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P06441

- POLG_HAVLA

UniProt

P06441 - POLG_HAVLA

Protein

Genome polyprotein

Gene
N/A
Organism
Human hepatitis A virus genotype IA (isolate LA) (HHAV) (Human hepatitis A virus (isolate Human/Northern California/LA/1974))
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (01 Jan 1988)
      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
    Sitei1496 – 14972Cleavage; by protease 3CSequence Analysis
    Sitei1519 – 15202Cleavage; by protease 3CSequence Analysis
    Active sitei1563 – 15631For protease 3C activityBy similarity
    Active sitei1603 – 16031For protease 3C activityBy similarity
    Active sitei1691 – 16911For protease 3C activityBy similarity
    Sitei1738 – 17392Cleavage; 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 IA (isolate LA) (HHAV) (Human hepatitis A virus (isolate Human/Northern California/LA/1974))
    Taxonomic identifieri12099 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeHepatovirus
    Virus hostiCercopithecus hamlyni (Owl-faced monkey) (Hamlyn's monkey) [TaxID: 9536]
    Homo sapiens (Human) [TaxID: 9606]
    Macaca (macaques) [TaxID: 9539]
    Pan troglodytes (Chimpanzee) [TaxID: 9598]
    ProteomesiUP000007903: 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 – 22272227Genome polyproteinPRO_0000311007Add
    BLAST
    Chaini1 – 245245Protein VP0Sequence AnalysisPRO_0000311008Add
    BLAST
    Chaini1 – 2323Protein VP4Sequence AnalysisPRO_0000039957Add
    BLAST
    Chaini24 – 245222Protein VP2Sequence AnalysisPRO_0000039958Add
    BLAST
    Chaini246 – 491246Protein VP3Sequence AnalysisPRO_0000039959Add
    BLAST
    Chaini492 – 836345Protein VP1-2ASequence AnalysisPRO_0000039960Add
    BLAST
    Chaini492 – 769278Protein VP1Sequence AnalysisPRO_0000311009Add
    BLAST
    Chaini770 – 83667Protein 2ASequence AnalysisPRO_0000039961Add
    BLAST
    Chaini837 – 1422586Protein 2BCSequence AnalysisPRO_0000311010Add
    BLAST
    Chaini837 – 1087251Protein 2BSequence AnalysisPRO_0000039962Add
    BLAST
    Chaini1088 – 1422335Protein 2CSequence AnalysisPRO_0000039963Add
    BLAST
    Chaini1423 – 2227805Protein 3ABCDSequence AnalysisPRO_0000311011Add
    BLAST
    Chaini1423 – 1738316Protein 3ABCSequence AnalysisPRO_0000311012Add
    BLAST
    Chaini1423 – 151997Protein 3ABSequence AnalysisPRO_0000311013Add
    BLAST
    Chaini1423 – 149674Protein 3ASequence AnalysisPRO_0000039964Add
    BLAST
    Chaini1497 – 151923Protein 3BSequence AnalysisPRO_0000039965Add
    BLAST
    Chaini1520 – 2227708Protein 3CDSequence AnalysisPRO_0000311014Add
    BLAST
    Chaini1520 – 1738219Protease 3CSequence AnalysisPRO_0000039966Add
    BLAST
    Chaini1739 – 2227489RNA-directed RNA polymerase 3D-POLPRO_0000039967Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1499 – 14991O-(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 By similarity.By similarity

    Structurei

    Secondary structure

    1
    2227
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1521 – 153111
    Beta strandi1532 – 15387
    Beta strandi1545 – 155511
    Beta strandi1557 – 15615
    Helixi1562 – 15643
    Turni1565 – 15673
    Helixi1571 – 15733
    Beta strandi1574 – 15807
    Beta strandi1583 – 15886
    Helixi1589 – 15913
    Beta strandi1592 – 16009
    Beta strandi1603 – 16086
    Helixi1619 – 16213
    Helixi1625 – 16317
    Beta strandi1636 – 16427
    Beta strandi1645 – 16517
    Beta strandi1655 – 166511
    Beta strandi1671 – 168313
    Beta strandi1694 – 16985
    Helixi1700 – 17023
    Beta strandi1706 – 17149
    Beta strandi1717 – 17226
    Helixi1725 – 17306

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2H6MX-ray1.40A1520-1731[»]
    2H9HX-ray1.39A1520-1731[»]
    ProteinModelPortaliP06441.
    SMRiP06441. Positions 1520-1735.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06441.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 14671467CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1483 – 2227745CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei1468 – 148215Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1204 – 1366163SF3 helicasePROSITE-ProRule annotationAdd
    BLAST
    Domaini1520 – 1716197Peptidase C3Add
    BLAST
    Domaini1976 – 2097122RdRp 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.
    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.
    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.

    P06441-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNMSKQGIFQ 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 FQMTNTNPDQ KCITALASIC 350
    QMFCFWRGDL VFDFQVFPTK YHSGRLLFCF VPGNELIDVT GITLKQATTA 400
    PCAVMDITGV QSTLRFRVPW ISDTPYRVNR YTKSAHQKGE YTAIGKLIVY 450
    CYNRLTSPSN VASHVRVNVY LSAINLECFA PLYHAMDVTT QVGDDSGGFS 500
    TTVSTEQNVP DPQVGITTMR DLKGKANRGK MDVSGVQAPR GSYQQQLNDP 550
    VLAKKVPETF PELKPGESRH TSDHMSIYKF MGRSHFLCTF TFNSNNKEYT 600
    FPITLSSTSN PPHGLPSTLR WFFNLFQLYR GPLDLTIIIT GATDVDGMAW 650
    FTPVGLAVDP WVEKESALSI DYKTALGAVR FNTRRTGNIQ IRLPWYSYLY 700
    AVSGALDGLG DKTDSTFGLF LFEIANYNHS DEYLSFSCYL SVTEQSEFYF 750
    PRAPLNSNAM LSTESMMSRI AAGDLESSVD DPRSEEDRRF ESHIECRKPY 800
    KELRLEVGKQ RLKYAQEELS NEVLPPPRKM KGLFSQAKIS LFYTEEHEIM 850
    KFSWRGVTAD TRALRRFGFS LAAGRSVWTL EMDAGVLTGR LIRLNDEKWT 900
    EMKDDKIVSL IEKFTSNKYW SKVNFPHGML DLEEIAANSK DFPNMSETDL 950
    CFLLHWLNPK KINLADRMLG LSGVQEIKEQ GVGLIAECRT FLDSIAGTLK 1000
    SMMFGFHHSV TVEIINTVLC FVKSGILLYV IQQLNQDEHS HIIGLLRVMN 1050
    YADIGCSVIS CGKVFSKMLE TVFNWQMDSR MMELRTQSFS NWLRDICSGI 1100
    TIFKSFKDAI YWLYTKLKDF YEVNYGKKKD ILNILKDNQQ KIEKAIEEAD 1150
    NFCILQIQDV EKFDQYQKGV DLIQKLRTVH SMAQVDPNLG VHLSPLRDCI 1200
    ARVHQKLKNL GSINQAMVTR CEPVVCYLYG KRGGGKSLTS IALATKICKH 1250
    YGVEPEKNIY TKPVASDYWD GYSGQLVCII DDIGQNTTDE DWSDFCQLVS 1300
    GCPMRLNMAS LEEKGRHFSS PFIIATSNWS NPSPKTVYVK EAIDRRLHFK 1350
    VEVKPASFFK NPHNDMLNVN LAKTNDAIKD MSCVDLIMDG HNISLMDLLS 1400
    SLVMTVEIRK QNMSEFMELW SQGISDDDND SAVAEFFQSF PSGEPSNWKL 1450
    SSFFQSVTNH KWVAVGAAVG ILGVLVGGWF VYKHFSRKEE EPIPAEGVYH 1500
    GVTKPKQVIK LDADPVESQS TLEIAGLVRK NLVQFGVGEK NGCVRWVMNA 1550
    LGVKDDWLLV PSHAYKFEKD YEMMEFYFNR GGTYYSISAG NVVIQSLDVG 1600
    FQDVVLMKVP TIPKFRDITQ HFIKKGDVPR ALNRLATLVT TVNGTPMLIS 1650
    EGPLKMEEKA TYVHKKNDGT TVDLTVDQAW RGKGEGLPGM CGGALVSSNQ 1700
    SIQNAILGIH VAGGNSILVA KLVTQEMFQN IDKKIESQRI MKVEFTQCSM 1750
    NVVSKTLFRK SPIHHHIDKT MINFPAAMPF SKAEIDPMAM MLSKYSLPIV 1800
    EEPEDYKEAS VFYQNKIVGK TQLVDDFLDL DMAITGAPGI DAINMDSSPG 1850
    FPYVQEKLTK RDLIWLDENG LLLGVHPRLA QRILFNTVMM ENCSDLDVVF 1900
    TTCPKDELRP LEKVLESKTR AIDACPLDYT ILCRMYWGPA ISYFHLNPGF 1950
    HTGVAIGIDP DRQWDELFKT MIRFGDVGLD LDFSAFDASL SPFMIREAGR 2000
    IMSELSGTPS HFGTALINTI IYSKHLLYNC CYHVCGSMPS GSPCTALLNS 2050
    IINNINLYYV FSKIFGKSPV FFCQALRILC YGDDVLIVFS RDVQIDNLDL 2100
    IGQKIVDEFK KLGMTATSAD KNVPQLKPVS ELTFLKRSFN LVEDRIRPAI 2150
    SEKTIWSLMA WQRSNAEFEQ NLENAQWFAF MHGYEFYQKF YYFVQSCLEK 2200
    EMIEYRLKSY DWWRMRFYDQ CFICDLS 2227
    Length:2,227
    Mass (Da):251,900
    Last modified:January 1, 1988 - v1
    Checksum:i99A7354B4CD2799C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K02990 Genomic RNA. Translation: AAA45472.1.
    PIRiA03903. GNNYHR.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K02990 Genomic RNA. Translation: AAA45472.1 .
    PIRi A03903. GNNYHR.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2H6M X-ray 1.40 A 1520-1731 [» ]
    2H9H X-ray 1.39 A 1520-1731 [» ]
    ProteinModelPortali P06441.
    SMRi P06441. Positions 1520-1735.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P06441.

    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.
    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.
    PROSITEi PS50507. RDRP_SSRNA_POS. 1 hit.
    PS51218. SF3_HELICASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

    Entry informationi

    Entry nameiPOLG_HAVLA
    AccessioniPrimary (citable) accession number: P06441
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 1, 1988
    Last modified: October 1, 2014
    This is version 121 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.

    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

    3D-structure, Complete proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3