ID S6DER3_9ENTO Unreviewed; 1366 AA.
AC S6DER3;
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 Coxsackievirus B5.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Ensavirinae; Enterovirus; Enterovirus B.
OX NCBI_TaxID=12074 {ECO:0000313|EMBL:CCW33424.1};
RN [1] {ECO:0000313|EMBL:CCW33424.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ANG700_FRA_03 {ECO:0000313|EMBL:CCW33424.1};
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:CCW33424.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ANG700_FRA_03 {ECO:0000313|EMBL:CCW33424.1};
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; HF948049; CCW33424.1; -; 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 637..793
FT /note="SF3 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51218"
FT DOMAIN 973..1151
FT /note="Peptidase C3"
FT /evidence="ECO:0000259|PROSITE:PS51874"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CCW33424.1"
FT NON_TER 1366
FT /evidence="ECO:0000313|EMBL:CCW33424.1"
SQ SEQUENCE 1366 AA; 152416 MW; 5108478253C58CD9 CRC64;
GPPGEAVERA IARVADTIGS GPVNSESIPA LTAAETGHTS QVVPADTMQT RHVKNYHSRS
ESTVENFLCR SACVFYTTYK NHGTDGDNFA YWVISTRQAA QLRRKLEMFT YARFDLELTF
VITSTQEQST IRGQDSPVLT HQIMYVPPGG PVPTKVNSYS WQTSTNPSVF WTEGSAPPRM
SIPFISIGNA YSMFYDGWAR FDKQGTYGIN TLNNMGTLYM RHVNDGSPGP IVSTVRIYFK
PKHVKTWVPR PPRLCQYQKA GNVNFEPTGV TKSRTDITTM QTTGVFGQQS GAVYVGNYRV
VNRHLATHTD WKNCVWEDYN RDLLVSTTTV HGCDTIARCH CNMGVYFCAS RNKHYPVVFE
GPGLVEVQES EYYPKRYQSH VLLATGFSEP GDCGGILRCE HGVIGLVTMG GEGIVGFADV
RDLLWLEDDV MEQGVRDYVE QLGNAFGSGF TNQICEQVNI LKESLVGQDS ILEKSLKALV
KIISALVIVV RNHDDLITVT ATLALIGCTS SPWRWLKQKV SQYYEIPMAE RQNNGWLKKF
TEMTNACKGM EWIAIKIQKF IEWLKVKILP EVKEKHEFLN RLKQLPLLES QIATIEQSAP
SQSDQEQLFS NVQYFAHYCR KYAPLYAAEA KRVFSLEKKM SNYIQFKSKC RIEPVCLLLH
GSPGAGKSVA TNLIGRSLAE KLNSSVYSLP PDPDHFDGYK QQAVVIMDDL CQNPDGKDVS
LFCQMVSSVD FVPPMAALEE KGILFTSPFV LASTNAGSIN APTVSDSRAL ARRFHFDMNI
EVISMYSQNG KVNMPMSVKT CDEECCPVNF KRCCPLVCGK AIQFIDRRTQ VRYSLDMLVT
EMFREYNHRH SVGATLEALF QGPPVYREIK ISVAPETPPP PAIADLLKSV DSEAVREYCK
ERGWLVPEIN STLQIEKHVS RAFICLQALT TFVSVAGIIY IIYKLFAGFQ GAYTGMPSQK
PKMPTLRQAK VQGPAFEFAV AMMKRNASTV KTEYGEFTML GIYDKWAVLP RHAKPGPTIL
MNDQEVGVLD AKELVDKDGT NLELTLLKLN RNEKFRDIRG FLAREEVEVS EAVLAINTSK
FPNMYIPVGQ VTDYGFLNLG GTPTKRMLMY NFPTRAGQCG GVLMSTGKVL GIHVGGNGHQ
GFSAALLRHY FNEEQGEIEF IESSKDAGYP VINAPSKTKL EPSVFHQVFE GNKEPAVLRN
GDPRLKTNFE EAIFSKYIGN INTHVDEYMQ EAVDHYAGQL ATLDISTEPM KLEDAVYGTE
GLEALDLTTS AGYPYVALGI KKRDILSKKT KDLTKLKECM DKYGLNLPMV TYVKDELRSA
EKVAKGKSRL IEASSLNDSV AMRQTFGNLY KTFHLNPGIV TGSAVG
//
