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Genome polyprotein

 I3W9E1_9ENTO            Unreviewed;      2193 AA.
I3W9E1;
05-SEP-2012, integrated into UniProtKB/TrEMBL.
05-SEP-2012, sequence version 1.
30-AUG-2017, entry version 45.
RecName: Full=Genome polyprotein {ECO:0000256|SAAS:SAAS00711595};
Coxsackievirus A16.
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Picornavirales; Picornaviridae; Enterovirus; Enterovirus A.
NCBI_TaxID=31704 {ECO:0000313|EMBL:AFK93187.1, ECO:0000313|Proteomes:UP000111855};
[1] {ECO:0000313|EMBL:AFK93187.1, ECO:0000313|Proteomes:UP000111855}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Ningbo.CHN/028-2/2009 {ECO:0000313|EMBL:AFK93187.1};
PubMed=22652041; DOI=10.1016/j.jcv.2012.04.021;
Ni H., Yi B., Yin J., Fang T., He T., Du Y., Wang J., Zhang H.,
Xie L., Ding Y., Gu W., Zhang S., Han Y., Dong H., Su T., Xu G.,
Cao G.;
"Epidemiological and etiological characteristics of hand, foot, and
mouth disease in Ningbo, China, 2008-2011.";
J. Clin. Virol. 54:342-348(2012).
[2] {ECO:0000213|PDB:4JGY, ECO:0000213|PDB:4JGZ}
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 566-862; 70-323 AND 324-565,
AND DISULFIDE BONDS.
PubMed=23728514; DOI=10.1038/ncomms2889;
Ren J., Wang X., Hu Z., Gao Q., Sun Y., Li X., Porta C., Walter T.S.,
Gilbert R.J., Zhao Y., Axford D., Williams M., McAuley K.,
Rowlands D.J., Yin W., Wang J., Stuart D.I., Rao Z., Fry E.E.;
"Picornavirus uncoating intermediate captured in atomic detail.";
Nat. Commun. 4:1929-1929(2013).
[3] {ECO:0000213|PDB:5C4W, ECO:0000213|PDB:5C9A}
X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 566-862; 70-323; 324-565 AND
1-69.
PubMed=26269176; DOI=10.1128/JVI.01102-15;
Ren J., Wang X., Zhu L., Hu Z., Gao Q., Yang P., Li X., Wang J.,
Shen X., Fry E.E., Rao Z., Stuart D.I.;
"Structures of Coxsackievirus A16 Capsids with Native Antigenicity:
Implications for Particle Expansion, Receptor Binding, and
Immunogenicity.";
J. Virol. 89:10500-10511(2015).
[4] {ECO:0000213|PDB:5ABJ}
X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 566-862; 70-323; 324-565 AND
1-69.
PubMed=26485389; DOI=10.1371/JOURNAL.PPAT.1005165;
De Colibus L., Wang X., Tijsma A., Neyts J., Spyrou J.A., Ren J.,
Grimes J.M., Puerstinger G., Leyssen P., Fry E.E., Rao Z.,
Stuart D.I.;
"Structure Elucidation of Coxsackievirus A16 in Complex with GPP3
Informs a Systematic Review of Highly Potent Capsid Binders to
Enteroviruses.";
PLoS Pathog. 11:e1005165-e1005165(2015).
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
{ECO:0000256|SAAS:SAAS00817576}.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000256|SAAS:SAAS00383097}.
-!- CATALYTIC ACTIVITY: Selective cleavage of Gln-|-Gly bond in the
poliovirus polyprotein. In other picornavirus reactions Glu may be
substituted for Gln, and Ser or Thr for Gly.
{ECO:0000256|SAAS:SAAS00711755}.
-!- SUBCELLULAR LOCATION: Host cytoplasmic vesicle membrane
{ECO:0000256|SAAS:SAAS00711512}; Peripheral membrane protein
{ECO:0000256|SAAS:SAAS00711512}; Cytoplasmic side
{ECO:0000256|SAAS:SAAS00711512}.
-!- SUBCELLULAR LOCATION: Virion {ECO:0000256|SAAS:SAAS00803776}.
-!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
{ECO:0000256|SAAS:SAAS00782306}.
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EMBL; JQ354992; AFK93187.1; -; Genomic_RNA.
PDB; 4JGY; X-ray; 3.00 A; A=566-862, B=70-323, C=324-565.
PDB; 4JGZ; X-ray; 3.00 A; A=566-862, B=70-323, C=324-565.
PDB; 5ABJ; X-ray; 2.75 A; A=566-862, B=70-323, C=324-565, D=1-69.
PDB; 5C4W; X-ray; 2.65 A; A=566-862, B=70-323, C=324-565, D=1-69.
PDB; 5C9A; X-ray; 2.70 A; A=566-862, B=1-323, C=324-565.
PDBsum; 4JGY; -.
PDBsum; 4JGZ; -.
PDBsum; 5ABJ; -.
PDBsum; 5C4W; -.
PDBsum; 5C9A; -.
SMR; I3W9E1; -.
Proteomes; UP000111855; Genome.
GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0005216; F:ion channel activity; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0051259; P:protein oligomerization; IEA:UniProtKB-KW.
GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:InterPro.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
CDD; cd00205; rhv_like; 3.
Gene3D; 4.10.80.10; -; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR014838; P3A.
InterPro; IPR000081; Peptidase_C3.
InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR003138; Pico_P1A.
InterPro; IPR002527; Pico_P2B.
InterPro; IPR001676; Picornavirus_capsid.
InterPro; IPR033703; Rhv-like.
InterPro; IPR001205; RNA-dir_pol_C.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
Pfam; PF08727; P3A; 1.
Pfam; PF00548; Peptidase_C3; 1.
Pfam; PF02226; Pico_P1A; 1.
Pfam; PF00947; Pico_P2A; 1.
Pfam; PF01552; Pico_P2B; 1.
Pfam; PF00680; RdRP_1; 1.
Pfam; PF00073; Rhv; 3.
Pfam; PF00910; RNA_helicase; 1.
ProDom; PD001306; Peptidase_C3; 1.
ProDom; PD649346; Pico_P2B; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF50494; SSF50494; 2.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF89043; SSF89043; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS51218; SF3_HELICASE_2; 1.
1: Evidence at protein level;
3D-structure {ECO:0000213|PDB:4JGY, ECO:0000213|PDB:4JGZ,
ECO:0000213|PDB:5ABJ, ECO:0000213|PDB:5C4W};
ATP-binding {ECO:0000256|SAAS:SAAS00124676};
Capsid protein {ECO:0000256|SAAS:SAAS00803779};
Complete proteome {ECO:0000313|Proteomes:UP000111855};
Helicase {ECO:0000256|SAAS:SAAS00124676};
Host cytoplasm {ECO:0000256|SAAS:SAAS00711571};
Host cytoplasmic vesicle {ECO:0000256|SAAS:SAAS00711589};
Host membrane {ECO:0000256|SAAS:SAAS00795395};
Host-virus interaction {ECO:0000256|SAAS:SAAS00711583};
Hydrolase {ECO:0000256|SAAS:SAAS00124676,
ECO:0000256|SAAS:SAAS00482329};
Ion channel {ECO:0000256|SAAS:SAAS00711569};
Ion transport {ECO:0000256|SAAS:SAAS00711569};
Membrane {ECO:0000256|SAAS:SAAS00795395};
Nucleotide-binding {ECO:0000256|SAAS:SAAS00124676};
Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00510600};
Protease {ECO:0000256|SAAS:SAAS00482329};
RNA-binding {ECO:0000256|SAAS:SAAS00711776};
RNA-directed RNA polymerase {ECO:0000256|SAAS:SAAS00510600};
Thiol protease {ECO:0000256|SAAS:SAAS00482329};
Transferase {ECO:0000256|SAAS:SAAS00510600};
Transport {ECO:0000256|SAAS:SAAS00711569};
Viral attachment to host cell {ECO:0000256|SAAS:SAAS00711583};
Viral ion channel {ECO:0000256|SAAS:SAAS00711569};
Viral RNA replication {ECO:0000256|SAAS:SAAS00664279};
Virion {ECO:0000256|SAAS:SAAS00711583, ECO:0000256|SAAS:SAAS00803779};
Virus entry into host cell {ECO:0000256|SAAS:SAAS00711583}.
DOMAIN 1216 1374 SF3 helicase.
{ECO:0000259|PROSITE:PS51218}.
DOMAIN 1958 2074 RdRp catalytic.
{ECO:0000259|PROSITE:PS50507}.
DISULFID 76 259 {ECO:0000213|PDB:4JGY,
ECO:0000213|PDB:4JGZ}.
SEQUENCE 2193 AA; 243240 MW; C0706DA9F91946C5 CRC64;
MGSQVSTQRS GSHENSNSAS EGSTINYTTI NYYKDAYAAS AGRQDMSQDP KKFTDPVMDV
IHEMAPPLKS PSAEACGYSD RVAQLTIGNS TITTQEAANI VIAYGEWPEY CPDTDATAVD
KPTRPDVSVN RFFTLDTKSW AKDSKGWYWK FPDVLTEVGV FGQNAQFHYL YRSGFCVHVQ
CNASKFHQGA LLVAVLPEYV LGTIAGGTGN ENSHPPYATT QPGQVGAVLT HPYVLDAGIP
LSQLTVCPHQ WINLRTNNCA TIIVPYMNTV PFDSALNHCN FGLLVIPVVP LDFNTGATSE
IPITVTIAPM CAEFAGLRQA VKQGIPTELK PGTNQFLTTD DGVSAPILPG FHPTPPIHIP
GEVHNLLEIC RVETILEVNN LKTNETTPMQ RLCFPVSVQS KTGELCAAFR ADPGRDGPWQ
STILGQLCRY YTQWSGSLEV TFMFAGSFMA TGKMLIAYTP PGGNVPADRI TAMLGTHVIW
DFGLQSSVTL VVPWISNTHY RAHARAGYFD YYTTGIITIW YQTNYVVPIG APTTAYIVAL
AAAQDNFTMK LCKDTEDIEQ TANIQGDPIA DMIDQTVNNQ VNRSLTALQV LPTAANTEAS
SHRLGTGVVP ALQAAETGAS SNASDKNLIE TRCVLNHHST QETAIGNFFS RAGLVSIITM
PTTGTQNTDG YVNWDIDLMG YAQLRRKCEL FTYMRFDAEF TFVVAKPNGE LVPQLLQYMY
VPPGAPKPTS RDSFAWQTAT NPSVFVKMTD PPAQVSVPFM SPASAYQWFY DGYPTFGEHL
QANDLDYGQC PNNMMGTFSI RTVGIEKSPH SITLRVYMRI KHVRAWIPRP LRNQPYLFKT
NPNYKGNDIK CTSTSRDKIT TLGEFGQQSG AIYVGNYRVV NRHLATHNDW ANLVWEDSSR
DLLVSSTTAQ GCDTIARCNC QTGIYYCSSK RKHYPVSFTK PSLIFVEASE YYPARYQSHL
MLAVGHSEPG DCGGILRCQH GVVGIVSTGG NGLVGFADVR DLLWLDEEAM EQGVSDYIKG
LGDAFGMGFT DAVSREVEAL KNHLIGSEGA VEKILKNLVK LISALVIVVR SDYDMVTLTA
TLALIGCHGS PWAWIKVKTA SILGIPIVQK QSASWLKKFN DMANAAKGLE WISSKISKFI
DWLKEKIIPA AKEKVEFLNN LKQLPLLENQ ISNLEQSAAS QEDLEAMFGN VSYLAHFCRK
FQPLYATEAK RVYALEKRMN NYMQFKSKHR IEPVCLIIRG SPGTGKSLAT GIIARAIADK
YHSSVYSLPP DPDHFDGYKQ QVVTVMDDLC QNPDGKDMSL FCQMVSTVDF IPPMASLEEK
GVSFTSKFVV ASTNASNIVV PTVSDSDAIR RRFYMDCDIE VTDSYKTDLG RLDAGRAAKL
CTENNTANFK RCSPLVCGKA IQLRDRKSKV RYSIDTVVSE LIREYNNRSA IGNTIEALFQ
GPPKFKPIRI SLEEKPAPDA ISDLLASVDS EEVRQYCREQ GWIIPETPAN VERHLNRAVL
VVQSIATVVA VVSLVYVIYK LFAGFQGAYS GAPKQALKKP VLRTATVQGP SLDFALSLLR
RNIRQVQTDQ GHFTMLGVRD RLAVLPRHSQ PGKTIWVEHK LINVLDAVEL VDEQGVNLEL
TLITLDTNEK FRDVTKFIPE TITGASDATL IINTEHMPSM FVPVGDVVQY GFLNLSGKPT
HRTMMYNFPT KAGQCGGVVT SVGKIIGIHI GGNGRQGFCA GLKRSYFASE QGEIQWMKPN
KETGRLNING PTRTKLEPSI FHDVFEGNKE PAVLTSKDPR LEVDFEQALF SKYVGNTLHE
PDEYVTQAAL HYANQLKQLD INTNKMSMEE ACYGTEYLEA IDLHTSAGYP YSALGVKKRD
ILDPITRDTT KMKFYMDKYG LDLPYSTYVK DELRSLDKIK KGKSRLIEAS SLNDSVYLRM
TFGHLYETFH ANPGTVTGSA VGCNPDVFWS KLPILLPGSL FAFDYSGYDA SLSPVWFRAL
EVVLREIGYS EEAVSLIEGI NHTHHVYRNK TYCVLGGMPS GCSGTSIFNS MINNIIIRTL
LIKTFKGIDL DELNMVAYGD DVLASYPFPV DCSELAKTGK EYGLTMTPAD KSPCFNEVTW
ENATFLKRGF LPDHQFPFLI HPTMPMREIH ESIRWTKDAR NTQDHVRSLC LLAWHNGKEE
YEKFVSTIRS VPVGKALAIP NFENLRRNWL ELF


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