ID W0NSZ8_9VIRU Unreviewed; 193 AA.
AC W0NSZ8;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 03-MAY-2023, entry version 30.
DE RecName: Full=Non-structural polyprotein 1AB {ECO:0000256|ARBA:ARBA00019743};
DE Flags: Fragment;
GN Name=ORF1b {ECO:0000313|EMBL:AHG54926.1};
OS Turkey astrovirus.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Stellavirales; Astroviridae; Avastrovirus.
OX NCBI_TaxID=70793 {ECO:0000313|EMBL:AHG54926.1};
RN [1] {ECO:0000313|EMBL:AHG54926.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PL/TK/G123/2010 {ECO:0000313|EMBL:AHG54926.1};
RA Domanska-Blicharz K., Jacukowicz A., Bocian L., Minta Z.;
RT "Astroviruses in Polish commercial turkey farms in 2009-2012.";
RL Avian Dis. 58:158-164(2014).
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; KF736865; AHG54926.1; -; 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 74..193
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AHG54926.1"
FT NON_TER 193
FT /evidence="ECO:0000313|EMBL:AHG54926.1"
SQ SEQUENCE 193 AA; 23021 MW; 650A848B1E031A8D CRC64;
LKNEVLKKEK IEDNDIRMIL CTDPVFTRIG AMFEQDQNNR MKQQTETRSA QVGWTPFFGG
LDRRVRRLCG DGDRYFVEMD WTRYDGTIPK PLFWRIRQIR FFFLHDSHKT SEMRRLYNWY
VKNLLEKIIL LPTGEVCQVK KGNPSGQYST TVDNNMINVW LTAFEISYLF FKQFGRLPTE
KELQENCSMI CYG
//
