SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P14553

- POLG_HAVS2

UniProt

P14553 - POLG_HAVS2

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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.
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
Sitei27 – 282Cleavage Reviewed prediction
Sitei249 – 2502Cleavage; by protease 3C Reviewed prediction
Sitei495 – 4962Cleavage; by protease 3C Reviewed prediction
Sitei773 – 7742Cleavage; by host Reviewed prediction
Sitei773 – 7731Important for VP1 folding and capsid assembly By similarity
Sitei840 – 8412Cleavage; by protease 3C By similarity
Sitei1091 – 10922Cleavage; by protease 3C Reviewed prediction
Sitei1426 – 14272Cleavage; by protease 3C Reviewed prediction
Sitei1498 – 14992Cleavage; by protease 3C Reviewed prediction
Sitei1521 – 15222Cleavage; by protease 3C Reviewed prediction
Active sitei1565 – 15651For protease 3C activity By similarity
Active sitei1605 – 16051For protease 3C activity By similarity
Active sitei1693 – 16931For protease 3C activity By similarity
Sitei1741 – 17422Cleavage; by protease 3C By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1234 – 12418ATP 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
Complete GO annotation...

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

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 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 domaini5 – 14711467Cytoplasmic Reviewed prediction
Add
BLAST
Intramembranei1472 – 148615 Reviewed prediction
Add
BLAST
Topological domaini1487 – 2230744Cytoplasmic 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 – 22302230Genome polyprotein
PRO_0000311023Add
BLAST
Chaini1 – 249249Protein VP0 Reviewed prediction
PRO_0000311024Add
BLAST
Chaini1 – 2727Protein VP4 Reviewed prediction
PRO_0000039979Add
BLAST
Chaini28 – 249222Protein VP2 Reviewed prediction
PRO_0000039980Add
BLAST
Chaini250 – 495246Protein VP3 Reviewed prediction
PRO_0000039981Add
BLAST
Chaini496 – 840345Protein VP1-2A Reviewed prediction
PRO_0000311025Add
BLAST
Chaini496 – 773278Protein VP1 Reviewed prediction
PRO_0000039982Add
BLAST
Chaini774 – 84067Protein 2A Reviewed prediction
PRO_0000039983Add
BLAST
Chaini841 – 1426586Protein 2BC Reviewed prediction
PRO_0000311026Add
BLAST
Chaini841 – 1091251Protein 2B Reviewed prediction
PRO_0000039984Add
BLAST
Chaini1092 – 1426335Protein 2C Reviewed prediction
PRO_0000039985Add
BLAST
Chaini1427 – 2230804Protein 3ABCD Reviewed prediction
PRO_0000311027Add
BLAST
Chaini1427 – 1741315Protein 3ABC Reviewed prediction
PRO_0000311028Add
BLAST
Chaini1427 – 152195Protein 3AB Reviewed prediction
PRO_0000311029Add
BLAST
Chaini1427 – 149872Protein 3A Reviewed prediction
PRO_0000039986Add
BLAST
Chaini1499 – 152123Protein 3B Reviewed prediction
PRO_0000039987Add
BLAST
Chaini1522 – 2230709Protein 3CD Reviewed prediction
PRO_0000311030Add
BLAST
Chaini1522 – 1741220Protease 3C Reviewed prediction
PRO_0000039988Add
BLAST
Chaini1742 – 2230489RNA-directed RNA polymerase 3D-POL Reviewed prediction
PRO_0000039989Add
BLAST

Amino acid modifications

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

Structurei

3D structure databases

ProteinModelPortaliP14553.
SMRiP14553. Positions 1522-1736.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1208 – 1370163SF3 helicase
Add
BLAST
Domaini1522 – 1718197Peptidase C3
Add
BLAST
Domaini1979 – 2100122RdRp catalytic
Add
BLAST

Coiled coil

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

P14553-1 [UniParc]FASTAAdd to Basket

« Hide

MFMMMNMSKQ GIFQTVGSGL DHILSLADVE EEQMIQSVDR TAVTGASYFT     50
SVDQSSVHTA EVGAHQTEPL KTSVDKPGSK KTQGEKFFLI HSADWLTTHA 100
LFHEVAKLDV VSLLYNEQFA VQGLLRYHTY ARFGIEIQVQ INPTPFQQGG 150
LICAMVPGDQ GYGSIASLTV YPHGLLNCNI NNVVRIKVPF IYTRGAYHFK 200
DPQYPVWELT IRVWSELNIG TGTSAYTSLN VLARFTDLEL HGLTPLSTQM 250
MRNEFRVSTT ENVVNLSNYE DARAKMSFAL DQEDWKTDPS QGGGIKITHF 300
TTWTSIPTLA AQFAFNASAS VGQQIKVIPV DPYFYQMTNS NPDQKCITAL 350
ASVCQMFCFW RGDLVFDFQV FPTKYHSGRL LFCFVPGNEL IDVSGITLKQ 400
ATTAPCAVMD ITGVQSTLRF RVPWISDTPY RVNRYTKSAH QKGEYTAIGK 450
LIVYCYNRLT SPSNVASHVR VNVYLSAINL ECFAPLYHAM DVTSQTGDDS 500
GGFSTTVSTE QNAPDPQVGI TTIKDLKGKA NRGKMDVSGI QAPVGAITTI 550
EDPVLAKKVP ETFPELRPGE SRHTSDHMSI YKFMGRSHFL CTFTFNANNR 600
EYTFPITLSS TSNPPHGLPS TLRWFFNLFQ LYRGPLDLTI IITGATDVDG 650
MAWFTPVGLA VDTPWVEKQS ALTIDYKTAL GAIRFNTRRT GNIQIRLPWY 700
SYLYAVSGAL DGLGDTTDST FGLVSIQIAN YNHSDEYLSF SCYLSVTEQS 750
EFYFPRAPLN SNAMMVSESM LDRIASGDLE SSVDDPRSAE DKRFESHIEQ 800
GKPYKELRME VGKQRLKYAM EELSNEILPP PRKVKGLFSQ AKISLFYTED 850
HEIVKLSWKG LTADTRALRR YGFSLAAGRS VWTLEMEAGV LTGRMIRLND 900
EKWTEIKDDK IVALVEKFTS NKNWSKVNFP HGMLDLEEIA SNSKDFPNMS 950
ETDLCFLLHW LNPKKINLAD RMLGLSGVQE IKEQGVGLIA ECRTFLDSIA 1000
GTLKSMMFGF HQSVTVEIIN TVLCFVKSGI LLYVIQQLNQ NEHSHIIGLL 1050
QVMNYADIGC SVISCGKIFS KMLETVFNWQ MDSRMMALRT QSFSNWLRDI 1100
CSGITIFKNF KDAIFWLYTK LKDYYDSNYG KKKDVLNVLK ENQHRIEKAI 1150
EEADQFCVLQ IQDVEKSEQY QKGVELIQKL RTVHSLAQVD SSLMSHLSPL 1200
RDCIARVHQK LKNLGSINQA MVTRCEPVVC YLYGKRGGGK SLTSIALATK 1250
ICKHYGVEPE KNIYTKPVAS DYWDGYSGQL VCIIDDIGQN TTDEDWSDFC 1300
QLVSGCPMRL NMASLEEKGR HFSSPFIIAT SNWSNPSPKT VYVKEAIDRR 1350
LHYKIEVKPA SFYKNAHNDM LNVNLARNND AIKDMSCVDL LMDGHTVSLS 1400
ELLNSLVMTV EIRKQNMSEF MKLWSQGVSD DDNDSAVAEF FQSFPSGEPS 1450
NSKLSSFFKA VTNHKWVAIG AAVGVLGVLV GGWFVYKHFT KEEPIPTEGV 1500
YHGVTKPKQV IKLDADPVDS QSTLEIAGLV RKNLVQFGVG EKNGCVRWVM 1550
NALGIKDDWL LVPSHAYKFE KDYQMMEFYF NRGGTYYSIS AGNVVIQSLD 1600
VGFQDVVLMK VPTIPKFRDI TEHFIKKNDV PRALNRLATL VTTVNGTPML 1650
ISEGPLKMEE KATYVHKRND GTTVDLTVDQ AWRGKGEGLP GMCGGALISS 1700
NQSIQNAILG IHVAGGNSIL VAKLVTQEMF QNIEQKAIES QRIMKVEFTQ 1750
CSMNVVSKTL FKKSPIHHHI DRNMINFPAV MPFSKAEIDP MAVMLSKYSL 1800
PIVEEPDDYK MASIYFQNKV MGKTFLVDDF LDIDMAITGA PGIDAINMDS 1850
SPGFPYVQEK LTKKDLIWLD ENGLLLGVHP RLAQRILYNT VMMENCSDLD 1900
VVFTTCPKDE LRPLDKVLES KTRAIDACPL DYTILCRIYW GPAISYFQLN 1950
PGFHTGVAIG IDPDRHWDEL FKTMVRFGDV GLDLDFSSFD ASLSPFMIRE 2000
AGRILSEMSG TPSHFGEALI NTIIYSKHLL YNCCYHVYGS MPSGSPCTAL 2050
LNSIVNNVNL YYVFSKIFRK SPVFFGDALK ILCYGDDVLI VFSRNVQIDN 2100
LESIGQKIVD EFGKLGMTAT SADKSVPKLK PISELTFLKR SFNLVEDRIR 2150
PAISEKTIWS LVAWQRSNAE FEQNLENAQW FAFMHGFEFY QKFYHFVQSC 2200
LEKEMVEYRL KSYDWWRMKF YDQCFVCDLT 2230
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...

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: July 9, 2014
This is version 119 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.
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

Similar proteinsi