ID A8QWX8_9POTV Unreviewed; 497 AA.
AC A8QWX8;
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:ABQ23278.1};
RN [1] {ECO:0000313|EMBL:ABQ23278.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=L33 {ECO:0000313|EMBL:ABQ23278.1};
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}.
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; EF213696; ABQ23278.1; -; 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..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABQ23278.1"
SQ SEQUENCE 497 AA; 56654 MW; EBBEE57B5C21BB8D CRC64;
GQPSTVVDNT LMVLVAMRYS LRRLGINYKD QNSRCVFFAN GDDLIVSVPP SDEWILDSLQ
EPFSELGLSY DFGERTKERS ELWFMSHQGI LIEDQYIPKL EPERIVSILE WDRAEQPEHR
LEAICASMIE AWGYKELLHE IRLFYRWVIE QAPYSQLVSE GKAPYISETA LRCLYMSKHG
ESDISPYLKA LIEGAKKEEL DDEGGEVTHQ SGESVDAGRV KGEDSSSKPA DKQATEKKNK
VGGQAQPQSR QSEMEVPQVR DRDVNVGTSG TFTIPRLKGI SSKLTIPKIK TKAVVNLEHL
LDYAPEQIHL SNTRALQSQF ASWYEGVKND YDVTDEQMQI ILNGLMVWCI ENGTSPNING
YWVMMDGEEQ VEYPIKPLID HAKPSFRQIM AHFSNLAEAY IEKRNSEKPY MPRYGLQRNL
TDMSLARYAF DFYEMTSKTP VRAREAHIQM KAAALRGVSN RMFGLDGRVG TQEEDTERHT
AEDVNRNMHN LLGVRGL
//
