ID C6EN30_9ENTO Unreviewed; 2208 AA. AC C6EN30; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 11-JUN-2014, entry version 36. DE SubName: Full=Polyprotein; OS Coxsackievirus A20. OC Viruses; ssRNA positive-strand viruses, no DNA stage; Picornavirales; OC Picornaviridae; Enterovirus; Enterovirus C. OX NCBI_TaxID=42782; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BAN00-10538; RX PubMed=19264596; DOI=10.1099/vir.0.008540-0; RA Brown B.A., Maher K., Flemister M.R., Naraghi-Arani P., Uddin M., RA Oberste M.S., Pallansch M.A.; RT "Resolving ambiguities in genetic typing of human enterovirus species RT C clinical isolates and identification of enterovirus 96, 99 and RT 102."; RL J. Gen. Virol. 90:1713-1723(2009). CC -!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). CC -!- CATALYTIC ACTIVITY: Selective cleavage of Gln-|-Gly bond in the CC poliovirus polyprotein. In other picornavirus reactions Glu may be CC substituted for Gln, and Ser or Thr for Gly. CC -!- SUBCELLULAR LOCATION: Host cytoplasm (By similarity). CC -!- SUBCELLULAR LOCATION: Host cytoplasmic vesicle membrane; CC Peripheral membrane protein; Cytoplasmic side (By similarity). CC -!- SIMILARITY: Contains RdRp catalytic domain. CC -!- SIMILARITY: Contains SF3 helicase domain. CC -!- SIMILARITY: Contains SFhelicase domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; EF015018; ABM54527.1; -; Genomic_RNA. DR ProteinModelPortal; C6EN30; -. DR MEROPS; C03.020; -. DR GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. 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:0005216; F: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-directed RNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW. DR GO; GO:0051259; P:protein oligomerization; IEA:UniProtKB-KW. DR GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro. DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW. DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro. DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW. DR Gene3D; 2.60.120.20; -; 3. DR Gene3D; 4.10.80.10; -; 2. DR InterPro; IPR003593; AAA+_ATPase. 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; IPR000081; Peptidase_C3. DR InterPro; IPR000199; Peptidase_C3A/C3B_picornavir. DR InterPro; IPR003138; Pico_P1A. DR InterPro; IPR002527; Pico_P2B. DR InterPro; IPR001676; Picornavirus_capsid. DR InterPro; IPR001205; RNA-dir_pol_C. DR InterPro; IPR007094; RNA-dir_pol_PSvirus. DR InterPro; IPR009003; Trypsin-like_Pept_dom. DR InterPro; IPR029053; viral_coat. DR Pfam; PF08727; P3A; 1. DR Pfam; PF00548; Peptidase_C3; 1. DR Pfam; PF02226; Pico_P1A; 1. DR Pfam; PF00947; Pico_P2A; 1. DR Pfam; PF01552; Pico_P2B; 1. DR Pfam; PF00680; RdRP_1; 1. DR Pfam; PF00073; Rhv; 3. DR Pfam; PF00910; RNA_helicase; 1. DR ProDom; PD001306; Peptidase_C3; 1. DR ProDom; PD649346; Pico_P2B; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF50494; SSF50494; 2. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF89043; SSF89043; 1. DR PROSITE; PS50507; RDRP_SSRNA_POS; 1. DR PROSITE; PS51218; SF3_HELICASE_2; 1. PE 3: Inferred from homology; KW ATP-binding; Capsid protein; Helicase; Host cytoplasm; KW Host cytoplasmic vesicle; Host membrane; Host-virus interaction; KW Hydrolase; Ion channel; Ion transport; Membrane; Nucleotide-binding; KW Nucleotidyltransferase; Phosphoprotein; Protease; RNA-binding; KW RNA-directed RNA polymerase; Thiol protease; Transferase; Transport; KW Viral attachment to host cell; Viral ion channel; KW Viral RNA replication; Virion; Virus entry into host cell. FT CHAIN 1 69 vp4. FT /FTId=PRO_5000488593. FT CHAIN 70 338 vp2. FT /FTId=PRO_5000488594. FT CHAIN 339 576 vp3. FT /FTId=PRO_5000488595. FT CHAIN 577 880 vp1. FT /FTId=PRO_5000488596. FT CHAIN 881 1029 2a. FT /FTId=PRO_5000488597. FT CHAIN 1030 1126 2b. FT /FTId=PRO_5000488598. FT CHAIN 1127 1455 2c. FT /FTId=PRO_5000488599. FT CHAIN 1456 1542 3a. FT /FTId=PRO_5000488600. FT CHAIN 1543 1564 3b. FT /FTId=PRO_5000488601. FT CHAIN 1565 1747 3c. FT /FTId=PRO_5000488602. FT CHAIN 1748 2208 3d. FT /FTId=PRO_5000488603. SQ SEQUENCE 2208 AA; 245950 MW; 01BBCC27F10EC582 CRC64; MGAQVSSQKV GAHENTNVAT GGSTVNYTTI NYYKDSASNA ASKQDFSQDP SKFTEPVKDI MLKSAPALNS PNVEACGYSD RVLQLTLGNS TITTQEAANS VVGYGQWPTY LNAKDANPVD QPTEPDVSAC RFYTLQSVEW KTESKGWWWK LPDALKDMGL FGQNMYYHYL GRSGYTVHVQ CNASKFHQGA LGVFAVPEYC LAGDSDVKNS YTTYKNANPG EAGGVFVDSF TATTQATRKF CPIDYLFGCG VLTGNAFVFP HQIINLRTNN SATLVLPYVN SLAIDCMAKH NNWGLAIIPL SKLQFPDTSS TEIPITVTIA PMCCEFNGLR NITIPSTQGL PVMNTPGSNQ YLTSDNFQSP CALPEFDVTQ AINIPGEVKN IMEIAEIDTM IPLNLSADRK NSMDMYRVPV STSANLNDPI LCLSLSPASD ERLSYTMLGE ILNYYTHWAG SIKYTFLFCG SMMATGKLLV AYAPPGAKPP RSRKEAMLGT HVIWDVGLQS SCTMVVPWIS NTAYRRTVKD DFTEGGYISM FYQTKIVVPA STPTNMDVLG FVSACNDFSV RLLRDTTHIS QKAMPQGIEE LISEVASNAL KLSQPKPNTQ QSLPNTSSSE PTHSQEVPAL TAVETGATSS VVPADLVQTR HVIQTRSRSE STVESFFARG ACVTIMSVEN YNEAASISNS KLFAKWNITY TDTVQLRRKL EMFTYSRFDI EFTFVVTERY YTANSGHALN QVYQIMYVPP GAPVPQKWDD YTWQTSSNPS VFYTYGTAPA RISIPYVGIA NAYSHFYDGF AKVPIEGETT DPGDAYYGAT SINDFGILAV RVVNEHNPVQ VSSKIRVYMK PKHVRVWCPR PPRAVPYFGP GVDYKGDSLT PLSQKNLTTY GFGHQNKAVY TAGYKICNYH LATQEDLQNA VSIMWNRDLI VVESKAQGTD SIARCNCNTG VYYCESRRKY YPVSFVGPTF QYMEANDYYP ARYQSHMLIG HGFASPGDCG GILRCQHGVI GIVTAGGEGL VAFSDIRDLY AYEEEAMEQG ISNYIESLGA AFGSGFTQQI GDKISELTNM VTSTITEKLL KNLIKIISSL VIITRNYEDT TTVLATLALL GCDISPWQWL KKKACDILEI PYVTRQGDSW LKKFTEACNA AKGLEWVSNK ISKFIDWLKD KIIPQARDKL EFVTKLKQLE MLENQISTIH QSCPSQEHQE ILFNNVRWLS IQSKRFAPLY AVEAKRIQKL EHTINNYIQF KSKHRIEPVC LLVHGSPGTG KSVATNLIAR AIAEKENTST YSLPPDPSHF DGYKQQGVVI MDDLNQNPDG ADMKLFCQMV STVEFIPPMA SLEEKGILFT SNYVLASTNS SRITPPTVAH SDALARRFAF DMDIQVMGEY SRDGKLNMAM ATEMCKNCHQ PANFKRCCPL VCGKAIQLMD KSSRVRYSID QMTTMIINER NRRSNIGNCM EALFQGPLQY KDLKIDIKTT PPPECINDLL QAVDSQEVRD YCEKKGWLVN ISSQVQLERN INRAMTILQA VTTFAAVAGV VYVMYKLFAG HQGAYTGLPN KKPNIPTIRT AKVQGPGFDY AVAMAKRNIV TATTSKGEFT MLGVHDNVAV LPTHSSPGET IVIDGKDVEV LDARALEDQA GTNLEITIVT LKRNEKFRDI RPHIPTQITE TNDGVLIVNT SKYPNMYVPV GAVTEQGYLN LGGRQTARTL MYNFPTRAGQ CGGIITCTGK VIGMHVGGNG SHGFAAALKR SYFTQSQGEI QWMRPSKEVG YPVINAPSKT KLEPSAFHYI FEGVKEPAVL TKNDPRLKTD FEEAIFSKYV GNKITEVDEY MREAVDHYAG QLMSLDINTE QMCLEDAMYG TDGLEALDLT TSAGYPYVAL GKKKRDILNK QTRDTKEMQR LLDTYGINLP LVTYVKDELR SKSKVEQGKS RLIEASSLND SVAMRMAFGN LYAAFHKNPG VITGSAVGCD PDLFWSKIPV LMEERLFAFD YTGYDASLSP AWFEALKMVL EKIGFGDRVD YIDYLNHSHH LYKNKTYCVK GGMPSGCSGT SIFNSMINNL IIRTLLLKTY KGIDLDHLKM IAYGDDVIAS YPHEVDASLL AQSGKDYGLT MTPADKSATF EKVTWENVTF LKRFFRADEK YPFLVHPVMP MKEIHESIRW TKDPRNTQDH VRSLCLLAWH NGEEEYNKFL AKIRSVPIGR ALLLPEYSTL YRRWLDSF //