ID A0A0B6C113_9NIDO Unreviewed; 3587 AA.
AC A0A0B6C113;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Replicase polyprotein 1ab {ECO:0000256|ARBA:ARBA00022087};
DE AltName: Full=ORF1ab polyprotein {ECO:0000256|ARBA:ARBA00029611};
GN Name=ORF1ab {ECO:0000313|EMBL:AJI43737.1};
OS DeBrazza's monkey arterivirus.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Arnidovirineae; Arteriviridae; Simarterivirinae;
OC Iotaarterivirus; Debiartevirus; Iotaarterivirus debrazmo.
OX NCBI_TaxID=1965063 {ECO:0000313|EMBL:AJI43737.1, ECO:0000313|Proteomes:UP000171565};
RN [1] {ECO:0000313|EMBL:AJI43737.1, ECO:0000313|Proteomes:UP000171565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PREDICT-06530 {ECO:0000313|EMBL:AJI43737.1};
RG USAID EPT PREDICT program;
RA Ng T.F.F., LeBreton M., Schneider B.S., Gillis A., Tamoufe U.,
RA Diffo L.D.D., Takuo J.M., Kondov N.O., Coffey L., Wolfe N.D., Delwart E.;
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AJI43737.1, ECO:0000313|Proteomes:UP000171565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PREDICT-06530 {ECO:0000313|EMBL:AJI43737.1};
RA Ng T.F.F., LeBreton M., Schneider B.S., Gillis A., Tamoufe U.,
RA Diffo L.D.D., Takuo J.M., Kondov N.O., Coffey L., Wolfe N.D., Delwart E.;
RT "Virome of African Animals.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001665};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=uridylyl-uridylyl-ribonucleotide-RNA = a 3'-end uridylyl-
CC 2',3'-cyclophospho-uridine-RNA + a 5'-end dephospho-ribonucleoside-
CC RNA; Xref=Rhea:RHEA:67732, Rhea:RHEA-COMP:13936, Rhea:RHEA-
CC COMP:17334, Rhea:RHEA-COMP:17335, ChEBI:CHEBI:138284,
CC ChEBI:CHEBI:173079, ChEBI:CHEBI:173080;
CC Evidence={ECO:0000256|ARBA:ARBA00024600};
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; KP126831; AJI43737.1; -; Genomic_RNA.
DR KEGG; vg:23632002; -.
DR Proteomes; UP000171565; Segment.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
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:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0004540; F:RNA nuclease activity; IEA:UniProt.
DR GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0019082; P:viral protein processing; 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; cd22528; av_Nsp3_ER-remodelling; 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; 3.90.70.160; -; 1.
DR Gene3D; 3.30.1330.220; Arterivirus nonstructural protein 7 alpha; 1.
DR Gene3D; 3.90.70.70; Arterivirus papain-like cysteine protease beta domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR InterPro; IPR031932; Arteri_nsp7a.
DR InterPro; IPR038451; Arteri_nsp7a_sf.
DR InterPro; IPR008743; Arterivirus_Nsp2_C33.
DR InterPro; IPR023338; Arterivirus_NSP4_peptidase.
DR InterPro; IPR046440; AV_NSP11N_COV_NSP15M.
DR InterPro; IPR025773; AV_PCPbeta.
DR InterPro; IPR038154; AV_PCPbeta_sf.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR008760; EAV_peptidase_S32.
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; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR Pfam; PF16749; Arteri_nsp7a; 1.
DR Pfam; PF19215; CoV_NSP15_C; 1.
DR Pfam; PF05411; Peptidase_C32; 1.
DR Pfam; PF05412; Peptidase_C33; 1.
DR Pfam; PF05579; Peptidase_S32; 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; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51538; AV_CP; 1.
DR PROSITE; PS51961; AV_NSP11N_COV_NSP15M; 1.
DR PROSITE; PS51493; AV_NSP4_PRO; 1.
DR PROSITE; PS51540; AV_PCP_BETA; 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 Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01303}; Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nuclease {ECO:0000256|PROSITE-ProRule:PRU01303};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000171565};
KW Ribosomal frameshifting {ECO:0000256|ARBA:ARBA00022758};
KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
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 TRANSMEM 891..915
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 977..996
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1002..1021
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1216..1236
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1285..1310
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1316..1343
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1350..1371
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1639..1658
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1664..1680
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1687..1708
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1720..1741
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1762..1784
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 245..356
FT /note="Peptidase C32"
FT /evidence="ECO:0000259|PROSITE:PS51540"
FT DOMAIN 589..692
FT /note="Peptidase C33"
FT /evidence="ECO:0000259|PROSITE:PS51538"
FT DOMAIN 1442..1642
FT /note="Peptidase S32"
FT /evidence="ECO:0000259|PROSITE:PS51493"
FT DOMAIN 2073..2236
FT /note="NiRAN"
FT /evidence="ECO:0000259|PROSITE:PS51947"
FT DOMAIN 2475..2609
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT DOMAIN 2732..2798
FT /note="AV ZBD"
FT /evidence="ECO:0000259|PROSITE:PS51652"
FT DOMAIN 2845..3135
FT /note="(+)RNA virus helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51657"
FT DOMAIN 3179..3275
FT /note="AV-Nsp11N/CoV-Nsp15M"
FT /evidence="ECO:0000259|PROSITE:PS51961"
FT DOMAIN 3277..3399
FT /note="NendoU"
FT /evidence="ECO:0000259|PROSITE:PS51958"
FT REGION 486..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1976..2003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1979..2003
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 3308
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT ACT_SITE 3323
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT ACT_SITE 3352
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
SQ SEQUENCE 3587 AA; 388760 MW; 8C5EE46A074F385B CRC64;
MPLTMKCECP RTNLVLVVSG KVCCINCGLV RSPAPTPAGI RAKFGPLSQY VDPTRASVYE
NLSVGSCSLE VLAVLMTECG MTNKPLETAV SIMAVARQGG ISRENFNRLP GSELFGFVSC
TGPVWGAKAY ISPLHASRDF FEGATHAMIK PLDYRGLGRV LREFPFETPP CGEVYQYGTN
TITETSTHVS WVQGVTPGTQ MCPLDKLEFA EAVVRSFPAG FVANKKWLGT KRGSLRVETV
DPYCLSFDHG TCWTQIFPDP ENELKVACTF GYQLGIGVQG KYISRRLQIA GCKLVYDSAG
PFVAYTFHKG SWLGHIQHAS EPLPEECCVT ARFSVIPYNQ YSPLPLCKLS GRVWYGGSAG
SSLRYESPRI SYIDATVPGF CWLQLLPPQS RADEAARAIM ACQVDGNGVS GSYLSYRLLQ
HHLQVEACDH GEYFIYRHRH DVMVRHISPV PLADTGMIFM GRVTVRPLNR TAPSFSLGFG
TRYGKRKRGG GLKQTADASA LSGDWGKAVD EQEKQAENLG SPAPPTAASP PKAPPRASKK
KVTVSFGAPS DAASAPVPQT SVRDALVRTT KERGVPTISH GKAQLPASTF IPPPDGACGV
HCLAAIQHHI ANGVWPTQQP VVDWAYEQWL DSDSLGDMIV ATGTPAAIAP CDHARYVIAL
VDSHWIVRFY PDRELFRASA CQRGFCISAV GPVGGVTVKQ PKSVAVGLYS LLGRFQSGEE
FGRVLVALSG GKWRGVAASI SDSELLRIVD SAAATPAKVP ASYVTTLPVK DEKDMAQNAI
PTTQHKDTAP SVAEVKVPDA APSVETQPPQ TPATASNAAA PLAAENTNNN AAPGTGPPPK
RKLTWRERGN NYLARLHNVI ADPAGRVFHL YPQLLALLAP RQNRYPLSRL VCAYSLFALA
LVCLSFGSWF CFLFGAAALG CIWSSRHARA LFGILVVCFV LRLFADESSS LCEHPDDRCH
EYLDSVRGRL SASFRTFITP GLLTVFLAFF RGLYPITSAL FVLHYFLLLL DLVFILALLF
VRRICLRCWG RCIRTAPEEV PLLTIPSSRV TRAFLLDIAN TFSSPQVDVI RMATGYAGCY
DGCVCPTGTS ANIAVGKVDV KKVTHKTSCS VPTCPTEAVK ALHVLASRGT IAPLNNNKVK
KVDALPCRNP LFPFDIKNKV ITCVDSDTYS LLSELGCDLS HLIIGTGDFF QEMGVPRPDY
FTVLRLKAAR IMGGGVAVRT VAAAAYIVVC VMLGSYLQLP TTCGISTRDP FCMSSFGVPV
VASQGVCRGG YCASPLGISR NTPDLLSLAP AVAPYIAILL LICFLLWQYV PTVVEAIAVL
IAAAMPSTPL VDAIRVILFF LALPRLSTKV IGFYLASTVL ISPAAACISA IGMACAWIVG
AFTGTVGLVT PFDIHRLSRS SRDAVAIANA PANTFLGAVR KAALTGKPTY FLADNTGIVL
EGLLRHSKPA DSSVSVFGVA CGSGGLFSDK GKTVVVTATH VCGQQPAIVK TGGEERSVTF
QTIGDFAHAE IDLPGSFPAF KIAPPTYMGR AYWYCNNGVE TGFVTPHGCV VFSGPGDSGS
PIVTPDGQLI GVHTGSDSNG CGAYTRPDGT LVSGGIQLSV AAPHYDGDLV DVPSRLPKNV
VADAQKIPAT LARLLSQSVL LEGALGTIQL LVVAAVMWKY FVDPTMIPFA VLFFLLNEML
PRCVMRGVYN LALFCLAAFT PLASRILLIR LLTAALNRNL TALLIHTGFA AVAVLNDYLI
LGNLQLALRT CSFYVSGVNH DPMIVFAIGV CVVLTCILLE LFGYPTLSNL ISGSGTFDPA
FFARYVHEGI RTGVSTGLVS ESLSASLACN LSEEDLRFLD SLVDAKAVVA AVNTQAALKD
YILSQNAKRL RSALATVHAN ANANKALASL DKFLAGTDTL LAPGDPVVLL GCTNQELITA
YAGNKEYIVT PVRSHKVAGT VCTLCKVQAT VECGLISVAR SSSGKTYQLV NGKPLADSPD
FKPENDARFN RASEDEERKL RRSEKVGQVT INGHTFDKMW DKATGDTWYS FVNESATDSE
IQARQQFDIK SAAAALNLDT TLSESDLQRL QTLITKLQGL TGSTALNLLT AAGCTSADRS
GLAVSLDGAK IVEHHERTRA FNGIDFKFVQ DAELERTTRL SITPQPVVAT LSDGYLIARR
HPASLLDVIT KGFDAEYQPA IHGPGDTGID GYLWDFEAPH AKDVVALSRE IIAACAVRRG
DAPSLGLPYD LHPVRGDPYR EGSKLLNTRF GNFRTTTIAD SSDPWLLTTA VTPAGAKVVS
GDKVIATTLP PGSEIYVPTI PETVLDYLDG RPDCPTFYTK HGTEEALLSD LEKFNLSTQG
FILPGVLHVV RNYLVKTIGY RPALYTPATV PSNDSHAGIN GLSFSTKMLQ ALPEVNQLCE
RAAKEVWQSV TPVTLKKQYC SKRKTRTILG TNALISLALR AALSGVTKGF QLAGKGSPIC
LGKSKFNPME VSVTGTCMET DLASCDRSTP AIIRWFTTNL LFELGCCKHM LPLYVVNCCH
DLLVSQSTAV TKRGGLSSGD PVTSVANTIY SLCLYTQHMV LSAFREGHPL TLKYMSGSLT
MEDLIAIQGF VVYSDDLVLL QEAADLPNFK YWNLHLDLAL GFKTDPSKTV ITTNPGFLGC
NFVHGKWLAP QRDRVLAALA YHLNAKDAQT YYENAVAILN DASALSVFDP DWFTDLVIGL
ADCARKDGYT MPGPQHYRDF FSRVAGYTPE ASVECSMCLS TAVTTSACGL MLCMFCAHRH
SHPECVVKSP FCKHPVGSKS CQQCSIDVVP AQDAFSKLLA DHPFSNVTFV NVTVVNGYTQ
ADPGRYLFHK HQYTLKRDPK GCALNLPDGE YCMKKLPNTC SGIVLPKALK NAALSTFIVG
PPGSGKTTTI TKMLDDDCVV YCPTHMSLIA YSKSLPAARF TVPKDQDQAE YGTPASHGPR
LQLLSLGYLP GKQHFVDEAC YANPLDLLKV LTRTPITAIG DPAQLPPVGF DKVLFVFKMM
RQKQLNTIYR FGPNLVESIQ RYYTHPLKSA KDSPTEIIFQ TKFQPRGLVL TPYHRDRVAG
AITIDSAQGM TRSVVTVYLP SPNSISASRA LVACTRATDR LYIYDPHGQL ASFLDLKPFS
LGEKPHAYVL GDRVVVRLND KTLADPKDFP GLLCTARPRT PADKEMLEAT PLKLDYLESG
SLSPLPRVAH NLGFYYSPDI PQFLPIPEEL AVHWPVVTNK NNPDWPDRLV VSATQLSPLS
QRATCAGYYV GKSLFLGVPR VVSYWMTQFL GGKAVPIESS LFSTGRIDLD IRSYLDEEER
DFAIAHPHAF IGDTKGTTVG GCHHITSRYL PKVIPSDSVV KVGVSAPGKA HKACCTLTDV
YLPYLREFDS PPTQSKVYKV RIDNKECRLM VWRDQTMYFQ ESNNPLALVE AATRHGFLSG
TGTFYLEKSL TPAVANRQFT SDAEIATDLG VTPWDSNSKF LVSTSSPYDV SDNWLLINSQ
SYAVETLLGK SVTNVYFYKQ LGTPYRSERA LPEHVQVVLA NVPRFKLHTR AKNFHFSPPS
CGCKVAVVDT FGEHVCDCRL TYLGEFLNRC CKLIQANPDL GCSSQSC
//
