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Database: UniProt
Entry: Q6PPS3_9CALI
LinkDB: Q6PPS3_9CALI
Original site: Q6PPS3_9CALI 
ID   Q6PPS3_9CALI            Unreviewed;       266 AA.
AC   Q6PPS3;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 72.
DE   SubName: Full=Non-structural polyprotein {ECO:0000313|EMBL:AAT00290.1};
DE   Flags: Fragment;
OS   Norovirus Hu/NLV/Oxford/B2S18/2002/UK.
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Caliciviridae; Norovirus; Norwalk virus.
OX   NCBI_TaxID=272589 {ECO:0000313|EMBL:AAT00290.1};
RN   [1] {ECO:0000313|EMBL:AAT00290.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Hu/NLV/Oxford/B2S18/2002/UK {ECO:0000313|EMBL:AAT00290.1};
RX   PubMed=15364974; DOI=10.1128/JCM.42.9.3950-3957.2004;
RA   Dingle K.E.;
RT   "Mutation in a Lordsdale norovirus epidemic strain as a potential indicator
RT   of transmission routes.";
RL   J. Clin. Microbiol. 42:3950-3957(2004).
CC   -!- FUNCTION: Viral genome-linked protein is covalently linked to the 5'-
CC       end of the positive-strand, negative-strand genomic RNAs and subgenomic
CC       RNA. Acts as a genome-linked replication primer. May recruit ribosome
CC       to viral RNA thereby promoting viral proteins translation.
CC       {ECO:0000256|ARBA:ARBA00025359}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC         diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC         Evidence={ECO:0000256|ARBA:ARBA00001491};
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DR   EMBL; AY588002; AAT00290.1; -; Genomic_RNA.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:InterPro.
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   Gene3D; 1.20.960.20; -; 1.
DR   Gene3D; 3.30.70.270; -; 1.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
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   PRINTS; PR00918; CALICVIRUSNS.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   4: Predicted;
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
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          1..113
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50507"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAT00290.1"
SQ   SEQUENCE   266 AA;  29841 MW;  55B3A2E124996389 CRC64;
     RWDSTQQRAV LASALEIMVK FSSEPHLAQV VAEDLLSPSV VDVGDFTISI NEGLPSGVPC
     TSQWNSIAHW LLTLCALSEV TNLSPDIIQA NSLFSFYGDD EIVSTDIKLD PEKLTAKLRE
     YGLKPTRPDK TEGPLVISED LNGLTFLRRT VTRDPAGWFG KLEQSSILRQ MYWTRGPNHE
     DPSETMIPHS QRPIQLMSLL GEAALHGPAF YSKISKLVIA ELKEGGMDFY VPRQEPMFRW
     MRFSDLSTWE GDRNLAPSFV NEDGVE
//
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