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Protein

Genome polyprotein

Gene
N/A
Organism
Human hepatitis A virus genotype IB (isolate MBB) (HHAV) (Human hepatitis A virus (isolate Human/Northern Africa/MBB/1978))
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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)DescriptionActionsGraphical viewLength
Sitei769Important for VP1 folding and capsid assemblyBy similarity1
Active sitei1563For protease 3C activity1
Active sitei1603For protease 3C activity1
Active sitei1691For protease 3C activity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1230 – 1237ATPPROSITE-ProRule annotation8

GO - Molecular functioni

GO - Biological processi

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 IB (isolate MBB) (HHAV) (Human hepatitis A virus (isolate Human/Northern Africa/MBB/1978))
Taxonomic identifieri12100 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA 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]
Proteomesi
  • UP000007904 Componenti: Genome

Subcellular locationi

Protein VP2 :
Protein VP3 :
Protein VP1 :
Protein VP1-2A :
Protein 2B :
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
Protein 3ABC :
Protein 3AB :
Protein 3A :
Protein 3B :
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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 1467CytoplasmicSequence analysisAdd BLAST1467
Intramembranei1468 – 1482Sequence analysisAdd BLAST15
Topological domaini1483 – 2227CytoplasmicSequence analysisAdd BLAST745

GO - Cellular componenti

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)DescriptionActionsGraphical viewLength
ChainiPRO_00003110151 – 2227Genome polyproteinAdd BLAST2227
ChainiPRO_00003110161 – 245Protein VP0Sequence analysisAdd BLAST245
ChainiPRO_00000399681 – 23Protein VP4Sequence analysisAdd BLAST23
ChainiPRO_000003996924 – 245Protein VP2Sequence analysisAdd BLAST222
ChainiPRO_0000039970246 – 491Protein VP3Sequence analysisAdd BLAST246
ChainiPRO_0000039971492 – 836Protein VP1-2ASequence analysisAdd BLAST345
ChainiPRO_0000311017492 – 769Protein VP1Sequence analysisAdd BLAST278
ChainiPRO_0000039972770 – 836Protein 2ASequence analysisAdd BLAST67
ChainiPRO_0000311018837 – 1422Protein 2BCSequence analysisAdd BLAST586
ChainiPRO_0000039973837 – 1087Protein 2BSequence analysisAdd BLAST251
ChainiPRO_00000399741088 – 1422Protein 2CSequence analysisAdd BLAST335
ChainiPRO_00003110191423 – 2227Protein 3ABCDSequence analysisAdd BLAST805
ChainiPRO_00003110201423 – 1738Protein 3ABCSequence analysisAdd BLAST316
ChainiPRO_00003110211423 – 1519Protein 3ABSequence analysisAdd BLAST97
ChainiPRO_00000399751423 – 1496Protein 3ASequence analysisAdd BLAST74
ChainiPRO_00000399761497 – 1519Protein 3BSequence analysisAdd BLAST23
ChainiPRO_00003110221520 – 2227Protein 3CDSequence analysisAdd BLAST708
ChainiPRO_00000399771520 – 1738Protease 3CSequence analysisAdd BLAST219
ChainiPRO_00000399781739 – 2227RNA-directed RNA polymerase 3D-POLAdd BLAST489

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1499O-(5'-phospho-RNA)-tyrosineBy similarity1

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei23 – 24CleavageSequence analysis2
Sitei245 – 246Cleavage; by protease 3CSequence analysis2
Sitei491 – 492Cleavage; by protease 3CSequence analysis2
Sitei769 – 770Cleavage; by hostSequence analysis2
Sitei836 – 837Cleavage; by protease 3CBy similarity2
Sitei1087 – 1088Cleavage; by protease 3CSequence analysis2
Sitei1422 – 1423Cleavage; by protease 3CSequence analysis2
Sitei1496 – 1497Cleavage; by protease 3CSequence analysis2
Sitei1519 – 1520Cleavage; by protease 3CSequence analysis2
Sitei1738 – 1739Cleavage; by protease 3CBy similarity2

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

Secondary structure

12227
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1521 – 1531Combined sources11
Beta strandi1532 – 1538Combined sources7
Beta strandi1545 – 1555Combined sources11
Beta strandi1557 – 1561Combined sources5
Helixi1562 – 1564Combined sources3
Turni1565 – 1567Combined sources3
Helixi1571 – 1573Combined sources3
Beta strandi1574 – 1580Combined sources7
Beta strandi1583 – 1588Combined sources6
Helixi1589 – 1591Combined sources3
Beta strandi1592 – 1600Combined sources9
Beta strandi1603 – 1608Combined sources6
Helixi1619 – 1621Combined sources3
Helixi1625 – 1631Combined sources7
Beta strandi1636 – 1642Combined sources7
Beta strandi1645 – 1651Combined sources7
Beta strandi1655 – 1665Combined sources11
Beta strandi1671 – 1683Combined sources13
Beta strandi1694 – 1698Combined sources5
Helixi1700 – 1702Combined sources3
Beta strandi1706 – 1714Combined sources9
Beta strandi1717 – 1722Combined sources6
Helixi1725 – 1730Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2A4OX-ray1.55A1520-1738[»]
2CXVX-ray1.40A1520-1738[»]
ProteinModelPortaliP13901.
SMRiP13901.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13901.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1204 – 1366SF3 helicasePROSITE-ProRule annotationAdd BLAST163
Domaini1520 – 1716Peptidase C3Add BLAST197
Domaini1976 – 2097RdRp catalyticPROSITE-ProRule annotationAdd BLAST122

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili1127 – 1152Sequence analysisAdd BLAST26

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi636 – 639Poly-Ile4

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

CDDicd00205. rhv_like. 2 hits.
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.
IPR009003. Peptidase_S1_PA.
IPR001676. Picornavirus_capsid.
IPR033703. Rhv-like.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR029053. Viral_coat.
[Graphical view]
PfamiPF12944. HAV_VP. 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.

P13901-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNMSRQGIFQ TVGSGLDHIL SLADIEEEQM IQSVDRTAVT GASYFTSVDQ
60 70 80 90 100
SSVHTAEVGS HQVEPLRTSV DKPGSKKTQG EKFFLIHSAD WLTTHALFHE
110 120 130 140 150
VAKLDVVKLL YNEQFAVQGL LRYHTYARFG IEIQVQINPT PFQQGGLICA
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 VPGNELIDVS 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 DPQVGITTMK DLKGKANRGK MDVSGVQAPV GAITTIEDPV
560 570 580 590 600
LAKKVPETFP ELKPGESRHT SDHMSIYKFM GRSHFLCTFT FNSNNKEYTF
610 620 630 640 650
PITLSSTSNP PHGLPSTLRW FFNLFQLYRG PLDLTIIIIG 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 DPRSEEDKRF ESHIECRKPY
810 820 830 840 850
KELRLEVGKQ RLKYAQEELS NEVLPPPRKK KGLFSQAKIS LFYTEEHEIM
860 870 880 890 900
KFSWRGVTAD TRALRRFGFS LAAGRSVWTL EMDAGVLTGR LIRLNDEKWT
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 MQQLNQDEHS HIIGLLRVMN
1060 1070 1080 1090 1100
YVDIGCSVIS CGKVFSKMLE TVFNWQMDSR MMELRTQSFS NWLRDICSGI
1110 1120 1130 1140 1150
TIFKNFKDAI YWLYTKLNDF YEVNYGKKKD ILNILKDNQQ KIEKAIEEAD
1160 1170 1180 1190 1200
KFSILQIQDV EKFEQYQKGV DLIQKLRTVH SMAQVDPNLM VHLSPLRDCI
1210 1220 1230 1240 1250
ARVHQKLKNL GSINQAMVTR CEPVVCYLYG KRGGGKSLTS IALATKICKH
1260 1270 1280 1290 1300
YGVEPEKNIY TKPVASDYWD GYSGQLVCII DDIGQNTTDE DWSDFCQLVS
1310 1320 1330 1340 1350
GCPLRLNMAS LEEKGRHFSS PFIIATSNWS NPSPKTVYVK EAIDRRLHFK
1360 1370 1380 1390 1400
VEVNPASFSK NPHNDMLNVN LAKTNDAIKD MSCVDLIMDG HNVSLMDLLS
1410 1420 1430 1440 1450
SLVMTVEIRK QNMTAFMELW SQGISDDDND SAMAEFFQSF PSGEPSNSKL
1460 1470 1480 1490 1500
SGFFQSVTNH KWVAVGAAVG ILGVLVGGWF VYKHFSRKEE EPIPAEGVYH
1510 1520 1530 1540 1550
GVTKPKQVIK LDADPVESQS TLEIAGLVRK 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 MKVEFTQCSM
1760 1770 1780 1790 1800
NVVSKTLFRK SPIHHHIDKT MINFPAAMPF SKAEIDPMAM MLSKYSLPIV
1810 1820 1830 1840 1850
EEPEDYKEAS IFYQNKIVGK TQLVDDFLDL DMAITGAPGI DAINMDSSPG
1860 1870 1880 1890 1900
FPYVQERLTK RDLIWLDENG LLLGVHPRLA QRILFNTVMM ENCSDLDVVF
1910 1920 1930 1940 1950
TTCPKDELRP LEKVLESKTR AIDACPLDYT ILCRMYWGPA ISYFHLNPGF
1960 1970 1980 1990 2000
HTGVAIGIDP DCQWDELFKT MIRFGDVGLD LDFSAFDASL SPFMIREAGR
2010 2020 2030 2040 2050
IMSELSGTPS HFGTALMNTI IYSKHLLYNC CYHVCGSMPS GSPCTALLNS
2060 2070 2080 2090 2100
IINNVNLYYV FSKIFGKSPV FFCQALKILC YGDDVLIVFS RDVQIDNLDL
2110 2120 2130 2140 2150
IGQKIVDEFK KLGMTATSAD KNVPQLKPVS ELTFLKRSFN LVEDRIRPAI
2160 2170 2180 2190 2200
SEKTIWSLIA WQRSNAEFEQ NLENAQWFAF MHGYEFYQKF YYFVQSCLEK
2210 2220
EMIEYRLKSY DWWRMRFYDQ CFICDLS
Length:2,227
Mass (Da):251,427
Last modified:January 1, 1990 - v1
Checksum:iEC983ED2A7C86349
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20273 Genomic RNA. Translation: AAA45474.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20273 Genomic RNA. Translation: AAA45474.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2A4OX-ray1.55A1520-1738[»]
2CXVX-ray1.40A1520-1738[»]
ProteinModelPortaliP13901.
SMRiP13901.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP13901.

Family and domain databases

CDDicd00205. rhv_like. 2 hits.
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.
IPR009003. Peptidase_S1_PA.
IPR001676. Picornavirus_capsid.
IPR033703. Rhv-like.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR029053. Viral_coat.
[Graphical view]
PfamiPF12944. HAV_VP. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiPOLG_HAVMB
AccessioniPrimary (citable) accession number: P13901
Secondary accession number(s): Q81083
, Q81084, Q81085, Q81086, Q81087, Q81088, Q81089, Q81090, Q81091, Q81092, Q81093
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: November 30, 2016
This is version 136 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.