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A3FMB2

- POLG_HAVH2

UniProt

A3FMB2 - POLG_HAVH2

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Protein
Genome polyprotein
Gene
N/A
Organism
Human hepatitis A virus genotype IA (isolate H2) (HHAV) (Human hepatitis A virus (isolate Human/China/H2/1982))
Status
Reviewed - Annotation score: 5 out of 5 - Protein inferred from homologyi

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.
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.
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.
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.
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.
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.
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.
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.
RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals By similarity.

Catalytic activityi

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
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 – 242Cleavage Reviewed prediction
Sitei245 – 2462Cleavage; by protease 3C Reviewed prediction
Sitei491 – 4922Cleavage; by protease 3C Reviewed prediction
Sitei769 – 7702Cleavage; by host Reviewed prediction
Sitei769 – 7691Important for VP1 folding and capsid assembly By similarity
Sitei836 – 8372Cleavage; by protease 3C By similarity
Sitei1087 – 10882Cleavage; by protease 3C Reviewed prediction
Sitei1422 – 14232Cleavage; by protease 3C Reviewed prediction
Sitei1496 – 14972Cleavage; by protease 3C Reviewed prediction
Sitei1519 – 15202Cleavage; by protease 3C Reviewed prediction
Active sitei1563 – 15631For protease 3C activity By similarity
Active sitei1603 – 16031For protease 3C activity By similarity
Active sitei1691 – 16911For protease 3C activity By similarity
Sitei1738 – 17392Cleavage; by protease 3C By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1230 – 12378ATP Reviewed prediction

GO - Molecular functioni

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

GO - Biological processi

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

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 H2) (HHAV) (Human hepatitis A virus (isolate Human/China/H2/1982))
Taxonomic identifieri470423 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeHepatovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000007901: Genome

Subcellular locationi

Chain Protein VP2 : Virion By similarity. Host cytoplasm Reviewed prediction
Chain Protein VP3 : Virion By similarity. Host cytoplasm Reviewed prediction
Chain Protein VP1 : Virion By similarity. Host cytoplasm Reviewed prediction
Chain Protein VP1-2A : Virion By similarity. Host cytoplasm Reviewed prediction
Chain Protein 2B : Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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.
Chain Protein 2C : Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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.
Chain Protein 3ABC : Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Reviewed prediction. Host mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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.
Chain Protein 3AB : Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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.
Chain Protein 3A : Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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.
Chain Protein 3B : Virion Reviewed prediction
Chain Protease 3C : Host cytoplasm Reviewed prediction
Chain RNA-directed RNA polymerase 3D-POL : Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 14671467Cytoplasmic Reviewed prediction
Add
BLAST
Intramembranei1468 – 148215 Reviewed prediction
Add
BLAST
Topological domaini1483 – 2227745Cytoplasmic Reviewed prediction
Add
BLAST

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
Complete GO annotation...

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 polyprotein
PRO_0000310655Add
BLAST
Chaini1 – 245245Protein VP0 Reviewed prediction
PRO_0000310656Add
BLAST
Chaini1 – 2323Protein VP4 Reviewed prediction
PRO_0000310657Add
BLAST
Chaini24 – 245222Protein VP2 Reviewed prediction
PRO_0000310658Add
BLAST
Chaini246 – 491246Protein VP3 Reviewed prediction
PRO_0000310659Add
BLAST
Chaini492 – 836345Protein VP1-2A Reviewed prediction
PRO_0000310660Add
BLAST
Chaini492 – 769278Protein VP1 Reviewed prediction
PRO_0000310661Add
BLAST
Chaini770 – 83667Protein 2A Reviewed prediction
PRO_0000310662Add
BLAST
Chaini837 – 1422586Protein 2BC Reviewed prediction
PRO_0000310663Add
BLAST
Chaini837 – 1087251Protein 2B Reviewed prediction
PRO_0000310664Add
BLAST
Chaini1088 – 1422335Protein 2C Reviewed prediction
PRO_0000310665Add
BLAST
Chaini1423 – 2227805Protein 3ABCD Reviewed prediction
PRO_0000310666Add
BLAST
Chaini1423 – 1738316Protein 3ABC Reviewed prediction
PRO_0000310667Add
BLAST
Chaini1423 – 151997Protein 3AB Reviewed prediction
PRO_0000310668Add
BLAST
Chaini1423 – 149674Protein 3A Reviewed prediction
PRO_0000310669Add
BLAST
Chaini1497 – 151923Protein 3B Reviewed prediction
PRO_0000310670Add
BLAST
Chaini1520 – 2227708Protein 3CD Reviewed prediction
PRO_0000310671Add
BLAST
Chaini1520 – 1738219Protease 3C Reviewed prediction
PRO_0000310672Add
BLAST
Chaini1739 – 2227489RNA-directed RNA polymerase 3D-POL Reviewed prediction
PRO_0000310673Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1499 – 14991O-(5'-phospho-RNA)-tyrosine By 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.
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.

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.

Structurei

3D structure databases

ProteinModelPortaliA3FMB2.
SMRiA3FMB2. Positions 1520-1735.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1204 – 1366163SF3 helicase
Add
BLAST
Domaini1520 – 1716197Peptidase C3
Add
BLAST
Domaini1976 – 2097122RdRp catalytic
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1127 – 115226 Reviewed prediction
Add
BLAST

Sequence similaritiesi

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.

A3FMB2-1 [UniParc]FASTAAdd to Basket

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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 KMSFALDPED 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 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 LSTESMMSRI AAGDLESSVD DPRSEEDRRF ESHIECRKPY 800
KELRLEVGKQ RLKYAQEELS NEVLPPPRKM KGLFSQAKIS LFYTEEHEIM 850
KFSWRGVTAD TRALRRFGFS MAAGRSVWTL EMDAGVLTGR LVRLNDEKWT 900
EMKDDKIVSL IEKFTSNKYW SKVSFPHGML DLEEIAANST 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 PSGEPSNSKL 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 MINFPAVMPF SKAEVDPMAV MLSKYSLPIV 1800
EEPEDYKEAS IFYQNKIVGK 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
SEKTIWSLIA WQRSNAEFEQ NLENAQWFAF MHGYEFYQKF YYFVQSCLEK 2200
EMIEYRLKSY DWWRMRFYDQ CFICDLS 2227
Length:2,227
Mass (Da):251,399
Last modified:March 20, 2007 - v1
Checksum:i22A9D3FE905DDEA5
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti5 – 51K → R in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti63 – 631I → V in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti67 – 671K → R in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti278 – 2781P → Q in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti390 – 3901T → S in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti520 – 5201R → K in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti788 – 7881R → K in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti871 – 8711M → L in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti892 – 8921V → I in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti924 – 9241S → N in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti940 – 9401T → K in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti996 – 9961A → T in strain: H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti998 – 9981T → A in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti1008 – 10081H → Q in strain: H2K20 and H2K25.
Natural varianti1052 – 10521A → V in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti1071 – 10711T → S in strain: H2K5.
Natural varianti1105 – 11051S → N in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti1151 – 11511N → K in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti1163 – 11631F → S in strain: H2K15, H2K20, H2K25 and H2K30.
Natural varianti1164 – 11641D → E in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti1190 – 11901G → M in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti1254 – 12541E → V in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti1354 – 13541K → E in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti1375 – 13751N → S in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti1393 – 13931I → V in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti1414 – 14141S → T in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti1428 – 14292Missing in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti1452 – 14521S → G in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti1458 – 14581T → S in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti1486 – 14861S → T in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti1495 – 14951A → T in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti1661 – 16611T → S in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti1744 – 17441E → D in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti1777 – 17771V → A in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti1785 – 17851V → I in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti1790 – 17901V → M in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti1857 – 18571K → R in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti1875 – 18751V → I in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti1962 – 19621R → K in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti2035 – 20351C → Y in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti2052 – 20521I → T in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti2055 – 20551I → V in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.
Natural varianti2077 – 20771R → K in strain: H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
EF406357 Genomic RNA. Translation: ABN59383.1.
EF406358 Genomic RNA. Translation: ABN59384.1.
EF406359 Genomic RNA. Translation: ABN59385.1.
EF406360 Genomic RNA. Translation: ABN59386.1.
EF406361 Genomic RNA. Translation: ABN59387.1.
EF406362 Genomic RNA. Translation: ABN59388.1.
EF406363 Genomic RNA. Translation: ABN59389.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
EF406357 Genomic RNA. Translation: ABN59383.1 .
EF406358 Genomic RNA. Translation: ABN59384.1 .
EF406359 Genomic RNA. Translation: ABN59385.1 .
EF406360 Genomic RNA. Translation: ABN59386.1 .
EF406361 Genomic RNA. Translation: ABN59387.1 .
EF406362 Genomic RNA. Translation: ABN59388.1 .
EF406363 Genomic RNA. Translation: ABN59389.1 .

3D structure databases

ProteinModelPortali A3FMB2.
SMRi A3FMB2. Positions 1520-1735.
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.
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. "Molecular evolution of hepatitis A virus in a human diploid cell line."
    Tang C.H., Mao J.S., Chai S.A., Chen Y., Zhuang F.C.
    World J. Gastroenterol. 13:4630-4635(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: H2/wt, H2K10, H2K15, H2K20, H2K25, H2K30 and H2K5.

Entry informationi

Entry nameiPOLG_HAVH2
AccessioniPrimary (citable) accession number: A3FMB2
Secondary accession number(s): A3FMB3
, A3FMB4, A3FMB5, A3FMB6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: March 20, 2007
Last modified: July 9, 2014
This is version 56 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.
Wild-type H2 (H2/wt) comes from a sample isolated from a patient in China in 1982. H2K5, H2K10, H2K15, H2K20, H2K25 and H2K30 are cell culture-adapted strains derived from H2 by 5 to 30 passages in KMB17 cells.

Caution

It is uncertain whether Met-1 or Met-3 is the initiator.
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.

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

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