POLG_PESV
ID POLG_PESV Reviewed; 2254 AA.
AC Q9QEJ5;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=Protein p11;
DE Contains:
DE RecName: Full=Protein p28;
DE Contains:
DE RecName: Full=NTPase;
DE EC=3.6.1.15;
DE AltName: Full=p35;
DE Contains:
DE RecName: Full=Protein p32;
DE Contains:
DE RecName: Full=Viral genome-linked protein;
DE AltName: Full=VPg;
DE AltName: Full=p14;
DE Contains:
DE RecName: Full=Protease-polymerase p70;
DE Short=Pro-Pol;
DE EC=2.7.7.48;
DE EC=3.4.22.66;
DE Contains:
DE RecName: Full=Capsid protein;
DE Short=CP;
DE AltName: Full=VP1;
DE AltName: Full=p60;
GN ORFNames=ORF1;
OS Porcine enteric sapovirus (isolate Swine/United States/Cowden/1980)
OS (Sw/SV/Cowden/1980/US).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Caliciviridae; Sapovirus.
OX NCBI_TaxID=523795;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=10516074; DOI=10.1128/jvi.73.11.9625-9631.1999;
RA Guo M., Chang K.O., Hardy M.E., Zhang Q., Parwani A.V., Saif L.J.;
RT "Molecular characterization of a porcine enteric calicivirus genetically
RT related to Sapporo-like human caliciviruses.";
RL J. Virol. 73:9625-9631(1999).
RN [2]
RP CHARACTERIZATION OF CAPSID PROTEIN.
RX PubMed=11283075; DOI=10.1128/jcm.39.4.1487-1493.2001;
RA Guo M., Qian Y., Chang K.O., Saif L.J.;
RT "Expression and self-assembly in baculovirus of porcine enteric calicivirus
RT capsids into virus-like particles and their use in an enzyme-linked
RT immunosorbent assay for antibody detection in swine.";
RL J. Clin. Microbiol. 39:1487-1493(2001).
CC -!- FUNCTION: NTPase presumably plays a role in replication. Despite having
CC similarities with helicases, does not seem to display any helicase
CC activity (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Viral genome-linked protein is covalently linked to the 5'-
CC end of the positive-strand, negative-strand genomic RNAs and subgenomic
CC RNA. Acts as a genome-linked replication primer. May recruit ribosome
CC to viral RNA thereby promoting viral proteins translation (By
CC similarity). {ECO:0000250}.
CC -!- FUNCTION: Protease-polymerase p70 processes the polyprotein: Pro-Pol is
CC first released by autocleavage, then all other proteins are cleaved (By
CC similarity). It is also an RNA-directed RNA polymerase which replicates
CC genomic and antigenomic viral RNA by recognizing specific signals.
CC Catalyzes the covalent attachment VPg with viral RNAs (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: Capsid protein self assembles to form an icosahedral capsid
CC with a T=3 symmetry, about 38 nm in diameter, and consisting of 180
CC capsid proteins. The capsid encapsulate the genomic RNA and VP2
CC proteins. Attaches virion to target cells, inducing endocytosis of the
CC viral particle. Acidification of the endosome induces conformational
CC change of capsid protein thereby injecting virus genomic RNA into host
CC cytoplasm (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endopeptidase with a preference for cleavage when the P1
CC position is occupied by Glu-|-Xaa and the P1' position is occupied by
CC Gly-|-Yaa.; EC=3.4.22.66; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU01242};
CC -!- SUBUNIT: [Capsid protein]: Homodimer. Homomultimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein]: Virion. Host cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=Genome polyprotein;
CC IsoId=Q9QEJ5-1; Sequence=Displayed;
CC Name=Subgenomic capsid protein; Synonyms=VP1;
CC IsoId=Q9QEJ5-2; Sequence=VSP_034378;
CC -!- DOMAIN: Protease-polymerase is composed of two domains displaying two
CC different catalytic activity. These activities may act independently.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. Pro-
CC Pol is first autocatalytically cleaved, then processes the whole
CC polyprotein.
CC -!- PTM: VPg is uridylylated by the polymerase and is covalently attached
CC to the 5'-end of the polyadenylated genomic and subgenomic RNAs. This
CC uridylylated form acts as a nucleotide-peptide primer for the
CC polymerase (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: Two different RNAs lead the expression of the capsid
CC protein. One arises from the cleavage of the polyprotein translated
CC from the genomic RNA and the other from the translation of a subgenomic
CC RNA derived from the (-)RNA template. Capsid protein expressed from the
CC subgenomic mRNA is produced in much larger amounts than the cleaved one
CC (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform Genome polyprotein]: Produced from the genomic
CC RNA.
CC -!- MISCELLANEOUS: [Isoform Subgenomic capsid protein]: Produced from the
CC subgenomic RNA. {ECO:0000305}.
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DR EMBL; AF182760; AAF04560.1; -; Genomic_RNA.
DR RefSeq; NP_051035.1; NC_000940.1.
DR PDB; 2MXD; NMR; -; A=948-1006.
DR PDBsum; 2MXD; -.
DR BMRB; Q9QEJ5; -.
DR SMR; Q9QEJ5; -.
DR MEROPS; C24.003; -.
DR PRIDE; Q9QEJ5; -.
DR GeneID; 1457802; -.
DR KEGG; vg:1457802; -.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR CDD; cd00205; rhv_like; 1.
DR Gene3D; 2.60.120.20; -; 1.
DR Gene3D; 3.30.70.270; -; 2.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR004005; Calicivirus_coat.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000317; Peptidase_C24.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR033703; Rhv-like.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR029053; Viral_coat.
DR Pfam; PF00915; Calici_coat; 1.
DR Pfam; PF03510; Peptidase_C24; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF00910; RNA_helicase; 1.
DR PRINTS; PR00916; 2CENDOPTASE.
DR PRINTS; PR00918; CALICVIRUSNS.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51894; CV_3CL_PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS51218; SF3_HELICASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative promoter usage; ATP-binding; Capsid protein;
KW Covalent protein-RNA linkage; DNA replication; Host cytoplasm; Hydrolase;
KW Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein; Protease;
KW RNA-directed RNA polymerase; Thiol protease; Transferase;
KW Viral RNA replication; Virion.
FT CHAIN 1..2254
FT /note="Genome polyprotein"
FT /id="PRO_0000341637"
FT CHAIN 1..56
FT /note="Protein p11"
FT /id="PRO_0000341638"
FT CHAIN 57..310
FT /note="Protein p28"
FT /id="PRO_0000341639"
FT CHAIN 311..650
FT /note="NTPase"
FT /id="PRO_0000341640"
FT CHAIN 651..934
FT /note="Protein p32"
FT /id="PRO_0000341641"
FT CHAIN 935..1048
FT /note="Viral genome-linked protein"
FT /id="PRO_0000341642"
FT CHAIN 1049..1712
FT /note="Protease-polymerase p70"
FT /id="PRO_0000341643"
FT CHAIN 1713..2254
FT /note="Capsid protein"
FT /id="PRO_0000341644"
FT DOMAIN 438..592
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1041..1196
FT /note="Peptidase C24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT DOMAIN 1434..1559
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 1714..1742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1720..1736
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1078
FT /note="For 3CLpro activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT ACT_SITE 1099
FT /note="For 3CLpro activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT ACT_SITE 1163
FT /note="For 3CLpro activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT BINDING 464..471
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT SITE 56..57
FT /note="Cleavage; by Pro-Pol"
FT /evidence="ECO:0000250"
FT SITE 310..311
FT /note="Cleavage; by Pro-Pol"
FT /evidence="ECO:0000250"
FT SITE 649..650
FT /note="Cleavage; by Pro-Pol"
FT /evidence="ECO:0000250"
FT SITE 934..935
FT /note="Cleavage; by Pro-Pol"
FT /evidence="ECO:0000250"
FT SITE 1047..1048
FT /note="Cleavage; by Pro-Pol"
FT /evidence="ECO:0000250"
FT SITE 1712..1713
FT /note="Cleavage; by Pro-Pol"
FT /evidence="ECO:0000250"
FT MOD_RES 956
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..1710
FT /note="Missing (in isoform Subgenomic capsid protein)"
FT /evidence="ECO:0000305"
FT /id="VSP_034378"
FT HELIX 953..966
FT /evidence="ECO:0007829|PDB:2MXD"
FT HELIX 972..983
FT /evidence="ECO:0007829|PDB:2MXD"
FT HELIX 989..1003
FT /evidence="ECO:0007829|PDB:2MXD"
SQ 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
