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Database: UniProt
Entry: Q071G7_9VIRU
LinkDB: Q071G7_9VIRU
Original site: Q071G7_9VIRU 
ID   Q071G7_9VIRU            Unreviewed;       172 AA.
AC   Q071G7;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   03-MAY-2023, entry version 62.
DE   RecName: Full=Non-structural polyprotein 1AB {ECO:0000256|ARBA:ARBA00019743};
DE   Flags: Fragment;
OS   Chicken astrovirus.
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC   Stellavirales; Astroviridae; Avastrovirus.
OX   NCBI_TaxID=336959 {ECO:0000313|EMBL:ABC60217.1};
RN   [1] {ECO:0000313|EMBL:ABC60217.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=GA-SEP-A457-05 {ECO:0000313|EMBL:ABC60217.1};
RX   PubMed=17039840; DOI=10.1637/7512-020606R.1;
RA   Pantin-Jackwood M.J., Spackman E., Woolcock P.R.;
RT   "Molecular characterization and typing of chicken and turkey astroviruses
RT   circulating in the United States: implications for diagnostics.";
RL   Avian Dis. 50:397-404(2006).
CC   -!- FUNCTION: Contains the viral protease participating in the cleavage of
CC       the polyprotein into functional products. It contains also the
CC       activities necessary for replication of genomic RNA, as well as
CC       transcription of subgenomic mRNA. {ECO:0000256|ARBA:ARBA00029407}.
CC   -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000256|ARBA:ARBA00004301};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004301}.
CC   -!- SIMILARITY: Belongs to the astroviridae polyprotein 1AB family.
CC       {ECO:0000256|ARBA:ARBA00005873}.
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DR   EMBL; DQ324846; ABC60217.1; -; Genomic_RNA.
DR   GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
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   CDD; cd23172; ps-ssRNAv_Astroviridae_RdRp; 1.
DR   Gene3D; 3.30.70.270; -; 1.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR001205; RNA-dir_pol_C.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
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   Ribosomal frameshifting {ECO:0000256|ARBA:ARBA00022758};
KW   RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Viral RNA replication {ECO:0000256|ARBA:ARBA00022953}.
FT   DOMAIN          51..172
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50507"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABC60217.1"
FT   NON_TER         172
FT                   /evidence="ECO:0000313|EMBL:ABC60217.1"
SQ   SEQUENCE   172 AA;  20418 MW;  B2C7E66E0B043989 CRC64;
     PVFTRIGAMF DQDQNSKMKN MTETRAAQVG WTPFFGGLDQ RMRRLEKIKN AQFVEMDWTR
     FDGTIPKALF WRIRQIRFFF LAPRYKTEDN KELFDWYTKN LLEKIILLPT GEVCQVKRGN
     PSGQFSTTVD NNMCNVWLTT FEISWLHRKQ KGRLPTPTEL SKNLRYICYG DD
//
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