ID   A2T0K6_9VIRU            Unreviewed;       217 AA.
AC   A2T0K6;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   03-MAY-2023, entry version 61.
DE   RecName: Full=Non-structural polyprotein 1AB {ECO:0000256|ARBA:ARBA00019743};
DE   Flags: Fragment;
OS   Turkey astrovirus.
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC   Stellavirales; Astroviridae; Avastrovirus.
OX   NCBI_TaxID=70793 {ECO:0000313|EMBL:ABF06838.1};
RN   [1] {ECO:0000313|EMBL:ABF06838.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=1722/7/04 {ECO:0000313|EMBL:ABF06838.1};
RX   PubMed=17106624; DOI=10.1007/s00705-006-0862-4;
RA   Cattoli G., De Battisti C., Toffan A., Salviato A., Lavazza A., Cerioli M.,
RA   Capua I.;
RT   "Co-circulation of distinct genetic lineages of astroviruses in turkeys and
RT   guinea fowl.";
RL   Arch. Virol. 152:595-602(2007).
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; DQ381373; ABF06838.1; -; 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          5..139
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50507"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABF06838.1"
FT   NON_TER         217
FT                   /evidence="ECO:0000313|EMBL:ABF06838.1"
SQ   SEQUENCE   217 AA;  25460 MW;  52E61EA7DC158DD6 CRC64;
     GDGDRYFVEM DWTRYDGTIP KPLFWRIRQI RFFFLXDSHK TQKMRRLYNW YVKNLLEKII
     LLPTGEVCQV KKGNPSGQYS TTVDNNMINV WLTTFEISYL FFKQRGRLPT EKELQENCSM
     ICYGDDRLLS IRKGFVEYEP DTVIEMYKNI FGMWVKRSNI KIQDTPEGLS FCGLTIVKSK
     TGTYVGVPNV DKILSTLENP VRRLPDVESL WGKLVSL
//