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Database: UniProt
Entry: F8SQS1_9VIRU
LinkDB: F8SQS1_9VIRU
Original site: F8SQS1_9VIRU 
ID   F8SQS1_9VIRU            Unreviewed;       149 AA.
AC   F8SQS1;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   08-NOV-2023, entry version 36.
DE   RecName: Full=Non-structural polyprotein 1AB {ECO:0000256|ARBA:ARBA00019743};
DE   Flags: Fragment;
OS   Avian nephritis virus pigeon/Shanghai/2010.
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC   Stellavirales; Astroviridae; Avastrovirus; Chicken astrovirus.
OX   NCBI_TaxID=1046308 {ECO:0000313|EMBL:AEI91105.1};
RN   [1] {ECO:0000313|EMBL:AEI91105.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PeANV-10 {ECO:0000313|EMBL:AEI91105.1};
RX   PubMed=21812714; DOI=10.1080/03079457.2011.587792;
RA   Zhao W., Zhu A.L., Yuan C.L., Yu Y., Zhu C.X., Lan D.L., Yang Z.B., Cui L.,
RA   Hua X.G.;
RT   "Detection of astrovirus infection in pigeons (Columbia livia) during an
RT   outbreak of diarrhoea.";
RL   Avian Pathol. 40:361-365(2011).
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; HQ662576; AEI91105.1; -; 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   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   ECO:0000313|EMBL:AEI91105.1}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Viral RNA replication {ECO:0000256|ARBA:ARBA00022953}.
FT   DOMAIN          1..82
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50507"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AEI91105.1"
FT   NON_TER         149
FT                   /evidence="ECO:0000313|EMBL:AEI91105.1"
SQ   SEQUENCE   149 AA;  16920 MW;  4B32FC85B9BC29D2 CRC64;
     RITLLPTGEV THVKKGNPSG QFSTTVDNNL VNEWLTAFEF AFQYLENHGT IPTVKDYRAN
     VGFLCYGDDR LLAYNPSFVN YDPQKTIDMY KNIFGMWVKP ENIKLFESPT GSSFCGFTLV
     KPHGKWVGVV NVDKLLQSLK TPTRRLPDI
//
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