ID E9M477_9VIRU Unreviewed; 280 AA.
AC E9M477;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-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 2.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Stellavirales; Astroviridae; Avastrovirus; Avastrovirus 2.
OX NCBI_TaxID=336961 {ECO:0000313|EMBL:ADQ43320.1};
RN [1] {ECO:0000313|EMBL:ADQ43320.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DE-CK-SEP ANV-811-2005 {ECO:0000313|EMBL:ADQ43320.1};
RX PubMed=21069394; DOI=10.1007/s00705-010-0849-z;
RA Pantin-Jackwood M.J., Strother K.O., Mundt E., Zsak L., Day J.M.,
RA Spackman E.;
RT "Molecular characterization of avian astroviruses.";
RL Arch. Virol. 156:235-244(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; HQ188693; ADQ43320.1; -; Viral_cRNA.
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 25..158
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADQ43320.1"
SQ SEQUENCE 280 AA; 32521 MW; 11CEBB44F687E5D6 CRC64;
AQVGWTPFFG GLDKRVRRIT SCGRTQVLEL DWTRFDGTIP VQLFQRMRTM RKFFLTRRSR
KKYGKLLDWY NAQLTDRITL LPTGEVTHVK KGNPSGQFST TVDNNLVNEW LTAFEFAFQH
LENHGTIPTV KDYRANVDFL CYGDDRLLAY NPSFVNYDPQ KTIDMYKNIF GMWVKPENIK
LFESPTGSSF CGFTLVKPHG KWVGVVNVDK LLQSLKTPTR RLPDIESLWG KLVSLKIMCY
HSDPEAVSYL SNQIKRVEEY ARAEGIELPE VGPDFYRKIW
//