R1AB_BCHK9
ID R1AB_BCHK9 Reviewed; 6930 AA.
AC P0C6W5; A3EXG5;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Replicase polyprotein 1ab;
DE Short=pp1ab;
DE AltName: Full=ORF1ab polyprotein;
DE Contains:
DE RecName: Full=Host translation inhibitor nsp1;
DE Short=nsp1;
DE AltName: Full=Leader protein;
DE Contains:
DE RecName: Full=Non-structural protein 2;
DE Short=nsp2;
DE AltName: Full=p65 homolog;
DE Contains:
DE RecName: Full=Papain-like proteinase;
DE Short=PL-PRO;
DE EC=3.4.19.12;
DE EC=3.4.22.-;
DE AltName: Full=Non-structural protein 3;
DE Short=nsp3;
DE Contains:
DE RecName: Full=Non-structural protein 4;
DE Short=nsp4;
DE Contains:
DE RecName: Full=3C-like proteinase;
DE Short=3CL-PRO;
DE Short=3CLp;
DE EC=3.4.22.-;
DE AltName: Full=nsp5;
DE Contains:
DE RecName: Full=Non-structural protein 6;
DE Short=nsp6;
DE Contains:
DE RecName: Full=Non-structural protein 7;
DE Short=nsp7;
DE Contains:
DE RecName: Full=Non-structural protein 8;
DE Short=nsp8;
DE Contains:
DE RecName: Full=Non-structural protein 9;
DE Short=nsp9;
DE Contains:
DE RecName: Full=Non-structural protein 10;
DE Short=nsp10;
DE AltName: Full=Growth factor-like peptide;
DE Short=GFL;
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase;
DE Short=Pol;
DE Short=RdRp;
DE EC=2.7.7.48;
DE AltName: Full=nsp12;
DE Contains:
DE RecName: Full=Helicase;
DE Short=Hel;
DE EC=3.6.4.12;
DE EC=3.6.4.13;
DE AltName: Full=nsp13;
DE Contains:
DE RecName: Full=Guanine-N7 methyltransferase;
DE Short=ExoN;
DE EC=2.1.1.-;
DE EC=3.1.13.-;
DE AltName: Full=nsp14;
DE Contains:
DE RecName: Full=Uridylate-specific endoribonuclease;
DE EC=4.6.1.-;
DE AltName: Full=NendoU;
DE AltName: Full=nsp15;
DE Contains:
DE RecName: Full=2'-O-methyltransferase;
DE EC=2.1.1.57;
DE AltName: Full=nsp16;
GN Name=rep; ORFNames=1a-1b;
OS Bat coronavirus HKU9 (BtCoV) (BtCoV/HKU9).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Nobecovirus.
OX NCBI_TaxID=694006;
OH NCBI_TaxID=9408; Rousettus leschenaultii (Leschenault's rousette).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate HKU9-1;
RX PubMed=17121802; DOI=10.1128/jvi.02182-06;
RA Woo P.C.Y., Wang M., Lau S.K.P., Xu H.F., Poon R.W.S., Guo R., Wong B.H.L.,
RA Gao K., Tsoi H.-W., Huang Y., Li K.S.M., Lam C.S.F., Chan K.-H.,
RA Zheng B.-J., Yuen K.-Y.;
RT "Comparative analysis of twelve genomes of three novel group 2c and group
RT 2d coronaviruses reveals unique group and subgroup features.";
RL J. Virol. 81:1574-1585(2007).
RN [2]
RP FUNCTION OF NSP1.
RX PubMed=19264783; DOI=10.1128/jvi.02485-08;
RA Tohya Y., Narayanan K., Kamitani W., Huang C., Lokugamage K., Makino S.;
RT "Suppression of host gene expression by nsp1 proteins of group 2 bat
RT coronaviruses.";
RL J. Virol. 83:5282-5288(2009).
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:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Host translation inhibitor nsp1]: Inhibits host translation
CC by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome
CC complex further induces an endonucleolytic cleavage near the 5'UTR of
CC host mRNAs, targeting them for degradation. Viral mRNAs are not
CC susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the
CC presence of a 5'-end leader sequence and are therefore protected from
CC degradation. By suppressing host gene expression, nsp1 facilitates
CC efficient viral gene expression in infected cells and evasion from host
CC immune response. {ECO:0000250|UniProtKB:P0C6X7,
CC ECO:0000269|PubMed:19264783}.
CC -!- FUNCTION: [Non-structural protein 2]: May play a role in the modulation
CC of host cell survival signaling pathway by interacting with host PHB
CC and PHB2. Indeed, these two proteins play a role in maintaining the
CC functional integrity of the mitochondria and protecting cells from
CC various stresses. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Papain-like proteinase]: Responsible for the cleavages
CC located at the N-terminus of the replicase polyprotein. In addition,
CC PL-PRO possesses a deubiquitinating/deISGylating activity and processes
CC both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular
CC substrates. Participates together with nsp4 in the assembly of virally-
CC induced cytoplasmic double-membrane vesicles necessary for viral
CC replication. Antagonizes innate immune induction of type I interferon
CC by blocking the phosphorylation, dimerization and subsequent nuclear
CC translocation of host IRF3. Prevents also host NF-kappa-B signaling.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Non-structural protein 4]: Participates in the assembly of
CC virally-induced cytoplasmic double-membrane vesicles necessary for
CC viral replication. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [3C-like proteinase]: Cleaves the C-terminus of replicase
CC polyprotein at 11 sites. Recognizes substrates containing the core
CC sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''-
CC phosphate (ADRP). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000255|PROSITE-
CC ProRule:PRU00772}.
CC -!- FUNCTION: [Non-structural protein 6]: Plays a role in the initial
CC induction of autophagosomes from host reticulum endoplasmic. Later,
CC limits the expansion of these phagosomes that are no longer able to
CC deliver viral components to lysosomes. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8
CC subunits of each) that may participate in viral replication by acting
CC as a primase. Alternatively, may synthesize substantially longer
CC products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8
CC subunits of each) that may participate in viral replication by acting
CC as a primase. Alternatively, may synthesize substantially longer
CC products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Non-structural protein 9]: May participate in viral
CC replication by acting as a ssRNA-binding protein.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Non-structural protein 10]: Plays a pivotal role in viral
CC transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16
CC 2'-O-methyltransferase activities. Therefore plays an essential role in
CC viral mRNAs cap methylation. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [RNA-directed RNA polymerase]: Responsible for replication
CC and transcription of the viral RNA genome.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Helicase]: Multi-functional protein with a zinc-binding
CC domain in N-terminus displaying RNA and DNA duplex-unwinding activities
CC with 5' to 3' polarity. Activity of helicase is dependent on magnesium.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Guanine-N7 methyltransferase]: Enzyme possessing two
CC different activities: an exoribonuclease activity acting on both ssRNA
CC and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase
CC activity. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Uridylate-specific endoribonuclease]: Plays a role in viral
CC transcription/replication and prevents the simultaneous activation of
CC host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By
CC similarity). Acts by degrading the 5'-polyuridines generated during
CC replication of the poly(A) region of viral genomic and subgenomic RNAs.
CC Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'-
CC cP) is first generated by 2'-O transesterification, which is then
CC hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded,
CC poly(U) RNA would hybridize with poly(A) RNA tails and activate host
CC dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [2'-O-methyltransferase]: Methyltransferase that mediates
CC mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral
CC mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16.
CC Therefore plays an essential role in viral mRNAs cap methylation which
CC is essential to evade immune system. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- CATALYTIC ACTIVITY: [RNA-directed RNA polymerase]:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC -!- CATALYTIC ACTIVITY: [Helicase]:
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 -!- CATALYTIC ACTIVITY: [Helicase]:
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 -!- CATALYTIC ACTIVITY: [Papain-like proteinase]:
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;
CC -!- CATALYTIC ACTIVITY: [2'-O-methyltransferase]:
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:0000250|UniProtKB:P0C6X7};
CC -!- CATALYTIC ACTIVITY: [Uridylate-specific endoribonuclease]:
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:0000250|UniProtKB:P0C6X7};
CC -!- COFACTOR: [Uridylate-specific endoribonuclease]:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P0C6X7};
CC Note=Likely affects Nsp15 binding to RNA.
CC {ECO:0000250|UniProtKB:P0C6X7};
CC -!- SUBUNIT: Nsp2 interacts with host PHB and PHB2. 3CL-PRO exists as
CC monomer and homodimer. Nsp4 interacts with PL-PRO and nsp6. Only the
CC homodimer shows catalytic activity. Eight copies of nsp7 and eight
CC copies of nsp8 assemble to form a heterohexadecamer dsRNA-encircling
CC ring structure. Nsp9 is a dimer. Nsp10 forms a dodecamer and interacts
CC with nsp14 and nsp16; these interactions enhance nsp14 and nsp16
CC enzymatic activities. Nsp14 interacts (via N-terminus) with DDX1.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SUBCELLULAR LOCATION: [Papain-like proteinase]: Host membrane; Multi-
CC pass membrane protein. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 4]: Host membrane; Multi-
CC pass membrane protein. Host cytoplasm. Note=Localizes in virally-
CC induced cytoplasmic double-membrane vesicles.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 6]: Host membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 7]: Host cytoplasm, host
CC perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC they merge into confluent complexes (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 8]: Host cytoplasm, host
CC perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC they merge into confluent complexes (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 9]: Host cytoplasm, host
CC perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC they merge into confluent complexes (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 10]: Host cytoplasm, host
CC perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC they merge into confluent complexes (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Helicase]: Host endoplasmic reticulum-Golgi
CC intermediate compartment {ECO:0000305}. Note=The helicase interacts
CC with the N protein in membranous complexes and colocalizes with sites
CC of synthesis of new viral RNA. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Uridylate-specific endoribonuclease]: Host
CC cytoplasm, host perinuclear region {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
CC IsoId=P0C6W5-1; Sequence=Displayed;
CC Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
CC IsoId=P0C6T6-1; Sequence=External;
CC -!- DOMAIN: The hydrophobic domains (HD) could mediate the membrane
CC association of the replication complex and thereby alter the
CC architecture of the host cell membrane. {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages in vivo by its own proteases yield
CC mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically
CC processed (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform Replicase polyprotein 1ab]: Produced by -1
CC ribosomal frameshifting at the 1a-1b genes boundary.
CC -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
CC {ECO:0000305}.
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DR EMBL; EF065513; ABN10910.1; -; Genomic_RNA.
DR RefSeq; YP_001039970.1; NC_009021.1. [P0C6W5-1]
DR PDB; 5UTV; NMR; -; A=1345-1418.
DR PDBsum; 5UTV; -.
DR SMR; P0C6W5; -.
DR IntAct; P0C6W5; 1.
DR BindingDB; P0C6W5; -.
DR GeneID; 4836014; -.
DR KEGG; vg:4836014; -.
DR Proteomes; UP000006576; Genome.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
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:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0004532; F:exoribonuclease activity; IEA:InterPro.
DR GO; GO:0002151; F:G-quadruplex RNA binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IEA:UniProt.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
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-directed 5'-3' 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:0039595; P:induction by virus of catabolism of host mRNA; IEA:UniProtKB-KW.
DR GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0039648; P:modulation by virus 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-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
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; cd21596; batCoV-HKU9-like_RdRp; 1.
DR CDD; cd21560; betaCoV-Nsp6; 1.
DR CDD; cd21659; betaCoV_Nsp14; 1.
DR CDD; cd21666; betaCoV_Nsp5_Mpro; 1.
DR CDD; cd20762; capping_2-OMTase_Nidovirales; 1.
DR CDD; cd21518; cv_beta_Nsp2_HKU9-like; 1.
DR CDD; cd21473; cv_Nsp4_TM; 1.
DR CDD; cd21167; M_alpha_beta_cv_Nsp15-like; 1.
DR CDD; cd21563; Macro_cv_SUD-M_Nsp3-like; 1.
DR CDD; cd21557; Macro_X_Nsp3-like; 1.
DR CDD; cd21161; NendoU_cv_Nsp15-like; 1.
DR CDD; cd21171; NTD_alpha_beta_cv_Nsp15-like; 1.
DR CDD; cd21537; SUD_C_HKU9_CoV_Nsp3; 1.
DR CDD; cd21467; Ubl1_cv_Nsp3_N-like; 1.
DR CDD; cd21466; Ubl2_cv_PLpro_N_Nsp3-like; 1.
DR CDD; cd21401; ZBD_cv_Nsp13-like; 1.
DR Gene3D; 1.10.150.420; -; 1.
DR Gene3D; 1.10.1840.10; -; 1.
DR Gene3D; 1.10.8.1190; -; 1.
DR Gene3D; 1.10.8.370; -; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 2.40.10.250; -; 1.
DR Gene3D; 2.60.120.1680; -; 1.
DR Gene3D; 3.10.20.350; -; 1.
DR Gene3D; 3.10.20.540; -; 1.
DR Gene3D; 3.30.160.820; -; 1.
DR Gene3D; 3.30.70.3540; -; 1.
DR Gene3D; 3.40.220.10; -; 1.
DR Gene3D; 3.40.220.20; -; 1.
DR Gene3D; 3.40.50.11020; -; 1.
DR Gene3D; 3.40.50.11580; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR InterPro; IPR043608; CoV_NSP15_M.
DR InterPro; IPR043606; CoV_NSP15_N.
DR InterPro; IPR043613; CoV_NSP2_C.
DR InterPro; IPR043611; CoV_NSP3_C.
DR InterPro; IPR032505; CoV_NSP4_C.
DR InterPro; IPR043612; CoV_NSP4_N.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
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; IPR043609; NendoU_nidovirus.
DR InterPro; IPR044863; NIRAN.
DR InterPro; IPR036333; NSP10_sf_CoV.
DR InterPro; IPR044343; NSP13_1B_dom_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; IPR021590; NSP1_bCoV.
DR InterPro; IPR044386; NSP2_HKU9-like.
DR InterPro; IPR043615; NSP2_N_CoV.
DR InterPro; IPR024375; NSP3_bCoV.
DR InterPro; IPR032592; NSP3_NAB_bCoV.
DR InterPro; IPR042570; NSP3_NAB_bCoV_sf.
DR InterPro; IPR038400; NSP3_SUD-M_sf_bCoV.
DR InterPro; IPR044352; Nsp3_SUD_C_HKU9_CoV.
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; 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; IPR044349; RdRp_batCoV_HKU9-like.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR009469; RNA_pol_N_CoV.
DR InterPro; IPR018995; RNA_synth_NSP10_CoV.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF11501; bCoV_NSP1; 1.
DR Pfam; PF11633; bCoV_SUD_M; 1.
DR Pfam; PF06471; CoV_ExoN; 1.
DR Pfam; PF06460; CoV_Methyltr_2; 1.
DR Pfam; PF09401; CoV_NSP10; 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; PF19211; CoV_NSP2_N; 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; PF05409; Peptidase_C30; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF01443; Viral_helicase1; 1.
DR SMART; SM00506; A1pp; 1.
DR SUPFAM; SSF101816; SSF101816; 1.
DR SUPFAM; SSF140367; SSF140367; 1.
DR SUPFAM; SSF142877; SSF142877; 1.
DR SUPFAM; SSF143076; SSF143076; 1.
DR SUPFAM; SSF144246; SSF144246; 1.
DR SUPFAM; SSF159936; SSF159936; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF52949; SSF52949; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF56672; SSF56672; 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; PS51941; BCOV_NSP3C_M; 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; 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; 1.
DR PROSITE; PS51657; PSRV_HELICASE; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activation of host autophagy by virus; ATP-binding;
KW Decay of host mRNAs by virus; Endonuclease;
KW Eukaryotic host gene expression shutoff by virus;
KW Eukaryotic host translation shutoff by virus; Exonuclease; Helicase;
KW Host cytoplasm; Host gene expression shutoff by virus; Host membrane;
KW Host mRNA suppression by virus; Host-virus interaction; Hydrolase;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host interferon signaling pathway by virus;
KW Inhibition of host ISG15 by virus; Inhibition of host NF-kappa-B by virus;
KW Lyase; Membrane; Metal-binding; Methyltransferase;
KW Modulation of host ubiquitin pathway by viral deubiquitinase;
KW Modulation of host ubiquitin pathway by virus; Nuclease;
KW Nucleotide-binding; Nucleotidyltransferase; Protease; Reference proteome;
KW Repeat; Ribosomal frameshifting; RNA-binding; RNA-directed RNA polymerase;
KW Thiol protease; Transferase; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway; Viral immunoevasion; Viral RNA replication; Zinc;
KW Zinc-finger.
FT CHAIN 1..175
FT /note="Host translation inhibitor nsp1"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000291350"
FT CHAIN 176..772
FT /note="Non-structural protein 2"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000291351"
FT CHAIN 773..2609
FT /note="Papain-like proteinase"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000291352"
FT CHAIN 2610..3103
FT /note="Non-structural protein 4"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000291353"
FT CHAIN 3104..3409
FT /note="3C-like proteinase"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000291354"
FT CHAIN 3410..3699
FT /note="Non-structural protein 6"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000291355"
FT CHAIN 3700..3782
FT /note="Non-structural protein 7"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000291356"
FT CHAIN 3783..3982
FT /note="Non-structural protein 8"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000291357"
FT CHAIN 3983..4094
FT /note="Non-structural protein 9"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000291358"
FT CHAIN 4095..4233
FT /note="Non-structural protein 10"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000291359"
FT CHAIN 4234..5165
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000291360"
FT CHAIN 5166..5766
FT /note="Helicase"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000291361"
FT CHAIN 5767..6296
FT /note="Guanine-N7 methyltransferase"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000291362"
FT CHAIN 6297..6633
FT /note="Uridylate-specific endoribonuclease"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000291363"
FT CHAIN 6634..6930
FT /note="2'-O-methyltransferase"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000291364"
FT TRANSMEM 2015..2035
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2040..2060
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2081..2101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2162..2182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2183..2203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2218..2238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2621..2641
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2719..2739
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2865..2885
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2887..2907
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2916..2936
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2946..2966
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2970..2990
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3423..3443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3449..3469
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3474..3494
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3517..3537
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3569..3589
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3592..3612
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3620..3640
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 10..131
FT /note="CoV Nsp1 globular"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01307"
FT DOMAIN 149..175
FT /note="BetaCoV Nsp1 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01308"
FT DOMAIN 177..431
FT /note="CoV Nsp2 N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT DOMAIN 432..644
FT /note="CoV Nsp2 middle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01334"
FT DOMAIN 646..772
FT /note="CoV Nsp2 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01335"
FT DOMAIN 775..885
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 930..1097
FT /note="Macro 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1216..1340
FT /note="Macro 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1345..1417
FT /note="DPUP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01289"
FT DOMAIN 1423..1478
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1492..1757
FT /note="Peptidase C16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT DOMAIN 1770..1870
FT /note="Nucleic acid-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01290"
FT DOMAIN 1883..2012
FT /note="G2M"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01338"
FT DOMAIN 2507..2609
FT /note="CoV Nsp3 Y3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT DOMAIN 3007..3103
FT /note="Nsp4C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01291"
FT DOMAIN 3104..3409
FT /note="Peptidase C30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT DOMAIN 3700..3782
FT /note="RdRp Nsp7 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01294"
FT DOMAIN 3783..3982
FT /note="RdRp Nsp8 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01295"
FT DOMAIN 3983..4094
FT /note="Nsp9 ssRNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01296"
FT DOMAIN 4095..4233
FT /note="ExoN/MTase coactivator"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT DOMAIN 4239..4494
FT /note="NiRAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01292"
FT DOMAIN 4598..5165
FT /note="Nsp12 RNA-dependent RNA polymerase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT DOMAIN 4845..5007
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 5166..5249
FT /note="CV ZBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT DOMAIN 5412..5603
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 5604..5778
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 5838..6056
FT /note="ExoN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT DOMAIN 6065..6296
FT /note="N7-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT DOMAIN 6297..6357
FT /note="Nsp15 N-terminal oligomerization"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01305"
FT DOMAIN 6358..6476
FT /note="AV-Nsp11N/CoV-Nsp15M"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01306"
FT DOMAIN 6493..6630
FT /note="NendoU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT DOMAIN 6635..6928
FT /note="Nidovirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ZN_FING 1610..1647
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ZN_FING 4168..4184
FT /evidence="ECO:0000250"
FT ZN_FING 4211..4224
FT /evidence="ECO:0000250"
FT REGION 312..333
FT /note="C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT REGION 1188..1207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2015..2238
FT /note="HD1"
FT /evidence="ECO:0000250"
FT REGION 2621..2990
FT /note="HD2"
FT /evidence="ECO:0000250"
FT REGION 3423..3640
FT /note="HD3"
FT /evidence="ECO:0000250"
FT REGION 6180..6194
FT /note="GpppA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT ACT_SITE 1533
FT /note="For PL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1694
FT /note="For PL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 3144
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT ACT_SITE 3248
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT ACT_SITE 4992
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 4993
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 4994
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 5856
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5858
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5957
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6037
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6042
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6523
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6537
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6576
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6679
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6763
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6803
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6836
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 331
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 4168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 5170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5215
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5447..5454
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 5973
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5976
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5992
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5995
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6026
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6030
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6033
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6048
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6100..6106
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6242
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT SITE 175..176
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 772..773
FT /note="Cleavage; by PL-PRO"
FT /evidence="ECO:0000255"
FT SITE 2609..2610
FT /note="Cleavage; by PL-PRO"
FT /evidence="ECO:0000255"
FT SITE 3103..3104
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 3409..3410
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 3699..3700
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 3782..3783
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 3982..3983
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 4094..4095
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 4233..4234
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 5165..5166
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 5766..5767
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 6296..6297
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 6633..6634
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT HELIX 1346..1355
FT /evidence="ECO:0007829|PDB:5UTV"
FT STRAND 1360..1364
FT /evidence="ECO:0007829|PDB:5UTV"
FT STRAND 1368..1371
FT /evidence="ECO:0007829|PDB:5UTV"
FT STRAND 1374..1382
FT /evidence="ECO:0007829|PDB:5UTV"
FT STRAND 1385..1389
FT /evidence="ECO:0007829|PDB:5UTV"
FT STRAND 1394..1398
FT /evidence="ECO:0007829|PDB:5UTV"
FT STRAND 1401..1404
FT /evidence="ECO:0007829|PDB:5UTV"
FT STRAND 1406..1408
FT /evidence="ECO:0007829|PDB:5UTV"
FT HELIX 1409..1415
FT /evidence="ECO:0007829|PDB:5UTV"
SQ SEQUENCE 6930 AA; 769729 MW; 9ED06D0888C7EC7B CRC64;
MEGVPDPPKL KSMVVTTLKW CDPFANPNVT GWDIPIEEAL EYAKQQLRTP EPQLVFVPYY
LSHAPGISGD RVVITDSIWY ATNFGWQPIR ELAMDKDGVR YGRGGTHGVL LPMQDPSFIM
GDIDIQIRKY GIGANSPPDV LPLWDGFSDP GPDVGPYLDF PDNCCPTKPK AKRGGDVYLS
DQYGFDNNGI LVEPVMKLLG VIKSDFTLEQ LLAALGKYRT EDGYDLPDGY VKVAIKVGRK
AVPVLKQSIF TVVGVTEQLV PGYYYPFSTS SVVEHTKPTR GGPVGKTVEA VMLSLYGTNN
YNPATPVARL KCSYCDYYGW TPLKDIGTVN CLCGAEFQLT SSCVDAESAG VIKPGCVMLL
DKSPGMRLIP GNRTYVSFGG AIWSPIGKVN GVTVWVPRAY SIVAGEHSGA VGSGDTVAIN
KELVEYLIEG IRVDADTLDN PTCATFIANL DCDTKAPVVH TVESLQGLCL ANKIMLGDKP
LPTDEFHPFI VGLAYHVQRA CWYGALASRT FEAFRDFVRT EEERFAQFFG KVCAPINGCV
YLAYTTGRVT LFSAYQVLNT AIAKSKDAFG GVAAIVVDML KPILEWVLKK MSIAKGAWLP
YAEGLLALFK AQFTVVKGKF QFLRASLNSK CHSLCDLLTT IMSKLLTSVK WAGCKVDALY
TGTYYYFSRK GVLTEVQLCA KRLGLLLTPK QQKMEVEVLD GDFDAPVTLT DLELEECTGV
LEEVFGASDV KLVKGTLVSL ASKLFVRTED GFLYRYVKSG GVLGKAFRLR GGGVSKVTFG
DEEVHTIPNT VTVNFSYDVC EGLDAILDKV MAPFQVEEGT KLEDLACVVQ KAVYERLSDL
FSDCPAELRP INLEDFLTSE CFVYSKDYEK ILMPEMYFSL EDAVPVDDEM VDDIEDTVEQ
ASDSDDQWLG DEGAEDCDNT IQDVDVATSM TTPCGYTKIA EHVYIKCADI VQEARNYSYA
VLVNAANVNL HHGGGVAGAL NRATNNAMQK ESSEYIKANG SLQPGGHVLL SSHGLASHGI
LHVVGPDKRL GQDLALLDAV YAAYTGFDSV LTPLVSAGIF GFTVEESLCS LVKNVACTTY
VVVYDRQLYE RALATSFDVP GPQSSVQHVP AIDWAEAVEV QESIVDQVET PSLGAVDTVD
SNADSGLNET ARSPENVVGS VPDDVVADVE SCVRDLVRQV VKKVKRDKRP PPIVPQQTVE
QQPQEISSPG DCNTVLVDVV SMSFSAMVNF GKEKGLLIPV VIDYPAFLKV LKRFSPKEGL
FSSNGYEFYG YSRDKPLHEV SKDLNSLGRP LIMIPFGFIV NGQTLAVSAV SMRGLTVPHT
VVVPSESSVP LYRAYFNGVF SGDTTAVQDF VVDILLNGAR DWDVLQTTCT VDRKVYKTIC
KRGNTYLCFD DTNLYAITGD VVLKFATVSK ARAYLETKLC APEPLIKVLT TVDGINYSTV
LVSTAQSYRA QIGTVFCDGH DWSNKNPMPT DEGTHLYKQD NFSSAEVTAI REYYGVDDSN
IIARAMSIRK TVQTWPYTVV DGRVLLAQRD SNCYLNVAIS LLQDIDVSFS TPWVCRAYDA
LKGGNPLPMA EVLIALGKAT PGVSDDAHMV LSAVLNHGTV TARRVMQTVC EHCGVSQMVF
TGTDACTFYG SVVLDDLYAP VSVVCQCGRP AIRYVSEQKS PWLLMSCTPT QVPLDTSGIW
KTAIVFRGPV TAGHYMYAVN GTLISVYDAN TRRRTSDLKL PATDILYGPT SFTSDSKVET
YYLDGVKRTT IDPDFSKYVK RGDYYFTTAP IEVVAAPKLV TSYDGFYLSS CQNPQLAESF
NKAINATKTG PMKLLTMYPN VAGDVVAISD DNVVAHPYGS LHMGKPVLFV TRPNTWKKLV
PLLSTVVVNT PNTYDVLAVD PLPVNNETSE EPISVKAPIP LYGLKATMVL NGTTYVPGNK
GHLLCLKEFT LTDLQTFYVE GVQPFVLLKA SHLSKVLGLR VSDSSLHVNH LSKGVVYAYA
ATRLTTRVTT SLLGGLVTRS VRKTADFVRS TNPGSKCVGL LCLFYQLFMR FWLLVKKPPI
VKVSGIIAYN TGCGVTTCVL NYLRSRCGNI SWSRLLKLLR YMLYIWFVWT CLTICGVWLS
EPYAPSLVTR FKYFLGIVMP CDYVLVNETG TGWLHHLCMA GMDSLDYPAL RMQQHRYGSP
YNYTYILMLL EAFFAYLLYT PALPIVGILA VLHLIVLYLP IPLGNSWLVV FLYYIIRLVP
FTSMLRMYIV IAFLWLCYKG FLHVRYGCNN VACLMCYKKN VAKRIECSTV VNGVKRMFYV
NANGGTHFCT KHNWNCVSCD TYTVDSTFIC RQVALDLSAQ FKRPIIHTDE AYYEVTSVEV
RNGYVYCYFE SDGQRSYERF PMDAFTNVSK LHYSELKGAA PAFNVLVFDA TNRIEENAVK
TAAIYYAQLA CKPILLVDKR MVGVVGDDAT IARAMFEAYA QNYLLKYSIA MDKVKHLYST
ALQQISSGMT VESVLKVFVG STRAEAKDLE SDVDTNDLVS CIRLCHQEGW EWTTDSWNNL
VPTYIKQDTL STLEVGQFMT ANAKYVNANI AKGAAVNLIW RYADFIKLSE SMRRQLKVAA
RKTGLNLLVT TSSLKADVPC MVTPFKIIGG HRRIVSWRRV LIHVFMLLVV LNPQWFTPWY
IMRPIEYNVV DFKVIDNAVI RDITSADQCF ANKFSAFENW YSNRYGSYVN SRGCPMVVGV
VSDIVGSLVP GLPARFLRVG TTLLPLVNYG LGAVGSVCYT PHYAINYDVF DTSACVLAAT
CTLFSSASGE RMPYCADAAL IQNASRYDML KPHVMYPFYE HSGYIRFPEV ISAGVHIVRT
MAMEYCKVGR CDVSEAGLCM SLQPRWVVNN AYFRQQSGVY CGTSAFDLFM NMLLPIFTPV
GAVDITTSIL MGALLAVVVS MSLYYLLRFR RAFGDYSGVI FTNILAFVLN VIVLCLEGPY
PMLPSIYAMV FLYATCYFGS DIACMMHVSF LIMFAGVVPL WVTVLYIVVV LSRHILWFAS
LCTKRTVQVG DLAFHSFQDA ALQTFMLDKE VFLRLKREIS SDAYFKYLAM YNKYKYYSGP
MDTAAYREAA CSHLVMALEK YSNGGGDTIY QPPRCSVASA ALQAGLTRMA HPSGLVEPCL
VKVNYGSMTL NGIWLDNFVI CPRHVMCSRD ELANPDYPRL SMRAANYDFH VSQNGHNIRV
IGHTMEGSLL KLTVDVNNPK TPAYSFIRVS TGQAMSLLAC YDGLPTGVYT CTLRSNGTMR
ASFLCGSCGS PGFVMNGKEV QFCYLHQLEL PNGTHTGTDF SGVFYGPFED KQVPQLAAPD
CTITVNVLAW LYAAVLSGEN WFLTKSSISP AEFNNCAVKY MCQSVTSESL QVLQPLAAKT
GISVERMLSA LKVLLSAGFC GRTIMGSCSL EDEHTPYDIG RQMLGVKLQG KFQSMFRWTL
QWFAIIFVLT ILILLQLAQW TFVGALPFTL LLPLIGFVAV CVGFVSLLIK HKHTYLTVYL
LPVAMVTAYY NFQYTPEGVQ GYLLSLYNYV NPGRIDVIGT DLLTMLIISV ACTLLSVRMV
RTDAYSRIWY VCTAVGWLYN CWTGSADTVA ISYLTFMVSV FTNYTGVACA SLYAAQFMVW
VLKFLDPTIL LLYGRFRCVL VCYLLVGYLC TCYFGVFNLI NRLFRCTLGN YEYVVSSQEL
RYMNSHGLLP PTNSWQALML NIKLAGIGGI PIYRVSTIQS NMTDLKCTSV VLLSVLQQLR
VESSSKLWAL CVKLHNEILA SNSPTEAFEA FVSLLSVLLS LPGAINLDEL CSSILENNSV
LQAVASEFSN LSSYVDYENA QKAYDTAVAT GAPASTVNAL KKAMNVAKSV LDKDVATTRK
LERMSELAMT AMYKQARAED RRSKVTAAMQ TMLFNMIRRL DSDALSNILN NARNGVVPLG
VIPRTAANKL LLVVPDFSVY TATITMPTLT YAGSAWDVMQ VADADGKTVN ATDITRENSV
NLAWPLVVTA QRQQATSPVK LQNNELMPQT VKRMNVVAGV SQTACVTDAV AYYNATKEGR
HVMAILADTD GLAFAKVEKS TGDGFVILEL EPPCKFMVDT PKGPALKYLY FTKGLKNLCR
GTVLGTLACT VRLHAGSATE VASNSSILSL CSFSVDPEAT YKDYLDNGGS PIGNCVKMLT
PHTGTGLAIT AKPDANIDQE SFGGASCCLY CRCHIEHPGA SGVCKYKGKF VQIPLVGVND
PIGFCIRNVV CAVCNMWQGY GCPCSSLREI NLQARDECFL NRVRGTSGVA RLVPLGSGVQ
PDIVLRAFDI CNTKVAGFGL HLKNNCCRYQ ELDADGTQLD SYFVVKRHTE SNYLLEQRCY
EKLKDCGVVA RHDFFKFNIE GVMTPHVSRE RLTKYTMADL VYSLRHFDNN NCDTLKEILV
LRGCCTADYF DRKDWYDPVE NPDIIRVYHN LGETVRKAVL SAVKMADSMV EQGLIGVLTL
DNQDLNGQWY DFGDFIEGPA GAGVAVMDTY YSLAMPVYTM TNMLAAECHV DGDFSKPKRV
WDICKYDYTQ FKYSLFSKYF KYWDMQYHPN CVACADDRCI LHCANFNILF SMVLPNTSFG
PLVQKIYVDG VPFVVSTGYH YRELGVVMNQ DIRQHAQRLS LRELLVYAAD PAMHVAASNA
LADKRTVCMS VAAMTTGVTF QTVKPGQFNE DFYNFAVKCG FFKEGSTISF KHFFYAQDGN
AAISDYDYYR YNLPTMCDIK QLLFSLEVVD KYFDCYDGGC LQASQVVVAN YDKSAGFPFN
KFGKARLYYE SLSYADQDEL FAYTKRNVLP TITQMNLKYA ISAKNRARTV AGVSIASTMT
NRQFHQKMLK SIAAARGASV VIGTTKFYGG WNRMLRTLCE GVENPHLMGW DYPKCDRAMP
NLLRIFASLI LARKHATCCN ASERFYRLAN ECAQVLSEMV LCGGGFYVKP GGTSSGDSTT
AYANSVFNIC QAVSANLNTF LSIDGNKIYT TYVQELQRRL YLGIYRSNTV DNELVLDYYN
YLRKHFSMMI LSDDGVVCYN ADYAQKGYVA DIQGFKELLY FQNNVFMSES KCWVEPDITK
GPHEFCSQHT MLVDMKGEQV YLPYPDPSRI LGAGCFVDDL LKTDGTLMME RYVSLAIDAY
PLTKHPDPEY QNVFWCYLQY IKKLHEELTG HLLDTYSVML ASDNASKYWE VEFYENMYME
SATLQSVGTC VVCNSQTSLR CGGCIRRPFL CCKCCYDHVV STTHKLVLSV TPYVCNNPSC
DVADVTQLYL GGMSYYCRDH RPPISFPLCA NGQVFGLYKN ICTGSPDVAD FNSLATCDWS
NSKDYVLANT ATERLKLFAA ETLRATEENA KQAYASAVVK EVLSDRELVL SWETGKTRPP
LNRNYVFTGF HITKNSKVQL GEYIFEKGDY GDVVNYRSST TYKLQVGDYF VLTSHSVQPL
SSPTLLPQER YTKLVGLYPA MNVPESFASN VVHYQRVGMS RYTTVQGPPG TGKSHLSIGL
ALYYPSAKIV YTACSHAAVD ALCEKAHKNL PINRCSRIVP AKARVECFSK FKVNDVGAQY
VFSTINALPE TTADILVVDE VSMCTNYDLS MINARVRAKH IVYVGDPAQL PAPRTLLTKG
TLAPEHFNSV CRLMVAVGPD IFLATCYRCP KEIVDTVSAL VYDKKLKANK VTTGECYKCY
YKGSVTHDSS SAINKPQLGL VKEFLIKNPK WQSAVFISPY NSQNSVARRM LGLQTQTVDS
SQGSEFDYVI YCQTSDTAHA LNVNRFNVAI TRAKKGILCV MSDSTLYESL EFTPLDVNDY
VKPKMQSEVT VGLFKDCAKA EPLGPAYAPT FVSVNDKFKL NESLCVHFDT TELQMPYNRL
ISKMGFKFDL NIPGYSKLFI TREQAIREVR GWVGFDVEGA HACGPNIGTN LPLQIGFSTG
VNFVVTPSGY IDTESGSRLA NVVSKAPPGD QFKHLIPLMR KGEPWSVVRK RIVEMLCDTL
DGVSDTVTFV TWAHGFELTT LHYFAKVGPE RKCFMCPRRA TLFSSVYGAY SCWSHHRHIG
GADFVYNPFL VDVQQWGYVG NLQVNHDNVC DVHKGAHVAS CDAIMTRCLA IHDCFCGEVN
WDVEYPIIAN ELAINRACRS VQRVVLKAAV KALHIETIYD IGNPKAIKVY GVNVNNWNFY
DTNPVVEGVK QLHYVYDVHR DQFKDGLAMF WNCNVDCYPH NALVCRFDTR VLSKLNLAGC
NGGSLYVNQH AFHTDAFNKN AFVNLKPLPF FYYSDTACEN ATGVSTNYVS EVDYVPLKSN
VCITRCNLGG AVCKKHADEY RNFLESYNTM VSAGFTLWVD KTFDVFNLWS TFVKLQSLEN
VAYNVLKSGH FTAVAGELPV AILNDRLYIK EDGADKLLFT NNTCLPTNVA FELWAKRSVN
VVPEVKLLRN LGVTCTYNLV IWDYESNAPL VPNTVGICTY TDLTKLDDQV VLVDGRQLDA
YSKFCQLKNA IYFSPSKPKC VCTRGPTHAS INGVVVEAPD RGTAFWYAMR KDGAFVQPTD
GYFTQSRTVD DFQPRTQLEI DFLDLEQSCF LDKYDLHDLG LEHIVYGQFD GTIGGLHLLI
GAVRRKRTAH LVMETVLGTD TVTSYAVIDQ PTASSKQVCS VVDIILDDFI ALIKAQDRSV
VSKVVQCCLD FKVFRFMLWC KGGKISTFYP QLQAKQDWKP GYSMPALYKV QNAVLEPCLL
HNYGQAARLP SGTLMNVAKY TQLCQYLNTC SLAVPAKMRV MHFGAGSDKG VCPGTAVLKQ
WLPADAYLVD NDLCYCASDA DSTYVGSCET FFSVNKWDFI FSDMYDARTK NTSGDNTSKE
GFFTYLTGFI RSKLALGGSI AIKITEHSWS ADLYAIMGHF NWWTCFCTSV NSSSSEAFLI
GVNYIGVGAL LDGWQMHANY VFWRNSTVMQ LSSYSLYDLQ RFPLRLKGTP VMSLKEDQLN
ELVLNLIRAG RLIVRDAVDI GVRGVACSGV
