ID Q80J95_MNV1 Unreviewed; 1687 AA. AC Q80J95; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 06-DEC-2005, sequence version 2. DT 27-MAR-2024, entry version 125. DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107}; OS Norovirus (isolate Mouse/NoV/United States/MNV1/2002/GV) (MNV-1) (Murine OS Norovirus 1). OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes; OC Picornavirales; Caliciviridae; Norovirus; Norwalk virus. OX NCBI_TaxID=223997 {ECO:0000313|EMBL:AAO63098.2, ECO:0000313|Proteomes:UP000109015}; RN [1] {ECO:0000313|EMBL:AAO63098.2, ECO:0000313|Proteomes:UP000109015} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Mu/NoV/GV/MNV1/2002/USA {ECO:0000313|EMBL:AAO63098.2}; RX PubMed=12624267; DOI=10.1126/science.1077905; RA Karst S.M., Wobus C.E., Lay M., Davidson J., Virgin H.W.; RT "STAT1-dependent innate immunity to a Norwalk-like virus."; RL Science 299:1575-1578(2003). RN [2] {ECO:0000313|EMBL:AAO63098.2, ECO:0000313|Proteomes:UP000109015} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Mu/NoV/GV/MNV1/2002/USA {ECO:0000313|EMBL:AAO63098.2}; RX PubMed=16210475; DOI=10.1128/CDLI.12.10.1145-1151.2005; RA Hsu C.C., Wobus C.E., Steffen E.K., Riley L.K., Livingston R.S.; RT "Development of a microsphere-based serologic multiplexed fluorescent RT immunoassay and a reverse transcriptase PCR assay to detect murine RT norovirus 1 infection in mice."; RL Clin. Diagn. Lab. Immunol. 12:1145-1151(2005). RN [3] {ECO:0007829|PDB:3NAH, ECO:0007829|PDB:3NAI} RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 1181-1686, AND X-RAY RP CRYSTALLOGRAPHY (2.56 ANGSTROMS) OF 1181-1686 IN COMPLEX WITH MAGNESIUM. RA Kim K.H., Lee J.H., Alam I., Park Y., Kang S.; RT "Crystal structures and functional analysis of murine norovirus RNA- RT dependent RNA polymerase."; RL Submitted (JUN-2010) to the PDB data bank. RN [4] {ECO:0007829|PDB:3QID} RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1181-1686. RX PubMed=21471315; DOI=10.1099/vir.0.031104-0; RA Lee J.H., Alam I., Han K.R., Cho S., Shin S., Kang S., Yang J.M., Kim K.H.; RT "Crystal structures of murine norovirus-1 RNA-dependent RNA polymerase."; RL J. Gen. Virol. 92:1607-1616(2011). RN [5] {ECO:0007829|PDB:3UPF, ECO:0007829|PDB:3UQS} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1181-1687, AND DISULFIDE BONDS. RX PubMed=22446684; DOI=10.1016/j.jmb.2012.03.008; RA Mastrangelo E., Pezzullo M., Tarantino D., Petazzi R., Germani F., RA Kramer D., Robel I., Rohayem J., Bolognesi M., Milani M.; RT "Structure-based inhibition of Norovirus RNA-dependent RNA polymerases."; RL J. Mol. Biol. 419:198-210(2012). RN [6] {ECO:0007829|PDB:4ASH} RP X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 995-1177. RX PubMed=22685603; DOI=10.1371/journal.pone.0038723; RA Leen E.N., Baeza G., Curry S.; RT "Structure of a murine norovirus NS6 protease-product complex revealed by RT adventitious crystallisation."; RL PLoS ONE 7:e38723-e38723(2012). RN [7] {ECO:0007829|PDB:3SFG, ECO:0007829|PDB:3SFU} RP X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 1181-1686 IN COMPLEX WITH RP MAGNESIUM, AND DISULFIDE BONDS. RX PubMed=22341781; DOI=10.1016/j.virol.2012.01.016; RA Alam I., Lee J.H., Cho K.J., Han K.R., Yang J.M., Chung M.S., Kim K.H.; RT "Crystal structures of murine norovirus-1 RNA-dependent RNA polymerase in RT complex with 2-thiouridine or ribavirin."; RL Virology 426:143-151(2012). RN [8] {ECO:0007829|PDB:2M4G} RP STRUCTURE BY NMR OF 881-955. RX PubMed=23487472; DOI=10.1128/JVI.03151-12; RA Leen E.N., Kwok K.Y., Birtley J.R., Simpson P.J., Subba-Reddy C.V., RA Chaudhry Y., Sosnovtsev S.V., Green K.Y., Prater S.N., Tong M., Young J.C., RA Chung L.M., Marchant J., Roberts L.O., Kao C.C., Matthews S., RA Goodfellow I.G., Curry S.; RT "Structures of the compact helical core domains of feline calicivirus and RT murine norovirus VPg proteins."; RL J. Virol. 87:5318-5330(2013). RN [9] {ECO:0007829|PDB:4O4R} RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1181-1687, AND DISULFIDE BONDS. RX PubMed=24657439; DOI=10.1016/j.febslet.2014.03.021; RA Croci R., Tarantino D., Milani M., Pezzullo M., Rohayem J., Bolognesi M., RA Mastrangelo E.; RT "PPNDS inhibits murine Norovirus RNA-dependent RNA-polymerase mimicking two RT RNA stacking bases."; RL FEBS Lett. 588:1720-1725(2014). RN [10] {ECO:0007829|PDB:4NRU} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1181-1687 IN COMPLEX WITH RP MAGNESIUM, AND DISULFIDE BONDS. RX PubMed=24622391; DOI=10.1371/journal.pone.0091765; RA Croci R., Pezzullo M., Tarantino D., Milani M., Tsay S.C., Sureshbabu R., RA Tsai Y.J., Mastrangelo E., Rohayem J., Bolognesi M., Hwu J.R.; RT "Structural bases of norovirus RNA dependent RNA polymerase inhibition by RT novel suramin-related compounds."; RL PLoS ONE 9:e91765-e91765(2014). RN [11] {ECO:0007829|PDB:2MCD, ECO:0007829|PDB:2MCH} RP STRUCTURE BY NMR OF 28-114. RX PubMed=24273131; DOI=10.1002/prot.24484; RA Borin B.N., Tang W., Nice T.J., McCune B.T., Virgin H.W., Krezel A.M.; RT "Murine norovirus protein NS1/2 aspartate to glutamate mutation, sufficient RT for persistence, reorients side chain of surface exposed tryptophan within RT a novel structured domain."; RL Proteins 82:1200-1209(2014). RN [12] {ECO:0007829|PDB:4X2V, ECO:0007829|PDB:4X2W} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 995-1178 AND 1174-1178. RX PubMed=25755927; DOI=10.7717/peerj.798; RA Fernandes H., Leen E.N., Cromwell H., Pfeil M.P., Curry S.; RT "Structure determination of Murine Norovirus NS6 proteases with C-terminal RT extensions designed to probe protease-substrate interactions."; RL PeerJ 3:e798-e798(2015). RN [13] {ECO:0007829|PDB:5Y3D} RP X-RAY CRYSTALLOGRAPHY (3.14 ANGSTROMS) OF 1181-1686. RX PubMed=30038601; DOI=10.3389/fmicb.2018.01466; RA Lee J.H., Park B.S., Han K.R., Biering S.B., Kim S.J., Choi J., Seok J.H., RA Alam I., Chung M.S., Kim H.M., Hwang S., Kim K.H.; RT "Insight Into the Interaction Between RNA Polymerase and VPg for Murine RT Norovirus Replication."; RL Front. Microbiol. 9:1466-1466(2018). RN [14] {ECO:0007829|PDB:8A5M, ECO:0007829|PDB:8A8X} RP X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS) OF 699-705. RX PubMed=35893676; DOI=10.3390/v14081610; RA Luptak J., Mallery D.L., Jahun A.S., Albecka A., Clift D., Ather O., RA Slodkowicz G., Goodfellow I., James L.C.; RT "TRIM7 Restricts Coxsackievirus and Norovirus Infection by Detecting the C- RT Terminal Glutamine Generated by 3C Protease Processing."; RL Viruses 14:1610-1610(2022). CC -!- FUNCTION: NTPase presumably plays a role in replication. Despite having CC similarities with helicases, does not seem to display any helicase CC activity. {ECO:0000256|ARBA:ARBA00025124}. 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00870}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY228235; AAO63098.2; -; Genomic_RNA. DR PDB; 2M4G; NMR; -; A=881-955. DR PDB; 2MCD; NMR; -; A=28-114. DR PDB; 2MCH; NMR; -; A=58-114. DR PDB; 3NAH; X-ray; 2.75 A; A/B/C=1181-1686. DR PDB; 3NAI; X-ray; 2.56 A; A/B/C=1181-1686. DR PDB; 3QID; X-ray; 2.50 A; A/B/C=1181-1686. DR PDB; 3SFG; X-ray; 2.21 A; A/B/C=1181-1686. DR PDB; 3SFU; X-ray; 2.50 A; A/B/C=1181-1686. DR PDB; 3UPF; X-ray; 2.60 A; A/B/C=1174-1687. DR PDB; 3UQS; X-ray; 2.00 A; A/B/C=1181-1687. DR PDB; 3UR0; X-ray; 2.45 A; A/B/C=1181-1687. DR PDB; 4ASH; X-ray; 1.58 A; A/B=995-1177. DR PDB; 4NRU; X-ray; 2.30 A; A/B/C/D/E/F=1181-1687. DR PDB; 4O4R; X-ray; 2.40 A; A/B/C=1181-1687. DR PDB; 4X2V; X-ray; 2.30 A; A/B/C/D=995-1178, E=1174-1178. DR PDB; 4X2W; X-ray; 2.70 A; A/B=997-1175. DR PDB; 4X2X; X-ray; 2.47 A; A=998-1173. DR PDB; 4X2Y; X-ray; 2.42 A; A/B=998-1173. DR PDB; 5Y3D; X-ray; 3.14 A; A/B/C/D/E/F=1181-1686. DR PDB; 8A5M; X-ray; 2.92 A; C/E=1171-1177. DR PDB; 8A8X; X-ray; 2.37 A; B/D=699-705. DR PDBsum; 2M4G; -. DR PDBsum; 2MCD; -. DR PDBsum; 2MCH; -. DR PDBsum; 3NAH; -. DR PDBsum; 3NAI; -. DR PDBsum; 3QID; -. DR PDBsum; 3SFG; -. DR PDBsum; 3SFU; -. DR PDBsum; 3UPF; -. DR PDBsum; 3UQS; -. DR PDBsum; 3UR0; -. DR PDBsum; 4ASH; -. DR PDBsum; 4NRU; -. DR PDBsum; 4O4R; -. DR PDBsum; 4X2V; -. DR PDBsum; 4X2W; -. DR PDBsum; 4X2X; -. DR PDBsum; 4X2Y; -. DR PDBsum; 5Y3D; -. DR SMR; Q80J95; -. DR BindingDB; Q80J95; -. DR MEROPS; C37.003; -. DR BRENDA; 2.7.7.48; 11649. DR EvolutionaryTrace; Q80J95; -. DR Proteomes; UP000109015; Genome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0003724; F:RNA helicase activity; 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:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro. DR CDD; cd23192; Caliciviridae_RdRp; 1. DR Gene3D; 1.20.960.20; -; 1. DR Gene3D; 3.30.70.270; -; 2. DR Gene3D; 6.10.20.70; -; 1. DR Gene3D; 6.10.250.3230; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2. DR InterPro; IPR043502; DNA/RNA_pol_sf. DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir. DR InterPro; IPR014759; Helicase_SF3_ssRNA_vir. DR InterPro; IPR001665; Norovirus_pept_C37. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin. DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase. DR InterPro; IPR001205; RNA-dir_pol_C. DR InterPro; IPR007094; RNA-dir_pol_PSvirus. DR InterPro; IPR013614; Viral_PP_Calicivir_N. DR Pfam; PF08405; Calici_PP_N; 1. DR Pfam; PF05416; Peptidase_C37; 1. DR Pfam; PF00680; RdRP_1; 1. DR Pfam; PF00910; RNA_helicase; 1. DR PRINTS; PR00917; SRSVCYSPTASE. DR SUPFAM; SSF56672; DNA/RNA polymerases; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1. DR PROSITE; PS51537; NV_3CL_PRO; 1. DR PROSITE; PS50507; RDRP_SSRNA_POS; 1. DR PROSITE; PS51218; SF3_HELICASE_2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:2M4G, ECO:0007829|PDB:2MCD}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Metal-binding {ECO:0007829|PDB:3NAI, ECO:0007829|PDB:3SFG}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695}; KW Protease {ECO:0000256|ARBA:ARBA00022670}; KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484}; KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953}. FT DOMAIN 476..641 FT /note="SF3 helicase" FT /evidence="ECO:0000259|PROSITE:PS51218" FT DOMAIN 995..1172 FT /note="Peptidase C37" FT /evidence="ECO:0000259|PROSITE:PS51537" FT DOMAIN 1416..1537 FT /note="RdRp catalytic" FT /evidence="ECO:0000259|PROSITE:PS50507" FT REGION 1..62 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 25..46 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 1420 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:3SFG, ECO:0007829|PDB:3SFU" FT BINDING 1422 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3NAI" FT BINDING 1523 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3NAI" FT BINDING 1524 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:3SFG, ECO:0007829|PDB:3SFU" FT BINDING 1525 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:3SFG, ECO:0007829|PDB:3SFU" FT BINDING 1569 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4NRU" FT DISULFID 1383..1484 FT /evidence="ECO:0007829|PDB:3SFG, ECO:0007829|PDB:3SFU" FT DISULFID 1482..1484 FT /evidence="ECO:0007829|PDB:3UR0, ECO:0007829|PDB:4NRU" SQ SEQUENCE 1687 AA; 187473 MW; EA493276296FDB23 CRC64; MRMATPSSAP SVRNTEKRKN KKASSKASVS FGAPSPLSSE SEDEINYMTP PEQEAQPGAL AALHAEGPLA GLPVTRSDAR VLIFNEWEER KKSDPWLRLD MSDKAIFRRY PHLRPKEDRP DAPSHAEDAM DAKEPVIGSI LEQDDHKFYH YSVYIGGGLV MGVNNPSAAV CQATIDVEKL HLWWRPVWEP RXPLDSAELR KCVGMTVPYV ATTVNCYQVC CWIVGIKDTW LKRAKISRDL PFYSPVQDWN VDPQEPFIPS KLRMVSDGIL VALSAVIGRP IKNLLASVKP LNILNIVLSC DWTFSGIVNA LILLAELFDI FWTPPDVTNW MISIFGEWQA EGPFDLALDV VPTLLGGIGM AFGLTSETIG RKLASTNSAL KAAQEMGKFA IEVFKQIMAW IWPSEDPVPA LLSNMEQAII KNECQLENQL TAMLRDRNAG AEFLRSLDEE EQEVRKIAAK CGNSATTGTT NALLARISMA RAAFEKARAE QTSRVRPVVI MVSGRPGIGK TCFCQNLAKR IAASLGDETS VGIIPRADVD HWDAYKGARV VLWDDFGMDN VVKDALRLQM LADTCPVTLN CDRIENKGKM FDSQVIIITT NQQTPVPLDY VNLEAVCRRI DFLVYAESPV VDDARARAPG DVNAVKAAMR PDYSHINFIL APQGGFDRQG NTPYGKGVTK IIGATALCAR AVALVHERHD DFGLQNKVYD FDAGKVTAFK AMAADAGIPW YKMAAIGCKA MGCTCVEEAM HLLKDYEVAP CQVIYNGATY NVSCIKGAPM VEKVKEPELP KTLVNCVRRI KEARLRCYCR MAADVITSIL QAAGTAFSIY HQIEKRSRPS FYWDXGYTYR DGPGSFDIFE DDDDGWYHSE GKKGKNKKGR GRPGVFRTRG LTDEEYDEFK KRRESRGGKY SIDDYLADRE REEELLERDE EEAIFGDGFG LKATRRSRKA ERAKLGLVSG GDIRARKPID WNVVGPSWAD DDRQVDYGEK INFEAPVSIW SRVVQFGTGW GFWVSGHVFI TAKHVAPPKG TEIFGRKPGD FTVTSSGDFL KYYFTSAVRP DIPAMVLENG CQEGVVASVL VKRASGEMLA LAVRMGSQAA IKIGSAVVHG QTGMLLTGSN AKAQDLGTIP GDCGCPYVYK KGNTWVVIGV HVAATRSGNT VIAATHGEPT LEALEFQGPP MLPRPSGTYA GLPIADYGDA PPLSTKTMFW RTSPEKLPPG AWEPAYLGSK DERVDGPSLQ QVMRDQLKPY SEPRGLLPPQ EILDAVCDAI ENRLENTLEP QKPWTFKKAC ESLDKNTSSG YPYHKQKSKD WTGSAFIGDL GDQATHANNM YEMGKSMRPI YTAALKDELV KPDKIYGKIK KRLLWGSDLG TMIRAARAFG PFCDALKETC IFNPIRVGMS MNEDGPFIFA RHANFRYHMD ADYTRWDSTQ QRAILKRAGD IMVRLSPEPD LARVVMDDLL APSLLDVGDY KIVVEEGLPS GCPCTTQLNS LAHWILTLCA MVEVTRVDPD IVMQESEFSF YGDDEVVSTN LELDMVKYTM ALRRYGLLPT RADKEEGPLE RRQTLQGISF LRRAIVGDQF GWYGRLDRAS IDRQLLWTKG PNHQNPFETL PGHAQRPSQL MALLGEAAMH GEKYYRTVAS RVSKEAAQSG IEMVVPRHRS VLRWVRFGTM DAETPQERSA VFVNEDE //