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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MAAMSRLTGM TTAILPEKKP LDFFLDLRDK TPPCCIRATG RLAWPVFPGQ
60 70 80 90 100
NGKEGPLETC NKCGKWLNGF GNFGLEDLGD VCLCSIAQQK HKFGPVCLCN
110 120 130 140 150
RVYIHDCGRW RRRSRFLKHY KALNKVIPCA YQFDESFPTP IFEGEVDDLF
160 170 180 190 200
VELGAPTSMG FMDKKLLKKG KKLMDKFVDV DEPCLTSRDT SLLDSIASDN
210 220 230 240 250
TIRAKLEEEY GVEMVQAARD RKDFMKNLRL ALDNRPANPV TWYTKLGNIT
260 270 280 290 300
EKGKQWAKKV VYGARKVTDP LKTLASILLV GLHNVIAVDT TVMLSTFKPV
310 320 330 340 350
NLLAILMDWN NDLTGFITTL VRLLELYGVV QATVNLIIEG VKSFWDKVVC
360 370 380 390 400
ATDRCFDLLK RLFDTFEDSV PTGPTAGCLI FMAFVFSTVV GYLPNNSVIT
410 420 430 440 450
TFMKGAGKLT TFAGVVGAIR TLWITINQHM VAKDLTSVQQ KVMTVVKMAN
460 470 480 490 500
EAATLDQLEI VSCLCSDLET TLTNRCTLPS YNQHLGILNA SQKVISDLHT
510 520 530 540 550
MVLGKINMTK QRPQPVAVIF KGAPGIGKTY LVHRIARDLG CQHPSTINFG
560 570 580 590 600
LDHFDSYTGE EVAIADEFNT CGDGESWVEL FIQMVNTNPC PLNCDKAENK
610 620 630 640 650
NKVFNSKYLL CTTNSNMILN ATHPRAGAFY RRVMIVEARN KAVESWQATR
660 670 680 690 700
HGSKPGKSCY SKDMSHLTFQ VYPHNMPAPG FVFVGDKLVK SQVTPREYKY
710 720 730 740 750
SELLDLIKSE HPDVASFEGA NKFNFVYPDA QYDQALLMWK QYFVMYGCVA
760 770 780 790 800
RLAKNFVDDI PYNQVHISRA SDPKIEGCVE YQCKFQHLWR MVPQFVLGCV
810 820 830 840 850
NMTNQLGTPL TQQQLDRITN GVEGVTVTTV NNILPFHSQT TLINPSFIKL
860 870 880 890 900
IWAVRKHLKG LSGVTKVAQF IWRVMTNPVD AYGTLVRTLT GAATFSDDPV
910 920 930 940 950
STTIICSNCT IQLHSCGGLL VRYSRDPVPV ASDNVDRGDQ GVDVFTDPNL
960 970 980 990 1000
ISGFSWRQIA HLFVEVISHL CANHLVNLAT MAALGAVATK AFQGVKGKTK
1010 1020 1030 1040 1050
RGRGARVNLG NDEYDEWQAA RREFVNAHDM TAEEYLAMKN KAAMGSDDQD
1060 1070 1080 1090 1100
SIMFRSWWTR RQLRPEEDQV TIVGRSGVRN EVIRTRVRQT PRGPKTLDDG
1110 1120 1130 1140 1150
GFYDNDYEGL PGFMRHNGSG WMIHIGNGLY ISNTHTARSS CSEIVTCSPT
1160 1170 1180 1190 1200
TDLCLVKGES IRSVAQIAEG TPVCDWKKSP ISTYGIKKTL SDSTKIDVLA
1210 1220 1230 1240 1250
YDGCTQTTHG DCGLPLYDSS GKIVAIHTGK LLGFSKMCTL IDLTITKGVY
1260 1270 1280 1290 1300
ETSNFFCGEP IDYRGITAHR LVGAEPRPPV SGTRYAKVPG VPDEYKTGYR
1310 1320 1330 1340 1350
PANLGRSDPD SDKSLMNIAV KNLQVYQQEP KLDKVDEFIE RAAADVLGYL
1360 1370 1380 1390 1400
RFLTKGERQA NLNFKAAFNT LDLSTSCGPF VPGKKIDHVK DGVMDQVLAK
1410 1420 1430 1440 1450
HLYKCWSVAN SGKALHHIYA CGLKDELRPL DKVKEGKKRL LWGCDVGVAV
1460 1470 1480 1490 1500
CAAAVFHNIC YKLKMVARFG PIAVGVDMTS RDVDVIINNL TSKASDFLCL
1510 1520 1530 1540 1550
DYSKWDSTMS PCVVRLAIDI LADCCEQTEL TKSVVLTLKS HPMTILDAMI
1560 1570 1580 1590 1600
VQTKRGLPSG MPFTSVINSI CHWLLWSAAV YKSCAEIGLH CSNLYEDAPF
1610 1620 1630 1640 1650
YTYGDDGVYA MTPMMVSLLP AIIENLRDYG LSPTAADKTE FIDVCPLNKI
1660 1670 1680 1690 1700
SFLKRTFELT DIGWVSKLDK SSILRQLEWS KTTSRHMVIE ETYDLAKEER
1710 1720 1730 1740 1750
GVQLEELQVA AAAHGQEFFN FVCRELERQQ AYTQFSVYSY DAARKILADR
1760 1770 1780 1790 1800
KRVVSVVPDD EFVNVMEGKA RAAPQGEAAG TATTASVPGT TTDGMDPGVV
1810 1820 1830 1840 1850
ATTSVITAEN SSASIATAGI GGPPQQVDQQ ETWRTNFYYN DVFTWSVADA
1860 1870 1880 1890 1900
PGSILYTVQH SPQNNPFTAV LSQMYAGWAG GMQFRFIVAG SGVFGGRLVR
1910 1920 1930 1940 1950
AVIPPGIEIG PGLEVRQFPH VVIDARSLEP VTITMPDLRP NMYHPTGDPG
1960 1970 1980 1990 2000
LVPTLVLSVY NNLINPFGGS TSAIQVTVET RPSEDFEFVM IRAPSSKTVD
2010 2020 2030 2040 2050
SISPAGLLTT PVLTGVGNDN RWNGQIVGLQ PVPGGFSTCN RHWNLNGSTY
2060 2070 2080 2090 2100
GWSSPRFGDI DHRRGSASYS GSNATNVLQF WYANAGSAID NPISQVAPDG
2110 2120 2130 2140 2150
FPDMSFVPFN GPGIPAAGWV GFGAIWNSNS GAPNVTTVQA YELGFATGAP
2160 2170 2180 2190 2200
GNLQPTTNTS GAQTVAKSIY AVVTGTAQNP AGLFVMASGI ISTPNASAIT
2210 2220 2230 2240 2250
YTPQPDRIVT TPGTPAAAPV GKNTPIMFAS VVRRTGDVNA TAGSANGTQY
2260 2270 2280 2290 2300
GTGSQPLPVT IGLSLNNYSS ALMPGQFFVW QLTFASGFME IGLSVDGYFY
2310 2320 2330 2340
AGTGASTTLI DLTELIDVRP VGPRPSKSTL VFNLGGTANG FSYV

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 110 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