ID B5AFN8_9VIRU Unreviewed; 742 AA.
AC B5AFN8;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 03-MAY-2023, entry version 60.
DE RecName: Full=Non-structural polyprotein 1AB {ECO:0000256|ARBA:ARBA00019743};
DE Flags: Fragment;
OS Bat astrovirus 1.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Stellavirales; Astroviridae; Mamastrovirus.
OX NCBI_TaxID=548468 {ECO:0000313|EMBL:ACF75858.1};
RN [1] {ECO:0000313|EMBL:ACF75858.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AFCD82 {ECO:0000313|EMBL:ACF75858.1};
RX PubMed=18550669; DOI=10.1128/JVI.00857-08;
RA Chu D.K., Poon L.L., Guan Y., Peiris J.S.;
RT "Novel astroviruses in insectivorous bats.";
RL J. Virol. 82:9107-9114(2008).
RN [2] {ECO:0000313|EMBL:ACF75858.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AFCD82 {ECO:0000313|EMBL:ACF75858.1};
RA Chu D.K.W., Poon L.L.M., Guan Y., Peiris J.S.M.;
RL Submitted (JUN-2008) 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; EU847150; ACF75858.1; -; 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; IPR045836; Astro_VPg.
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; PF19416; Astro_VPg; 1.
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 Coiled coil {ECO:0000256|SAM:Coils};
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 484..616
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT REGION 212..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 19..47
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACF75858.1"
FT NON_TER 742
FT /evidence="ECO:0000313|EMBL:ACF75858.1"
SQ SEQUENCE 742 AA; 87275 MW; B93C38ABFD35AD95 CRC64;
EVEVLRHELD TDFGQAKGKT KAKARLNKHK KRVKAFTEEE YKALQEKGYT RDQLRDMAAV
ILERMNETIY DEDEVGYPEY GDIDEEERRE IEREWLGVEP DHEDYVRDTY RQSYTVEVVP
VELDYNPKTH PWDVHDKYSL SMYHVTDADV KMVGQALLDY DHYLVKWMAK NLRGNEWQSG
IDIAKELKEL AEAKLRLEMV MTQNGLTPFC QRKKKERKSK TIKKVPKNPQ EPPGRGERIK
YEYMKLGYWK NDLDLPYRVV VPSNFPLIGN IHIDRPISDW SEPKDPLVGL LPKPPCYEDH
YGPSVWGYDA YAKSFEKFFY AEPVKNIQDV YPKQWNFASR WLLREYGYLK NTHVLDITAT
TKNVHSTPAY PKFMYWKTEE EYLEERGYCD YVRQLEDIRS GERPDVLWYL FLKKEILKKA
KINESDIRQI VCADPIYTRI GAMFEQDQNN RMKEMTPWKQ AQCGWSPFEG GFHTVIDRLN
REGNTYIEFD WTRYDGTIPN EIFRHIKEFR FSMLDPVYKT DQNKSIYDWY VDQLLYRYVL
LPSGEVTVQT RGNPSGQIST TMDNNLVNTF LQAFEFAYIH PELDLDELDV LYSQCDSLIY
GDDRLSSWPC VPTDYVNLVV GMYKHVFGMW VKPEKVKISD TLIGLTFCGF TIISDGQVFL
PVPNDAWKFI SSTLHPTKQL PDFDALVGKI LSYQILTHNL PDDDPVKNWF EEAHAALVLH
NRVSGGEPLP TMTRDMRDFL WS
//
