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P27410

- POLG_RHDVF

UniProt

P27410 - POLG_RHDVF

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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

Functioni

NTPase presumably plays a role in replication By similarity.2 Publications
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.2 Publications
3C-like protease processes the polyprotein: 3CLpro-RdRp (p72) is first released by autocleavage, then all other proteins are cleaved By similarity.2 Publications
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.2 Publications
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.2 Publications

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).

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 activity By similarity
Active sitei1159 – 11591For 3CLpro activity By similarity
Active sitei1212 – 12121For 3CLpro activity By similarity
Sitei1251 – 12522Cleavage; by 3CLpro
Sitei1767 – 17682Cleavage; by 3CLpro

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi522 – 5298ATP Reviewed prediction

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
Complete GO annotation...

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
Complete GO annotation...

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)-tyrosine By 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.

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.

Miscellaneous databases

EvolutionaryTraceiP27410.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini492 – 653162SF3 helicaseAdd
BLAST
Domaini1120 – 121899Peptidase C24Add
BLAST
Domaini1495 – 1619125RdRp catalyticAdd
BLAST

Sequence similaritiesi

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. VSP_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: July 9, 2014
This is version 107 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.

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

Similar proteinsi