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Genome polyprotein [Cleaved into: Protein p11; Protein p28; NTPase (EC 3.6.1.15) (p35); Protein p32; Viral genome-linked protein (VPg) (p14); Protease-polymerase p70 (Pro-Pol) (EC 2.7.7.48) (EC 3.4.22.66); Capsid protein (CP) (VP1) (p60)]

 POLG_PESV               Reviewed;        2254 AA.
Q9QEJ5;
01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
28-MAR-2018, entry version 91.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Protein p11;
Contains:
RecName: Full=Protein p28;
Contains:
RecName: Full=NTPase;
EC=3.6.1.15;
AltName: Full=p35;
Contains:
RecName: Full=Protein p32;
Contains:
RecName: Full=Viral genome-linked protein;
AltName: Full=VPg;
AltName: Full=p14;
Contains:
RecName: Full=Protease-polymerase p70;
Short=Pro-Pol;
EC=2.7.7.48;
EC=3.4.22.66;
Contains:
RecName: Full=Capsid protein;
Short=CP;
AltName: Full=VP1;
AltName: Full=p60;
ORFNames=ORF1;
Porcine enteric sapovirus (isolate Swine/United States/Cowden/1980)
(Sw/SV/Cowden/1980/US).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Caliciviridae; Sapovirus.
NCBI_TaxID=523795;
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=10516074;
Guo M., Chang K.O., Hardy M.E., Zhang Q., Parwani A.V., Saif L.J.;
"Molecular characterization of a porcine enteric calicivirus
genetically related to Sapporo-like human caliciviruses.";
J. Virol. 73:9625-9631(1999).
[2]
CHARACTERIZATION OF CAPSID PROTEIN.
PubMed=11283075; DOI=10.1128/JCM.39.4.1487-1493.2001;
Guo M., Qian Y., Chang K.O., Saif L.J.;
"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.";
J. Clin. Microbiol. 39:1487-1493(2001).
-!- FUNCTION: NTPase presumably plays a role in replication. Despite
having similarities with helicases, does not seem to display any
helicase activity (By similarity). {ECO:0000250}.
-!- FUNCTION: 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). {ECO:0000250}.
-!- FUNCTION: 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). {ECO:0000250}.
-!- FUNCTION: 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).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
-!- CATALYTIC ACTIVITY: Endopeptidase with a preference for cleavage
when the P1 position is occupied by Glu-|-Xaa and the P1' position
is occupied by Gly-|-Yaa.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- SUBUNIT: Capsid protein homodimerizes, then multimerizes.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Capsid protein: Virion. Host cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage; Named isoforms=2;
Name=Genome polyprotein;
IsoId=Q9QEJ5-1; Sequence=Displayed;
Note=Produced from the genomic RNA.;
Name=Subgenomic capsid protein; Synonyms=VP1;
IsoId=Q9QEJ5-2; Sequence=VSP_034378;
Note=Produced from the subgenomic RNA.;
-!- DOMAIN: Protease-polymerase is composed of two domains displaying
two different catalytic activity. These activities may act
independently.
-!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
Pro-Pol is first autocatalytically cleaved, then processes the
whole polyprotein.
-!- PTM: 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). {ECO:0000250}.
-!- MISCELLANEOUS: Two different 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).
{ECO:0000250}.
-----------------------------------------------------------------------
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EMBL; AF182760; AAF04560.1; -; Genomic_RNA.
RefSeq; NP_051035.1; NC_000940.1.
PDB; 2MXD; NMR; -; A=948-1006.
PDBsum; 2MXD; -.
ProteinModelPortal; Q9QEJ5; -.
SMR; Q9QEJ5; -.
MEROPS; C24.003; -.
GeneID; 1457802; -.
KEGG; vg:1457802; -.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0003723; F:RNA binding; IEA:InterPro.
GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
CDD; cd00205; rhv_like; 1.
Gene3D; 2.60.120.20; -; 1.
InterPro; IPR004005; Calicivirus_coat.
InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000317; Peptidase_C24.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR033703; Rhv-like.
InterPro; IPR001205; RNA-dir_pol_C.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR029053; Viral_coat.
Pfam; PF00915; Calici_coat; 1.
Pfam; PF03510; Peptidase_C24; 1.
Pfam; PF00680; RdRP_1; 1.
Pfam; PF00910; RNA_helicase; 1.
PRINTS; PR00916; 2CENDOPTASE.
PRINTS; PR00918; CALICVIRUSNS.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS51218; SF3_HELICASE_2; 1.
1: Evidence at protein level;
3D-structure; Alternative promoter usage; ATP-binding; Capsid protein;
Covalent protein-RNA linkage; DNA replication; Host cytoplasm;
Hydrolase; Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
Protease; RNA-directed RNA polymerase; Thiol protease; Transferase;
Viral RNA replication; Virion.
CHAIN 1 2254 Genome polyprotein.
/FTId=PRO_0000341637.
CHAIN 1 56 Protein p11.
/FTId=PRO_0000341638.
CHAIN 57 310 Protein p28.
/FTId=PRO_0000341639.
CHAIN 311 650 NTPase.
/FTId=PRO_0000341640.
CHAIN 651 934 Protein p32.
/FTId=PRO_0000341641.
CHAIN 935 1048 Viral genome-linked protein.
/FTId=PRO_0000341642.
CHAIN 1049 1712 Protease-polymerase p70.
/FTId=PRO_0000341643.
CHAIN 1713 2254 Capsid protein.
/FTId=PRO_0000341644.
DOMAIN 438 592 SF3 helicase. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
DOMAIN 1063 1169 Peptidase C24.
DOMAIN 1434 1559 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 464 471 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
ACT_SITE 1078 1078 For protease activity. {ECO:0000250}.
ACT_SITE 1099 1099 For protease activity. {ECO:0000250}.
ACT_SITE 1163 1163 For protease activity. {ECO:0000250}.
SITE 56 57 Cleavage; by Pro-Pol. {ECO:0000250}.
SITE 310 311 Cleavage; by Pro-Pol. {ECO:0000250}.
SITE 649 650 Cleavage; by Pro-Pol. {ECO:0000250}.
SITE 934 935 Cleavage; by Pro-Pol. {ECO:0000250}.
SITE 1047 1048 Cleavage; by Pro-Pol. {ECO:0000250}.
SITE 1712 1713 Cleavage; by Pro-Pol. {ECO:0000250}.
MOD_RES 956 956 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
VAR_SEQ 1 1710 Missing (in isoform Subgenomic capsid
protein). {ECO:0000305}.
/FTId=VSP_034378.
HELIX 953 966 {ECO:0000244|PDB:2MXD}.
HELIX 972 983 {ECO:0000244|PDB:2MXD}.
HELIX 989 1003 {ECO:0000244|PDB:2MXD}.
SEQUENCE 2254 AA; 247170 MW; 90CA9F0314FAF739 CRC64;
MANCRPLPIG QLPNRIFDTP RLTPGWVWAC TSEATFKLEW LQDPVVIRPP DVFVAQGVVD
DFFRPKRVLQ GDPQLIAQVL LGDANGPLVG PVSMQQLTSL LHEVSQALSD HKHPLANRYT
RASLQRYADT LSNYIPLVDI LTGPKDLTPR DVLEQLAAGR EWECVPDSAL KKVFRDMWQY
ICEGCDSVYI KLQDVKRKMP HIDTTVLKQF IITLTDTISM ATALDTKTWL AHILGWLKPT
CLVMIMQQHV NSPQGWAATL TALAELYYGI MPLTETLGSV ASWVTDKFAD MATSTWGKFK
SWWDSLYTPQ AGNDLIILGG VVGLVYFMVF GDAPTQMFTK KLMRVCGFIT STVAAIKAAM
WIVDYFKQRE HEHQVRITLA RWAALQEVIK QNRCAGLSEV TKLKECCEVL LNEVTELMYK
LGASPLAGLI RSTSDVIQTT INELAQLMAY DTQRKPPAMV VFGGPPGIGK TRLVEALAKQ
LGEVSHFTMT VDHYDTYTGN TVAIWDEFDV DSKQAFIEAT IGIVNCAPYP LNCDRPEAKG
RVFTSKYVLA TTNCPTPVMP DHPRAMAFWR RITFIDVTAP TIEQWLVDNP GRKAPTSLFK
DDFSHLQCSV RGYTAYDEKG NTLSGKVARA RYVSVNNLLD LIKEKYNSEA ADVKHLWFTV
PQAIHKQARD IILGWLRFHS YPNTVADNIP LSEVRDPTCF GYVVISDVDP PRHVAEHVAH
IEVESILRTD IVGLLREGGG GLFRALKVKS APRNCIINKV MMQAHHTTLQ VLTSQEPHPP
NLPRPRRLVF VESPIDIISA LRHHVGFCTI PGIVKLITSG VGLGVENLGN FLQSIAGNVR
FPLQSECSLL RTPSGDVLFY TSGQAAVWAT PARFPIVTPG EASVGKEVCS ESSWWDILKA
LFSTLVVAFG PIATLVLTAH NLAYLNTREN TLSEAKGKNK RGRGARRAIA LRDDEYDEWQ
DIIRDWRKEM TVQQFLDLKE RALSGASDPD SQRYNAWLEL RAKRLSAGAY QHAVVDIIGK
SGHRREVIRT QVMRAPREPK GDTYDSEGRG YVVPMTAQEK HTGWAVHIGN GRLVTCTHVA
NMCDRVAEVE FKVAETDRDT CIITAPLGHL PSVALGNGPP AFYTTNFHPI RVLDEGSWDT
TTTRVTGWRV VINNGTTTAP GDCGQPYLNA RRQLVGVHAA TSTCGVKKLV SRVQTKKTAK
ATFPWKGLPV TTMPDAGGLP TGTRYHRSIA WPKLLPEETH APAPYGVNDP RHPFSQHQMI
ANNLQPYINT PVALDQTLLQ RAVKHTKGYL DQIIGTHRSP NLTYAAAVES MAHDTACGPN
LPGRKKDYMT DQGEPIGPLK QMLEEAWDMA HRGVPRRHEY KLALKDELRP IEKNDQGKKR
LLWGCDAGVS MIANAVFKPV TERLVDTVPM HPVAVGICMD SPQIEQMNQA LTGRVLYCLD
YSKWDSTQNP AVTCASVDIL ASYAEDTPLS SAAIATLCSP AVGRLDDIGL TVTSGLPSGM
PFTSVINSVN HMIYFAMAVL EAYEEFKVPY MGNIFDNETI YTYGDDCVYG LTPATASIMP
VVVKNLTSYG LVPTAADKSQ SIEPTDTPVF LKRTFSQTPF GLRALLDETS LARQCYWVKA
NRTTDLFEPA AVDVDIRKNQ LEVMLAYASQ HPRSVFDKLA GMAEVTASAE GYQLVNVNWA
NAVATYNAWY GGTDGGRAPT NEDEEPEVFV MEAPAPTRSV ASNPEGTQNS NESRPVQPAG
PMPVAAAQAL EMAVATGQIN DTIPSVVRET FSTYTNVTWT TRQPTGTLLA RMSLGPGLNP
YTLHLSAMWA GWGGSFEIKV IISGSGMYAG KLLCALIPPG VDPSAVDQPG AFPHALVDAR
ITDGVTFTLG DVRAVDYHET GVGGAIASLA LYVYQPLINP FETAVSAAMV TIETRPGPDF
GFTLLKPPNQ AMEVGFDPRS LLPRTARTLR GNRFGRPITA VVIVGVAQQI NRHFSAEGTT
LGWSTAPIGP CVARVNGKHT DNTGRAVFQL GPLSNGPLYP NIINHYPDVA ASTIFNTGTA
VNDNTTGGGG PMVIFNDVGD VVEDVAYQMR FIASHATSQS PTLIDQINAT SMAVCSFGNS
RADLNQNQLN VGIELTYTCG NTAINGIVTS FMDRQYTFGP QGPNNIMLWV ESVLGTHTGN
NTVYSSQPDT VSAALQGQPF NIPDGYMAVW NVNADSADFQ IGLRRDGYFV TNGAIGTRMV
ISEDTTFSFN GMYTLTTPLI GPSGTSGRSI HSSR


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