ID S6DZ53_ECHO9 Unreviewed; 1383 AA.
AC S6DZ53;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
DE Flags: Fragment;
OS Echo 9 virus (EV-9) (Coxsackievirus A23).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Ensavirinae; Enterovirus; Enterovirus B.
OX NCBI_TaxID=12060 {ECO:0000313|EMBL:CCW33473.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:CCW33473.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=E9_CF155022_FRA07 {ECO:0000313|EMBL:CCW33473.1};
RX PubMed=24006446; DOI=10.1128/JVI.02075-13;
RA Henquell C., Mirand A., Richter J., Schuffenecker I., Bottiger B.,
RA Diedrich S., Terletskaia-Ladwig E., Christodoulou C., Peigue-Lafeuille H.,
RA Bailly J.L.;
RT "Phylogenetic Patterns of Human Coxsackievirus B5 Arise from Population
RT Dynamics between Two Genogroups and Reveal Evolutionary Factors of
RT Molecular Adaptation and Transmission.";
RL J. Virol. 87:12249-12259(2013).
RN [2] {ECO:0000313|EMBL:CCW33473.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=E9_CF155022_FRA07 {ECO:0000313|EMBL:CCW33473.1};
RA Bailly J.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a primer for viral RNA replication and remains
CC covalently bound to viral genomic RNA. VPg is uridylylated prior to
CC priming replication into VPg-pUpU (By similarity). The oriI viral
CC genomic sequence may act as a template for this. The VPg-pUpU is then
CC used as primer on the genomic RNA poly(A) by the RNA-dependent RNA
CC polymerase to replicate the viral genome (By similarity). Following
CC genome release from the infecting virion in the cytoplasm, the VPg-RNA
CC linkage is probably removed by host TDP2 (By similarity). During the
CC late stage of the replication cycle, host TDP2 is excluded from sites
CC of viral RNA synthesis and encapsidation, allowing for the generation
CC of progeny virions. {ECO:0000256|ARBA:ARBA00024846}.
CC -!- FUNCTION: Component of immature procapsids, which is cleaved into
CC capsid proteins VP4 and VP2 after maturation (By similarity). Allows
CC the capsid to remain inactive before the maturation step.
CC {ECO:0000256|ARBA:ARBA00025202}.
CC -!- FUNCTION: Induces and associates with structural rearrangements of
CC intracellular membranes. Displays RNA-binding, nucleotide binding and
CC NTPase activities. May play a role in virion morphogenesis and viral
CC RNA encapsidation by interacting with the capsid protein VP3.
CC {ECO:0000256|ARBA:ARBA00002372}.
CC -!- FUNCTION: Localizes the viral replication complex to the surface of
CC membranous vesicles. Together with protein 3CD binds the Cis-Active RNA
CC Element (CRE) which is involved in RNA synthesis initiation. Acts as a
CC cofactor to stimulate the activity of 3D polymerase, maybe through a
CC nucleid acid chaperone activity. {ECO:0000256|ARBA:ARBA00002750}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Selective cleavage of Tyr-|-Gly bond in the picornavirus
CC polyprotein.; EC=3.4.22.29; Evidence={ECO:0000256|ARBA:ARBA00024513};
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 Evidence={ECO:0000256|ARBA:ARBA00001491};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBUNIT: Interacts with RNA-directed RNA polymerase.
CC {ECO:0000256|ARBA:ARBA00011124}.
CC -!- SUBUNIT: Interacts with capsid protein VP1 and capsid protein VP3.
CC {ECO:0000256|ARBA:ARBA00011519}.
CC -!- SUBUNIT: Interacts with protein 3CD. {ECO:0000256|ARBA:ARBA00011647}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000256|ARBA:ARBA00004180}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004180}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004180}. Host cytoplasmic vesicle membrane
CC {ECO:0000256|ARBA:ARBA00004295}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004295}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004295}. Host nucleus
CC {ECO:0000256|ARBA:ARBA00004147}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}. Virion
CC {ECO:0000256|ARBA:ARBA00004328}.
CC -!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
CC {ECO:0000256|ARBA:ARBA00008303}.
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DR EMBL; HF948098; CCW33473.1; -; Genomic_RNA.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0039618; C:T=pseudo3 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005216; F:monoatomic ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR GO; GO:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039503; P:suppression by virus of host innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0039522; P:suppression by virus of host mRNA export from nucleus; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR GO; GO:0039707; P:virus-mediated pore formation in host cell membrane; IEA:UniProtKB-KW.
DR CDD; cd00205; rhv_like; 1.
DR Gene3D; 2.60.120.20; -; 1.
DR Gene3D; 6.10.20.20; Poliovirus 3A protein-like; 1.
DR Gene3D; 4.10.880.10; Poliovirus 3D polymerase Domain 1 (Nucleotidyltransferase); 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 4.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014838; P3A.
DR InterPro; IPR036203; P3A_soluble_dom.
DR InterPro; IPR044067; PCV_3C_PRO.
DR InterPro; IPR000081; Peptidase_C3.
DR InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR002527; Pico_P2B.
DR InterPro; IPR001676; Picornavirus_capsid.
DR InterPro; IPR033703; Rhv-like.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR029053; Viral_coat.
DR Pfam; PF08727; P3A; 1.
DR Pfam; PF00548; Peptidase_C3; 1.
DR Pfam; PF00947; Pico_P2A; 1.
DR Pfam; PF01552; Pico_P2B; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF00073; Rhv; 1.
DR Pfam; PF00910; RNA_helicase; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF88633; Positive stranded ssRNA viruses; 1.
DR SUPFAM; SSF89043; Soluble domain of poliovirus core protein 3a; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 2.
DR PROSITE; PS51874; PCV_3C_PRO; 1.
DR PROSITE; PS51218; SF3_HELICASE_2; 1.
PE 3: Inferred from homology;
KW Activation of host autophagy by virus {ECO:0000256|ARBA:ARBA00023050};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Capsid protein {ECO:0000256|ARBA:ARBA00022561};
KW Covalent protein-RNA linkage {ECO:0000256|ARBA:ARBA00022520};
KW Eukaryotic host gene expression shutoff by virus
KW {ECO:0000256|ARBA:ARBA00023197}; Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW Host cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00022488};
KW Host gene expression shutoff by virus {ECO:0000256|ARBA:ARBA00023197};
KW Host mRNA suppression by virus {ECO:0000256|ARBA:ARBA00022557};
KW Host nucleus {ECO:0000256|ARBA:ARBA00022562};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Inhibition of host innate immune response by virus
KW {ECO:0000256|ARBA:ARBA00022632};
KW Inhibition of host mRNA nuclear export by virus
KW {ECO:0000256|ARBA:ARBA00023197};
KW Inhibition of host RLR pathway by virus {ECO:0000256|ARBA:ARBA00022482};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484};
KW T=pseudo3 icosahedral capsid protein {ECO:0000256|ARBA:ARBA00022706};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transport {ECO:0000256|ARBA:ARBA00022448};
KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
KW Viral immunoevasion {ECO:0000256|ARBA:ARBA00023280};
KW Viral ion channel {ECO:0000256|ARBA:ARBA00023039};
KW Viral penetration into host cytoplasm {ECO:0000256|ARBA:ARBA00022890};
KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953};
KW Virion {ECO:0000256|ARBA:ARBA00022706};
KW Virus endocytosis by host {ECO:0000256|ARBA:ARBA00022890};
KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 654..810
FT /note="SF3 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51218"
FT DOMAIN 990..1168
FT /note="Peptidase C3"
FT /evidence="ECO:0000259|PROSITE:PS51874"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CCW33473.1"
FT NON_TER 1383
FT /evidence="ECO:0000313|EMBL:CCW33473.1"
SQ SEQUENCE 1383 AA; 154581 MW; D21DE0D039D23736 CRC64;
NDVRQAVEGA IGRVADTIRS GPSNSEAVPA LTAAETGHTS QVVPSDTMQT RHVKNYHSRS
ESTIENFLCR AACVRMAKYE ARGNPESTDR FDAWEISIRD MVQLRRKCEM FTYLRFDVEV
TFVITSYQHQ GTINQDMPPM THQIMYVPPG GPIPKKVDGY EWQTSTNPSI FWTEGNAPPR
MSIPFISIGN AYSSFYDGWS HFDSKGAYGF NTLNKMGHIY CRHVNKETPT KVTSYIRIYF
KPKHVRAWVP RPPRLCQYKN KANVNFDATA VTETRDTINT VPVSNHGGDR RGDLAALNTH
GKFGQQSGAV YVGNYRLVNR HLATHTDWQN CVWEDYNRDL LVSTTTAQGC DIIARCQCTT
GVYFCASRNK HYPVSFEGPG LVEVQESEYY PKRYQSHVLL AVGFSEPGDC GGILRCEHGV
IGLVTMGGEG VVGFADVRDL LWLEDDAMEQ GVRNYVEQLG NAFGSGFTNP ICEQVSLLKE
SLVGQDSILE KSLKALVKII SALVIVVRNH DDLMTVTATL ALVGCTSSPW RWLKQKVAQY
YGIPMAERQN NGWLKKFTEM TNACKGMEWI AIKIQKFIEW LKVKILPEVK EKHEFLTRLK
QLPLLESQIA TIEQSAPSQS DQEQLFSNVH YFAHYCRKYA PLYATEAKRV FSLEKKMSNY
IQFKSKCRVE PVCLLLHGSP GAGKSVATNL IGRALAEKLN SSVYSLPPDP DHFDGYKQQA
VVIMDDLCQN PDGKDVSLFC QMVSSVDFVP PMAALEEKGI LFTSPFVLAS TNAGSINAPT
VSDSRALARR FHFDMNIEVI SMYSQNGKIN MPMSVKTCDE ECCPVNFKKC CPLVCGKAIQ
FIDRRTQVRY SLDMLVTEMF REYNHRHSVG ATLEALFQGP PVYREIKISV APEVPPPPAI
ADLLKSVDSE AVREYCKEKG WLVPEVNSTL QIEKHVSRAF ICLQALTTFV SVAGIIYIIY
KLFAGFQGAY TGMPNQKPKV PTLRQAKVQG PAFEFAVAMM KRNASTVKTE YGEFTMLGIH
DRWAVLPRHA KPGPTILMND QEVGVMDAKE LVDKDGTNLE LTLLKLNRNE KFRDIRGFLA
REEVEVNEAV LAINTSKFPN MYIPVGQVTD YGFLNLGGTP TKRMLMYNFP TRAGQCGGVL
MSTGKVLGIH VGGNGHQGFS AALLRHYFNE EQGEIEFIEN SKDAGYPVIN TPSKTKLEPS
VFYQVFEGDK EPAVLRNGDP RLKADFEEAI FSKYIGNVNT HVDEYMQEAV DHYAGQLATL
DISTEPMKLE DAVYGTEGLE ALDLTTSAGY PYVALGIKKR DILSKKTKDL TKLKECMDKY
GLNLPMVTYV KDELRSAEKV AKGKSRLIEA SSLNDSVAMR QTFGNLYKSF HLNPGIVTGS
AVG
//
