ID Q99HQ2_9POTV Unreviewed; 488 AA.
AC Q99HQ2;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
DE Flags: Fragment;
OS Hibbertia virus Y.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=114892 {ECO:0000313|EMBL:AAK00712.1, ECO:0000313|Proteomes:UP000232817};
RN [1] {ECO:0000313|EMBL:AAK00712.1, ECO:0000313|Proteomes:UP000232817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kioloa {ECO:0000313|EMBL:AAK00712.1,
RC ECO:0000313|Proteomes:UP000232817};
RX PubMed=9015271; DOI=10.1016/S0166-0934(96)02103-9;
RA Gibbs A., Mackenzie A.;
RT "A primer pair for amplifying part of the genome of all potyvirids by RT-
RT PCR.";
RL J. Virol. Methods 63:9-16(1997).
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; AF228516; AAK00712.1; -; Genomic_RNA.
DR Proteomes; UP000232817; Genome.
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..60
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT REGION 217..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAK00712.1"
SQ SEQUENCE 488 AA; 55519 MW; E193169C25CBDBD8 CRC64;
GNNSGQPSTV VDNTLMVVVS VYYSCIKLGW TEADIRNQLV FFANGDDIIL AVPTNCEYLY
DAMGESFMEL GLNYDFSERT QQREDLWFMS HQAKEIEGVY IPKLEMERIV SILEWDRSKE
LMHRTEAICA AMIEAWGHTE LLQEIRKFYM WLIQKSEFKE LALLGKTPYI AETALKKLYT
DKDATQEEIE AYLKVLCMHR DECNEAVSLQ SKREETIDAG VEKEQTTGKK AVGSSSDTEK
NKEKGGSGVV KDKDVNAGSK GSVVPRLQRI TKKMNLPMVK GNMILNLEHL IEYKPDQTKL
FNTRATDSQF AAWYEGIKEK YEVDDNQMSV IMNGFMVWCI DNGTSPDING VWVMMDGNEQ
IEYPLKPMVE NAKPILRQIM HHFSDAAEAY IEMRCASGPY MPRYGLLRDL RDKNLARYAF
DFYEVNVKTS DRAREAVAQM KAAALSNVTN KLFGLDGNVA TTSEDTERHT ARDVSQNMHS
LLGMGSMQ
//
