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Database: UniProt
Entry: D0UV44_HASV6
LinkDB: D0UV44_HASV6
Original site: D0UV44_HASV6 
ID   D0UV44_HASV6            Unreviewed;       515 AA.
AC   D0UV44;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   08-NOV-2023, entry version 43.
DE   RecName: Full=Non-structural polyprotein 1AB {ECO:0000256|ARBA:ARBA00019743};
DE   Flags: Fragment;
OS   Human astrovirus-6 (HAstV-6).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC   Stellavirales; Astroviridae; Mamastrovirus; Mamastrovirus 1.
OX   NCBI_TaxID=37130 {ECO:0000313|EMBL:ACX83560.1};
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1] {ECO:0000313|EMBL:ACX83560.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Rus-Nsc09-B4 {ECO:0000313|EMBL:ACX83560.1};
RX   PubMed=22326537; DOI=10.1016/j.meegid.2012.01.019;
RA   Babkin I.V., Tikunov A.Y., Zhirakovskaia E.V., Netesov S.V., Tikunova N.V.;
RT   "High evolutionary rate of human astrovirus.";
RL   Infect. Genet. Evol. 12:435-442(2012).
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; GQ901902; ACX83560.1; -; 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   ECO:0000313|EMBL:ACX83560.1}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Viral RNA replication {ECO:0000256|ARBA:ARBA00022953}.
FT   DOMAIN          260..386
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50507"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACX83560.1"
SQ   SEQUENCE   515 AA;  60294 MW;  D0A72B8AA13D59AC CRC64;
     GSKKLQRAPE DQGAQNYHSL DAWQVLLEPP RERRCVPTNF PLVGHLPINR PIYDDKKPRD
     DLLGLLPEPT WHAFEEYGPT TWGPQAFIKS FDKFFYAEPI DFFSEYPQLC AFADWATYRE
     FRYLEDTRVI HITATEKNTD STPAYPKMNY FDSEEEYLEA HGWAPYIREF TRVFRGEKPE
     VLWYLFLKKE IIKEEKIRNS DIRQIVCADP IYTRIGACLE AHQNSLMKQH TETAVGQCGW
     SPMEGGFKKT MQRLVNRGNK YFIEFDWTRY DGTIPPALFR HIKEIRWNFI NKDQREKYRH
     VHEWYVDNLL NRHVLLPSGE VTVQTRGNPS GQFSTTMDNN MVNFWLQAFE FAYFNGPDKD
     LWKTYDTVVY GDDRLSTTPS VPENYEERVI NMYRDIFGMW VKPGKVICRE SIVGLSFCGF
     TVNADLEPVP TSPEKLMASL LKPYKILPDL ESLHGKLLCY QLLAAFMAED HPFKVYVEHC
     LSRTAKQLRD SGLPARLTEE QLHRIWRGGP KKCDG
//
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