ID Q9WMA2_9PICO Unreviewed; 2216 AA.
AC Q9WMA2;
DT 01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1999, sequence version 1.
DT 27-MAR-2024, entry version 140.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
OS Hepatovirus A.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Heptrevirinae; Hepatovirus.
OX NCBI_TaxID=12092 {ECO:0000313|EMBL:BAA35104.1, ECO:0000313|Proteomes:UP000098819};
RN [1] {ECO:0000313|EMBL:BAA35104.1, ECO:0000313|Proteomes:UP000098819}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11495028; DOI=10.1016/S0168-8278(01)00074-5;
RA Fujiwara K., Yokosuka O., Fukai K., Imazeki F., Saisho H., Omata M.;
RT "Analysis of full-length hepatitis A virus genome in sera from patients
RT with fulminant and self-limited acute type A hepatitis.";
RL J. Hepatol. 35:112-119(2001).
CC -!- FUNCTION: Acts as a primer for viral RNA replication and remains
CC covalently bound to viral genomic RNA. VPg is uridylylated prior to
CC priming replication into VPg-pUpU. The VPg-pUpU is then used as primer
CC on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to
CC replicate the viral genome. {ECO:0000256|ARBA:ARBA00002133}.
CC -!- FUNCTION: Affects membrane integrity and causes an increase in membrane
CC permeability. {ECO:0000256|ARBA:ARBA00004017}.
CC -!- FUNCTION: Plays a role in the assembly of the 12 pentamers into an
CC icosahedral structure. Has not been detected in mature virions,
CC supposedly owing to its small size. {ECO:0000256|ARBA:ARBA00002016}.
CC -!- FUNCTION: VP0 precursor is a component of the immature procapsids.
CC {ECO:0000256|ARBA:ARBA00003724}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000256|ARBA:ARBA00024517};
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000256|ARBA:ARBA00004180}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004180}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004180}. Host cytoplasmic vesicle membrane
CC {ECO:0000256|ARBA:ARBA00004295}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004295}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004295}. Host endosome, host multivesicular
CC body {ECO:0000256|ARBA:ARBA00004560}. Host membrane
CC {ECO:0000256|ARBA:ARBA00004242}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004242}. Host membrane
CC {ECO:0000256|ARBA:ARBA00004379}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004379}. Host mitochondrion outer membrane
CC {ECO:0000256|ARBA:ARBA00004538}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004538}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}. Mitochondrion outer membrane
CC {ECO:0000256|ARBA:ARBA00004572}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004572}. Virion
CC {ECO:0000256|ARBA:ARBA00004328}.
CC -!- SIMILARITY: Belongs to the picornaviridae polyprotein family.
CC {ECO:0000256|ARBA:ARBA00006029}.
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; AB020566; BAA35104.1; -; Genomic_RNA.
DR PIR; JH0135; JH0135.
DR PIR; PQ0427; PQ0427.
DR PIR; PQ0428; PQ0428.
DR PIR; PQ0430; PQ0430.
DR PIR; PQ0431; PQ0431.
DR MEROPS; C03.005; -.
DR Proteomes; UP000098819; Genome.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044193; C:host cell mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0072494; C:host multivesicular body; IEA:UniProtKB-SubCell.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0005216; F:monoatomic ion channel activity; 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:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039545; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR GO; GO:0039707; P:virus-mediated pore formation in host cell membrane; IEA:UniProtKB-KW.
DR CDD; cd00205; rhv_like; 2.
DR Gene3D; 1.20.960.20; -; 1.
DR Gene3D; 2.60.120.20; -; 3.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR049133; 2B_soluble.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR InterPro; IPR024354; Hepatitis_A_VP1-2A.
DR InterPro; IPR044067; PCV_3C_PRO.
DR InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001676; Picornavirus_capsid.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR033703; Rhv-like.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR029053; Viral_coat.
DR Pfam; PF20758; 2B_soluble; 1.
DR Pfam; PF12944; HAV_VP; 1.
DR Pfam; PF00548; Peptidase_C3; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF00073; Rhv; 2.
DR Pfam; PF00910; RNA_helicase; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF88633; Positive stranded ssRNA viruses; 3.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51874; PCV_3C_PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS51218; SF3_HELICASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Capsid protein {ECO:0000256|ARBA:ARBA00022561};
KW Covalent protein-RNA linkage {ECO:0000256|ARBA:ARBA00022520};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW Host cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00022488};
KW Host endosome {ECO:0000256|ARBA:ARBA00023046};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW Host mitochondrion {ECO:0000256|ARBA:ARBA00023147};
KW Host mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022983};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Inhibition of host innate immune response by virus
KW {ECO:0000256|ARBA:ARBA00022986};
KW Inhibition of host MAVS by virus {ECO:0000256|ARBA:ARBA00022986};
KW Inhibition of host RLR pathway by virus {ECO:0000256|ARBA:ARBA00022986};
KW Interferon antiviral system evasion {ECO:0000256|ARBA:ARBA00023258};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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 Transport {ECO:0000256|ARBA:ARBA00022448};
KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
KW Viral immunoevasion {ECO:0000256|ARBA:ARBA00022986};
KW Viral ion channel {ECO:0000256|ARBA:ARBA00023039};
KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953};
KW Virion {ECO:0000256|ARBA:ARBA00022804};
KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}.
FT DOMAIN 1204..1366
FT /note="SF3 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51218"
FT DOMAIN 1514..1728
FT /note="Peptidase C3"
FT /evidence="ECO:0000259|PROSITE:PS51874"
FT DOMAIN 1965..2086
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
SQ SEQUENCE 2216 AA; 250211 MW; 1A9D93FEC21FBE82 CRC64;
MNMSRQGIFQ TVGSGLDHIL SLADIEEEQM IQSVDRTAVT GASYFTSVDQ SSVHTAEVGS
HQIEPLKTSV DKPGSKKTQG EKFFLIHSAD WLTTHALFHE VAKLDVVKLL YNEQFAVQGL
LRYHTYARFG IEIQVQINPT PFQQGGLICA MVPGDQSYGS IASLTVYPHG LLNCNINNVV
RIKVPFIYTR GAYHFKDPQY PVWELTIRVW SELNIGTGTS AYTSLNVLAR FTDLELHGLT
PLSTQMMRNE FRVSTTENVV NLSNYEDARA KMSFALDQED WKSDPSQGGG IKITHFTTWT
SIPTLAAQFP FNASDSVGQQ IKVIPVDPYF FQMTNTNPDQ KCITALASIC QMFCFWRGDL
VFDFQVFPTK YHSGRLLFCF VPGNELIDVT GITLKQATTA PCAVMDITGV QSTLRFRVPW
ISDTPYRVNR YTKSAHQKGE YTAIGKLIVY CYNRLTSPSN VASHVRVNVY LSAINLECFA
PLYHAMDVTT QVGDDSGGFS TTVSTEQNVP DPQVGITTMR DLKGKANRGK MDVSGVQAPV
GAITTIEDPV LAKKVPETFP ELKPGESRHT SDHMSIYKFM GRSHFLCTFT FNSNNKEYTF
PITLSSTSNP PHGLPSTLRW FFNLFQLYRG PLDLTIIITG ATDVDGMAWF TPVGLAVDTP
WVEKESALSI DYKTALGAVR FNTRRTGNIQ IRLPWYSYLY AVSGALDGLG DKTDSTFGLV
SIQIANYNHS DEYLSFSCYL SVTEQSEFYF PRAPLNSNAM LSTESMMSRI AAGDLESSVD
DPRSEEDRRF ESHIECRKPY KELRLEVGKQ RLKYAQEELS NEVLPPPRKM KGVFSQAKIS
LFYTEEHEIM KFSWRGVTAD TRALRRFGFS MAAGRSVWTL EMDAGVLTGR LVRLNDEKWT
EMKDDKIVSL IEKFTSNKYW SKVNFPHGML DLEEIAANSK DFPNMSETDL CFLLHWLNPK
KINLADRMLG LSGVQEIKEQ GVGLIAECRT FLDSIAGTLK SMMFGFHHSV TVEIINTVLC
FVKSGILLYV IQQLNQDEHS HIIGLLRIMN YADIGCSVIS CGKVFSKMLE TVFNWQMDSR
MMELRTQSFS NWLRDICSGI TIFKSFKDAI YWLYTKLKDF YEVNYGKKKD VLNILKDNQQ
KIEKAIEEAD NFCILQIQDV EKFDQYQKGV DLIQKLRTVH SMAQVDPNLG VHLSPLRDCI
ARVHQKLKNL GSINQAMVTR CEPVVCYLYG KRGGGKSLTS IALATKICKH YGVEPEKNIY
TKPVASDYWD GYSGQLVCII DDIGQNTTDE DWSDFCQLVS GCPMRLNMAS LEEKGRHFSS
PFIIATSNWS NPSPKTVYVK EAIDRRLHFK VEVKPASFFK NPHNDMLNVN LAKTNDAIKD
MSCVDLIMDG HNISLMDLLS SLVMTVEIRK QNMSEFMELW SQGISDDDND SAVAEFFQSF
PSGEPSNSKL SSFFQSVTNH KWVAVGAAVG ILGVLVGGWF VYKHFSRREE EPIPAEGVYH
GVTKPKQVIK LDADPVESQS TLEIAGLVRK NLVQFGVGEK NGCVRWVMNA LGVKDDWLLV
PSHAYKFEKD YEMMEFYFNR GGTYYSISAG NVVIQSLDVG FQDVVLMKVP TIPKFRDITQ
HFIKKGDVPR ALNRLATLVT TVNGTPMLIS EGQLKMEEKA TYVHKKNDGT TVDLTVDQAW
RGKGEGLPGM CGGALVSSNQ SIQNAILGIH VAGGNSILVA KLVTQEMFQN IDKKIESQRI
MKVEFTQCSM NVVSKTLFRK SPIHHHIDKT MINFPAAMPF SKAEIDPMAV MLSKYSLPIV
EEPEDYKEAS VFYQNKIVGK TQLVDDFLDL DMAITGAPGI DAINMDSSPG FPYVQEKLTK
RDLIWLDKNG LLLGVHPRLA QRILFNTVMM ENCSDLNVVF TTCPKDELRP LEKVLESKTR
AIDACPLDYT ILCHLNPRFH TSVAIGIDPD RQWDELFKTM IRFGDVGLDL NFSAFDASLS
PFMIREAGRI MSELSGTPSH FGTALINTII YSKHLLYNCC YHVCGSMPSG SPCTALLNSI
INNINLYYVF SKIFGKSPVF FCQALRILCY GDDVLIVFSR DVQIDNLDLI GQKIVDEFKK
LGMTATSADK NVPQLKPVSE LTFLKRSFNL VGDRIRPAIS EKTIWSLIAW QRSNAEFEQN
LENAQWFAFM HGYEFYQKFY YFVQSCLEKE MIEYRLKSYD WWRMRFYDQC FICDLS
//
