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P14553

- POLG_HAVS2

UniProt

P14553 - POLG_HAVS2

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Protein

Genome polyprotein

Gene
N/A
Organism
Simian hepatitis A virus genotype V (isolate AGM-27) (SHAV) (Simian hepatitis A virus (isolate Cercopithecus/Kenya/AGM-27/1985))
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
Sitei27 – 282CleavageSequence Analysis
Sitei249 – 2502Cleavage; by protease 3CSequence Analysis
Sitei495 – 4962Cleavage; by protease 3CSequence Analysis
Sitei773 – 7742Cleavage; by hostSequence Analysis
Sitei773 – 7731Important for VP1 folding and capsid assemblyBy similarity
Sitei840 – 8412Cleavage; by protease 3CBy similarity
Sitei1091 – 10922Cleavage; by protease 3CSequence Analysis
Sitei1426 – 14272Cleavage; by protease 3CSequence Analysis
Sitei1498 – 14992Cleavage; by protease 3CSequence Analysis
Sitei1521 – 15222Cleavage; by protease 3CSequence Analysis
Active sitei1565 – 15651For protease 3C activityBy similarity
Active sitei1605 – 16051For protease 3C activityBy similarity
Active sitei1693 – 16931For protease 3C activityBy similarity
Sitei1741 – 17422Cleavage; by protease 3CBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1234 – 12418ATPPROSITE-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

Protein family/group databases

MEROPSiC03.005.

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
OrganismiSimian hepatitis A virus genotype V (isolate AGM-27) (SHAV) (Simian hepatitis A virus (isolate Cercopithecus/Kenya/AGM-27/1985))
Taxonomic identifieri12102 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeHepatovirus
Virus hostiCallithrix [TaxID: 9481]
Cercopithecus hamlyni (Owl-faced monkey) (Hamlyn's monkey) [TaxID: 9536]
Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops) [TaxID: 9534]
Macaca (macaques) [TaxID: 9539]
Pan troglodytes (Chimpanzee) [TaxID: 9598]
ProteomesiUP000008613: 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 – 22302230Genome polyproteinPRO_0000311023Add
BLAST
Chaini1 – 249249Protein VP0Sequence AnalysisPRO_0000311024Add
BLAST
Chaini1 – 2727Protein VP4Sequence AnalysisPRO_0000039979Add
BLAST
Chaini28 – 249222Protein VP2Sequence AnalysisPRO_0000039980Add
BLAST
Chaini250 – 495246Protein VP3Sequence AnalysisPRO_0000039981Add
BLAST
Chaini496 – 840345Protein VP1-2ASequence AnalysisPRO_0000311025Add
BLAST
Chaini496 – 773278Protein VP1Sequence AnalysisPRO_0000039982Add
BLAST
Chaini774 – 84067Protein 2ASequence AnalysisPRO_0000039983Add
BLAST
Chaini841 – 1426586Protein 2BCSequence AnalysisPRO_0000311026Add
BLAST
Chaini841 – 1091251Protein 2BSequence AnalysisPRO_0000039984Add
BLAST
Chaini1092 – 1426335Protein 2CSequence AnalysisPRO_0000039985Add
BLAST
Chaini1427 – 2230804Protein 3ABCDSequence AnalysisPRO_0000311027Add
BLAST
Chaini1427 – 1741315Protein 3ABCSequence AnalysisPRO_0000311028Add
BLAST
Chaini1427 – 152195Protein 3ABSequence AnalysisPRO_0000311029Add
BLAST
Chaini1427 – 149872Protein 3ASequence AnalysisPRO_0000039986Add
BLAST
Chaini1499 – 152123Protein 3BSequence AnalysisPRO_0000039987Add
BLAST
Chaini1522 – 2230709Protein 3CDSequence AnalysisPRO_0000311030Add
BLAST
Chaini1522 – 1741220Protease 3CSequence AnalysisPRO_0000039988Add
BLAST
Chaini1742 – 2230489RNA-directed RNA polymerase 3D-POLSequence AnalysisPRO_0000039989Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1501 – 15011O-(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

3D structure databases

ProteinModelPortaliP14553.
SMRiP14553. Positions 1522-1736.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini5 – 14711467CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini1487 – 2230744CytoplasmicSequence AnalysisAdd
BLAST

Intramembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Intramembranei1472 – 148615Sequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1208 – 1370163SF3 helicasePROSITE-ProRule annotationAdd
BLAST
Domaini1522 – 1718197Peptidase C3Add
BLAST
Domaini1979 – 2100122RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1131 – 115626Sequence 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.

P14553-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MFMMMNMSKQ GIFQTVGSGL DHILSLADVE EEQMIQSVDR TAVTGASYFT
60 70 80 90 100
SVDQSSVHTA EVGAHQTEPL KTSVDKPGSK KTQGEKFFLI HSADWLTTHA
110 120 130 140 150
LFHEVAKLDV VSLLYNEQFA VQGLLRYHTY ARFGIEIQVQ INPTPFQQGG
160 170 180 190 200
LICAMVPGDQ GYGSIASLTV YPHGLLNCNI NNVVRIKVPF IYTRGAYHFK
210 220 230 240 250
DPQYPVWELT IRVWSELNIG TGTSAYTSLN VLARFTDLEL HGLTPLSTQM
260 270 280 290 300
MRNEFRVSTT ENVVNLSNYE DARAKMSFAL DQEDWKTDPS QGGGIKITHF
310 320 330 340 350
TTWTSIPTLA AQFAFNASAS VGQQIKVIPV DPYFYQMTNS NPDQKCITAL
360 370 380 390 400
ASVCQMFCFW RGDLVFDFQV FPTKYHSGRL LFCFVPGNEL IDVSGITLKQ
410 420 430 440 450
ATTAPCAVMD ITGVQSTLRF RVPWISDTPY RVNRYTKSAH QKGEYTAIGK
460 470 480 490 500
LIVYCYNRLT SPSNVASHVR VNVYLSAINL ECFAPLYHAM DVTSQTGDDS
510 520 530 540 550
GGFSTTVSTE QNAPDPQVGI TTIKDLKGKA NRGKMDVSGI QAPVGAITTI
560 570 580 590 600
EDPVLAKKVP ETFPELRPGE SRHTSDHMSI YKFMGRSHFL CTFTFNANNR
610 620 630 640 650
EYTFPITLSS TSNPPHGLPS TLRWFFNLFQ LYRGPLDLTI IITGATDVDG
660 670 680 690 700
MAWFTPVGLA VDTPWVEKQS ALTIDYKTAL GAIRFNTRRT GNIQIRLPWY
710 720 730 740 750
SYLYAVSGAL DGLGDTTDST FGLVSIQIAN YNHSDEYLSF SCYLSVTEQS
760 770 780 790 800
EFYFPRAPLN SNAMMVSESM LDRIASGDLE SSVDDPRSAE DKRFESHIEQ
810 820 830 840 850
GKPYKELRME VGKQRLKYAM EELSNEILPP PRKVKGLFSQ AKISLFYTED
860 870 880 890 900
HEIVKLSWKG LTADTRALRR YGFSLAAGRS VWTLEMEAGV LTGRMIRLND
910 920 930 940 950
EKWTEIKDDK IVALVEKFTS NKNWSKVNFP HGMLDLEEIA SNSKDFPNMS
960 970 980 990 1000
ETDLCFLLHW LNPKKINLAD RMLGLSGVQE IKEQGVGLIA ECRTFLDSIA
1010 1020 1030 1040 1050
GTLKSMMFGF HQSVTVEIIN TVLCFVKSGI LLYVIQQLNQ NEHSHIIGLL
1060 1070 1080 1090 1100
QVMNYADIGC SVISCGKIFS KMLETVFNWQ MDSRMMALRT QSFSNWLRDI
1110 1120 1130 1140 1150
CSGITIFKNF KDAIFWLYTK LKDYYDSNYG KKKDVLNVLK ENQHRIEKAI
1160 1170 1180 1190 1200
EEADQFCVLQ IQDVEKSEQY QKGVELIQKL RTVHSLAQVD SSLMSHLSPL
1210 1220 1230 1240 1250
RDCIARVHQK LKNLGSINQA MVTRCEPVVC YLYGKRGGGK SLTSIALATK
1260 1270 1280 1290 1300
ICKHYGVEPE KNIYTKPVAS DYWDGYSGQL VCIIDDIGQN TTDEDWSDFC
1310 1320 1330 1340 1350
QLVSGCPMRL NMASLEEKGR HFSSPFIIAT SNWSNPSPKT VYVKEAIDRR
1360 1370 1380 1390 1400
LHYKIEVKPA SFYKNAHNDM LNVNLARNND AIKDMSCVDL LMDGHTVSLS
1410 1420 1430 1440 1450
ELLNSLVMTV EIRKQNMSEF MKLWSQGVSD DDNDSAVAEF FQSFPSGEPS
1460 1470 1480 1490 1500
NSKLSSFFKA VTNHKWVAIG AAVGVLGVLV GGWFVYKHFT KEEPIPTEGV
1510 1520 1530 1540 1550
YHGVTKPKQV IKLDADPVDS QSTLEIAGLV RKNLVQFGVG EKNGCVRWVM
1560 1570 1580 1590 1600
NALGIKDDWL LVPSHAYKFE KDYQMMEFYF NRGGTYYSIS AGNVVIQSLD
1610 1620 1630 1640 1650
VGFQDVVLMK VPTIPKFRDI TEHFIKKNDV PRALNRLATL VTTVNGTPML
1660 1670 1680 1690 1700
ISEGPLKMEE KATYVHKRND GTTVDLTVDQ AWRGKGEGLP GMCGGALISS
1710 1720 1730 1740 1750
NQSIQNAILG IHVAGGNSIL VAKLVTQEMF QNIEQKAIES QRIMKVEFTQ
1760 1770 1780 1790 1800
CSMNVVSKTL FKKSPIHHHI DRNMINFPAV MPFSKAEIDP MAVMLSKYSL
1810 1820 1830 1840 1850
PIVEEPDDYK MASIYFQNKV MGKTFLVDDF LDIDMAITGA PGIDAINMDS
1860 1870 1880 1890 1900
SPGFPYVQEK LTKKDLIWLD ENGLLLGVHP RLAQRILYNT VMMENCSDLD
1910 1920 1930 1940 1950
VVFTTCPKDE LRPLDKVLES KTRAIDACPL DYTILCRIYW GPAISYFQLN
1960 1970 1980 1990 2000
PGFHTGVAIG IDPDRHWDEL FKTMVRFGDV GLDLDFSSFD ASLSPFMIRE
2010 2020 2030 2040 2050
AGRILSEMSG TPSHFGEALI NTIIYSKHLL YNCCYHVYGS MPSGSPCTAL
2060 2070 2080 2090 2100
LNSIVNNVNL YYVFSKIFRK SPVFFGDALK ILCYGDDVLI VFSRNVQIDN
2110 2120 2130 2140 2150
LESIGQKIVD EFGKLGMTAT SADKSVPKLK PISELTFLKR SFNLVEDRIR
2160 2170 2180 2190 2200
PAISEKTIWS LVAWQRSNAE FEQNLENAQW FAFMHGFEFY QKFYHFVQSC
2210 2220 2230
LEKEMVEYRL KSYDWWRMKF YDQCFVCDLT
Length:2,230
Mass (Da):251,298
Last modified:August 1, 1992 - v2
Checksum:i87B3230E324E1F19
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D00924 Genomic RNA. Translation: BAA00766.1.
X15461 Genomic RNA. Translation: CAA33490.1.
PIRiA30470. GNNYSA.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D00924 Genomic RNA. Translation: BAA00766.1 .
X15461 Genomic RNA. Translation: CAA33490.1 .
PIRi A30470. GNNYSA.

3D structure databases

ProteinModelPortali P14553.
SMRi P14553. Positions 1522-1736.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C03.005.

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. "Simian hepatitis A virus (HAV) strain AGM-27: comparison of genome structure and growth in cell culture with other HAV strains."
    Tsarev S.A., Emerson S.U., Balayan M.S., Ticehurst J.R., Purcell R.H.
    J. Gen. Virol. 72:1677-1683(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Variations in genome fragments coding for RNA polymerase in human and simian hepatitis A viruses."
    Balayan M.S., Kusov Y.Y., Andjaparidze A.G., Tsarev S.A., Sverdlov E.D., Chizhikov V.E., Blinov V.M., Vasilenko S.K.
    FEBS Lett. 247:425-428(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1750-2164.

Entry informationi

Entry nameiPOLG_HAVS2
AccessioniPrimary (citable) accession number: P14553
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: August 1, 1992
Last modified: October 29, 2014
This is version 121 of the entry and version 2 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 results in an inability to shut off host protein synthesis by a mechanism similar to that of other picornaviruses.By similarity

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