ID F1DB19_9ALPC Unreviewed; 2682 AA.
AC F1DB19;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=ORF1ab polyprotein {ECO:0000256|PROSITE-ProRule:PRU01344};
DE Flags: Fragment;
GN Name=ORF1ab {ECO:0000313|EMBL:ADX59501.1};
OS Chaerephon bat coronavirus/Kenya/KY22/2006.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Alphacoronavirus.
OX NCBI_TaxID=983929 {ECO:0000313|EMBL:ADX59501.1};
RN [1] {ECO:0000313|EMBL:ADX59501.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BtKY22 {ECO:0000313|EMBL:ADX59501.1};
RX PubMed=19239771; DOI=10.3201/eid1503.081013;
RA Tong S., Conrardy C., Ruone S., Kuzmin I.V., Guo X., Tao Y., Niezgoda M.,
RA Haynes L., Agwanda B., Breiman R.F., Anderson L.J., Rupprecht C.E.;
RT "Detection of novel SARS-like and other coronaviruses in bats from Kenya.";
RL Emerg. Infect. Dis. 15:482-485(2009).
RN [2] {ECO:0000313|EMBL:ADX59501.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BtKY22 {ECO:0000313|EMBL:ADX59501.1};
RX PubMed=22561208; DOI=10.1016/j.virusres.2012.04.007;
RA Tao Y., Tang K., Shi M., Conrardy C., Li K.S., Lau S.K., Anderson L.J.,
RA Tong S.;
RT "Genomic characterization of seven distinct bat coronaviruses in Kenya.";
RL Virus Res. 167:67-73(2012).
CC -!- FUNCTION: Forms a primer, NSP9-pU, which is utilized by the polymerase
CC for the initiation of RNA chains. Interacts with ribosome signal
CC recognition particle RNA (SRP). Together with NSP8, suppress protein
CC integration into the cell membrane, thereby disrupting host immune
CC defenses. {ECO:0000256|ARBA:ARBA00043928}.
CC -!- FUNCTION: RNA-directed RNA polymerase that catalyzes the transcription
CC of viral genomic and subgenomic RNAs. Acts in complex with nsp7 and
CC nsp8 to transcribe both the minus and positive strands of genomic RNA.
CC The kinase-like NiRAN domain of NSP12 attaches one or more nucleotides
CC to the amino terminus of NSP9, forming a covalent RNA-protein
CC intermediate that serves as transcription/replication primer.
CC Subgenomic RNAs (sgRNAs) are formed by discontinuous transcription: The
CC polymerase has the ability to pause at transcription-regulating
CC sequences (TRS) and jump to the leader TRS, resulting in a major
CC deletion. This creates a series of subgenomic RNAs that are replicated,
CC transcribed and translated. In addition, Nsp12 is a subunit of the
CC viral RNA capping enzyme that catalyzes the RNA guanylyltransferase
CC reaction for genomic and sub-genomic RNAs. Subsequently, the NiRAN
CC domain transfers RNA to GDP, and forms the core cap structure GpppA-
CC RNA. {ECO:0000256|ARBA:ARBA00043918}.
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}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
CC {ECO:0000256|ARBA:ARBA00008087, ECO:0000256|PROSITE-ProRule:PRU01299}.
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; HQ728486; ADX59501.1; -; Genomic_RNA.
DR SMR; F1DB19; -.
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:0000175; F:3'-5'-RNA exonuclease activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0004482; F:mRNA 5'-cap (guanine-N7-)-methyltransferase activity; IEA:InterPro.
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 CDD; cd21409; 1B_cv_Nsp13-like; 1.
DR CDD; cd21723; alphaCoV_Nsp13-helicase; 1.
DR CDD; cd21660; alphaCoV_Nsp14; 1.
DR CDD; cd21588; alphaCoV_RdRp; 1.
DR CDD; cd20762; capping_2-OMTase_Nidovirales; 1.
DR CDD; cd21167; M_alpha_beta_cv_Nsp15-like; 1.
DR CDD; cd21161; NendoU_cv_Nsp15-like; 1.
DR CDD; cd21171; NTD_alpha_betaCoV_Nsp15-like; 1.
DR CDD; cd21689; stalk_CoV_Nsp13-like; 1.
DR CDD; cd21401; ZBD_cv_Nsp13-like; 1.
DR Gene3D; 3.40.50.11580; -; 1.
DR Gene3D; 3.30.160.820; Nsp15 N-terminal domain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR InterPro; IPR046440; AV_NSP11N_COV_NSP15M.
DR InterPro; IPR043608; CoV_NSP15_M.
DR InterPro; IPR043606; CoV_NSP15_N.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR037227; EndoU-like.
DR InterPro; IPR046435; N7_MTase_CoV.
DR InterPro; IPR043609; NendoU_nidovirus.
DR InterPro; IPR044863; NIRAN.
DR InterPro; IPR046438; NIV_2_O_MTASE.
DR InterPro; IPR046436; NIV_EXON.
DR InterPro; IPR047570; NSP12_IF_CoV.
DR InterPro; IPR044343; NSP13_1B_dom_CoV.
DR InterPro; IPR047912; Nsp13_helicase_alphaCoV.
DR InterPro; IPR048673; NSP13_stalk_CoV.
DR InterPro; IPR048672; NSP13_ZBD_CoV.
DR InterPro; IPR027352; NSP13_ZBD_CoV-like.
DR InterPro; IPR044313; NSP14_alphaCoV.
DR InterPro; IPR009466; NSP14_CoV.
DR InterPro; IPR044330; NSP15_alpha_betaCoV_N.
DR InterPro; IPR044322; NSP15_M_alpha_beta_CoV.
DR InterPro; IPR043174; NSP15_middle_sf.
DR InterPro; IPR042515; NSP15_N_CoV.
DR InterPro; IPR044401; NSP15_NendoU_CoV.
DR InterPro; IPR009461; NSP16_CoV-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR044356; RdRp_alphaCoV.
DR InterPro; IPR046441; RdRp_CoV.
DR InterPro; IPR009469; RdRp_N_CoV.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR PANTHER; PTHR43788:SF8; HELICASE WITH ZINC FINGER 2; 1.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF13604; AAA_30; 1.
DR Pfam; PF06471; CoV_ExoN; 1.
DR Pfam; PF06460; CoV_Methyltr_2; 1.
DR Pfam; PF20631; CoV_NSP13_1B; 1.
DR Pfam; PF20633; CoV_NSP13_stalk; 1.
DR Pfam; PF20632; CoV_NSP13_ZBD; 1.
DR Pfam; PF19215; CoV_NSP15_C; 1.
DR Pfam; PF19216; CoV_NSP15_M; 1.
DR Pfam; PF19219; CoV_NSP15_N; 1.
DR Pfam; PF06478; CoV_RPol_N; 1.
DR Pfam; PF00680; RdRP_1; 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; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51961; AV_NSP11N_COV_NSP15M; 1.
DR PROSITE; PS51954; COV_N7_MTASE; 1.
DR PROSITE; PS52000; COV_NSP12_IF; 1.
DR PROSITE; PS51948; COV_NSP12_RDRP; 1.
DR PROSITE; PS51960; COV_NSP15_NTD; 1.
DR PROSITE; PS51653; CV_ZBD; 1.
DR PROSITE; PS51958; NENDOU; 1.
DR PROSITE; PS51947; NIRAN; 1.
DR PROSITE; PS51955; NIV_2_O_MTASE; 1.
DR PROSITE; PS51953; NIV_EXON; 1.
DR PROSITE; PS51657; PSRV_HELICASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|PROSITE-
KW ProRule:PRU01303}; Exonuclease {ECO:0000256|PROSITE-ProRule:PRU01298};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01303}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01299};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|PROSITE-
KW ProRule:PRU01298}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Ribosomal frameshifting {ECO:0000256|ARBA:ARBA00022758};
KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01299};
KW Zinc {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-ProRule:PRU00986};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00986}.
FT DOMAIN 6..255
FT /note="NiRAN"
FT /evidence="ECO:0000259|PROSITE:PS51947"
FT DOMAIN 261..359
FT /note="Nsp12 Interface"
FT /evidence="ECO:0000259|PROSITE:PS52000"
FT DOMAIN 360..927
FT /note="Nsp12 RNA-dependent RNA polymerase"
FT /evidence="ECO:0000259|PROSITE:PS51948"
FT DOMAIN 928..1011
FT /note="CV ZBD"
FT /evidence="ECO:0000259|PROSITE:PS51653"
FT DOMAIN 1176..1515
FT /note="(+)RNA virus helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51657"
FT DOMAIN 1597..1811
FT /note="ExoN"
FT /evidence="ECO:0000259|PROSITE:PS51953"
FT DOMAIN 1820..2041
FT /note="N7-MTase"
FT /evidence="ECO:0000259|PROSITE:PS51954"
FT DOMAIN 2044..2104
FT /note="Nsp15 N-terminal oligomerization"
FT /evidence="ECO:0000259|PROSITE:PS51960"
FT DOMAIN 2105..2222
FT /note="AV-Nsp11N/CoV-Nsp15M"
FT /evidence="ECO:0000259|PROSITE:PS51961"
FT DOMAIN 2239..2379
FT /note="NendoU"
FT /evidence="ECO:0000259|PROSITE:PS51958"
FT DOMAIN 2383..2679
FT /note="Nidovirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000259|PROSITE:PS51955"
FT REGION 1932..1946
FT /note="GpppA-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01299"
FT ACT_SITE 1615
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 1617
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 1716
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 1792
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 1797
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 2269
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT ACT_SITE 2284
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT ACT_SITE 2325
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT BINDING 1855..1861
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01299"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADX59501.1"
SQ SEQUENCE 2682 AA; 301746 MW; 930D1C8CAA78751A CRC64;
SVDTSYLNRA RGSSAARLEP CNGTDTDRVV RAFDIYNKDV ACIGKFLKVN CVRFENLDKH
DAFFVVKRCT KSVMEHEQSI YDKLHKCGAV AAHDFFLWKD GRSVFGNISR QNLTKYTMMD
LCYALRNFDE RNCETLKEIL VLTGCCDYSY FENKDWYDPV ENEDIHKVYA HLGTVVANAL
LKCVKLCDAM VEAGVVGVLT LDNQDLNGDF YDFGDFATTI PKMGVPLCTS YYSYMMPVMG
MTNCLASECF IKSDIFGSDF KTYDLLEYDF TEHKEALFQK YFKYWGQDYH PNCADCHDEL
CIVHCANFNT LFSTTIPNTA FGPLCRKVFV DGVPLVTTAG YHFKQLGLVW NKDINTHSTR
LSVNELLQFV TDPALLVASS PALVDQRTVC FSVAALSTGM TNQTVKPGHF NKEFYDFLRS
QGFFEEGSEL TLKHFFFAQK GDAAVKDFDY YRYNRPTMLD ICQARVTYKI VQRYFECYEG
GCIAAKDVVV TNLNKSAGYP LNKFGKAGLY YESLSYEEQD ALYALTKRNV LPTMTQLNLK
YAISGKERAR TVGGVSLLST MTTRQFHQKH LKSIVNTRNA SVVIGTTKFY GGWDNMLKNL
IEGVDNACLM GWDYPKCDRA LPNMIRMISA MILGSKHVTC CDSSDKYYRL CNELAQVLTE
VVYSNGGFYL KPGGTTSGDA TTAYANSVFN IFQAVSANIN RLLSIDSNVC NNIGVKSLQR
QLYDCCYRSS SVDDSFVDSY YGYLRKHFSM MILSDDGVVC YNKDYADLGY VADINAFKAT
LYYQNNVFMS TAKCWVEPDI SKGPHEFCSQ HTMQIVDSDG KYYLPYPDPS RILSAGVFVD
DVVKTDAVIL LERYVSLAID AYPLSKHHNP EYRKVFYTLL EWVKHLHNTL NQGVLESFSV
TLLEDASSKF WDESFYASLY EKSTALQAAG LCVVCGSQTV LRCGDCLRRP MLCTKCAYDH
VVTTNHKFIL AITPYVCNAS GCTVNDVTKL YLGGLSYWCI DHKPTLSFPL CSAGNVFGLY
KNSATGSPDV EVFNTLATSD WTDVKDYKLA NECKDSLRLF AAETVKAKEE SVKSSYACAT
LKEVVGPREL ILSWECGKIK PPLNRNSVFT CFQISKDSKF QVGEFTFEKL DYGSDAVCYK
STATVKLVPG MIFVLTSHNV QPLRAPTIAN QERYASIYKL HPTFNISDAY ANLVPYYQMI
GKQRITTIQG PPGSGKSHCV IGLGLYYPGA RMVFAACSHA AVDSLCVKAA TAYSVDKCTR
IIPARARVEC YNGFKANNTQ AQYIFSTVNA LPECNVDIVV IDEVSMCTNY DLSVINQRLS
YKHIVYVGDP QQLPAPRTMI TKGVLEPKDY NVVTQRMCAV GPDVFLHKCY RCPAEIVKTV
SELVYENKFV PVHADSKQCF KLLCKGNVQV DNGSSINRKQ LDVVKMFLAK NPRWSKAVFI
SPYNSQNYVA SRVLGLQIQT VDSSQGSEYD YVIYTQTSDT AHACNVNRFN VAITRAKKGI
LCVMCDRELF DALKFFEIKL SDLQASGDGC GLFKDCYRKD DELPPSHAAT YMALSDNFKV
NGDLAVQIGF KGVCKYEHVI SFMGFRFDIN VPDQHSLFCT RNFAMRHVRG WLGMDVEGAH
VIGENVGTNV PLQVGFSNGV DFVVQPEGCV VTETGSKIVP VRARAPPGEQ FSHLVPLLRK
GQPWSVVRKR IVQMCCDYLV NLSDILIFVL WAGGLELTTM RYFVKIGPSK VCECGKVATC
YNSVTHAYYC FKHALGCDYL YNPYVIDIQQ WDYTGSLSHN HHEHCNVHRN EHVASGDAIM
TRCLAVYDCF VKNVDWSITY PFIANEHAIN KSGRVVQSMV VKSAIKLYNP KAIHDIGNPK
GIRCAVTDAH WFCYDKQPLN SNVKLLEYDY ITHGQMDGLC LFWNCNVDMY PEFSIVCRFD
TRCRSNLNLE GVNGGSLYVN NHAFFTPAFD KRAMAKLKPM PFFFYDDTPC DRVQDQINYV
PLRASTCITK CNIGGAVCSK HANMFHAYVN AYNTFTQAGF TIWVPVTFDL FNLWQTFVET
NLQGLENIAF NVLKKGSFVG EEGELPVAIV NDRVLVRDGT VDNLVFTNKT SLPTNVAFEL
YAKRKVGLTP PLAVLRNLGV VSTYKFVLWD YEAERPFTTF TKNVCSYTDF DEDVCTCFDN
SIQGSFERFS MANNAVLIST SAVKKLTCIK LTYGLLNGVA VAKNEDKPVT WYIYVRKNGQ
FVDQFDGYFT QGRTTADFLP RSTMEEDFLN LDMGLFINKY GLEDYAFEHV VYGDVSGTTL
GGLHLLISQV RLGKMGVLKV DEFTHSEDST LKSCTVTYSN DPSSKMVCTY MDLLLDDFVT
ILKSLDLSVT SKVHDVVVDC KVWRWMLWCK DHKVQTFYPQ LQSSEWKCGY SMPALYKIQR
MCLEPCNLYN YGASLKLPDG VMFNVVKYTQ LCQYLNSTTM CVPHNMRVLH LGAGSDKGVA
PGTAVLRRWL PSDAIIVDND VNDYVSDADF SVTGDCATLY LQDKFDLVIS DMYDGRIKQC
DGANVSKDGF FTYINGVICE KLALGGTVAI KITEYSWNKR LYELIQKFEF WTLFCTSVNT
SSSEAFLIGV NYLGDYSTQP IMDGNTMHAN YVFWRNSTIM SMSYNSVLDL AKFNCRHKAT
VVIALKESDL SDVIVGLIKN GRLLVRKNGA ICNYGNHLVS TK
//
