ID Q5XUU1_POL1S Unreviewed; 1063 AA.
AC Q5XUU1;
DT 23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 126.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
DE Flags: Fragment;
OS Poliovirus type 1 (strain Sabin).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Ensavirinae; Enterovirus; Enterovirus C.
OX NCBI_TaxID=12082 {ECO:0000313|EMBL:AAU85843.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:AAU85843.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Sabin {ECO:0000313|EMBL:AAU85843.1};
RX PubMed=16604453; DOI=10.1007/s11262-005-6877-1;
RA Paximadi E., Karakasiliotis I., Mamuris Z., Stathopoulos C., Krikelis V.,
RA Markoulatos P.;
RT "Genomic analysis of recombinant sabin clinical isolates.";
RL Virus Genes 32:203-210(2006).
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 -!- 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; AY736181; AAU85843.1; -; 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:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
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: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 CDD; cd23213; Enterovirus_RdRp; 1.
DR Gene3D; 1.20.960.20; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 6.10.20.20; Poliovirus 3A protein-like; 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; 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; 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; PF08727; P3A; 1.
DR Pfam; PF00548; Peptidase_C3; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF00910; RNA_helicase; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF89043; Soluble domain of poliovirus core protein 3a; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51874; PCV_3C_PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS51218; SF3_HELICASE_2; 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 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 RNA replication {ECO:0000256|ARBA:ARBA00022953};
KW Virion {ECO:0000256|ARBA:ARBA00022706}.
FT DOMAIN 86..242
FT /note="SF3 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51218"
FT DOMAIN 420..598
FT /note="Peptidase C3"
FT /evidence="ECO:0000259|PROSITE:PS51874"
FT DOMAIN 829..944
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAU85843.1"
SQ SEQUENCE 1063 AA; 119572 MW; 460364351F055468 CRC64;
WVSNKISKFI DWLRERIIPQ ARDKLEFVTK LKQLEMLENQ ISTIHQSCPS QEHQEILFNN
VRWLSIQSKR FAPLYALEAK RIQKLEHTIN NYIQFKSKHR IEPVCLLVHG SPGTGKSVAT
NLIARAIAEK ENTSTYSLPP DPSHFDGYKQ QGVVIMDDLN QNPDGADMKL FCQMVSTVEF
IPPMASLEEK GILFTSNYVL ASTNSSRITP PTVAHSDALA RRFAFDMDIQ VMGEYSRDGK
LNMAMATEMC KNCHQPANFK RCCPLVCGKA IQLMDKSSRV RYSIDQITTM IINERNRRSN
IGNCMEALFQ GPLQYKDLKI DIKTSPPPEC INDLLQAVDS QEVRDYCEKK GWIVNITSQV
QTERNINRAM TILQAVTTFA AVAGVVYVMY KLFAGHQGAY TGLPNKKPNV PTIRTAKVQG
PGFDYAVAMA KRNIVTATTS KGEFTMLGVH DNVAILPTHA SPGESIVIDG KEVEILDAKA
LEDQAGTNLE ITIITLKRNE KFRDIRPHIP TQITETNDGV LIVNTSKYPN MYVPVGAVTE
QGYLNLGGRQ TARTLMYNFP TRAGQCGGVI TCTGKVIGMH VGGNGSHGFA AALKRSYFTQ
SQGEIQWMRP SKEVGYPIIN APSKTKLEPS AFHYVFEGVK EPAVLTKNDP RLKTNFEEAI
FSKYVGNKIT EVDEHMKEAV DHYAGQLMSL DINTEQMCLE DAMYGTDGLE ALDLSTSAGY
PYVAMGKKKR DILNKQTRDT KEMQKLLDTY GINLPLVTYV KDELKSKTKV EQGKSRLIEA
SSLNDSVAMR MAFGNLYAAF HKNPGVITGS AVGCDPDLFW SKIPVLMEEK LFAFDYTGYD
ASLSPAWFEA LKMVLEKIGF GDRVDYIDYL NHSHHLYKNK TYCVKGGMPS GCSGTSIFNS
MINNLIIRTL LLKTYKGIDL DHLKMIAYGD DVIASYPHEV DASLLAQSGK DYGLTMTPAD
KSAIFETVTW ENVTFLKRFF RADEKYPFLI HPVMPMKEIH ESIRWTKDPR NTQDHVRSLC
LLAWHNGEEE YNKFLAKIRS VPIGRALLLP EYSTLYRRWL DSF
//
