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Q67825

- POLG_HAVGB

UniProt

Q67825 - POLG_HAVGB

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Protein

Genome polyprotein

Gene
N/A
Organism
Human hepatitis A virus genotype IA (isolate GBM) (HHAV) (Human hepatitis A virus (isolate Human/Germany/GBM/1976))
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.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
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 GBM) (HHAV) (Human hepatitis A virus (isolate Human/Germany/GBM/1976))
Taxonomic identifieri470422 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeHepatovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000007900: 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 Source: UniProtKB-KW
  2. host cell mitochondrial outer membrane Source: UniProtKB-KW
  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 polyproteinPRO_0000310618Add
BLAST
Chaini1 – 245245Protein VP0Sequence AnalysisPRO_0000310619Add
BLAST
Chaini1 – 2323Protein VP4Sequence AnalysisPRO_0000310620Add
BLAST
Chaini24 – 245222Protein VP2Sequence AnalysisPRO_0000310621Add
BLAST
Chaini246 – 491246Protein VP3Sequence AnalysisPRO_0000310622Add
BLAST
Chaini492 – 836345Protein VP1-2ASequence AnalysisPRO_0000310623Add
BLAST
Chaini492 – 769278Protein VP1Sequence AnalysisPRO_0000310624Add
BLAST
Chaini770 – 83667Protein 2ASequence AnalysisPRO_0000310625Add
BLAST
Chaini837 – 1422586Protein 2BCSequence AnalysisPRO_0000310626Add
BLAST
Chaini837 – 1087251Protein 2BSequence AnalysisPRO_0000310627Add
BLAST
Chaini1088 – 1422335Protein 2CSequence AnalysisPRO_0000310628Add
BLAST
Chaini1423 – 2227805Protein 3ABCDSequence AnalysisPRO_5000146143Add
BLAST
Chaini1423 – 1738316Protein 3ABCSequence AnalysisPRO_0000310629Add
BLAST
Chaini1423 – 151997Protein 3ABSequence AnalysisPRO_0000310630Add
BLAST
Chaini1423 – 149674Protein 3ASequence AnalysisPRO_0000310631Add
BLAST
Chaini1497 – 151923Protein 3BSequence AnalysisPRO_0000310632Add
BLAST
Chaini1520 – 2227708Protein 3CDSequence AnalysisPRO_0000310633Add
BLAST
Chaini1520 – 1738219Protease 3CSequence AnalysisPRO_0000310634Add
BLAST
Chaini1739 – 2227489RNA-directed RNA polymerase 3D-POLSequence AnalysisPRO_0000310635Add
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. Protein 3ABC interacts with human MAVS By similarity.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ67825.
SMRiQ67825. Positions 1520-1735.
ModBaseiSearch...
MobiDBiSearch...

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 – 115529Sequence 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.

Q67825-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MNMSKQGIFQ TVGSGLDHIL SLADIEEEQM IQSVDRTAVT GASYFTSVDQ
60 70 80 90 100
SSVHTAEVGS HQIEPLKTSV DKPGSKKTQG EKFFLIHSAD WLTTHALFHE
110 120 130 140 150
VAKLDVVKLL YNEQFAVQGL LRYHTYARFG IEIQVQINPT PFSQGGLICA
160 170 180 190 200
MVPGDQSYGS IASLTVYPHG LLNCNINNVV RIKVPFIYTR GAYHFKDPQY
210 220 230 240 250
PVWELTIRVW SELNIGTGTS AYTSLNVLAR FTDLELHGLT PLSTQMMRNE
260 270 280 290 300
FRVSTTENVV NLSNYEDARA KMSFALDQED WKSDPSQGGG IKITHFTTWT
310 320 330 340 350
SIPTLAAQFP FNASDSVGQQ IKVIPVDPYF FQMTNTNPDQ KCITALASIC
360 370 380 390 400
QMFCFWRGDL VFDFQVFPTK YHSGRLLFCF VPGNELIDVT GITLKQATTA
410 420 430 440 450
PCAVMDITGV QSTLRFRVPW ISDTPYRVNR YTKSAHQKGE YTAIGKLIVY
460 470 480 490 500
CYNRLTSPSN VASHVRVNVY LSAINLECFA PLYHAMDVTT QVGDDSGGFS
510 520 530 540 550
TTVSTEQNVP DPQVGIITMR DLKGKANRGK MDVSGVQAPV GAITTIEDPV
560 570 580 590 600
LAKKVPETFP ELKPGESRHT SDHMSIYKFM GRSHFLCTFI FNSNNKEYTF
610 620 630 640 650
PITLSSTSNP PHGLPSTLRW FFNLFQLYRG PLDLTIIITG ATDVDGMAWF
660 670 680 690 700
TPVGLAVDTP WVEKESALSI DYKTALGAVR FNTRRTGNIQ IRLPWYSYLY
710 720 730 740 750
AVSGALDGLG DKTDSTFGLV SIQIANYNHS DEYLSFSCYL SVTEQSEFYF
760 770 780 790 800
PRAPLNSNAM LSTESMMSRI AAGDLESSVD DPRSEEDRRF ESHIECRKPY
810 820 830 840 850
KELRLEVGKQ RLKYAQEELS NEVLPPPRKM KGVFSQAKIS LFYTEEHEIM
860 870 880 890 900
KFSWRGVTAD TRALRRFGFS MAAGRSVWTL EMDAGVLTGR LVRLNDEKWT
910 920 930 940 950
EMKDDKIVSL IEKFTSNKYW SKVNFPHGML DLEEIAANSK DFPNMSETDL
960 970 980 990 1000
CFLLHWLNPK KINLADRMLG LSGVQEIKEQ GVGLIAECRT FLDSIAGTLK
1010 1020 1030 1040 1050
SMMFGFHHSV TVEIINTVLC FVKSGILLYV IQQLNQDEHS HIIGLLRVMN
1060 1070 1080 1090 1100
YVDIGCSVIS CGKVFSKMLE TVFNWQMDSR MMELRTQSFS NWLRDICSGI
1110 1120 1130 1140 1150
TIFKSFKDAI YWLYTKLKDF YEVNYGKKKD VLNILKDNRQ KIEKAIEEAD
1160 1170 1180 1190 1200
NLCILQIQDV EKFDQYQKGV DLIQKLRTVH SMAQVDPNLG VHLSPLRDCI
1210 1220 1230 1240 1250
ARVHQKLKNL GSINQAMVTR CEPVVCYLIG KRGGGKSLTS IALATKICKH
1260 1270 1280 1290 1300
YGVEPEKNIY TKPVASDYWD GYSGQLVCII DDIGQNTTDE DWSDFCQLVS
1310 1320 1330 1340 1350
GCPMRLNMAS LEEKGRHFSS PFIIATSNWS NPSPKTVYVK EAIDRRLHFK
1360 1370 1380 1390 1400
VEVKPASFFK NPHNDMLNVN LAKTNDAIKD MSCVDLIMDG HNISLMDLLS
1410 1420 1430 1440 1450
SLVMTVEIRK QNMSEFMELW SQGISDYDND SAVAEFFQSF PSGKPSNSKL
1460 1470 1480 1490 1500
SSFFQSVTNH KWVAVGAAVG ILGVLVAGWF VYRHFSRKEE EPIPTEGVYY
1510 1520 1530 1540 1550
GVTKPKQVIK LDADPVESQS PLEIAGLVRK NLVQFGVGEK NGCVRWVMNA
1560 1570 1580 1590 1600
LGVKDDWLLV PSHAYKFEKD YEMMEFYFNR GGTYYSISAG NVVIQSLDVG
1610 1620 1630 1640 1650
FQDVVLMKVP TIPKFRDITQ HFIKKGDVPR ALNRLATLVT TVNGTPMLIS
1660 1670 1680 1690 1700
EGPLKMEEKA TYVHKKNDGT TVDLTVDQAW RGKGEGLPGM CGGALVSSNQ
1710 1720 1730 1740 1750
SIQNAILGIH VAGGNSILVA KLVTQEMFQN IDKKIESQRI MKVEFSQCSM
1760 1770 1780 1790 1800
NVVSKTLFRK SPIHHHIDKT MINFPAALPF SKAEIDPMAI MLSKYSLPIV
1810 1820 1830 1840 1850
EEPEDYKEAS VFYQNKIVGK TQLVDDFLDL DMAITGAPGI DAINMDSSPG
1860 1870 1880 1890 1900
FPYVQEKLTK RDLIWLDENG LLLGVHPRLA QRILFNTVMM ENCSDLDVVF
1910 1920 1930 1940 1950
TTCPKDELRP LEKVLESKTR AIDACPLDYT ILCRMYWGPA ISYFHLNPGF
1960 1970 1980 1990 2000
HTGVAIGIDP DRQWDELFKT MIRFGDVGLD LDFSAFDASL SPFMIREAGR
2010 2020 2030 2040 2050
IMSELSGTPS HFGTALINTI IYSKHLLYNC CYHVYGSMPS GSPCTALLNS
2060 2070 2080 2090 2100
IINNINLYYV FSKIFGKSPV FFCQALRILC YGDDVLIVFS RDVQIDNLDL
2110 2120 2130 2140 2150
IGQKIVDEFR KLGMTATSAD KNVPQLKPVS ELTFLKRSFN LVEDRIRPAI
2160 2170 2180 2190 2200
SEKTIWSLIA WQRGNAEFEQ NLENAQWFAF MHGYEFYQKF YYFVQSCLEK
2210 2220
EMIEYRLKSY DWWRMRFYDQ CFICDLS
Length:2,227
Mass (Da):251,565
Last modified:November 1, 1996 - v1
Checksum:i4C4D79D352F936B4
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti143 – 1431S → Q in strain: GBM/HFS and GBM/FRhK.
Natural varianti517 – 5226Missing in strain: GBM/FRhK.
Natural varianti517 – 5171I → T in strain: GBM/HFS.
Natural varianti590 – 5901I → T in strain: GBM/HFS and GBM/FRhK.
Natural varianti647 – 6471M → I in strain: GBM/FRhK.
Natural varianti707 – 7071D → H in strain: GBM/FRhK.
Natural varianti1014 – 10141I → V in strain: GBM/FRhK.
Natural varianti1052 – 10521V → A in strain: GBM/HFS.
Natural varianti1118 – 11181K → Q in strain: GBM/FRhK.
Natural varianti1139 – 11391R → Q in strain: GBM/FRhK and GBM/HFS.
Natural varianti1152 – 11521L → F in strain: GBM/HFS and GBM/FRhK.
Natural varianti1229 – 12291I → Y in strain: GBM/HFS and GBM/FRhK.
Natural varianti1231 – 12311K → T in strain: GBM/FRhK.
Natural varianti1375 – 13751N → S in strain: GBM/FRhK.
Natural varianti1427 – 14293Missing in strain: GBM/FRhK.
Natural varianti1427 – 14271Y → D in strain: GBM/HFS.
Natural varianti1444 – 14441K → E in strain: GBM/HFS and GBM/FRhK.
Natural varianti1477 – 14771A → G in strain: GBM/HFS.
Natural varianti1495 – 14951T → A in strain: GBM/HFS and GBM/FRhK.
Natural varianti1500 – 15001Y → H in strain: GBM/HFS and GBM/FRhK.
Natural varianti1521 – 15211P → T in strain: GBM/HFS and GBM/FRhK.
Natural varianti1652 – 16521G → D in strain: GBM/FRhK.
Natural varianti1661 – 16611T → S in strain: GBM/FRhK.
Natural varianti1746 – 17461S → T in strain: GBM/HFS.
Natural varianti1778 – 17781L → M in strain: GBM/HFS and GBM/FRhK.
Natural varianti2035 – 20351Y → C in strain: GBM/HFS.
Natural varianti2164 – 21641G → S in strain: GBM/HFS and GBM/FRhK.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X75214 Genomic RNA. Translation: CAA53024.1.
X75215 Genomic RNA. Translation: CAA53025.1.
X75216 Genomic RNA. Translation: CAA53026.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X75214 Genomic RNA. Translation: CAA53024.1 .
X75215 Genomic RNA. Translation: CAA53025.1 .
X75216 Genomic RNA. Translation: CAA53026.1 .

3D structure databases

ProteinModelPortali Q67825.
SMRi Q67825. 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. "Nucleotide sequence of wild-type hepatitis A virus GBM in comparison with two cell culture-adapted variants."
    Graff J., Normann A., Feinstone S.M., Flehmig B.
    J. Virol. 68:548-554(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: GBM/FRhK, GBM/HFS and GBM/wt.

Entry informationi

Entry nameiPOLG_HAVGB
AccessioniPrimary (citable) accession number: Q67825
Secondary accession number(s): Q67824, Q67826
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 90 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 GBM (GBM/wt) comes from a sample isolated from a patient in Germany in 1976. GBM/HFS, and GBM/FRhK are cell culture-adapted strains derived from GBM by serial passages in HFS 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