ID A8QWX1_9POTV Unreviewed; 497 AA.
AC A8QWX1;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
DE Flags: Fragment;
OS Chilli veinal mottle virus.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=52280 {ECO:0000313|EMBL:ABQ23271.1};
RN [1] {ECO:0000313|EMBL:ABQ23271.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CHM19 {ECO:0000313|EMBL:ABQ23271.1};
RA Reddy C.N.L., Devaraju, Madhavi Reddy K., Krishnareddy M.,
RA Venkataravanappa V., Jalali S., Usha Rani T.R., Raman L., Jalali S.,
RA Ajith Prasad H.N.;
RT "Molecular genetic diversity of Chilli veinal mottle virus infecting chilli
RT pepper in India.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
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; EF213689; ABQ23271.1; -; Genomic_RNA.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; 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 Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR001592; Poty_coat.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
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..56
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT REGION 199..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABQ23271.1"
SQ SEQUENCE 497 AA; 56926 MW; 5B34498D41849132 CRC64;
GQPSTVVDNT LMVLVAMRYS LRRLGINYKD QNERCVFFAN GDDLIVSVPP RDEWILDSLQ
EPFSELGLSY DFNERTRKRS ELWFMSHQGI LIEDQYVPKL EPERIVSILE WDRAEQPEHQ
LEAIWASMIE AWGYKELLHE IRLFYKWVIE QAPYSRLVSE GKAPYISETA LTCLYMSEHG
ESDISPYLRA LIEGAKKEEL DDEGGEVAHQ AGDSVDAGRV KGEDSSSKPA DNRATEMKNK
VSEQDQPQSR QSEMEVPQVR DRDVNVGTSG TFTIPRLKGI SSKLTIPTIK TKAVVNLEHL
LDYAPEQIHL SNTRALQSQF ASWYEGVKND YDVTDEQMQI ILNGLMVWCI ENGTSPNING
YWVMMDGDEQ VEYPIKPLID HAKPSFRQIM AHFSNLAEAY IEKRNSEKPY MPRYGLQRNL
TDMSLARYAF DFYEMTSKTP VRAREAHIQM KAAALRGVSN RMFGLDGRVG TQEEDTERHT
AEDVNRNMHN LLGVRGL
//
