ID I3QJ35_PRRSV Unreviewed; 1460 AA.
AC I3QJ35;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=Replicase polyprotein 1ab {ECO:0000256|ARBA:ARBA00022087};
DE AltName: Full=ORF1ab polyprotein {ECO:0000256|ARBA:ARBA00029611};
DE Flags: Fragment;
OS Porcine reproductive and respiratory syndrome virus (PRRSV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Arnidovirineae; Arteriviridae; Variarterivirinae;
OC Betaarterivirus; Ampobartevirus; Betaarterivirus suid 2.
OX NCBI_TaxID=28344 {ECO:0000313|EMBL:AFK09172.1, ECO:0000313|Proteomes:UP000168363};
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1] {ECO:0000313|EMBL:AFK09172.1, ECO:0000313|Proteomes:UP000168363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10-LW2-6 {ECO:0000313|EMBL:AFK09172.1};
RX PubMed=22525010; DOI=10.1016/j.vetmic.2012.02.036;
RA Yu X., Chen N., Wang L., Wu J., Zhou Z., Ni J., Li X., Zhai X., Shi J.,
RA Tian K.;
RT "New genomic characteristics of highly pathogenic porcine reproductive and
RT respiratory syndrome viruses do not lead to significant changes in
RT pathogenicity.";
RL Vet. Microbiol. 158:291-299(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001556};
CC -!- SUBCELLULAR LOCATION: Host cytoplasm, host perinuclear region
CC {ECO:0000256|ARBA:ARBA00004407}. Host membrane
CC {ECO:0000256|ARBA:ARBA00004301}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004301}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; JQ663563; AFK09172.1; -; Genomic_RNA.
DR Proteomes; UP000168363; Genome.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-KW.
DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR CDD; cd21410; 1B_av_Nsp10-like; 1.
DR CDD; cd23189; Arteriviridae_RdRp; 1.
DR CDD; cd17937; DEXXYc_viral_SF1-N; 1.
DR CDD; cd21160; NendoU_av_Nsp11-like; 1.
DR CDD; cd21166; NTD_av_Nsp11-like; 1.
DR CDD; cd18786; SF1_C; 1.
DR CDD; cd21405; ZBD_av_Nsp10-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR InterPro; IPR046440; AV_NSP11N_COV_NSP15M.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR037227; EndoU-like.
DR InterPro; IPR043609; NendoU_nidovirus.
DR InterPro; IPR044863; NIRAN.
DR InterPro; IPR044348; NSP10_1B_Av.
DR InterPro; IPR027355; NSP10_Av_ZBD.
DR InterPro; IPR044320; NSP11_Av_N.
DR InterPro; IPR044314; NSP11_NendoU_Av.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR Pfam; PF19215; CoV_NSP15_C; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF01443; Viral_helicase1; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF142877; EndoU-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51961; AV_NSP11N_COV_NSP15M; 1.
DR PROSITE; PS51652; AV_ZBD; 1.
DR PROSITE; PS51958; NENDOU; 1.
DR PROSITE; PS51947; NIRAN; 1.
DR PROSITE; PS51657; PSRV_HELICASE; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Endonuclease {ECO:0000256|PROSITE-ProRule:PRU01303};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01303}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00985}; Nuclease {ECO:0000256|PROSITE-ProRule:PRU01303};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Protease {ECO:0000256|ARBA:ARBA00022825};
KW Ribosomal frameshifting {ECO:0000256|ARBA:ARBA00022758};
KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953};
KW Zinc {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-ProRule:PRU00985};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00985}.
FT DOMAIN 1..150
FT /note="NiRAN"
FT /evidence="ECO:0000259|PROSITE:PS51947"
FT DOMAIN 389..523
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT DOMAIN 644..707
FT /note="AV ZBD"
FT /evidence="ECO:0000259|PROSITE:PS51652"
FT DOMAIN 764..1045
FT /note="(+)RNA virus helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51657"
FT DOMAIN 1084..1180
FT /note="AV-Nsp11N/CoV-Nsp15M"
FT /evidence="ECO:0000259|PROSITE:PS51961"
FT DOMAIN 1182..1304
FT /note="NendoU"
FT /evidence="ECO:0000259|PROSITE:PS51958"
FT ACT_SITE 1213
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT ACT_SITE 1228
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT ACT_SITE 1257
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFK09172.1"
SQ SEQUENCE 1460 AA; 161560 MW; 1ADFFA37A3C01E4F CRC64;
FKLLAASGLT RCGRGGLVVT ETAVKIVKFH NRTFTLGPVN LKVASEVELK DAVEHNQHPV
ARPVDGGVVL LRSAVPSLID VLISGADASP KLLARHGPGN TGIDGTLWDF EAEATKEEVA
LSAQIIQACD IRRGDAPEIG LPYKLHPVRG NPERVKGVLQ NTRFGDIPYK TPSDTGSPVH
AAACLTPNAT PVTDGRSVLA TTMPSGFELY VPTIPASVLD YLDSRPDCPK QLTEHGCEDA
ALRDLSKYDL STQGFVLPGV LRLVRKYLFA HVGKCPPVHR PSTYPAKNSM AGINGNRFPT
KDIQSVPEID VLCAQAVREN WQTVTPCTLK KQYCGKKKTR TILGTNNFIA LAHRAALSGV
TQGFMKKAFN SPIALGKNKF KELQAPVLGR CLEADLASCD RSTPAIVRWF AANLLYELAC
AEEHLPSYVL NCCHDLLVTQ SGAVTKRGGL SSGDPITSVS NTIYSLVIYA QHMVLSYFKS
GHPHGLLFLQ DQLKFEDMLK VQPLIVYSDD LVLYAESPSM PNYHWWVEHL NLMLGFQTDP
KKTTITDSPS FLGCRIINGR QLVPNRDRIL AALAYHMKAS NVSEYYASAA AILMDSCACL
EYDPEWFEEL VVGIAQCARK DGYSFPGPPF FLSMWEKLRS NHEGKKSRMC GYCGAPAPYA
TACGLDVCVY HTHFHQHCPV IIWCGHPAGS GSCSECEPPL GKGTSPLDEV LEQVPYKPPR
TVIMHVEQGL TPLDPGRYQT RRGLVSVRRG IRGNEVDLPD GDYASTALLP TCKEINMVAV
ASNVLRSRFI IGPPGAGKTH WLLQQVQDGD VIYTPTHQTM LDMIRALGTC RFNVPAGTTL
QFPAPSRTGP WVRILAGGWC PGKNSFLDEA AYCNHLDVLR LLSKTTLTCL GDFKQLHPVG
FDSHCYVFDI MPQTQLKTIW RFGQNICDAI QPDYRDKLMS MVNTTRVTYV EKPVRYGQVL
TPYHRDREDG AITIDSSQGA TFDVVTLHLP TKDSLNRQRA LVAITRARHA IFVYDPHRQL
QSMFDLPAKG TPVNLAVHRD EQLIVLDRNN REITVAQALG NGDKFRATDK RVVDSLRAIC
ADLEGSSSPL PKVAHNLGFY FSPDLTQFAK LPAELAPHWP VVTTQNNERW PDRLVASLRP
IHKYSRACIG AGYMVGPSVF LGTPGVVSYY LTKFVRGEAQ VLPETVFSTG RIEVDCREYL
DDREREVAES LPHAFIGDVK GTTVGGCHHV TSKYLPRFLP KESVAVVGVS SPGKAAKAVC
TLTDVYLPDL EAYLHPETQS RCWKVMLDFK EVRLMVWKDK TAYFQLEGRH FTWYQLASYA
SYIRVPVNST VYLDPCMGPA LCNRKVVGST HWGADLAVTP YDYGAKIILS SAYHGEMPPG
YKILACAEFS LDDPVRYKHT WGFESDTAYL YEFTGNGEDW EDYNDAFRAR QKGKIYKANA
TSMRFHFPPG PVIEPTLGLN
//