ID U3M6G6_CVHOC Unreviewed; 7095 AA.
AC U3M6G6;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=ORF1ab polyprotein {ECO:0000256|PROSITE-ProRule:PRU01344};
GN Name=Pp1ab {ECO:0000313|EMBL:AGT51577.1};
OS Human coronavirus OC43 (HCoV-OC43).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Embecovirus; Betacoronavirus 1.
OX NCBI_TaxID=31631 {ECO:0000313|EMBL:AGT51577.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:AGT51577.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OC43/human/USA/873-16/1987 {ECO:0000313|EMBL:AGT51577.1};
RA Town C.D., Halpin R.A., Ransier A., Fedorova N., Tsitrin T., Stockwell T.,
RA Amedeo P., Appalla L., Bishop B., Edworthy P., Gupta N., Hoover J.,
RA Katzel D., Schobel S., Shrivastava S., Thovarai V., Wang S., Talbot H.K.,
RA Wentworth D.E., Williams J.V.;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cleaves the C-terminus of replicase polyprotein at 11 sites.
CC Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN].
CC Also able to bind an ADP-ribose-1''-phosphate (ADRP).
CC {ECO:0000256|ARBA:ARBA00002223}.
CC -!- FUNCTION: Forms a hexadecamer with nsp7 (8 subunits of each) that may
CC participate in viral replication by acting as a primase. Alternatively,
CC may synthesize substantially longer products than oligonucleotide
CC primers. {ECO:0000256|ARBA:ARBA00002182}.
CC -!- FUNCTION: Forms a hexadecamer with nsp8 (8 subunits of each) that may
CC participate in viral replication by acting as a primase. Alternatively,
CC may synthesize substantially longer products than oligonucleotide
CC primers. {ECO:0000256|ARBA:ARBA00003443}.
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: Inhibits host translation by interacting with the 40S
CC ribosomal subunit. The nsp1-40S ribosome complex further induces an
CC endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them
CC for degradation. Viral mRNAs are not susceptible to nsp1-mediated
CC endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader
CC sequence and are therefore protected from degradation. By suppressing
CC host gene expression, nsp1 facilitates efficient viral gene expression
CC in infected cells and evasion from host immune response.
CC {ECO:0000256|ARBA:ARBA00002872}.
CC -!- FUNCTION: May play a role in the modulation of host cell survival
CC signaling pathway by interacting with host PHB and PHB2. Indeed, these
CC two proteins play a role in maintaining the functional integrity of the
CC mitochondria and protecting cells from various stresses.
CC {ECO:0000256|ARBA:ARBA00003115}.
CC -!- FUNCTION: Methyltransferase that mediates mRNA cap 2'-O-ribose
CC methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine
CC cap is a prerequisite for binding of nsp16. Therefore plays an
CC essential role in viral mRNAs cap methylation which is essential to
CC evade immune system. {ECO:0000256|ARBA:ARBA00002840}.
CC -!- FUNCTION: Multi-functional protein with a zinc-binding domain in N-
CC terminus displaying RNA and DNA duplex-unwinding activities with 5' to
CC 3' polarity. Activity of helicase is dependent on magnesium.
CC {ECO:0000256|ARBA:ARBA00002960}.
CC -!- FUNCTION: Participates in the assembly of virally-induced cytoplasmic
CC double-membrane vesicles necessary for viral replication.
CC {ECO:0000256|ARBA:ARBA00003070}.
CC -!- FUNCTION: Plays a pivotal role in viral transcription by stimulating
CC both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase
CC activities. Therefore plays an essential role in viral mRNAs cap
CC methylation. {ECO:0000256|ARBA:ARBA00002697}.
CC -!- FUNCTION: Plays a role in the initial induction of autophagosomes from
CC host reticulum endoplasmic. Later, limits the expansion of these
CC phagosomes that are no longer able to deliver viral components to
CC lysosomes. {ECO:0000256|ARBA:ARBA00003748}.
CC -!- FUNCTION: Plays a role in viral RNA synthesis through two distinct
CC activities. The N7-guanine methyltransferase activity plays a role in
CC the formation of the cap structure GpppA-RNA. The proofreading
CC exoribonuclease reduces the sensitivity of the virus to RNA mutagens
CC during replication. This activity acts on both ssRNA and dsRNA in a 3'-
CC 5' direction. {ECO:0000256|ARBA:ARBA00034456}.
CC -!- FUNCTION: Plays a role in viral transcription/replication and prevents
CC the simultaneous activation of host cell dsRNA sensors, such as
CC MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-
CC polyuridines generated during replication of the poly(A) region of
CC viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in
CC which a 2'3'-cyclic phosphate (2'3'-cP) is first generated by 2'-O
CC transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P)
CC (By similarity). If not degraded, poly(U) RNA would hybridize with
CC poly(A) RNA tails and activate host dsRNA sensors.
CC {ECO:0000256|ARBA:ARBA00025521}.
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 -!- FUNCTION: Responsible for the cleavages located at the N-terminus of
CC the replicase polyprotein. In addition, PL-PRO possesses a
CC deubiquitinating/deISGylating activity and processes both 'Lys-48'- and
CC 'Lys-63'-linked polyubiquitin chains from cellular substrates.
CC Participates together with nsp4 in the assembly of virally-induced
CC cytoplasmic double-membrane vesicles necessary for viral replication.
CC Antagonizes innate immune induction of type I interferon by blocking
CC the phosphorylation, dimerization and subsequent nuclear translocation
CC of host IRF3. Prevents also host NF-kappa-B signaling.
CC {ECO:0000256|ARBA:ARBA00003569}.
CC -!- FUNCTION: The replicase polyprotein of coronaviruses is a
CC multifunctional protein: it contains the activities necessary for the
CC transcription of negative stranded RNA, leader RNA, subgenomic mRNAs
CC and progeny virion RNA as well as proteinases responsible for the
CC cleavage of the polyprotein into functional products.
CC {ECO:0000256|ARBA:ARBA00003368}.
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=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000256|ARBA:ARBA00000707};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA +
CC S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-
CC COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461,
CC ChEBI:CHEBI:167617; EC=2.1.1.56;
CC Evidence={ECO:0000256|ARBA:ARBA00034403};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67009;
CC Evidence={ECO:0000256|ARBA:ARBA00034403};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
CC in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167,
CC Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609;
CC EC=2.1.1.57; Evidence={ECO:0000256|ARBA:ARBA00024256};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-
CC end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + diphosphate;
CC Xref=Rhea:RHEA:67012, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17166,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:167616, ChEBI:CHEBI:167617; EC=2.7.7.50;
CC Evidence={ECO:0000256|ARBA:ARBA00024520};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67013;
CC Evidence={ECO:0000256|ARBA:ARBA00024520};
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBUNIT: Interacts with host PHB and PHB2.
CC {ECO:0000256|ARBA:ARBA00025984}.
CC -!- SUBUNIT: Interacts with nsp12. {ECO:0000256|ARBA:ARBA00034503}.
CC -!- SUBUNIT: Interacts with nsp7 and nsp8 to form the replication-
CC transcription complex (RTC): nsp12, nsp7, two subunits of nsp8, and up
CC to two subunits of nsp13. Interacts with nsp9.
CC {ECO:0000256|ARBA:ARBA00034511}.
CC -!- SUBUNIT: Interacts with nsp7, nsp13 and nsp12 to form the replication-
CC transcription complex (RTC): nsp12, nsp7, two subunits of nsp8, and up
CC to two subunits of nsp13. {ECO:0000256|ARBA:ARBA00034514}.
CC -!- SUBUNIT: Interacts with nsp8 and nsp12 to form the replication-
CC transcription complex (RTC): nsp12, nsp7, two subunits of nsp8, and up
CC to two subunits of nsp13. {ECO:0000256|ARBA:ARBA00034507}.
CC -!- SUBUNIT: Interacts with nsp8 to form the replication-transcription
CC complex (RTC): nsp12, nsp7, two subunits of nsp8, and up to two
CC subunits of nsp13. {ECO:0000256|ARBA:ARBA00034500}.
CC -!- SUBUNIT: Interacts with papain-like protease nsp3 and non-structural
CC protein 6. {ECO:0000256|ARBA:ARBA00034512}.
CC -!- SUBUNIT: Interacts with proofreading exoribonuclease nsp14 and 2'-O-
CC methyltransferase nsp16; these interactions enhance nsp14 and nsp16
CC enzymatic activities. {ECO:0000256|ARBA:ARBA00034506}.
CC -!- SUBUNIT: Monomer. Homodimer. Only the homodimer shows catalytic
CC activity. {ECO:0000256|ARBA:ARBA00034508}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC compartment {ECO:0000256|ARBA:ARBA00004399}. Host cytoplasm, host
CC perinuclear region {ECO:0000256|ARBA:ARBA00004407}. Host endoplasmic
CC reticulum-Golgi intermediate compartment
CC {ECO:0000256|ARBA:ARBA00004452}. 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}.
CC -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
CC {ECO:0000256|ARBA:ARBA00008087, ECO:0000256|PROSITE-ProRule:PRU01294}.
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; KF530077; AGT51577.1; -; Genomic_RNA.
DR Proteomes; UP000159503; Genome.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0044172; C:host cell endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
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:0000175; F:3'-5'-RNA exonuclease activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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:0008242; F:omega peptidase activity; 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:0003727; F:single-stranded RNA binding; 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:0039595; P:induction by virus of catabolism of host mRNA; IEA:UniProtKB-UniRule.
DR GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
DR GO; GO:0039648; P:modulation by symbiont of host protein ubiquitination; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR GO; GO:0039579; P:suppression by virus of host ISG15-protein conjugation; IEA:UniProtKB-KW.
DR GO; GO:0039644; P:suppression by virus of host NF-kappaB cascade; IEA:UniProtKB-KW.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-UniRule.
DR GO; GO:0019082; P:viral protein processing; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR CDD; cd21409; 1B_cv_Nsp13-like; 1.
DR CDD; cd21901; alpha_betaCoV_Nsp10; 1.
DR CDD; cd21560; betaCoV-Nsp6; 1.
DR CDD; cd21722; betaCoV_Nsp13-helicase; 1.
DR CDD; cd21659; betaCoV_Nsp14; 1.
DR CDD; cd21519; betaCoV_Nsp2_MHV-like; 1.
DR CDD; cd21666; betaCoV_Nsp5_Mpro; 1.
DR CDD; cd21827; betaCoV_Nsp7; 1.
DR CDD; cd21831; betaCoV_Nsp8; 1.
DR CDD; cd21898; betaCoV_Nsp9; 1.
DR CDD; cd21732; betaCoV_PLPro; 1.
DR CDD; cd20762; capping_2-OMTase_Nidovirales; 1.
DR CDD; cd21473; cv_Nsp4_TM; 1.
DR CDD; cd21524; DPUP_MHV_Nsp3; 1.
DR CDD; cd21593; HCoV_HKU1-like_RdRp; 1.
DR CDD; cd21167; M_alpha_beta_cv_Nsp15-like; 1.
DR CDD; cd21557; Macro_X_Nsp3-like; 1.
DR CDD; cd21879; MHV-like_Nsp1; 1.
DR CDD; cd21812; MHV-like_Nsp3_betaSM; 1.
DR CDD; cd21824; MHV-like_Nsp3_NAB; 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; cd21714; TM_Y_MHV-like_Nsp3_C; 1.
DR CDD; cd21467; Ubl1_cv_Nsp3_N-like; 1.
DR CDD; cd21401; ZBD_cv_Nsp13-like; 1.
DR Gene3D; 1.10.8.1190; -; 2.
DR Gene3D; 2.60.120.1680; -; 1.
DR Gene3D; 3.10.20.350; -; 1.
DR Gene3D; 3.10.20.540; -; 1.
DR Gene3D; 3.40.50.11580; -; 1.
DR Gene3D; 6.10.140.2090; -; 1.
DR Gene3D; 1.10.150.420; Coronavirus nonstructural protein 4 C-terminus; 1.
DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR Gene3D; 1.10.1840.10; main proteinase (3clpro) structure, domain 3; 1.
DR Gene3D; 3.30.160.820; Nsp15 N-terminal domain-like; 1.
DR Gene3D; 1.10.8.370; nsp7 replicase; 1.
DR Gene3D; 3.30.70.3540; Nsp8 replicase, head domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 2.40.10.250; Replicase NSP9; 1.
DR Gene3D; 3.40.50.11020; Replicase polyprotein, nucleic acid-binding domain; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR InterPro; IPR046443; a/bCoV_NSP1_glob.
DR InterPro; IPR046440; AV_NSP11N_COV_NSP15M.
DR InterPro; IPR022570; B-CoV_A_NSP1.
DR InterPro; IPR046442; bCoV_NSP1_C.
DR InterPro; IPR043608; CoV_NSP15_M.
DR InterPro; IPR043606; CoV_NSP15_N.
DR InterPro; IPR043613; CoV_NSP2_C.
DR InterPro; IPR047573; CoV_NSP2_M.
DR InterPro; IPR043611; CoV_NSP3_C.
DR InterPro; IPR047566; CoV_NSP3_Y3.
DR InterPro; IPR032505; CoV_NSP4_C.
DR InterPro; IPR043612; CoV_NSP4_N.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR022733; DPUP_SUD_C_bCoV.
DR InterPro; IPR037227; EndoU-like.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR044371; Macro_X_NSP3-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; IPR036333; NSP10_sf_CoV.
DR InterPro; IPR047570; NSP12_IF_CoV.
DR InterPro; IPR044343; NSP13_1B_dom_CoV.
DR InterPro; IPR048673; NSP13_stalk_CoV.
DR InterPro; IPR048672; NSP13_ZBD_CoV.
DR InterPro; IPR027352; NSP13_ZBD_CoV-like.
DR InterPro; IPR044315; NSP14_betaCoV.
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; IPR044384; NSP2_MHV-like.
DR InterPro; IPR043615; NSP2_N_CoV.
DR InterPro; IPR044381; NSP3_DPUP_MHV.
DR InterPro; IPR047567; NSP3_G2M_bCoV.
DR InterPro; IPR032592; NSP3_NAB_bCoV.
DR InterPro; IPR042570; NSP3_NAB_bCoV_sf.
DR InterPro; IPR044357; NSP3_Ubl1_dom_CoV.
DR InterPro; IPR044353; Nsp3_Ubl2_dom_CoV.
DR InterPro; IPR038083; NSP3A-like.
DR InterPro; IPR038123; NSP4_C_sf_CoV.
DR InterPro; IPR044367; NSP6_betaCoV.
DR InterPro; IPR043610; NSP6_CoV.
DR InterPro; IPR014828; NSP7_CoV.
DR InterPro; IPR037204; NSP7_sf_CoV.
DR InterPro; IPR014829; NSP8_CoV.
DR InterPro; IPR037230; NSP8_sf_CoV.
DR InterPro; IPR014822; NSP9_CoV.
DR InterPro; IPR036499; NSP9_sf_CoV.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002705; Pept_C30/C16_B_coronavir.
DR InterPro; IPR013016; Peptidase_C16_CoV.
DR InterPro; IPR008740; Peptidase_C30_CoV.
DR InterPro; IPR043477; Peptidase_C30_dom3_CoV.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR043177; PLpro_N_sf_CoV.
DR InterPro; IPR043503; PLpro_palm_finger_dom_CoV.
DR InterPro; IPR043178; PLpro_thumb_sf_CoV.
DR InterPro; IPR046441; RdRp_CoV.
DR InterPro; IPR044347; RdRp_HCoV_HKU1-like.
DR InterPro; IPR009469; RdRp_N_CoV.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR018995; RNA_synth_NSP10_CoV.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF13604; AAA_30; 1.
DR Pfam; PF11963; B-CoV_A_NSP1; 1.
DR Pfam; PF16251; bCoV_NAB; 1.
DR Pfam; PF06471; CoV_ExoN; 1.
DR Pfam; PF06460; CoV_Methyltr_2; 1.
DR Pfam; PF09401; CoV_NSP10; 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; PF19212; CoV_NSP2_C; 1.
DR Pfam; PF19218; CoV_NSP3_C; 1.
DR Pfam; PF16348; CoV_NSP4_C; 1.
DR Pfam; PF19217; CoV_NSP4_N; 1.
DR Pfam; PF19213; CoV_NSP6; 1.
DR Pfam; PF08716; CoV_NSP7; 1.
DR Pfam; PF08717; CoV_NSP8; 1.
DR Pfam; PF08710; CoV_NSP9; 1.
DR Pfam; PF08715; CoV_peptidase; 1.
DR Pfam; PF06478; CoV_RPol_N; 1.
DR Pfam; PF01661; Macro; 1.
DR Pfam; PF01831; Peptidase_C16; 1.
DR Pfam; PF05409; Peptidase_C30; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR SMART; SM00506; A1pp; 1.
DR SUPFAM; SSF144246; Coronavirus NSP10-like; 1.
DR SUPFAM; SSF140367; Coronavirus NSP7-like; 1.
DR SUPFAM; SSF143076; Coronavirus NSP8-like; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF142877; EndoU-like; 1.
DR SUPFAM; SSF52949; Macro domain-like; 1.
DR SUPFAM; SSF159936; NSP3A-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF101816; Replicase NSP9; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51961; AV_NSP11N_COV_NSP15M; 1.
DR PROSITE; PS51963; BCOV_NSP1_C; 1.
DR PROSITE; PS51942; BCOV_NSP3C_C; 1.
DR PROSITE; PS51994; BCOV_NSP3E_G2M; 1.
DR PROSITE; PS51945; BCOV_NSP3E_NAB; 1.
DR PROSITE; PS51952; COV_EXON_MTASE_COACT; 1.
DR PROSITE; PS51954; COV_N7_MTASE; 1.
DR PROSITE; PS51962; COV_NSP1; 1.
DR PROSITE; PS52000; COV_NSP12_IF; 1.
DR PROSITE; PS51948; COV_NSP12_RDRP; 1.
DR PROSITE; PS51960; COV_NSP15_NTD; 1.
DR PROSITE; PS51991; COV_NSP2_C; 1.
DR PROSITE; PS51990; COV_NSP2_M; 1.
DR PROSITE; PS51989; COV_NSP2_N; 1.
DR PROSITE; PS51992; COV_NSP3_Y3; 1.
DR PROSITE; PS51943; COV_NSP3A_UBL; 1.
DR PROSITE; PS51944; COV_NSP3D_UBL; 1.
DR PROSITE; PS51946; COV_NSP4C; 1.
DR PROSITE; PS51949; COV_NSP7; 1.
DR PROSITE; PS51950; COV_NSP8; 1.
DR PROSITE; PS51951; COV_NSP9_SSRNA_BD; 1.
DR PROSITE; PS51653; CV_ZBD; 1.
DR PROSITE; PS51442; M_PRO; 1.
DR PROSITE; PS51154; MACRO; 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; PS51124; PEPTIDASE_C16; 2.
DR PROSITE; PS51657; PSRV_HELICASE; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 3: Inferred from homology;
KW Activation of host autophagy by virus {ECO:0000256|ARBA:ARBA00023050};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Decay of host mRNAs by virus {ECO:0000256|ARBA:ARBA00022616};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|PROSITE-
KW ProRule:PRU01303};
KW Eukaryotic host gene expression shutoff by virus
KW {ECO:0000256|ARBA:ARBA00023247};
KW Eukaryotic host translation shutoff by virus
KW {ECO:0000256|ARBA:ARBA00022809, ECO:0000256|PROSITE-ProRule:PRU01308};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|PROSITE-
KW ProRule:PRU01298}; Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW Host gene expression shutoff by virus {ECO:0000256|ARBA:ARBA00022995};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW Host mRNA suppression by virus {ECO:0000256|ARBA:ARBA00022557,
KW ECO:0000256|PROSITE-ProRule:PRU01308};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01303};
KW Inhibition of host innate immune response by virus
KW {ECO:0000256|ARBA:ARBA00022632, ECO:0000256|PROSITE-ProRule:PRU01308};
KW Inhibition of host interferon signaling pathway by virus
KW {ECO:0000256|ARBA:ARBA00022830, ECO:0000256|PROSITE-ProRule:PRU01308};
KW Inhibition of host ISG15 by virus {ECO:0000256|ARBA:ARBA00023208};
KW Inhibition of host NF-kappa-B by virus {ECO:0000256|ARBA:ARBA00022863};
KW Interferon antiviral system evasion {ECO:0000256|ARBA:ARBA00023208};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01299};
KW Modulation of host ubiquitin pathway by viral deubiquitinase
KW {ECO:0000256|ARBA:ARBA00022876};
KW Modulation of host ubiquitin pathway by virus
KW {ECO:0000256|ARBA:ARBA00022662};
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 Protease {ECO:0000256|ARBA:ARBA00022670};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ribosomal frameshifting {ECO:0000256|ARBA:ARBA00022758};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU01289};
KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01299};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Viral immunoevasion {ECO:0000256|ARBA:ARBA00023280, ECO:0000256|PROSITE-
KW ProRule:PRU01308}; Viral RNA replication {ECO:0000256|ARBA:ARBA00022953};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00444}.
FT TRANSMEM 2194..2219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2317..2339
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2351..2373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2755..2778
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3026..3051
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3063..3084
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3090..3112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3124..3143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3555..3578
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3590..3608
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3615..3636
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3656..3677
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3684..3702
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3722..3748
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3755..3774
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 54..196
FT /note="CoV Nsp1 globular"
FT /evidence="ECO:0000259|PROSITE:PS51962"
FT DOMAIN 216..246
FT /note="BetaCoV Nsp1 C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51963"
FT DOMAIN 250..514
FT /note="CoV Nsp2 N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51989"
FT DOMAIN 524..713
FT /note="CoV Nsp2 middle"
FT /evidence="ECO:0000259|PROSITE:PS51990"
FT DOMAIN 733..851
FT /note="CoV Nsp2 C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51991"
FT DOMAIN 853..966
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS51943"
FT DOMAIN 1036..1286
FT /note="Peptidase C16"
FT /evidence="ECO:0000259|PROSITE:PS51124"
FT DOMAIN 1264..1435
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT DOMAIN 1491..1563
FT /note="DPUP"
FT /evidence="ECO:0000259|PROSITE:PS51942"
FT DOMAIN 1562..1617
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS51944"
FT DOMAIN 1631..1892
FT /note="Peptidase C16"
FT /evidence="ECO:0000259|PROSITE:PS51124"
FT DOMAIN 1906..2007
FT /note="Nucleic acid-binding"
FT /evidence="ECO:0000259|PROSITE:PS51945"
FT DOMAIN 2020..2169
FT /note="G2M"
FT /evidence="ECO:0000259|PROSITE:PS51994"
FT DOMAIN 2647..2750
FT /note="CoV Nsp3 Y"
FT /evidence="ECO:0000259|PROSITE:PS51992"
FT DOMAIN 3149..3246
FT /note="Nsp4C"
FT /evidence="ECO:0000259|PROSITE:PS51946"
FT DOMAIN 3247..3549
FT /note="Peptidase C30"
FT /evidence="ECO:0000259|PROSITE:PS51442"
FT DOMAIN 3837..3925
FT /note="RdRp Nsp7 cofactor"
FT /evidence="ECO:0000259|PROSITE:PS51949"
FT DOMAIN 3926..4122
FT /note="RdRp Nsp8 cofactor"
FT /evidence="ECO:0000259|PROSITE:PS51950"
FT DOMAIN 4123..4232
FT /note="Nsp9 ssRNA-binding"
FT /evidence="ECO:0000259|PROSITE:PS51951"
FT DOMAIN 4233..4370
FT /note="ExoN/MTase coactivator"
FT /evidence="ECO:0000259|PROSITE:PS51952"
FT DOMAIN 4375..4630
FT /note="NiRAN"
FT /evidence="ECO:0000259|PROSITE:PS51947"
FT DOMAIN 4631..4729
FT /note="Nsp12 Interface"
FT /evidence="ECO:0000259|PROSITE:PS52000"
FT DOMAIN 4730..5297
FT /note="Nsp12 RNA-dependent RNA polymerase"
FT /evidence="ECO:0000259|PROSITE:PS51948"
FT DOMAIN 4977..5139
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT DOMAIN 5298..5381
FT /note="CV ZBD"
FT /evidence="ECO:0000259|PROSITE:PS51653"
FT DOMAIN 5553..5904
FT /note="(+)RNA virus helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51657"
FT DOMAIN 5971..6186
FT /note="ExoN"
FT /evidence="ECO:0000259|PROSITE:PS51953"
FT DOMAIN 6195..6421
FT /note="N7-MTase"
FT /evidence="ECO:0000259|PROSITE:PS51954"
FT DOMAIN 6422..6482
FT /note="Nsp15 N-terminal oligomerization"
FT /evidence="ECO:0000259|PROSITE:PS51960"
FT DOMAIN 6483..6603
FT /note="AV-Nsp11N/CoV-Nsp15M"
FT /evidence="ECO:0000259|PROSITE:PS51961"
FT DOMAIN 6654..6793
FT /note="NendoU"
FT /evidence="ECO:0000259|PROSITE:PS51958"
FT DOMAIN 6798..7092
FT /note="Nidovirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000259|PROSITE:PS51955"
FT REGION 970..1025
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 6308..6322
FT /note="GpppA-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01299"
FT COMPBIAS 970..986
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..1001
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 5989
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5991
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6090
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6167
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6172
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6684
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6699
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6739
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT BINDING 6230..6236
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01299"
SQ SEQUENCE 7095 AA; 797924 MW; 7ECB4C8750DC8082 CRC64;
MSKINKYGLE LHWAPEFPWM FEDAEEKLDN PSSSEVDMIC STTAQKLETD GICPENHVMV
DCRRLLKQEC CVQSSLIREI VMNASPYDLE VLLQDALQSR EAVLVTTPLG MSLEACYVRG
CNPKGWTMGL FRRRSVCNTG RCTVNKHVAY QLYMIDPAGV CLGAGQFVGW VIPLAFMPVQ
SRKFIVPWVM YLRKRGEKGA YNKDHGRGGF GHVYDFKVED AYDQVHDEPK GKFSKKAYAL
IRGYRGVKPL LYVDQYGCDY TGSLADGLEA YADKTLQEMK ALFPTWSQEL LFDVIVAWHV
VRDPRYVMRL QSAATIRSVA YVANPTEDLC NGSVVIKEPV HVYADDSIIL RQYNLVDIMS
HFYMEADTVV NAFYGVALKD CGFVMQFGYI DCEQDSCDFK GWIPGNMIDG FACTTCGHVY
EVGDLIAQSS GVLPVNPVLH TKSAAGYGGF GCKDSFTLYG QTVVYFGGCV YWSPARNIWI
PILKSSVKSY DSLVYTGVLG CKAIVKETNL ICKALYLDYV QHKCGNLHQR ELLGVSDVWH
KQLLLNRGVY KPLLENIDYF NMRRAKFSLE TFTVCADGFM PFLLDDLVPR AYYLAVSGQA
FCDYTDKLCH AVVSKSKELL DVSLDSLGAA IHYLNSKIVD LAQHFSDFGT SFVSKIVHFF
KTFTTSTALA FAWVLFHVLH GAYIVVESDI YFVKNIPRYA SAVAQAFQSV AKVVLDSLRV
TFIDGLSCFK IGRRRICLSG RKIYEIERGL LHSSQLPLDV YDLTMPSQVQ KAKQKPIYLK
GSGSDFSLAD SVVEVVTTSL TPCGYSEPPK VADKICIVDN VYMAKAGDKY YPVVVDDHVG
LLDQAWRVPC AGRRVTFKEQ PTVKEIISMP KIIKVFYELD NDFNTILNTA CGVFEVDDTV
DMEEFYAVVI DAIEEKLSPC KELEGVGAKV SAFLQKLEDN SLFLFDEAGE EVLAPKLYCA
FTAPEDDDFL EESDVEEDDV EDEETDLTVT SAGQPCVASE QEESSEVLED TLNDGPSVET
SDSQVEEDVE MSDFVDLESV IQDYENVCFE FYTTEPEFVK VLGLYVPKAT RNNCWLRSVL
AVMQKLPCQF KDKNLQDLWV LYKQQYSQLF VDTLVNKIPA NIVLPQGGYV ADFAYWFLTL
CDWQCVAYWK CIKCDLALKL KGLDAMFFYG DVVSHICKCG ESMVLIDVDV PFTAHFALKD
KLFCAFITKR IVYKAACVVD VNDSHSMAVV DGKQIDDHRI TSITSDKFDF IIGHGMSFSM
TTFEIAQLYG SCITPNVCFV KGDIIKVSKL VKAEVVVNPA NGHMAHGGGV AKAIAVAAGQ
QFVKETTDMV KSKGVCATGD CYVSTGGKLC KTVLNVVGPD ARTQGKQSYV LLERVYKHFN
NYDCVVTTLI SAGIFSVPSD VSLTYLLGTA KKQVVLVSNN QEDFDLISKC QITAVEGTKK
LAARLSFNVG RSIVYETDAN KLILINDVAF VSTFNVLQDV LSLRHDIALD DDARTFVQSN
VDVVPEGWRV VNKFYQINGV RTVKYFECTG GIDICSQDKV FGYVQQGIFN KATVAQIKAL
FLDKVDILLT VDGVNFTNRF VPVGESFGKS LGNVFCDGVN VTKHKCDINY KGKVFFQFDN
LSSEDLKAVR SSFNFDQKEL LAYYNMLVSC FKWQVVVNGK YFTFKQANNN CFVNVSCLML
QSLHLTFKIV QWQEAWLEFR SGRPARFVAL VLAKGGFKFG DPADSRDFLR VVFSQVDLTG
AICDFEIACK CGVKQEQRTG LDAVMHFGTL SREDLEIGYT VDCSCGKKLI HCVRFDVPFL
ICSNTPASVK LPKGVGSANI FIGDKVGHYV HVKCEQSYQL YDASNVKKVT DVTGKLSDCL
YFKNLKQTFK SVLTTYYLDD VKKIEYKPDL SQYYCDGGKY YTQRIIKAQF KTFEKVDGVY
TNFKLIGHTV CDSLNAKLGF DSSKEFVEYK ITEWPTATGD VVLATDDLYV KRYERGCITF
GKPVIWLSHE KASLNSLTYF NRSSLVDDNK FDVLKVDDVD DGVDSSEGDA KETKEINIIK
LSGVKKPFKV EDSVIVNDDT SETKYVKSLS IVDVYDMWLT GCKYVVRTAN ALSRAVNVPT
IRKFIKFGMT LVSIPIDLLN LREIKPAVNV VKAVRNKISA CFNFIKWLFV LLFGWIKISA
DNKVIYTTEI ASKLTCKLVA LAFKNAFLTF KWSMVARGAC IIATIFLLWF NFIYANVIFS
DFYLPKIGFL PTFVGKIAQW IKNTFSLVTI CDLYSIQDVG FKNQHCNGSI ACQFCLAGFD
MLDNYKAIDV VQYEADRRAF VDYTGVLKIV IELIVSYALY TAWFYPLFAL ISIQILTTWL
PELFMLSTLH WSFRLLVALA NMLPAHVFMR FYIIIASFTK LFSLFRHVAY GCNKSGCLFC
YKRNRSLRVK CSTIVGGMIR YYDVMANGGT GFCSKHQWNC IDCDSYKPGN TFITVEAALD
LSKELKRPIQ PTDVAYHTVT DVKQVGCSMR LFYDRDGQRT YDDVNASLFV DYSNLLHSKV
KSVPNMHVVV VENDADKANF LNAAVFYAQS LFRPILMVDK NLITTANTGT SVTETMFDVY
VDTFLSMFDV DKKSLNALIA TAHSSIKQGT QIYKVLDTFL SCARKSCSID SDVDTKCLAD
SVMSAVSAGL ELTDESCNNL VPTYLKSDNI VAADLGVLIQ NSAKHVQGNV AKLAGVSCIW
SVDAFNQFSS DFQHKLKKAC CKTGLKLKLT YNKQMANVSV LTTPFSLKGG AVFSYFVYVC
FVLSLICFIG LWCLMPTYTV HKSDFQLPVY ASYKVLDNGV IRDVSVEDVC FANKFEQFDQ
WYESTFGLSY YSNSMACPIV VAVIDQDFGS TVFNVPTKVL RYGYHVLHFI THALSADGVQ
CYTPHSQISY SNFYASGCVL SSACTMFTMA DGSPQPYCYT EGLMQNASLY SSLVPHVRYN
LANAKGFIRF PEVLREGLVR IVRTRSMSYC RVGLCEEADE GICFNFNGSW VLNNDYYRSL
PGTFCGRDVF DLIYQLFKGL AQPVDFLALT ASSIAGAILA VIVVLVFYYL IKLKRAFGDY
TSVVFVNVIV WCVNFMMLFV FQVYPTLSCV YAICYFYVTL YFPSEISVIM HLQWLVMYGT
IMPLWFCLLY IAVVVSNHAF WVFSYCRKLG TSVRSDGTFE EMALTTFMIT KDSYCKLKNS
LSDVAFNRYL SLYNKYRYYS GKMDTAAYRE AACSQLAKAM DTFTNNNGSD VLYQPPTASV
STSFLQSGIV KMVNPTSKVE PCVVSVTYGN MTLNGLWLDD KVYCPRHVIC SASDMTNPDY
TNLLCRVTSS DFTVLFDRLS LTVMSYQMRG CMLVLTVTLQ NSRTPKYTFG VVKPGETFTV
LAAYNGKPQG AFHVTMRSSY TIKGSFLCGS CGSVGYVIMG DCVKFVYMHQ LELSTGCHTG
TDFNGDFYGP YKDAQVVQLP IQDYIQSVNF VAWLYAAILN NCNWFVQSDK CSVEDFNVWA
LSNGFSQVKS DLVIDALASM TGVSLETLLA AIKRLKNGFQ GRQIMGSCSF EDELTPSDVY
QQLAGIKLQS KRTRLFKGTV CWIMASTFLF SCIITAFVKW TMFMYVTTNM LSITFCALCV
ISLAMLLVKH KHLYLTMYIT PVLFTLLYNN YLVVYKHTFR GYVYAWLSYY VPSVEYTYTD
EVIYGMLLLV GMVFVTLRSI NHDLFSFIMF VGRLISVFSL WYKGSNLEEE ILLMLASLFG
TYTWTTVLSM AVAKVIAKWV AVNVLYFTDI PQIKVVLLCY LFIGYIISCY WGLFSLMNSL
FRMPLGVYNY KISVQELRYM NANGLRPPKN SFEALMLNFK LLGIGGVPII EVSQFQSKLT
DVKCANVVLL NCLQHLHVAS NSKLWQYCST LHNEILATSD LSVAFEKLAQ LLIVLFANPA
AVDSKCLTSI EEVCDDYAKD NTVLQALQSE FVNMASFVEY EVAKKNLDEA RFSGSANQQQ
LKQLEKACNI AKSAYERDRA VAKKLERMAD LALTNMYKEA RINDKKSKVV SALQTMLFSM
VRKLDNQALN SILDNAVKGC VPLNAIPSLA ANTLNIIVPD KSVYDQVVDN VYVTYAGNVW
QIQTIQDSDG TNKQLNEISD DCNWPLVIIA NRYNEVSATV LQNNELMPAK LKIQVVNSGP
DQTCNTPTQC YYNNSNNGKI VYAILSDVDG LKYTKILKDD GNFVVLELDP PCKFTVQDAK
GLKIKYLYFV KGCNTLARGW VVGTISSTVR LQAGTATEYA SNSSILSLCA FSVDPKKTYL
DFIQQGGTPI ANCVKMLCDH AGTGMAITVK PDATTSQDSY GGASVCIYCR ARVEHPDVDG
LCKLRGKFVQ VPVGIKDPVS YVLTHDVCRV CGFWRDGSCS CVSTDTTVQS KDTNFLNRVR
GTSVDARLVP CASGLSTDVQ LRAFDIYNAN VAGIGLHLKV NCCRFQRVDE NGDKLDQFFV
VKRTDLTIYN REMKCYERVK DCKFVAEHDF FTFDVEGSRV PHIVRKDLTK YTMLDLCYAL
RHFDRNDCML LCDILSIYAG CEQSYFTKKD WYDFVENPDI INVYKKLGPI FNRALVSATE
FADKLVEVGL VGVLTLDNQD LNGKWYDFGD YVIAAPGCGV AIADSYYSYI MPMLTMCHAL
DCELYVNNAY RLFDLVQYDF TDYKLELFNK YFKHWSMPYH PNTVDCQDDR CIIHCANFNI
LFSMVLPNTC FGPLVRQIFV DGVPFVVSIG YHYKELGIVM NMDVDTHRYR LSLKDLLLYA
ADPALHVASA SALYDLRTCC FSVAAITSGV KFQTVKPGNF NQDFYDFVLS KGLLKEGSSV
DLKHFFFTQD GNAAITDYNY YKYNLPTMVD IKQLLFVLEV VYKYFEIYDG GCIPASQVIV
NNYDKSAGYP FNKFGKARLY YEALSFEEQD EIYAYTKRNV LPTLTQMNLK YAISAKNRAR
TVAGVSILST MTGRMFHQKC LKSIAATRGV PVVIGTTKFY GGWDDMLRRL IKDVDNPVLM
GWDYPKCDRA MPNLLRIVSS LVLARKHETC CSQSDRFYRL ANECAQVLSE IVMCGGCYYV
KPGGTSSGDA TTAFANSVFN ICQAVSANVC ALMSCNGNKI EDLSIRALQK RLYSHVYRSD
KVDSTFVTEY YEFLNKHFSM MILSDDGVVC YNSDYASKGY IANISAFQQV LYYQNNVFMS
ESKCWVEHDI NNGPHEFCSQ HTMLVKMDGD DVYLPYPNPS RILGAGCFVD DLLKTDSVLL
IERFVSLAID AYPLVYHENE EYQKVFRVYL AYIKKLYNDL GNQILDSYSV ILSTCDGQKF
TDESFYKNMY LRSAVMQSVG ACVVCSSQTS LRCGSCIRKP LLCCKCCYDH VMATDHKYVL
SVSPYVCNAP GCDVNDVTKL YLGGMSYYCE DHKPQYSFKL VMNGLVFGLY KQSCTGSPYI
DDFNRIASCK WTDVDDYILA NECTERLKLF AAETQKATEE AFKQSYASAT IQEIVSEREL
ILSWEIGKVK PPLNKNYVFT GYHFTKNGKT VLGEYVFDKS ELTNGVYYRA TTTYKLSVGD
VFVLTSHSVA NLSAPTLVPQ ENYSSIRFAS VYSVLETFQN NVVNYQHIGM KRYCTVQGPP
GTGKSHLAIG LAVFYCTARV VYTAASHAAV DALCEKAYKF LNINDCTRII PAKVRVECYD
KFKINDTTRK YVFTTINALP EMVTDIVIVD EVSMLTNYEL SVINARIRAK HYVYIGDPAQ
LPAPRVLLSK GTLEPKYFNT VTKLMCCLGP DIFLGTCYRC PKEIVDTVSA LVYENKLKAK
NESSSLCFKV YYKGVTTHES SSAVNMQQIY LINKFLKANP LWHKAVFISP YNSQNFAAKR
VLGLQTQTVD SAQGSEYDYV IYSQTAETAH SVNVNRFNVA ITRAKKGILC VMSNMQLFEA
LQFTTLTLDK VPQAVETKVQ CSTNLFKDCS NSYSGYHPAH APSFLAVDDK YKATGDLAVC
LGIGDSAVTY SRLISLMGFK LDVTLDGYCK LFITKEEAVK RVRAWVGFDA EGAHATRDSI
GTNFPLQLGF STGIDFVVEA TGLFADRDGY SFKKAVAKAP PGEQFKHLIP LMTRGHRWDV
VRPRIVQMFA DHLIDLSDCV VLVTWAANFE LTCLRYFAKV GREISCNVCT KRATVYNSRT
GYYGCWRHSV TCDYLYNPLI VDIQQWGYIG SLSSNHDLYC SVHKGAHVAS SDAIMTRCLA
VYDCFCNNIN WNVEYPIISN ELSINTSCRV LQRVILKAAM LCNRYTLCYD IGNPKAIACV
KDFDFKFYDA QPIVKSVKTL LYSFEAHKDS FKDGLCMFWN CNVDKYPPNA VVCRFDTRVL
NNLNLPGCNG GSLYVNKHAF HTKPFARAAF EYLKPMPFFY YSDTPCVYMD GMDAKQVDYV
PLKSATCITR CNLGGAVCLK HAEEYREYLE SYNTATTAGF TFWVYKTFDF YNLWNTFTKL
QSLENVVYNL VKTGHYTGQA GEMPCAIIND KVVAKIDKED VVIFINNTTY PTNVAVELFA
KRSVRHHPEL KLFRNLNIDV CWKHVIWDYA RESIFCSNTY GVCIYTDLKF IDKLNVLFDG
RDNGALEAFK RSNNGVYIST TKVKSLSMIR GPPRAELNGV VVDKVGDTDC VFYFAVRKEG
QDVIFSQFDS LGVSSNQSPQ GNLGSNGKPG NVGGNDALSI STIFTQSRVI SSFTCRTDME
KDFIALDQDV FIQKYGLEDY AFEHIVYGNF NQKIIGGLHL LIGLYRRQQT SNLVAQEFVS
YDSSIHSYFI TDEKSGGSKS VCTVIDILLD DFVALVKSLN LNCVSKVVNV NVDFKDFQFM
LWCNDEKVMT FYPRLQAASD WKPGYSMPVL YKYLNSPMER VSLWNYGKPV TLPTGCMMNV
AKYTQLCQYL NTTTLAVPVN MRVLHLGAGS EKGVAPGSAV LRQWLPAGTI LVDNDLYPFV
SDSVATYFGD CITLPFDCQW DLIISDMYDP ITKNIGEYNV SKDGFFTYIC HMIRDKLALG
GSVAIKITEF SWNAELYKLM GYFAFWTVFC TNANASSSEG FLIGINYLCK PKVEIDGNVM
HANYLFWRNS TVWNGGAYSL FDMAKFPLKL AGTAVINLRA DQINDMVYSL LEKGKLLIRD
TNKEVFVGDS LVNVI
//
