon P., Palkovics L.;
RT   "Virus and virus diseases of cultivated and wild-growing solanaceous plants
RT   in Hungary. 5. Ocurence, natural hosts and identification of Colombian
RT   datura virus (CDV).";
RL   Novenyvedelem 39:581-588(2003).
RN   [3] {ECO:0000313|EMBL:CAD26690.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Godollo {ECO:0000313|EMBL:CAD26690.1};
RX   PubMed=16047739;
RA   Salamon P., Palkovics L.;
RT   "Occurrence of Colombian datura virus in Brugmansia hybrids, Physalis
RT   peruviana L. and Solanum muricatum Ait. in Hungary.";
RL   Acta Virol. 49:117-122(2005).
CC   -!- FUNCTION: Involved in aphid transmission, cell-to-cell and systemis
CC       movement, encapsidation of the viral RNA and in the regulation of viral
CC       RNA amplification. {ECO:0000256|ARBA:ARBA00029405}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000256|ARBA:ARBA00004328}.
CC   -!- SIMILARITY: Belongs to the potyviridae genome polyprotein family.
CC       {ECO:0000256|ARBA:ARBA00006064, ECO:0000256|RuleBase:RU003351}.
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DR   EMBL; AJ437482; CAD26690.1; -; Genomic_RNA.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR001592; Poty_coat.
DR   InterPro; IPR001205; RNA-dir_pol_C.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   Pfam; PF00767; Poty_coat; 1.
DR   Pfam; PF00680; RdRP_1; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   3: Inferred from homology;
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Viral RNA replication {ECO:0000256|ARBA:ARBA00022953};
KW   Virion {ECO:0000256|ARBA:ARBA00022844}.
FT   DOMAIN          1..49
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50507"
FT   REGION          209..228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..223
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CAD26690.1"
SQ   SEQUENCE   475 AA;  54585 MW;  AB015C21610D32EA CRC64;
     STVVDSTLMV NIAMFYAMHS RDIPKESVRF YVNGDDLLIA IEPQYEDELK HFQALFLELG
     LIYTFDDITK DRSDVEFMSH KAVLREGIYI PKLEPERIVS ILEWDRSGEP SHRLEAICAS
     IIESWGYDEL TKRIRMFYLW ILEQAPYKQL AEEGRAPYLA ETALRKLYLD AEPTESELLK
     YAGCIRGDYD DSLASEDIYL QADKVDAGSN TQAGKNQSKE KDTSVVTTGE RKDLVAKQDR
     DVNAGSSGTF SVPRIKAIPT KMNLPKIKNK QVISLDHLLN YKPEQHDISN TRATHQQFEQ
     WHNRVRDAYE VTDEQMQIIL NGLMVWCIEN GTSPNIHGVW TMMDGEEQVE YALKPIIENA
     QPTFRQIMAH FSDLAEAYIE MRNRDRAYMP RYGLQRNLTD MSLSRYAFDF YEVTPRTPTR
     AREAHMQMKA AAIRNNTTKL FGLDGNVSTA EEDTERHTAQ DVNRGMHTLL GVRQG
//
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