Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

P27410

- POLG_RHDVF

UniProt

P27410 - POLG_RHDVF

Protein

Genome polyprotein

Gene

ORF1

Organism
Rabbit hemorrhagic disease virus (strain Rabbit/Germany/FRG/1989) (Ra/LV/RHDV/GH/1989/GE) (RHDV-FRG)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    NTPase presumably plays a role in replication.By similarity
    Viral genome-linked protein is covalently linked to the 5'-end of the positive-strand, negative-strand genomic RNAs and subgenomic RNA. Acts as a genome-linked replication primer. May recruit ribosome to viral RNA thereby promoting viral proteins translation By similarity.By similarity
    3C-like protease processes the polyprotein: 3CLpro-RdRp (p72) is first released by autocleavage, then all other proteins are cleaved.By similarity
    RNA-directed RNA polymerase replicates genomic and antigenomic RNA by recognizing replications specific signals. Transcribes also a subgenomic mRNA by initiating RNA synthesis internally on antigenomic RNA. This sgRNA codes for structural proteins. Catalyzes the covalent attachment VPg with viral RNAs By similarity.PROSITE-ProRule annotation
    Capsid protein VP60 self assembles to form an icosahedral capsid with a T=3 symmetry, about 35 nm in diameter, and consisting of 180 capsid proteins. A smaller form of capsid with a diameter of 23 nm might be capsid proteins assembled as icosahedron with T=1 symmetry. The capsid encapsulate VP2 proteins and genomic or subgenomic RNA. Attaches virion to target cells by binding histo-blood group antigens, inducing endocytosis of the viral particle. Acidification of the endosome induces conformational change of capsid protein thereby injecting virus genomic RNA into host cytoplasm By similarity.By similarity

    Catalytic activityi

    NTP + H2O = NDP + phosphate.
    Endopeptidase with a preference for cleavage when the P1 position is occupied by Glu-|-Xaa and the P1' position is occupied by Gly-|-Yaa.
    Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei143 – 1442Cleavage; by 3CLpro
    Sitei339 – 3402Cleavage; by 3CLpro
    Sitei718 – 7192Cleavage; by 3CLpro
    Sitei936 – 9372Cleavage; by host
    Sitei993 – 9942Cleavage; by 3CLpro
    Sitei1108 – 11092Cleavage; by 3CLpro
    Active sitei1135 – 11351For 3CLpro activityBy similarity
    Active sitei1159 – 11591For 3CLpro activityBy similarity
    Active sitei1212 – 12121For 3CLpro activityBy similarity
    Sitei1251 – 12522Cleavage; by 3CLpro
    Sitei1767 – 17682Cleavage; by 3CLpro

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi522 – 5298ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. cysteine-type endopeptidase activity Source: InterPro
    3. RNA binding Source: InterPro
    4. RNA-directed RNA polymerase activity Source: UniProtKB-KW
    5. RNA helicase activity Source: InterPro

    GO - Biological processi

    1. RNA-protein covalent cross-linking Source: UniProtKB-KW
    2. transcription, DNA-templated Source: InterPro
    3. viral RNA genome replication Source: InterPro

    Keywords - Molecular functioni

    Helicase, Hydrolase, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Thiol protease, Transferase

    Keywords - Biological processi

    Viral RNA replication

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Genome polyprotein
    Alternative name(s):
    p254
    Cleaved into the following 11 chains:
    Alternative name(s):
    2C-like protein
    P2C
    p37
    Alternative name(s):
    VPg
    p13
    3C-like protease (EC:3.4.22.66)
    Short name:
    3CLpro
    Alternative name(s):
    Calicivirin
    Thiol protease P3C
    p15
    Alternative name(s):
    3Dpol
    p58
    Gene namesi
    ORF Names:ORF1
    OrganismiRabbit hemorrhagic disease virus (strain Rabbit/Germany/FRG/1989) (Ra/LV/RHDV/GH/1989/GE) (RHDV-FRG)
    Taxonomic identifieri314536 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageCaliciviridaeLagovirus
    Virus hostiOryctolagus cuniculus (Rabbit) [TaxID: 9986]
    ProteomesiUP000000413: Genome

    Subcellular locationi

    GO - Cellular componenti

    1. host cell cytoplasm Source: UniProtKB-SubCell
    2. viral capsid Source: UniProtKB-KW

    Keywords - Cellular componenti

    Capsid protein, Host cytoplasm, Virion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1135 – 11351H → N: Complete loss of 3CLpro activity in vitro. 1 Publication
    Mutagenesisi1152 – 11521D → E: Partial loss of 3CLpro activity in vitro. 1 Publication
    Mutagenesisi1152 – 11521D → G or N: Complete loss of 3CLpro activity in vitro. 1 Publication
    Mutagenesisi1175 – 11751D → G or E: Complete loss of 3CLpro activity in vitro. 1 Publication
    Mutagenesisi1175 – 11751D → N: Partial loss of 3CLpro activity in vitro. 1 Publication
    Mutagenesisi1212 – 12121C → G: Complete loss of 3CLpro activity in vitro. 1 Publication
    Mutagenesisi1212 – 12121C → S: Partial loss of 3CLpro activity in vitro. 1 Publication
    Mutagenesisi1227 – 12271H → L or N: Complete loss of 3CLpro activity in vitro. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 23442344Genome polyproteinPRO_0000341645Add
    BLAST
    Chaini1 – 143143Protein p16PRO_0000036959Add
    BLAST
    Chaini144 – 339196Protein p23PRO_0000036960Add
    BLAST
    Chaini340 – 718379NTPasePRO_0000036961Add
    BLAST
    Chaini719 – 1108390Precursor p41PRO_0000341646Add
    BLAST
    Chaini719 – 993275Protein p29PRO_0000036962Add
    BLAST
    Chaini719 – 936218Protein p23/2PRO_0000341647Add
    BLAST
    Chaini937 – 1108172Protein p18PRO_0000341648Add
    BLAST
    Chaini994 – 1108115Viral genome-linked proteinPRO_0000036963Add
    BLAST
    Chaini1109 – 12511433C-like proteasePRO_0000036964Add
    BLAST
    Chaini1252 – 1767516RNA-directed RNA polymerasePRO_0000036965Add
    BLAST
    Chaini1768 – 2344577Capsid protein VP60PRO_0000036967Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1014 – 10141O-(5'-phospho-RNA)-tyrosineBy similarity
    Disulfide bondi1584 ↔ 1591

    Post-translational modificationi

    Specific enzymatic cleavages by its own cysteine protease yield mature proteins. The protease cleaves itself from the nascent polyprotein autocatalytically. Precursor p41 can be cleaved by viral 3CLpro into protein p19 and VPg, or cleaved by host protease into protein p23/2 and protein p18.5 Publications
    VPg is uridylylated by the polymerase and is covalently attached to the 5'-end of the polyadenylated genomic and subgenomic RNAs. This uridylylated form acts as a nucleotide-peptide primer for the polymerase By similarity.By similarity

    Keywords - PTMi

    Covalent protein-RNA linkage, Disulfide bond, Phosphoprotein

    Interactioni

    Subunit structurei

    Binds to histo-blood group antigens at surface of target cells.By similarity

    Structurei

    Secondary structure

    1
    2344
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1257 – 12637
    Beta strandi1266 – 12716
    Beta strandi1282 – 12876
    Helixi1293 – 12953
    Beta strandi1300 – 13023
    Helixi1305 – 13073
    Helixi1315 – 132410
    Helixi1325 – 13273
    Helixi1337 – 135317
    Turni1354 – 13563
    Helixi1364 – 13707
    Beta strandi1373 – 13764
    Beta strandi1379 – 13813
    Helixi1385 – 13873
    Beta strandi1391 – 13933
    Helixi1396 – 141015
    Beta strandi1418 – 14236
    Beta strandi1440 – 14445
    Helixi1446 – 146520
    Turni1466 – 14694
    Beta strandi1470 – 14723
    Helixi1482 – 149312
    Beta strandi1495 – 15028
    Helixi1505 – 15084
    Helixi1511 – 152212
    Helixi1529 – 153911
    Beta strandi1543 – 15453
    Beta strandi1547 – 15515
    Helixi1564 – 158623
    Helixi1594 – 15974
    Beta strandi1600 – 16034
    Beta strandi1606 – 16116
    Helixi1613 – 16175
    Helixi1619 – 162810
    Beta strandi1633 – 16375
    Helixi1647 – 16493
    Beta strandi1655 – 16606
    Beta strandi1663 – 16686
    Helixi1670 – 16789
    Beta strandi1679 – 168911
    Helixi1698 – 171215
    Helixi1716 – 172914
    Turni1730 – 17323
    Helixi1740 – 175011

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1KHVX-ray2.50A/B1252-1767[»]
    1KHWX-ray2.70A/B1252-1767[»]
    ProteinModelPortaliP27410.
    SMRiP27410. Positions 1256-1752.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP27410.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini492 – 653162SF3 helicasePROSITE-ProRule annotationAdd
    BLAST
    Domaini1120 – 121899Peptidase C24Add
    BLAST
    Domaini1495 – 1619125RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 peptidase C24 domain.Curated
    Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation
    Contains 1 SF3 helicase domain.PROSITE-ProRule annotation

    Family and domain databases

    Gene3Di2.60.120.20. 1 hit.
    3.40.50.300. 2 hits.
    InterProiIPR003593. AAA+_ATPase.
    IPR004005. Calicivirus_coat.
    IPR004004. Helic/Pol/Pept_Calicivir-typ.
    IPR000605. Helicase_SF3_ssDNA/RNA_vir.
    IPR014759. Helicase_SF3_ssRNA_vir.
    IPR027417. P-loop_NTPase.
    IPR000317. Peptidase_C24.
    IPR001205. RNA-dir_pol_C.
    IPR007094. RNA-dir_pol_PSvirus.
    IPR009003. Trypsin-like_Pept_dom.
    IPR029053. Viral_coat.
    [Graphical view]
    PfamiPF00915. Calici_coat. 1 hit.
    PF03510. Peptidase_C24. 1 hit.
    PF00680. RdRP_1. 1 hit.
    PF00910. RNA_helicase. 1 hit.
    [Graphical view]
    PRINTSiPR00916. 2CENDOPTASE.
    PR00918. CALICVIRUSNS.
    SMARTiSM00382. AAA. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEiPS50507. RDRP_SSRNA_POS. 1 hit.
    PS51218. SF3_HELICASE_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative promoter usage. Align

    Isoform Genome polyprotein (identifier: P27410-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAAMSRLTGM TTAILPEKKP LDFFLDLRDK TPPCCIRATG RLAWPVFPGQ     50
    NGKEGPLETC NKCGKWLNGF GNFGLEDLGD VCLCSIAQQK HKFGPVCLCN 100
    RVYIHDCGRW RRRSRFLKHY KALNKVIPCA YQFDESFPTP IFEGEVDDLF 150
    VELGAPTSMG FMDKKLLKKG KKLMDKFVDV DEPCLTSRDT SLLDSIASDN 200
    TIRAKLEEEY GVEMVQAARD RKDFMKNLRL ALDNRPANPV TWYTKLGNIT 250
    EKGKQWAKKV VYGARKVTDP LKTLASILLV GLHNVIAVDT TVMLSTFKPV 300
    NLLAILMDWN NDLTGFITTL VRLLELYGVV QATVNLIIEG VKSFWDKVVC 350
    ATDRCFDLLK RLFDTFEDSV PTGPTAGCLI FMAFVFSTVV GYLPNNSVIT 400
    TFMKGAGKLT TFAGVVGAIR TLWITINQHM VAKDLTSVQQ KVMTVVKMAN 450
    EAATLDQLEI VSCLCSDLET TLTNRCTLPS YNQHLGILNA SQKVISDLHT 500
    MVLGKINMTK QRPQPVAVIF KGAPGIGKTY LVHRIARDLG CQHPSTINFG 550
    LDHFDSYTGE EVAIADEFNT CGDGESWVEL FIQMVNTNPC PLNCDKAENK 600
    NKVFNSKYLL CTTNSNMILN ATHPRAGAFY RRVMIVEARN KAVESWQATR 650
    HGSKPGKSCY SKDMSHLTFQ VYPHNMPAPG FVFVGDKLVK SQVTPREYKY 700
    SELLDLIKSE HPDVASFEGA NKFNFVYPDA QYDQALLMWK QYFVMYGCVA 750
    RLAKNFVDDI PYNQVHISRA SDPKIEGCVE YQCKFQHLWR MVPQFVLGCV 800
    NMTNQLGTPL TQQQLDRITN GVEGVTVTTV NNILPFHSQT TLINPSFIKL 850
    IWAVRKHLKG LSGVTKVAQF IWRVMTNPVD AYGTLVRTLT GAATFSDDPV 900
    STTIICSNCT IQLHSCGGLL VRYSRDPVPV ASDNVDRGDQ GVDVFTDPNL 950
    ISGFSWRQIA HLFVEVISHL CANHLVNLAT MAALGAVATK AFQGVKGKTK 1000
    RGRGARVNLG NDEYDEWQAA RREFVNAHDM TAEEYLAMKN KAAMGSDDQD 1050
    SIMFRSWWTR RQLRPEEDQV TIVGRSGVRN EVIRTRVRQT PRGPKTLDDG 1100
    GFYDNDYEGL PGFMRHNGSG WMIHIGNGLY ISNTHTARSS CSEIVTCSPT 1150
    TDLCLVKGES IRSVAQIAEG TPVCDWKKSP ISTYGIKKTL SDSTKIDVLA 1200
    YDGCTQTTHG DCGLPLYDSS GKIVAIHTGK LLGFSKMCTL IDLTITKGVY 1250
    ETSNFFCGEP IDYRGITAHR LVGAEPRPPV SGTRYAKVPG VPDEYKTGYR 1300
    PANLGRSDPD SDKSLMNIAV KNLQVYQQEP KLDKVDEFIE RAAADVLGYL 1350
    RFLTKGERQA NLNFKAAFNT LDLSTSCGPF VPGKKIDHVK DGVMDQVLAK 1400
    HLYKCWSVAN SGKALHHIYA CGLKDELRPL DKVKEGKKRL LWGCDVGVAV 1450
    CAAAVFHNIC YKLKMVARFG PIAVGVDMTS RDVDVIINNL TSKASDFLCL 1500
    DYSKWDSTMS PCVVRLAIDI LADCCEQTEL TKSVVLTLKS HPMTILDAMI 1550
    VQTKRGLPSG MPFTSVINSI CHWLLWSAAV YKSCAEIGLH CSNLYEDAPF 1600
    YTYGDDGVYA MTPMMVSLLP AIIENLRDYG LSPTAADKTE FIDVCPLNKI 1650
    SFLKRTFELT DIGWVSKLDK SSILRQLEWS KTTSRHMVIE ETYDLAKEER 1700
    GVQLEELQVA AAAHGQEFFN FVCRELERQQ AYTQFSVYSY DAARKILADR 1750
    KRVVSVVPDD EFVNVMEGKA RAAPQGEAAG TATTASVPGT TTDGMDPGVV 1800
    ATTSVITAEN SSASIATAGI GGPPQQVDQQ ETWRTNFYYN DVFTWSVADA 1850
    PGSILYTVQH SPQNNPFTAV LSQMYAGWAG GMQFRFIVAG SGVFGGRLVR 1900
    AVIPPGIEIG PGLEVRQFPH VVIDARSLEP VTITMPDLRP NMYHPTGDPG 1950
    LVPTLVLSVY NNLINPFGGS TSAIQVTVET RPSEDFEFVM IRAPSSKTVD 2000
    SISPAGLLTT PVLTGVGNDN RWNGQIVGLQ PVPGGFSTCN RHWNLNGSTY 2050
    GWSSPRFGDI DHRRGSASYS GSNATNVLQF WYANAGSAID NPISQVAPDG 2100
    FPDMSFVPFN GPGIPAAGWV GFGAIWNSNS GAPNVTTVQA YELGFATGAP 2150
    GNLQPTTNTS GAQTVAKSIY AVVTGTAQNP AGLFVMASGI ISTPNASAIT 2200
    YTPQPDRIVT TPGTPAAAPV GKNTPIMFAS VVRRTGDVNA TAGSANGTQY 2250
    GTGSQPLPVT IGLSLNNYSS ALMPGQFFVW QLTFASGFME IGLSVDGYFY 2300
    AGTGASTTLI DLTELIDVRP VGPRPSKSTL VFNLGGTANG FSYV 2344

    Note: Produced from the genomic RNA.

    Length:2,344
    Mass (Da):257,068
    Last modified:August 1, 1992 - v1
    Checksum:i1454C248F81E9212
    GO
    Isoform Subgenomic capsid protein VP60 (identifier: P27410-2) [UniParc]FASTAAdd to Basket

    Also known as: VP1

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1765: Missing.

    Note: Produced from the subgenomic RNA.

    Show »
    Length:579
    Mass (Da):60,257
    Checksum:i20857900C4107D20
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 17651765Missing in isoform Subgenomic capsid protein VP60. CuratedVSP_034381Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M67473 Genomic RNA. Translation: AAA47285.1.
    PIRiA41039. RRWWRH.
    RefSeqiNP_062875.1. NC_001543.1.

    Genome annotation databases

    GeneIDi1491968.

    Keywords - Coding sequence diversityi

    Alternative promoter usage

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M67473 Genomic RNA. Translation: AAA47285.1 .
    PIRi A41039. RRWWRH.
    RefSeqi NP_062875.1. NC_001543.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KHV X-ray 2.50 A/B 1252-1767 [» ]
    1KHW X-ray 2.70 A/B 1252-1767 [» ]
    ProteinModelPortali P27410.
    SMRi P27410. Positions 1256-1752.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 1491968.

    Miscellaneous databases

    EvolutionaryTracei P27410.

    Family and domain databases

    Gene3Di 2.60.120.20. 1 hit.
    3.40.50.300. 2 hits.
    InterProi IPR003593. AAA+_ATPase.
    IPR004005. Calicivirus_coat.
    IPR004004. Helic/Pol/Pept_Calicivir-typ.
    IPR000605. Helicase_SF3_ssDNA/RNA_vir.
    IPR014759. Helicase_SF3_ssRNA_vir.
    IPR027417. P-loop_NTPase.
    IPR000317. Peptidase_C24.
    IPR001205. RNA-dir_pol_C.
    IPR007094. RNA-dir_pol_PSvirus.
    IPR009003. Trypsin-like_Pept_dom.
    IPR029053. Viral_coat.
    [Graphical view ]
    Pfami PF00915. Calici_coat. 1 hit.
    PF03510. Peptidase_C24. 1 hit.
    PF00680. RdRP_1. 1 hit.
    PF00910. RNA_helicase. 1 hit.
    [Graphical view ]
    PRINTSi PR00916. 2CENDOPTASE.
    PR00918. CALICVIRUSNS.
    SMARTi SM00382. AAA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEi PS50507. RDRP_SSRNA_POS. 1 hit.
    PS51218. SF3_HELICASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Rabbit hemorrhagic disease virus -- molecular cloning and nucleotide sequencing of a calicivirus genome."
      Meyers G., Wirblich C., Thiel H.-J.
      Virology 184:664-676(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Genomic and subgenomic RNAs of rabbit hemorrhagic disease virus are both protein-linked and packaged into particles."
      Meyers G., Wirblich C., Thiel H.-J.
      Virology 184:677-686(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF VPG.
    3. "Identification and characterization of a 3C-like protease from rabbit hemorrhagic disease virus, a calicivirus."
      Boniotti B., Wirblich C., Sibilia M., Meyers G., Thiel H.J., Rossi C.
      J. Virol. 68:6487-6495(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF HIS-1135; ASP-1152; ASP-1175; CYS-1212 AND HIS-1227.
    4. "3C-like protease of rabbit hemorrhagic disease virus: identification of cleavage sites in the ORF1 polyprotein and analysis of cleavage specificity."
      Wirblich C., Sibilia M., Boniotti M.B., Rossi C., Thiel H.-J., Meyers G.
      J. Virol. 69:7159-7168(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
    5. "Two independent pathways of expression lead to self-assembly of the rabbit hemorrhagic disease virus capsid protein."
      Sibilia M., Boniotti M.B., Angoscini P., Capucci L., Rossi C.
      J. Virol. 69:5812-5815(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBGENOMIC ORIGIN OF VP60.
    6. "Detection of viral proteins after infection of cultured hepatocytes with rabbit hemorrhagic disease virus."
      Konig M., Thiel H.J., Meyers G.
      J. Virol. 72:4492-4497(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
    7. "Rabbit hemorrhagic disease virus: genome organization and polyprotein processing of a calicivirus studied after transient expression of cDNA constructs."
      Meyers G., Wirblich C., Thiel H.J., Thumfart J.O.
      Virology 276:349-363(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
    8. "Identification of a new cleavage site of the 3C-like protease of rabbit haemorrhagic disease virus."
      Joubert P., Pautigny C., Madelaine M.-F., Rasschaert D.
      J. Gen. Virol. 81:481-488(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
    9. "Characterisation of the RNA-dependent RNA polymerase from Rabbit hemorrhagic disease virus produced in Escherichia coli."
      Lopez Vazquez A.L., Martin Alonso J.M., Parra F.
      Arch. Virol. 146:59-69(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF RNA-DIRECTED RNA POLYMERASE.
    10. "Rabbit hemorrhagic disease virus: identification of a cleavage site in the viral polyprotein that is not processed by the known calicivirus protease."
      Thumfart J.O., Meyers G.
      Virology 304:352-363(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
    11. "The coat protein of Rabbit hemorrhagic disease virus contains a molecular switch at the N-terminal region facing the inner surface of the capsid."
      Barcena J., Verdaguer N., Roca R., Morales M., Angulo I., Risco C., Carrascosa J.L., Torres J.M., Caston J.R.
      Virology 322:118-134(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF CAPSID PROTEIN VP60.
    12. "Crystal structures of active and inactive conformations of a caliciviral RNA-dependent RNA polymerase."
      Ng K.K.S., Cherney M.M., Vazquez A.L., Machin A., Martin-Alonso J.M., Parra F., James M.N.G.
      J. Biol. Chem. 277:1381-1387(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1252-1767.

    Entry informationi

    Entry nameiPOLG_RHDVF
    AccessioniPrimary (citable) accession number: P27410
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 108 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Two differents RNAs lead the expression of the capsid protein. One arises from the cleavage of the polyprotein translated from the genomic RNA and the other from the translation of a subgenomic RNA derived from the (-)RNA template. Capsid protein expressed from the subgenomic mRNA is produced in much larger amounts than the cleaved one By similarity.By similarity

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference 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

    External Data

    Dasty 3