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Q5Y944

- POLG_HAVCF

UniProt

Q5Y944 - POLG_HAVCF

Protein

Genome polyprotein

Gene
N/A
Organism
Human hepatitis A virus genotype IIA (isolate CF-53) (HHAV) (Human hepatitis A virus (isolate Human/France/CF-53/1979))
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 1 (23 Nov 2004)
      Previous versions | rss
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    Functioni

    Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The capsid interacts with HAVCR1 to provide virion attachment to target cell By similarity.By similarity
    Protein VP0: VP0 precursor is a component of immature procapsids. The N-terminal domain of VP0, protein VP4, is needed for the assembly of 12 pentamers into the icosahedral structure. Unlike other picornaviruses, HAV VP4 does not seem to be myristoylated and has not been detected in mature virions, supposedly owing to its small size By similarity.By similarity
    VP1-2A precursor is a component of immature procapsids and corresponds to an extended form of the structural protein VP1. The C-terminal domain of VP1-2A, protein 2A, acts as an assembly signal that allows multimerization of VP1-2A and formation of pentamers of VP1-VP2-VP3 trimers. It is proteolytically removed from the precursor by a host protease and does not seem to be found in mature particles By similarity.By similarity
    Protein 2B and 2BC precursor affect membrane integrity and cause an increase in membrane permeability.By similarity
    Protein 2C: Associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities By similarity.By similarity
    Protein 3A, via its hydrophobic domain, serves as membrane anchor to the 3AB and 3ABC precursors.By similarity
    The 3AB precursor interacts with the 3CD precursor and with RNA structures found at both the 5'- and 3'-termini of the viral genome. Since the 3AB precursor contains the hydrophobic domain 3A, it probably anchors the whole viral replicase complex to intracellular membranes on which viral RNA synthesis occurs By similarity.By similarity
    The 3ABC precursor is targeted to the mitochondrial membrane where protease 3C activity cleaves and inhibits the host antiviral protein MAVS, thereby disrupting activation of IRF3 through the IFIH1/MDA5 pathway. In vivo, the protease activity of 3ABC precursor is more efficient in cleaving the 2BC precursor than that of protein 3C. The 3ABC precursor may therefore play a role in the proteolytic processing of the polyprotein By similarity.By similarity
    Protein 3B is covalently linked to the 5'-end of both the positive-strand and negative-strand genomic RNAs. It acts as a genome-linked replication primer By similarity.By similarity
    Protease 3C: cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease. Also cleaves host proteins such as PCBP2 By similarity.By similarity
    RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals.PROSITE-ProRule annotation

    Catalytic activityi

    Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation
    Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
    NTP + H2O = NDP + phosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei23 – 242CleavageSequence Analysis
    Sitei245 – 2462Cleavage; by protease 3CSequence Analysis
    Sitei491 – 4922Cleavage; by protease 3CSequence Analysis
    Sitei769 – 7702Cleavage; by hostSequence Analysis
    Sitei769 – 7691Important for VP1 folding and capsid assemblyBy similarity
    Sitei836 – 8372Cleavage; by protease 3CBy similarity
    Sitei1087 – 10882Cleavage; by protease 3CSequence Analysis
    Sitei1422 – 14232Cleavage; by protease 3CSequence Analysis
    Sitei1494 – 14952Cleavage; by protease 3CSequence Analysis
    Sitei1517 – 15182Cleavage; by protease 3CSequence Analysis
    Active sitei1561 – 15611For protease 3C activityBy similarity
    Active sitei1601 – 16011For protease 3C activityBy similarity
    Active sitei1689 – 16891For protease 3C activityBy similarity
    Sitei1736 – 17372Cleavage; by protease 3CBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1230 – 12378ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. cysteine-type endopeptidase activity Source: InterPro
    3. ion channel activity Source: UniProtKB-KW
    4. RNA binding Source: UniProtKB-KW
    5. RNA-directed RNA polymerase activity Source: UniProtKB-KW
    6. RNA helicase activity Source: InterPro
    7. structural molecule activity Source: InterPro

    GO - Biological processi

    1. pore formation by virus in membrane of host cell Source: UniProtKB-KW
    2. protein oligomerization Source: UniProtKB-KW
    3. RNA-protein covalent cross-linking Source: UniProtKB-KW
    4. suppression by virus of host gene expression Source: UniProtKB-KW
    5. suppression by virus of host MAVS activity Source: UniProtKB-KW
    6. suppression by virus of host MAVS activity by MAVS proteolysis Source: UniProtKB
    7. transcription, DNA-templated Source: InterPro
    8. viral entry into host cell Source: UniProtKB-KW
    9. viral RNA genome replication Source: InterPro
    10. virion attachment to host cell Source: UniProtKB-KW

    Keywords - Molecular functioni

    Helicase, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Thiol protease, Transferase, Viral ion channel

    Keywords - Biological processi

    Eukaryotic host gene expression shutoff by virus, Eukaryotic host translation shutoff by virus, Host gene expression shutoff by virus, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host MAVS by virus, Inhibition of host RLR pathway by virus, Interferon antiviral system evasion, Ion transport, Transport, Viral attachment to host cell, Viral immunoevasion, Viral RNA replication, Virus entry into host cell

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding, RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Genome polyprotein
    Cleaved into the following 18 chains:
    Alternative name(s):
    VP4-VP2
    Alternative name(s):
    P1A
    Virion protein 4
    Alternative name(s):
    P1B
    Virion protein 2
    Alternative name(s):
    P1C
    Virion protein 3
    Alternative name(s):
    PX
    Alternative name(s):
    P1D
    Virion protein 1
    Protein 2A
    Short name:
    P2A
    Protein 2B
    Short name:
    P2B
    Protein 2C (EC:3.6.1.15)
    Short name:
    P2C
    Protein 3ABCD
    Short name:
    P3
    Protein 3A
    Short name:
    P3A
    Protein 3B
    Short name:
    P3B
    Alternative name(s):
    VPg
    Protease 3C (EC:3.4.22.28)
    Short name:
    P3C
    Alternative name(s):
    Picornain 3C
    OrganismiHuman hepatitis A virus genotype IIA (isolate CF-53) (HHAV) (Human hepatitis A virus (isolate Human/France/CF-53/1979))
    Taxonomic identifieri470591 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeHepatovirus
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000007899: Genome

    Subcellular locationi

    Chain Protein VP2 : Virion By similarity. Host cytoplasm Curated
    Chain Protein VP3 : Virion By similarity. Host cytoplasm Curated
    Chain Protein VP1 : Virion By similarity. Host cytoplasm Curated
    Chain Protein VP1-2A : Virion By similarity. Host cytoplasm Curated
    Chain Protein 2B : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
    Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum By similarity.By similarity
    Chain Protein 2C : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
    Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum. May associate with membranes through a N-terminal amphipathic helix By similarity.By similarity
    Chain Protein 3ABC : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated. Host mitochondrion outer membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
    Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum By similarity.By similarity
    Chain Protein 3AB : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
    Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum By similarity.By similarity
    Chain Protein 3A : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
    Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum By similarity.By similarity
    Chain RNA-directed RNA polymerase 3D-POL : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
    Note: Interacts with membranes in a complex with viral protein 3AB. Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum By similarity.By similarity

    GO - Cellular componenti

    1. host cell cytoplasmic vesicle membrane Source: UniProtKB-SubCell
    2. host cell mitochondrial outer membrane Source: UniProtKB-SubCell
    3. integral to membrane of host cell Source: UniProtKB-KW
    4. membrane Source: UniProtKB-KW
    5. viral capsid Source: UniProtKB-KW

    Keywords - Cellular componenti

    Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Host mitochondrion, Host mitochondrion outer membrane, Membrane, Virion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 22252225Genome polyproteinPRO_0000310599Add
    BLAST
    Chaini1 – 245245Protein VP0Sequence AnalysisPRO_0000310600Add
    BLAST
    Chaini1 – 2323Protein VP4Sequence AnalysisPRO_0000310601Add
    BLAST
    Chaini24 – 245222Protein VP2Sequence AnalysisPRO_0000310602Add
    BLAST
    Chaini246 – 491246Protein VP3Sequence AnalysisPRO_0000310603Add
    BLAST
    Chaini492 – 836345Protein VP1-2ASequence AnalysisPRO_0000310604Add
    BLAST
    Chaini492 – 769278Protein VP1Sequence AnalysisPRO_0000310605Add
    BLAST
    Chaini770 – 83667Protein 2ASequence AnalysisPRO_0000310606Add
    BLAST
    Chaini837 – 1422586Protein 2BCSequence AnalysisPRO_0000310607Add
    BLAST
    Chaini837 – 1087251Protein 2BSequence AnalysisPRO_0000310608Add
    BLAST
    Chaini1088 – 1422335Protein 2CSequence AnalysisPRO_0000310609Add
    BLAST
    Chaini1423 – 2225803Protein 3ABCDSequence AnalysisPRO_0000310610Add
    BLAST
    Chaini1423 – 1736314Protein 3ABCSequence AnalysisPRO_0000310611Add
    BLAST
    Chaini1423 – 151795Protein 3ABSequence AnalysisPRO_0000310612Add
    BLAST
    Chaini1423 – 149472Protein 3ASequence AnalysisPRO_0000310613Add
    BLAST
    Chaini1495 – 151723Protein 3BSequence AnalysisPRO_0000310614Add
    BLAST
    Chaini1518 – 2225708Protein 3CDSequence AnalysisPRO_0000310615Add
    BLAST
    Chaini1518 – 1736219Protease 3CSequence AnalysisPRO_0000310616Add
    BLAST
    Chaini1737 – 2225489RNA-directed RNA polymerase 3D-POLSequence AnalysisPRO_0000310617Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1497 – 14971O-(5'-phospho-RNA)-tyrosineBy similarity

    Post-translational modificationi

    Specific enzymatic cleavages by the viral protease in vivo yield a variety of precursors and mature proteins. Polyprotein processing intermediates are produced, such as P1-2A which is a functional precursor of the structural proteins, VP0 which is a VP4-VP2 precursor, VP1-2A precursor, 3ABC precursor which is a stable and catalytically active precursor of 3A, 3B and 3C proteins, 3AB and 3CD precursors. The assembly signal 2A is removed from VP1-2A by a host protease. During virion maturation, non-infectious particles are rendered infectious following cleavage of VP0. This maturation cleavage is followed by a conformational change of the particle By similarity.By similarity
    VPg is uridylylated by the polymerase and is covalently linked to the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase By similarity.By similarity

    Keywords - PTMi

    Covalent protein-RNA linkage, Phosphoprotein

    Interactioni

    Subunit structurei

    3AB precursor is a homodimer. 3AB precursor interacts with 3CD precursor. Protein 3ABC interacts with human MAVS By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ5Y944.
    SMRiQ5Y944. Positions 1518-1733.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 14651465CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1481 – 2225745CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei1466 – 148015Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1204 – 1366163SF3 helicasePROSITE-ProRule annotationAdd
    BLAST
    Domaini1518 – 1714197Peptidase C3Add
    BLAST
    Domaini1974 – 2095122RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1127 – 115226Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the picornaviridae polyprotein family.Curated
    Contains 1 peptidase C3 domain.Curated
    Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation
    Contains 1 SF3 helicase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Family and domain databases

    Gene3Di2.60.120.20. 3 hits.
    InterProiIPR004004. Helic/Pol/Pept_Calicivir-typ.
    IPR000605. Helicase_SF3_ssDNA/RNA_vir.
    IPR014759. Helicase_SF3_ssRNA_vir.
    IPR024354. Hepatitis_A_VP1-2A.
    IPR027417. P-loop_NTPase.
    IPR000199. Peptidase_C3A/C3B_picornavir.
    IPR001676. Picornavirus_capsid.
    IPR001205. RNA-dir_pol_C.
    IPR007094. RNA-dir_pol_PSvirus.
    IPR009003. Trypsin-like_Pept_dom.
    IPR029053. Viral_coat.
    [Graphical view]
    PfamiPF12944. DUF3840. 1 hit.
    PF00548. Peptidase_C3. 1 hit.
    PF00680. RdRP_1. 1 hit.
    PF00073. Rhv. 2 hits.
    PF00910. RNA_helicase. 1 hit.
    [Graphical view]
    PRINTSiPR00918. CALICVIRUSNS.
    SUPFAMiSSF50494. SSF50494. 1 hit.
    SSF52540. SSF52540. 2 hits.
    PROSITEiPS50507. RDRP_SSRNA_POS. 1 hit.
    PS51218. SF3_HELICASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q5Y944-1 [UniParc]FASTAAdd to Basket

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    MNMSRQGIFQ TVGSGLDHIL SLADIEEEQM IQSVDRTAVT GASYFTSVDQ     50
    SSVHTAEVGS HQIEPLKTSV DKPGSKKTQG EKFFLIHSAD WLTTHALFHE 100
    VAKLDVVKLL YNEQFAVQGL LRYHTYARFG IEIQVQINPT PFQQGGLICA 150
    MVPGDQSYGS IASLTVYPHG LLNCNINNVV RIKVPFIYTR GAYHFKDPQY 200
    PVWELTIRVW SELNIGTGTS AYTSLNVLAR FTDLELHGLT PLSTQMMRNE 250
    FRVSTTENVV NLSNYEDARA KMSFALDQED WKSDPSQGGG IKITHFTTWT 300
    SIPTLAAQFP FNASDSVGQQ IKVIPVDPYF FQMTNSNPDQ KCITALASIC 350
    QMFCFWRGDL VFDFQVFPTK YHSGRLLFCF VPGNELIDVS GITLKQATTA 400
    PCAVMDIAGV QSTLRFRVPW IPDTRYRVNR YTKSAHQKGE YTAIGKLIVY 450
    CYNRLTSPSN VASHVRVNVY LSAINLECFA PLYHAMDVTT QVGDDSGGFS 500
    TTVSTEQNVP DPQVGITTMR DLKGKANRGK MDVSGVQAPV GAITTIEDPV 550
    LAKKVPETFP ELKPGESRHT SDHMSIYKFM GRSHFLCTFT FNSNNKEYTF 600
    PITLSSTSNP PHGLPSTLRW FFNLFQLYRG PLDLTIIITG ATDVDGMAWF 650
    TPVGLAVDTP WVEKESALSI DYKTALGAVR FNTRRTGNIQ IRLPWYSYLY 700
    AVSGALDGLG DKTDSTFGLV SIQIANYNHS DEYLSFSCYL SVTEQSEFYF 750
    PRAPLNSNAM LSTETMMSRI AAGDLESSVD DPRSEEDRRF ESHIESRKPY 800
    KELRLEVGKQ RLKYAQEELS NEVLPPPRKM KGLFSQAKIS LFYTEEHEIM 850
    KFSWRGVTAD TRALRRFGFS LAAGRSVWTL EMDAGVLTGR LVRLNDEKWT 900
    EMKDDKIVSL VEKFTSNKHW SKVNFPHGML DLEEIAANSK DFPNMSETDL 950
    CFLLHWLNPK KINLADRMLG LSGVQEIKEQ GIGLIAECRT FLDSITGSLK 1000
    SMMFGFHHSV TVDIVNIVLC FVKSGILLYV IQQLNQDEHS HIIGLLRVMN 1050
    YADIGCSVIS CGKVFSKMLE TVFNWQMDSR MMELRTQSFS NWLRDICSGI 1100
    TIFKSFKDAI YWLYTKLKDF YDMNYGKKKD VLNVLKDNQQ RIERAIEEAD 1150
    NFCMLQIQDV EKFEQFQKGV DLIQKLRTVH SMAQVDSSLM IHLSPLRDCI 1200
    ARVHQKLKNL GSINQAMVTR CEPVVCYLYG KRGGGKSLTS IALATKICKH 1250
    YGVEPEKNIY TKPVASDYWD GYSGQLVCII DDIGQNTTDE DWSDFCQLVS 1300
    GCPMRLNMAS LEEKGRHFSS PFIIATSNWS NPSPKTVYVK EAIDRRLHFK 1350
    IEVKPASFFQ NPHNDMLNVN LAKTSDAIKD MSCVDLIMDG HNISLMDLLS 1400
    SLVMTVEIRK QNMTEFMELW SQGISDDDSA VAEFFQSFPS GEPSSSKLSG 1450
    FFQSVTNHKW VAVGAAVGIL GVLVGGWFVY KHFSRKEEEP IPTEGVYHGV 1500
    TKPKQVIKLD ADPVESQSTL EIAGLVRKNL VQFGVGEKNG CVRWVMNALG 1550
    VKDDWLLVPS HAYKFEKDYE MMEFYFNRGG TYYSISAGNV VIQSLDVGFQ 1600
    DVVLMKVPTI PKFRDITEHF IKKGDVPRAL NRLATLVTTV NGTPMLISEG 1650
    PLKMEEKATY VHKKNDGTTV DLTVDQAWRG KGEGLPGMCG GALISSNQSI 1700
    QNAILGIHVA GGNSILVAKL VTQEMFQNID KKIESQRIMK VEFSQCSMNV 1750
    VSKTLFKKSP IHHHIDKDMI NFPAAMPFSR AEIDPMAVML SKYSLPMVEE 1800
    PEGYKDVSIF FQNKIMGKSI LVDDFLDLDM AITGTPGIDA INMDSSPGFP 1850
    YVQEKLTKRD LIWLHENGLL LGIHPRLAQR ILFNTVMMEN CSDLDVVFTT 1900
    CPKDELRPLD KVLESKTRAI DACPLDYTIL CRMYWGPAIS YFHLNPGFHT 1950
    GVAIGIDPDK QWDELFKTMI RFGDVGLDLD FSAFDASLSP FMIREAGRIM 2000
    SEISGTPSHF GTALINTIIY SKHLLYNCCY HVYGSMPSGS PCTALLNSII 2050
    NNINLYYVFA KIFRKSPVFF SQAVRILCYG DDVLVVFSRD IQIDNLDQIG 2100
    QKIVHEFKEL GMTATSADKT VPQLKPVSEL TFLKRSFNLV EDRIRPAISE 2150
    KTIWSLVAWQ RSNAEFEQNL ENAQWFAFMH GFEFYQKFYY FVQSCLEKEM 2200
    IEYRLKSYDW WRMRFYDQCF VCDLS 2225
    Length:2,225
    Mass (Da):251,415
    Last modified:November 23, 2004 - v1
    Checksum:i2BDABEBDF163C22D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY644676 Genomic RNA. Translation: AAU87586.1.
    L07693 Genomic RNA. No translation available.
    PIRiPQ0432.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY644676 Genomic RNA. Translation: AAU87586.1 .
    L07693 Genomic RNA. No translation available.
    PIRi PQ0432.

    3D structure databases

    ProteinModelPortali Q5Y944.
    SMRi Q5Y944. Positions 1518-1733.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 2.60.120.20. 3 hits.
    InterProi IPR004004. Helic/Pol/Pept_Calicivir-typ.
    IPR000605. Helicase_SF3_ssDNA/RNA_vir.
    IPR014759. Helicase_SF3_ssRNA_vir.
    IPR024354. Hepatitis_A_VP1-2A.
    IPR027417. P-loop_NTPase.
    IPR000199. Peptidase_C3A/C3B_picornavir.
    IPR001676. Picornavirus_capsid.
    IPR001205. RNA-dir_pol_C.
    IPR007094. RNA-dir_pol_PSvirus.
    IPR009003. Trypsin-like_Pept_dom.
    IPR029053. Viral_coat.
    [Graphical view ]
    Pfami PF12944. DUF3840. 1 hit.
    PF00548. Peptidase_C3. 1 hit.
    PF00680. RdRP_1. 1 hit.
    PF00073. Rhv. 2 hits.
    PF00910. RNA_helicase. 1 hit.
    [Graphical view ]
    PRINTSi PR00918. CALICVIRUSNS.
    SUPFAMi SSF50494. SSF50494. 1 hit.
    SSF52540. SSF52540. 2 hits.
    PROSITEi PS50507. RDRP_SSRNA_POS. 1 hit.
    PS51218. SF3_HELICASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of the complete genomic sequence of genotype II hepatitis A virus (CF53/Berne isolate)."
      Lu L., Ching K.Z., de Paula V.S., Nakano T., Siegl G., Weitz M., Robertson B.H.
      J. Gen. Virol. 85:2943-2952(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: CF53/Berne.
    2. "Genetic relatedness of hepatitis A virus strains recovered from different geographical regions."
      Robertson B.H., Jansen R.W., Khanna B., Totsuka A., Nainan O.V., Siegl G., Widell A., Margolis H.S., Isomura S., Ito K., Ishizu T., Moritsugu Y., Lemon S.M.
      J. Gen. Virol. 73:1365-1377(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 764-819.

    Entry informationi

    Entry nameiPOLG_HAVCF
    AccessioniPrimary (citable) accession number: Q5Y944
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2007
    Last sequence update: November 23, 2004
    Last modified: October 1, 2014
    This is version 70 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The need for an intact eIF4G factor for the initiation of translation of HAV results in an inability to shut off host protein synthesis by a mechanism similar to that of other picornaviruses.
    CF53/Berne is a cell culture-adapted strain derived from CF-53 by serial passages in PLC/PRF/5 and FRhK-4 cells.

    Caution

    It is uncertain whether Met-1 or Met-3 is the initiator.Curated
    Protein VP1 seems to have a heterogeneous C-terminus in cell culture. It may be reduced by a few amino acids compared to the sequence shown.Curated

    Keywords - Technical termi

    Complete proteome

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3