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Database: UniProt
Entry: C6ZF19_9ENTO
LinkDB: C6ZF19_9ENTO
Original site: C6ZF19_9ENTO 
ID   C6ZF19_9ENTO            Unreviewed;       449 AA.
AC   C6ZF19;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 76.
DE   RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
DE   Flags: Fragment;
OS   Human rhinovirus sp.
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Picornaviridae; Ensavirinae; Enterovirus.
OX   NCBI_TaxID=169066 {ECO:0000313|EMBL:ACU27123.1};
RN   [1] {ECO:0000313|EMBL:ACU27123.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CL-030103 {ECO:0000313|EMBL:ACU27123.1};
RX   PubMed=19402957; DOI=10.3201/eid1505.081286;
RA   Tapparel C., Junier T., Gerlach D., Van-Belle S., Turin L., Cordey S.,
RA   Muhlemann K., Regamey N., Aubert J.D., Soccal P.M., Eigenmann P.,
RA   Zdobnov E., Kaiser L.;
RT   "New respiratory enterovirus and recombinant rhinoviruses among circulating
RT   picornaviruses.";
RL   Emerg. Infect. Dis. 15:719-726(2009).
CC   -!- SUBUNIT: Interacts with RNA-directed RNA polymerase.
CC       {ECO:0000256|ARBA:ARBA00011124}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Host
CC       cytoplasm {ECO:0000256|ARBA:ARBA00004192}.
CC   -!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
CC       {ECO:0000256|ARBA:ARBA00008303}.
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DR   EMBL; EU840753; ACU27123.1; -; Genomic_RNA.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030430; C:host cell cytoplasm; 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:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; 3.30.70.270; -; 1.
DR   Gene3D; 4.10.880.10; Poliovirus 3D polymerase Domain 1 (Nucleotidyltransferase); 2.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR044067; PCV_3C_PRO.
DR   InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR001205; RNA-dir_pol_C.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   Pfam; PF00548; Peptidase_C3; 1.
DR   Pfam; PF00680; RdRP_1; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS51874; PCV_3C_PRO; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Capsid protein {ECO:0000256|ARBA:ARBA00022706};
KW   Covalent protein-RNA linkage {ECO:0000256|ARBA:ARBA00022520};
KW   Host cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW   Host-virus interaction {ECO:0000256|ARBA:ARBA00022804};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
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   Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
KW   Viral RNA replication {ECO:0000256|ARBA:ARBA00022953};
KW   Virion {ECO:0000256|ARBA:ARBA00022706};
KW   Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}.
FT   DOMAIN          1..121
FT                   /note="Peptidase C3"
FT                   /evidence="ECO:0000259|PROSITE:PS51874"
FT   DOMAIN          353..449
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50507"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACU27123.1"
FT   NON_TER         449
FT                   /evidence="ECO:0000313|EMBL:ACU27123.1"
SQ   SEQUENCE   449 AA;  49959 MW;  A570F4687B05AD1B CRC64;
     SFDLFNKDGV KLEITVLKLK RNEKFKDIRK YIPEHEDDYP DCNLALSANQ PETTIIKVGD
     VVSYGNILLS GNQTARMLKY NYPTKSGYCG GILYKIGQVL GIHVGGNGRD GFAAMLLRSY
     FTEAQGQITT SKSTTECNLP SIHTPSKTKL QPSVFYDVFP GNKEPAVLSD HDPRLKVNFN
     DALFSKYKGN NQCTVNDHIK VAISHYSAQL TTLDIDPNPI TLEESVFGIE GLEALDSNTS
     AGFPYVSMGI KKRDLINKQT KDISKLKMAL DKYGVDLPMV TFLKDELRKK EKISAGKTRV
     IEASSVNDTV LFRTTFGNLF SKFHLNPGIV TGSAVGCDPE TFWSKIPVML DGDCIMAFDY
     TNYDGSIHPI WFQALKQVLS NLSFEASLID RLCNSKHIFK NIYYEVEGGV PSGCSGTSIF
     NTMINNIIIR TLVLDAYKNI DLDKLKIIA
//
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