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Q9QEJ5

- POLG_PESV

UniProt

Q9QEJ5 - POLG_PESV

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Protein

Genome polyprotein

Gene

ORF1

Organism
Porcine enteric sapovirus (isolate Swine/United States/Cowden/1980) (Sw/SV/Cowden/1980/US)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

NTPase presumably plays a role in replication. Despite having similarities with helicases, does not seem to display any helicase activity (By similarity).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
Protease-polymerase p70 processes the polyprotein: Pro-Pol is first released by autocleavage, then all other proteins are cleaved (By similarity). It is also an RNA-directed RNA polymerase which replicates genomic and antigenomic viral RNA by recognizing specific signals. Catalyzes the covalent attachment VPg with viral RNAs (By similarity).By similarity
Capsid protein self assembles to form an icosahedral capsid with a T=3 symmetry, about 38 nm in diameter, and consisting of 180 capsid proteins. The capsid encapsulate the genomic RNA and VP2 proteins. Attaches virion to target cells, 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
Sitei56 – 572Cleavage; by Pro-PolBy similarity
Sitei310 – 3112Cleavage; by Pro-PolBy similarity
Sitei649 – 6502Cleavage; by Pro-PolBy similarity
Sitei934 – 9352Cleavage; by Pro-PolBy similarity
Sitei1047 – 10482Cleavage; by Pro-PolBy similarity
Active sitei1078 – 10781For protease activityBy similarity
Active sitei1099 – 10991For protease activityBy similarity
Active sitei1163 – 11631For protease activityBy similarity
Sitei1712 – 17132Cleavage; by Pro-PolBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi464 – 4718ATPPROSITE-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. DNA replication Source: UniProtKB-KW
  2. RNA-protein covalent cross-linking Source: UniProtKB-KW
  3. transcription, DNA-templated Source: InterPro
  4. viral RNA genome replication Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

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

Keywords - Biological processi

DNA replication, Viral RNA replication

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Protein family/group databases

MEROPSiC24.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 7 chains:
Alternative name(s):
p35
Alternative name(s):
VPg
p14
Protease-polymerase p70 (EC:2.7.7.48, EC:3.4.22.66)
Short name:
Pro-Pol
Capsid protein
Short name:
CP
Alternative name(s):
VP1
p60
Gene namesi
ORF Names:ORF1
OrganismiPorcine enteric sapovirus (isolate Swine/United States/Cowden/1980) (Sw/SV/Cowden/1980/US)
Taxonomic identifieri523795 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageCaliciviridaeSapovirus
Virus hostiSus scrofa (Pig) [TaxID: 9823]

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 22542254Genome polyproteinPRO_0000341637Add
BLAST
Chaini1 – 5656Protein p11PRO_0000341638Add
BLAST
Chaini57 – 310254Protein p28PRO_0000341639Add
BLAST
Chaini311 – 650340NTPasePRO_0000341640Add
BLAST
Chaini651 – 934284Protein p32PRO_0000341641Add
BLAST
Chaini935 – 1048114Viral genome-linked proteinPRO_0000341642Add
BLAST
Chaini1049 – 1712664Protease-polymerase p70PRO_0000341643Add
BLAST
Chaini1713 – 2254542Capsid proteinPRO_0000341644Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei956 – 9561O-(5'-phospho-RNA)-tyrosineBy similarity

Post-translational modificationi

Specific enzymatic cleavages in vivo yield mature proteins. Pro-Pol is first autocatalytically cleaved, then processes the whole polyprotein.
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, Phosphoprotein

Interactioni

Subunit structurei

Capsid protein homodimerizes, then multimerizes.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ9QEJ5.
SMRiQ9QEJ5. Positions 1202-1693.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini438 – 592155SF3 helicasePROSITE-ProRule annotationAdd
BLAST
Domaini1063 – 1169107Peptidase C24Add
BLAST
Domaini1434 – 1559126RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Domaini

Protease-polymerase is composed of two domains displaying two different catalytic activity. These activities may act independently.

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. 1 hit.
InterProiIPR004005. 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.
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: Q9QEJ5-1) [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
MANCRPLPIG QLPNRIFDTP RLTPGWVWAC TSEATFKLEW LQDPVVIRPP
60 70 80 90 100
DVFVAQGVVD DFFRPKRVLQ GDPQLIAQVL LGDANGPLVG PVSMQQLTSL
110 120 130 140 150
LHEVSQALSD HKHPLANRYT RASLQRYADT LSNYIPLVDI LTGPKDLTPR
160 170 180 190 200
DVLEQLAAGR EWECVPDSAL KKVFRDMWQY ICEGCDSVYI KLQDVKRKMP
210 220 230 240 250
HIDTTVLKQF IITLTDTISM ATALDTKTWL AHILGWLKPT CLVMIMQQHV
260 270 280 290 300
NSPQGWAATL TALAELYYGI MPLTETLGSV ASWVTDKFAD MATSTWGKFK
310 320 330 340 350
SWWDSLYTPQ AGNDLIILGG VVGLVYFMVF GDAPTQMFTK KLMRVCGFIT
360 370 380 390 400
STVAAIKAAM WIVDYFKQRE HEHQVRITLA RWAALQEVIK QNRCAGLSEV
410 420 430 440 450
TKLKECCEVL LNEVTELMYK LGASPLAGLI RSTSDVIQTT INELAQLMAY
460 470 480 490 500
DTQRKPPAMV VFGGPPGIGK TRLVEALAKQ LGEVSHFTMT VDHYDTYTGN
510 520 530 540 550
TVAIWDEFDV DSKQAFIEAT IGIVNCAPYP LNCDRPEAKG RVFTSKYVLA
560 570 580 590 600
TTNCPTPVMP DHPRAMAFWR RITFIDVTAP TIEQWLVDNP GRKAPTSLFK
610 620 630 640 650
DDFSHLQCSV RGYTAYDEKG NTLSGKVARA RYVSVNNLLD LIKEKYNSEA
660 670 680 690 700
ADVKHLWFTV PQAIHKQARD IILGWLRFHS YPNTVADNIP LSEVRDPTCF
710 720 730 740 750
GYVVISDVDP PRHVAEHVAH IEVESILRTD IVGLLREGGG GLFRALKVKS
760 770 780 790 800
APRNCIINKV MMQAHHTTLQ VLTSQEPHPP NLPRPRRLVF VESPIDIISA
810 820 830 840 850
LRHHVGFCTI PGIVKLITSG VGLGVENLGN FLQSIAGNVR FPLQSECSLL
860 870 880 890 900
RTPSGDVLFY TSGQAAVWAT PARFPIVTPG EASVGKEVCS ESSWWDILKA
910 920 930 940 950
LFSTLVVAFG PIATLVLTAH NLAYLNTREN TLSEAKGKNK RGRGARRAIA
960 970 980 990 1000
LRDDEYDEWQ DIIRDWRKEM TVQQFLDLKE RALSGASDPD SQRYNAWLEL
1010 1020 1030 1040 1050
RAKRLSAGAY QHAVVDIIGK SGHRREVIRT QVMRAPREPK GDTYDSEGRG
1060 1070 1080 1090 1100
YVVPMTAQEK HTGWAVHIGN GRLVTCTHVA NMCDRVAEVE FKVAETDRDT
1110 1120 1130 1140 1150
CIITAPLGHL PSVALGNGPP AFYTTNFHPI RVLDEGSWDT TTTRVTGWRV
1160 1170 1180 1190 1200
VINNGTTTAP GDCGQPYLNA RRQLVGVHAA TSTCGVKKLV SRVQTKKTAK
1210 1220 1230 1240 1250
ATFPWKGLPV TTMPDAGGLP TGTRYHRSIA WPKLLPEETH APAPYGVNDP
1260 1270 1280 1290 1300
RHPFSQHQMI ANNLQPYINT PVALDQTLLQ RAVKHTKGYL DQIIGTHRSP
1310 1320 1330 1340 1350
NLTYAAAVES MAHDTACGPN LPGRKKDYMT DQGEPIGPLK QMLEEAWDMA
1360 1370 1380 1390 1400
HRGVPRRHEY KLALKDELRP IEKNDQGKKR LLWGCDAGVS MIANAVFKPV
1410 1420 1430 1440 1450
TERLVDTVPM HPVAVGICMD SPQIEQMNQA LTGRVLYCLD YSKWDSTQNP
1460 1470 1480 1490 1500
AVTCASVDIL ASYAEDTPLS SAAIATLCSP AVGRLDDIGL TVTSGLPSGM
1510 1520 1530 1540 1550
PFTSVINSVN HMIYFAMAVL EAYEEFKVPY MGNIFDNETI YTYGDDCVYG
1560 1570 1580 1590 1600
LTPATASIMP VVVKNLTSYG LVPTAADKSQ SIEPTDTPVF LKRTFSQTPF
1610 1620 1630 1640 1650
GLRALLDETS LARQCYWVKA NRTTDLFEPA AVDVDIRKNQ LEVMLAYASQ
1660 1670 1680 1690 1700
HPRSVFDKLA GMAEVTASAE GYQLVNVNWA NAVATYNAWY GGTDGGRAPT
1710 1720 1730 1740 1750
NEDEEPEVFV MEAPAPTRSV ASNPEGTQNS NESRPVQPAG PMPVAAAQAL
1760 1770 1780 1790 1800
EMAVATGQIN DTIPSVVRET FSTYTNVTWT TRQPTGTLLA RMSLGPGLNP
1810 1820 1830 1840 1850
YTLHLSAMWA GWGGSFEIKV IISGSGMYAG KLLCALIPPG VDPSAVDQPG
1860 1870 1880 1890 1900
AFPHALVDAR ITDGVTFTLG DVRAVDYHET GVGGAIASLA LYVYQPLINP
1910 1920 1930 1940 1950
FETAVSAAMV TIETRPGPDF GFTLLKPPNQ AMEVGFDPRS LLPRTARTLR
1960 1970 1980 1990 2000
GNRFGRPITA VVIVGVAQQI NRHFSAEGTT LGWSTAPIGP CVARVNGKHT
2010 2020 2030 2040 2050
DNTGRAVFQL GPLSNGPLYP NIINHYPDVA ASTIFNTGTA VNDNTTGGGG
2060 2070 2080 2090 2100
PMVIFNDVGD VVEDVAYQMR FIASHATSQS PTLIDQINAT SMAVCSFGNS
2110 2120 2130 2140 2150
RADLNQNQLN VGIELTYTCG NTAINGIVTS FMDRQYTFGP QGPNNIMLWV
2160 2170 2180 2190 2200
ESVLGTHTGN NTVYSSQPDT VSAALQGQPF NIPDGYMAVW NVNADSADFQ
2210 2220 2230 2240 2250
IGLRRDGYFV TNGAIGTRMV ISEDTTFSFN GMYTLTTPLI GPSGTSGRSI

HSSR

Note: Produced from the genomic RNA.

Length:2,254
Mass (Da):247,170
Last modified:May 1, 2000 - v1
Checksum:i90CA9F0314FAF739
GO
Isoform Subgenomic capsid protein (identifier: Q9QEJ5-2) [UniParc]FASTAAdd to Basket

Also known as: VP1

The sequence of this isoform differs from the canonical sequence as follows:
     1-1710: Missing.

Note: Produced from the subgenomic RNA.

Show »
Length:544
Mass (Da):57,615
Checksum:i15FA9B93FA05D946
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 17101710Missing in isoform Subgenomic capsid protein. CuratedVSP_034378Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF182760 Genomic RNA. Translation: AAF04560.1.
RefSeqiNP_051035.1. NC_000940.1.

Genome annotation databases

GeneIDi1457802.

Keywords - Coding sequence diversityi

Alternative promoter usage

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF182760 Genomic RNA. Translation: AAF04560.1 .
RefSeqi NP_051035.1. NC_000940.1.

3D structure databases

ProteinModelPortali Q9QEJ5.
SMRi Q9QEJ5. Positions 1202-1693.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C24.003.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 1457802.

Family and domain databases

Gene3Di 2.60.120.20. 1 hit.
3.40.50.300. 1 hit.
InterProi 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.
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. "Molecular characterization of a porcine enteric calicivirus genetically related to Sapporo-like human caliciviruses."
    Guo M., Chang K.O., Hardy M.E., Zhang Q., Parwani A.V., Saif L.J.
    J. Virol. 73:9625-9631(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Expression and self-assembly in baculovirus of porcine enteric calicivirus capsids into virus-like particles and their use in an enzyme-linked immunosorbent assay for antibody detection in swine."
    Guo M., Qian Y., Chang K.O., Saif L.J.
    J. Clin. Microbiol. 39:1487-1493(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF CAPSID PROTEIN.

Entry informationi

Entry nameiPOLG_PESV
AccessioniPrimary (citable) accession number: Q9QEJ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 76 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

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