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Database: UniProt
Entry: D9MNM2_9VIRU
LinkDB: D9MNM2_9VIRU
Original site: D9MNM2_9VIRU 
ID   D9MNM2_9VIRU            Unreviewed;       516 AA.
AC   D9MNM2;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   03-MAY-2023, entry version 41.
DE   RecName: Full=Non-structural polyprotein 1AB {ECO:0000256|ARBA:ARBA00019743};
DE   Flags: Fragment;
GN   Name=ORF1b {ECO:0000313|EMBL:ADJ38390.1};
OS   Astrovirus rat/RS118/HKG/2007.
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC   Stellavirales; Astroviridae.
OX   NCBI_TaxID=858506 {ECO:0000313|EMBL:ADJ38390.1};
RN   [1] {ECO:0000313|EMBL:ADJ38390.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=RS118 {ECO:0000313|EMBL:ADJ38390.1};
RX   PubMed=20554799; DOI=10.1099/vir.0.022764-0;
RA   Chu D.K., Chin A.W., Smith G.J., Chan K.H., Guan Y., Peiris J.S.,
RA   Poon L.L.;
RT   "Detection of novel astroviruses in urban brown rats and previously known
RT   astroviruses in humans.";
RL   J. Gen. Virol. 91:2457-2462(2010).
RN   [2] {ECO:0000313|EMBL:ADJ38390.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=RS118 {ECO:0000313|EMBL:ADJ38390.1};
RA   Chu D.K.W., Chin A.W.H., Smith G.J., Chan K.H., Guan Y., Peiris J.S.,
RA   Poon L.L.M.;
RL   Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
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; HM450381; ADJ38390.1; -; 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          261..387
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50507"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADJ38390.1"
SQ   SEQUENCE   516 AA;  60673 MW;  08194A47014A431F CRC64;
     KKREKGPQAG PKEWYQLDYW RLLVTPGVRR RLVPDDYPLV GVVPMNRPIC DFDEPVDPHL
     GVLPPPPKVQ QLEDYGPTIW DESAYLKSFE KFYYAEPSDF FQDYPELCAF ADAAFRKHFS
     FLQDTRVVHI TATEKNLDSS PAYPKLCWYS TERDFLEEQM WAPYIKEFAR VDRLTKDGKG
     PRVLWYCFLK KEILKAQKIK DGDIRQILCA DPIYSRMGAC FEQHQNQLMK EMADVSSGQC
     GWTPFEGGFR AVCERLQEKN GVFIEFDWTR FDGTIPTCLF LHIKKLRWSF MEKTHQERYG
     KMYRWYCKNL VDRYVVMPSG EVTKQKRGNP SGQISTTMDN NMVNYWLQAF EWAWFNGPDF
     EKFNEFETVV YGDDRLSTWS RVPDDFSTLA SDMYRRVFGM WVKPEKVKVS SQLEGLSFCG
     FTIGPGFNPR PAEPFKLMAS LLKPSKKLPD YLALHGKLLC YQILMHFVED EHPFKRYVLR
     CLDVTWRLSG KKLLRRFTEQ QLNALWWGGP KKCDGR
//
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