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R1AB_FIPV
ID   R1AB_FIPV               Reviewed;        6709 AA.
AC   Q98VG9; Q4U5G1; Q4U5G2; Q52PA4;
DT   10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 2.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Replicase polyprotein 1ab;
DE            Short=pp1ab;
DE   AltName: Full=ORF1ab polyprotein;
DE   Contains:
DE     RecName: Full=Non-structural protein 1;
DE              Short=nsp1;
DE   Contains:
DE     RecName: Full=Non-structural protein 2;
DE              Short=nsp2;
DE   Contains:
DE     RecName: Full=Non-structural protein 3;
DE              Short=nsp3;
DE              EC=3.4.19.12;
DE              EC=3.4.22.-;
DE     AltName: Full=PL1-PRO/PL2-PRO;
DE     AltName: Full=PLP1/PLP2;
DE     AltName: Full=Papain-like proteinases 1/2;
DE     AltName: Full=p195;
DE   Contains:
DE     RecName: Full=Non-structural protein 4;
DE              Short=nsp4;
DE     AltName: Full=Peptide HD2;
DE   Contains:
DE     RecName: Full=3C-like proteinase;
DE              Short=3CL-PRO;
DE              Short=3CLp;
DE              EC=3.4.22.-;
DE     AltName: Full=M-PRO;
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   Contains:
DE     RecName: Full=Non-structural protein 11;
DE              Short=nsp11;
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=Exoribonuclease;
DE              Short=ExoN;
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=Putative 2'-O-methyl transferase;
DE              EC=2.1.1.57;
DE     AltName: Full=nsp16;
GN   Name=rep; ORFNames=1a-1b;
OS   Feline coronavirus (strain FIPV WSU-79/1146) (FCoV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC   Alphacoronavirus; Tegacovirus.
OX   NCBI_TaxID=33734;
OH   NCBI_TaxID=9681; Felidae (cat family).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=16033972; DOI=10.1099/vir.0.80985-0;
RA   Dye C., Siddell S.G.;
RT   "Genomic RNA sequence of Feline coronavirus strain FIPV WSU-79/1146.";
RL   J. Gen. Virol. 86:2249-2253(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Haijema B.J., de Groot-Mijnes J.D.F., Vennema H., Raamsman M.J.,
RA   Rottier P.J.M., de Groot R.J.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 2894-3215, AND MUTAGENESIS OF
RP   HIS-2944; ASN-2967; GLY-2986; SER-3041; CYS-3047; TYR-3063; MET-3064 AND
RP   HIS-3065.
RX   PubMed=11842253; DOI=10.1099/0022-1317-83-3-581;
RA   Hegyi A., Friebe A., Gorbalenya A.E., Ziebuhr J.;
RT   "Mutational analysis of the active centre of coronavirus 3C-like
RT   proteases.";
RL   J. Gen. Virol. 83:581-593(2002).
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   -!- FUNCTION: The papain-like proteinase 1 (PLP1) and papain-like
CC       proteinase 2 (PLP2) are responsible for the cleavages located at the N-
CC       terminus of the replicase polyprotein. In addition, PLP2 possesses a
CC       deubiquitinating/deISGylating activity and processes both 'Lys-48'- and
CC       'Lys-63'-linked polyubiquitin chains from cellular substrates. PLP2
CC       also antagonizes innate immune induction of type I interferon by
CC       blocking the nuclear translocation of host IRF-3 (By similarity).
CC       {ECO:0000250}.
CC   -!- FUNCTION: [3C-like proteinase]: Responsible for the majority of
CC       cleavages as it cleaves the C-terminus of replicase polyprotein at 11
CC       sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-
CC       [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln-
CC       CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function
CC       (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}.
CC   -!- FUNCTION: The helicase which contains a zinc finger structure displays
CC       RNA and DNA duplex-unwinding activities with 5' to 3' polarity. ATPase
CC       activity is strongly stimulated by poly(U), poly(dT), poly(C),
CC       poly(dA), but not by poly(G) (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: The exoribonuclease acts on both ssRNA and dsRNA in a 3' to
CC       5' direction. {ECO:0000250}.
CC   -!- FUNCTION: Nsp7-nsp8 hexadecamer may possibly confer processivity to the
CC       polymerase, maybe by binding to dsRNA or by producing primers utilized
CC       by the latter. {ECO:0000250}.
CC   -!- FUNCTION: Nsp9 is a ssRNA-binding protein. {ECO:0000250}.
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   -!- CATALYTIC ACTIVITY: [Non-structural protein 3]:
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: [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;
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: [Putative 2'-O-methyl transferase]:
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: 3CL-PRO exists as monomer and homodimer. Eight copies of nsp7
CC       and eight copies of nsp8 assemble to form a heterohexadecamer. Nsp9 is
CC       a dimer. Nsp10 forms a dodecamer (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       PRO_5000140215; PRO_5000140214 [Q98VG9]: rep; NbExp=3; IntAct=EBI-26365785, EBI-26365769;
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 3]: Host membrane
CC       {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 4]: Host membrane
CC       {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
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=Q98VG9-1; Sequence=Displayed;
CC       Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
CC         IsoId=Q98VG9-2; Sequence=VSP_032885;
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   -!- MISCELLANEOUS: [Isoform Replicase polyprotein 1a]: Produced by
CC       conventional translation. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAY16374.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; DQ010921; AAY32594.1; -; Genomic_RNA.
DR   EMBL; DQ010921; AAY32595.1; -; Genomic_RNA.
DR   EMBL; AY994055; AAY16374.1; ALT_FRAME; Genomic_RNA.
DR   EMBL; AF326575; AAK09095.1; -; Genomic_RNA.
DR   PDB; 3ETI; X-ray; 2.20 A; A/B/C/D/E/F/G/H=1331-1498.
DR   PDB; 3EW5; X-ray; 3.10 A; A/B/C=1331-1498.
DR   PDB; 3GZF; X-ray; 2.76 A; A/B/C/D/E=2808-2902.
DR   PDB; 3JZT; X-ray; 3.91 A; A/B/C/D/E/F/G/H=1331-1498.
DR   PDB; 3UB0; X-ray; 2.60 A; A/D=3583-3777, B/C/E/F=3500-3582.
DR   PDB; 4ZRO; X-ray; 2.06 A; A/B/C/D=2904-3202.
DR   PDB; 5EU8; X-ray; 2.45 A; A=2904-3205.
DR   PDB; 6LP9; X-ray; 1.80 A; A/B/C/D=1-110.
DR   PDBsum; 3ETI; -.
DR   PDBsum; 3EW5; -.
DR   PDBsum; 3GZF; -.
DR   PDBsum; 3JZT; -.
DR   PDBsum; 3UB0; -.
DR   PDBsum; 4ZRO; -.
DR   PDBsum; 5EU8; -.
DR   PDBsum; 6LP9; -.
DR   SMR; Q98VG9; -.
DR   IntAct; Q98VG9; 5.
DR   BindingDB; Q98VG9; -.
DR   ChEMBL; CHEMBL4295624; -.
DR   DrugBank; DB15797; GC-373.
DR   DrugBank; DB15796; GC-376 free acid.
DR   MEROPS; C30.004; -.
DR   PRIDE; Q98VG9; -.
DR   SABIO-RK; Q98VG9; -.
DR   EvolutionaryTrace; Q98VG9; -.
DR   Proteomes; UP000000835; Genome.
DR   Proteomes; UP000140386; 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: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:0003723; F:RNA binding; IEA:UniProtKB-KW.
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:0008270; F:zinc ion binding; IEA:InterPro.
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:0039548; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0019079; P:viral genome replication; IEA:InterPro.
DR   GO; GO:0019082; P:viral protein processing; IEA:InterPro.
DR   CDD; cd21409; 1B_cv_Nsp13-like; 1.
DR   CDD; cd21558; alphaCoV-Nsp6; 1.
DR   CDD; cd21660; alphaCoV_Nsp14; 1.
DR   CDD; cd21665; alphaCoV_Nsp5_Mpro; 1.
DR   CDD; cd21588; alphaCoV_RdRp; 1.
DR   CDD; cd20762; capping_2-OMTase_Nidovirales; 1.
DR   CDD; cd21514; cv_alpha_Nsp2_HCoV-229E-like; 1.
DR   CDD; cd21473; cv_Nsp4_TM; 1.
DR   CDD; cd21167; M_alpha_beta_cv_Nsp15-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; 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; -; 2.
DR   Gene3D; 1.10.8.370; -; 1.
DR   Gene3D; 2.30.30.1000; -; 1.
DR   Gene3D; 2.40.10.10; -; 2.
DR   Gene3D; 2.40.10.250; -; 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; 3.40.50.11580; -; 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; IPR032039; A-CoV_nsp1.
DR   InterPro; IPR038634; A-CoV_nsp1_sf.
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; IPR041679; DNA2/NAM7-like_C.
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; 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; IPR044385; NSP2_HCoV-229E-like.
DR   InterPro; IPR043615; NSP2_N_CoV.
DR   InterPro; IPR044357; NSP3_Ubl1_dom_CoV.
DR   InterPro; IPR044353; Nsp3_Ubl2_dom_CoV.
DR   InterPro; IPR038123; NSP4_C_sf_CoV.
DR   InterPro; IPR044309; NSP5_Mpro_alphaCoV.
DR   InterPro; IPR044369; NSP6_alphaCoV.
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; IPR043178; PLpro_thumb_sf_CoV.
DR   InterPro; IPR044356; RdRp_alphaCoV.
DR   InterPro; IPR001205; RNA-dir_pol_C.
DR   InterPro; IPR009469; RNA_pol_N_CoV.
DR   InterPro; IPR018995; RNA_synth_NSP10_CoV.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF13087; AAA_12; 1.
DR   Pfam; PF16688; CNV-Replicase_N; 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; 2.
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; 2.
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   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; 2.
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; 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; 2.
DR   PROSITE; PS51657; PSRV_HELICASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activation of host autophagy by virus; ATP-binding;
KW   Endonuclease; Exonuclease; Helicase; Host cytoplasm; Host membrane;
KW   Host-virus interaction; Hydrolase;
KW   Inhibition of host innate immune response by virus;
KW   Inhibition of host IRF3 by virus; Inhibition of host RLR pathway 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..6709
FT                   /note="Replicase polyprotein 1ab"
FT                   /id="PRO_0000283825"
FT   CHAIN           1..110
FT                   /note="Non-structural protein 1"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_5000140208"
FT   CHAIN           111..879
FT                   /note="Non-structural protein 2"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_5000140209"
FT   CHAIN           880..2413
FT                   /note="Non-structural protein 3"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_5000140210"
FT   CHAIN           2414..2903
FT                   /note="Non-structural protein 4"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_5000140211"
FT   CHAIN           2904..3205
FT                   /note="3C-like proteinase"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_5000140212"
FT   CHAIN           3206..3499
FT                   /note="Non-structural protein 6"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_5000140213"
FT   CHAIN           3500..3582
FT                   /note="Non-structural protein 7"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_5000140214"
FT   CHAIN           3583..3777
FT                   /note="Non-structural protein 8"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_5000140215"
FT   CHAIN           3778..3888
FT                   /note="Non-structural protein 9"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_5000140216"
FT   CHAIN           3889..4023
FT                   /note="Non-structural protein 10"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_5000140217"
FT   CHAIN           4024..4952
FT                   /note="RNA-directed RNA polymerase"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_5000140219"
FT   CHAIN           4024..4042
FT                   /note="Non-structural protein 11"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_5000140218"
FT   CHAIN           4953..5551
FT                   /note="Helicase"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_5000140220"
FT   CHAIN           5552..6070
FT                   /note="Exoribonuclease"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5000140221"
FT   CHAIN           6071..6409
FT                   /note="Uridylate-specific endoribonuclease"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5000140222"
FT   CHAIN           6410..6709
FT                   /note="Putative 2'-O-methyl transferase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5000140223"
FT   TRANSMEM        1860..1878
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1921..1941
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2006..2026
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2043..2065
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2426..2446
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2691..2711
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2720..2740
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2771..2791
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3212..3232
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3242..3262
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3267..3287
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3306..3326
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3339..3359
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3396..3416
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3419..3439
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          2..108
FT                   /note="CoV Nsp1 globular"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01307"
FT   DOMAIN          111..345
FT                   /note="CoV Nsp2 N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   DOMAIN          378..773
FT                   /note="CoV Nsp2 middle"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01334"
FT   DOMAIN          768..879
FT                   /note="CoV Nsp2 C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01335"
FT   DOMAIN          882..983
FT                   /note="Ubiquitin-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          1079..1330
FT                   /note="Peptidase C16 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   DOMAIN          1329..1500
FT                   /note="Macro"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT   DOMAIN          1497..1553
FT                   /note="Ubiquitin-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          1561..1814
FT                   /note="Peptidase C16 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   DOMAIN          2304..2409
FT                   /note="CoV Nsp3 Y3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   DOMAIN          2808..2903
FT                   /note="Nsp4C"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01291"
FT   DOMAIN          2904..3205
FT                   /note="Peptidase C30"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT   DOMAIN          3500..3582
FT                   /note="RdRp Nsp7 cofactor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01294"
FT   DOMAIN          3583..3777
FT                   /note="RdRp Nsp8 cofactor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01295"
FT   DOMAIN          3778..3888
FT                   /note="Nsp9 ssRNA-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01296"
FT   DOMAIN          3889..4029
FT                   /note="ExoN/MTase coactivator"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   DOMAIN          4018..4280
FT                   /note="NiRAN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01292"
FT   DOMAIN          4385..4952
FT                   /note="Nsp12 RNA-dependent RNA polymerase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   DOMAIN          4632..4794
FT                   /note="RdRp catalytic"
FT   DOMAIN          4953..5036
FT                   /note="CV ZBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   DOMAIN          5200..5391
FT                   /note="(+)RNA virus helicase ATP-binding"
FT   DOMAIN          5392..5561
FT                   /note="(+)RNA virus helicase C-terminal"
FT   DOMAIN          5623..5837
FT                   /note="ExoN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   DOMAIN          5846..6067
FT                   /note="N7-MTase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   DOMAIN          6071..6131
FT                   /note="Nsp15 N-terminal oligomerization"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01305"
FT   DOMAIN          6132..6249
FT                   /note="AV-Nsp11N/CoV-Nsp15M"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01306"
FT   DOMAIN          6266..6406
FT                   /note="NendoU"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT   DOMAIN          6410..6706
FT                   /note="Nidovirus-type SAM-dependent 2'-O-MTase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT   ZN_FING         1188..1219
FT                   /note="C4-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ZN_FING         1678..1707
FT                   /note="C4-type 2; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ZN_FING         3962..3978
FT                   /evidence="ECO:0000250"
FT   ZN_FING         4004..4017
FT                   /evidence="ECO:0000250"
FT   REGION          240..260
FT                   /note="C4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   REGION          1005..1029
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1062..1097
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1860..2065
FT                   /note="HD1"
FT                   /evidence="ECO:0000250"
FT   REGION          2426..2791
FT                   /note="HD2"
FT                   /evidence="ECO:0000250"
FT   REGION          3212..3439
FT                   /note="HD3"
FT                   /evidence="ECO:0000250"
FT   REGION          5958..5972
FT                   /note="GpppA-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   COMPBIAS        1005..1027
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1117
FT                   /note="For PL1-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        1268
FT                   /note="For PL1-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        1599
FT                   /note="For PL2-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        1752
FT                   /note="For PL2-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        2944
FT                   /note="For 3CL-PRO activity"
FT   ACT_SITE        3047
FT                   /note="For 3CL-PRO activity"
FT   ACT_SITE        4779
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   ACT_SITE        4780
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   ACT_SITE        4781
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   ACT_SITE        5641
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        5643
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        5742
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        5818
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        5823
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        6296
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT   ACT_SITE        6311
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT   ACT_SITE        6352
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT   ACT_SITE        6454
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT   ACT_SITE        6538
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT   ACT_SITE        6578
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT   ACT_SITE        6611
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT   BINDING         240
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         242
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         259
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         260
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         3962
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         3965
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         3971
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         3978
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4004
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4007
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4015
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4017
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4957
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         4960
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         4968
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         4971
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         4978
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         4981
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         4985
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         4991
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5002
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5007
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5024
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5027
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5235..5242
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         5758
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         5760
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         5776
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         5779
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         5807
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         5811
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         5814
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         5829
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         5881..5887
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   BINDING         5996
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   BINDING         6013
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   BINDING         6024
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   BINDING         6027
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   SITE            110..111
FT                   /note="Cleavage; by PL1-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            879..880
FT                   /note="Cleavage; by PL1-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            2413..2414
FT                   /note="Cleavage; by PL2-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            2903..2904
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            3053
FT                   /note="Important for substrate recognition"
FT   SITE            3205..3206
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            3499..3500
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            3582..3583
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            3777..3778
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            3888..3889
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            4023..4024
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            4952..4953
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            5551..5552
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            6070..6071
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   SITE            6409..6410
FT                   /note="Cleavage; by 3CL-PRO"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         4043..6709
FT                   /note="Missing (in isoform Replicase polyprotein 1a)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_032885"
FT   VARIANT         162
FT                   /note="W -> C"
FT   VARIANT         177
FT                   /note="D -> G"
FT   VARIANT         388
FT                   /note="W -> C"
FT   VARIANT         808
FT                   /note="K -> T"
FT   VARIANT         1784
FT                   /note="A -> V"
FT   VARIANT         2889
FT                   /note="M -> K"
FT   VARIANT         3280
FT                   /note="A -> V"
FT   VARIANT         3992
FT                   /note="Q -> R"
FT   VARIANT         4304
FT                   /note="H -> Q"
FT   VARIANT         5846
FT                   /note="Y -> H"
FT   MUTAGEN         2944
FT                   /note="H->Y,R: Complete loss of 3CL-PRO activity."
FT                   /evidence="ECO:0000269|PubMed:11842253"
FT   MUTAGEN         2967
FT                   /note="N->A,D: Increase of 3CL-PRO activity."
FT                   /evidence="ECO:0000269|PubMed:11842253"
FT   MUTAGEN         2986
FT                   /note="G->A: 5% loss of 3CL-PRO activity."
FT                   /evidence="ECO:0000269|PubMed:11842253"
FT   MUTAGEN         2986
FT                   /note="G->D: Increase of 3CL-PRO activity."
FT                   /evidence="ECO:0000269|PubMed:11842253"
FT   MUTAGEN         2986
FT                   /note="G->E: 50% loss of 3CL-PRO activity."
FT                   /evidence="ECO:0000269|PubMed:11842253"
FT   MUTAGEN         2986
FT                   /note="G->P,V: 95% loss of 3CL-PRO activity."
FT                   /evidence="ECO:0000269|PubMed:11842253"
FT   MUTAGEN         2986
FT                   /note="G->R,T,W: 70% loss of 3CL-PRO activity."
FT                   /evidence="ECO:0000269|PubMed:11842253"
FT   MUTAGEN         3041
FT                   /note="S->A: 80% loss of 3CL-PRO activity."
FT                   /evidence="ECO:0000269|PubMed:11842253"
FT   MUTAGEN         3041
FT                   /note="S->T: 40% loss of 3CL-PRO activity."
FT                   /evidence="ECO:0000269|PubMed:11842253"
FT   MUTAGEN         3047
FT                   /note="C->A,S: Complete loss of 3CL-PRO activity."
FT                   /evidence="ECO:0000269|PubMed:11842253"
FT   MUTAGEN         3063
FT                   /note="Y->A,F,G,T: Almost complete loss of 3CL-PRO
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:11842253"
FT   MUTAGEN         3064
FT                   /note="M->A: Increase of 3CL-PRO activity."
FT                   /evidence="ECO:0000269|PubMed:11842253"
FT   MUTAGEN         3065
FT                   /note="H->A: Complete loss of 3CL-PRO activity."
FT                   /evidence="ECO:0000269|PubMed:11842253"
FT   CONFLICT        1016..1092
FT                   /note="Missing (in Ref. 1; AAY32594)"
FT                   /evidence="ECO:0000305"
FT   STRAND          4..10
FT                   /evidence="ECO:0007829|PDB:6LP9"
FT   STRAND          16..18
FT                   /evidence="ECO:0007829|PDB:6LP9"
FT   HELIX           23..36
FT                   /evidence="ECO:0007829|PDB:6LP9"
FT   STRAND          41..45
FT                   /evidence="ECO:0007829|PDB:6LP9"
FT   HELIX           46..51
FT                   /evidence="ECO:0007829|PDB:6LP9"
FT   STRAND          52..55
FT                   /evidence="ECO:0007829|PDB:6LP9"
FT   STRAND          59..75
FT                   /evidence="ECO:0007829|PDB:6LP9"
FT   STRAND          84..90
FT                   /evidence="ECO:0007829|PDB:6LP9"
FT   STRAND          96..104
FT                   /evidence="ECO:0007829|PDB:6LP9"
FT   STRAND          1336..1339
FT                   /evidence="ECO:0007829|PDB:3ETI"
FT   STRAND          1342..1347
FT                   /evidence="ECO:0007829|PDB:3ETI"
FT   HELIX           1349..1356
FT                   /evidence="ECO:0007829|PDB:3ETI"
FT   STRAND          1359..1365
FT                   /evidence="ECO:0007829|PDB:3ETI"
FT   HELIX           1376..1382
FT                   /evidence="ECO:0007829|PDB:3ETI"
FT   TURN            1383..1385
FT                   /evidence="ECO:0007829|PDB:3ETI"
FT   HELIX           1386..1395
FT                   /evidence="ECO:0007829|PDB:3ETI"
FT   STRAND          1405..1413
FT                   /evidence="ECO:0007829|PDB:3ETI"
FT   STRAND          1416..1422
FT                   /evidence="ECO:0007829|PDB:3ETI"
FT   HELIX           1431..1443
FT                   /evidence="ECO:0007829|PDB:3ETI"
FT   STRAND          1449..1451
FT                   /evidence="ECO:0007829|PDB:3ETI"
FT   HELIX           1463..1473
FT                   /evidence="ECO:0007829|PDB:3ETI"
FT   STRAND          1479..1483
FT                   /evidence="ECO:0007829|PDB:3ETI"
FT   HELIX           1486..1497
FT                   /evidence="ECO:0007829|PDB:3ETI"
FT   HELIX           2818..2823
FT                   /evidence="ECO:0007829|PDB:3GZF"
FT   STRAND          2826..2828
FT                   /evidence="ECO:0007829|PDB:3GZF"
FT   HELIX           2830..2837
FT                   /evidence="ECO:0007829|PDB:3GZF"
FT   TURN            2838..2840
FT                   /evidence="ECO:0007829|PDB:3GZF"
FT   HELIX           2842..2850
FT                   /evidence="ECO:0007829|PDB:3GZF"
FT   HELIX           2852..2856
FT                   /evidence="ECO:0007829|PDB:3GZF"
FT   HELIX           2864..2884
FT                   /evidence="ECO:0007829|PDB:3GZF"
FT   STRAND          2889..2891
FT                   /evidence="ECO:0007829|PDB:3GZF"
FT   STRAND          2895..2899
FT                   /evidence="ECO:0007829|PDB:3GZF"
FT   TURN            2914..2916
FT                   /evidence="ECO:0007829|PDB:4ZRO"
FT   HELIX           2917..2919
FT                   /evidence="ECO:0007829|PDB:4ZRO"
FT   STRAND          2920..2925
FT                   /evidence="ECO:0007829|PDB:4ZRO"
FT   STRAND          2928..2935
FT                   /evidence="ECO:0007829|PDB:4ZRO"
FT   STRAND          2938..2942
FT                   /evidence="ECO:0007829|PDB:4ZRO"
FT   HELIX           2943..2946
FT                   /evidence="ECO:0007829|PDB:4ZRO"
FT   STRAND          2950..2952
FT                   /evidence="ECO:0007829|PDB:5EU8"
FT   HELIX           2956..2962
FT                   /evidence="ECO:0007829|PDB:4ZRO"
FT   HELIX           2965..2967
FT                   /evidence="ECO:0007829|PDB:4ZRO"
FT   STRAND          2968..2972
FT                   /evidence="ECO:0007829|PDB:4ZRO"
FT   STRAND          2975..2977
FT                   /evidence="ECO:0007829|PDB:4ZRO"
FT   STRAND          2979..2985
FT                   /evidence="ECO:0007829|PDB:4ZRO"
FT   STRAND          2988..2995
FT                   /evidence="ECO:0007829|PDB:4ZRO"
FT   STRAND          3013..3020
FT                   /evidence="ECO:0007829|PDB:4ZRO"
FT   STRAND          3023..3031
FT                   /evidence="ECO:0007829|PDB:4ZRO"
FT   STRAND          3050..3055
FT                   /evidence="ECO:0007829|PDB:4ZRO"
FT   STRAND          3058..3068
FT                   /evidence="ECO:0007829|PDB:4ZRO"
FT   STRAND          3074..3077
FT                   /evidence="ECO:0007829|PDB:4ZRO"
FT   STRAND          3079..3081
FT                   /evidence="ECO:0007829|PDB:5EU8"
FT   HELIX           3084..3086
FT                   /evidence="ECO:0007829|PDB:4ZRO"
FT   STRAND          3089..3092
FT                   /evidence="ECO:0007829|PDB:4ZRO"
FT   HELIX           3103..3115
FT                   /evidence="ECO:0007829|PDB:4ZRO"
FT   HELIX           3129..3136
FT                   /evidence="ECO:0007829|PDB:4ZRO"
FT   TURN            3137..3140
FT                   /evidence="ECO:0007829|PDB:4ZRO"
FT   HELIX           3147..3150
FT                   /evidence="ECO:0007829|PDB:4ZRO"
FT   HELIX           3151..3157
FT                   /evidence="ECO:0007829|PDB:4ZRO"
FT   HELIX           3161..3171
FT                   /evidence="ECO:0007829|PDB:4ZRO"
FT   STRAND          3183..3185
FT                   /evidence="ECO:0007829|PDB:4ZRO"
FT   HELIX           3192..3200
FT                   /evidence="ECO:0007829|PDB:4ZRO"
FT   HELIX           3510..3518
FT                   /evidence="ECO:0007829|PDB:3UB0"
FT   HELIX           3521..3523
FT                   /evidence="ECO:0007829|PDB:3UB0"
FT   HELIX           3525..3540
FT                   /evidence="ECO:0007829|PDB:3UB0"
FT   HELIX           3544..3561
FT                   /evidence="ECO:0007829|PDB:3UB0"
FT   HELIX           3568..3577
FT                   /evidence="ECO:0007829|PDB:3UB0"
FT   HELIX           3579..3581
FT                   /evidence="ECO:0007829|PDB:3UB0"
FT   STRAND          3583..3585
FT                   /evidence="ECO:0007829|PDB:3UB0"
FT   HELIX           3587..3609
FT                   /evidence="ECO:0007829|PDB:3UB0"
FT   HELIX           3614..3652
FT                   /evidence="ECO:0007829|PDB:3UB0"
FT   HELIX           3663..3680
FT                   /evidence="ECO:0007829|PDB:3UB0"
FT   HELIX           3683..3693
FT                   /evidence="ECO:0007829|PDB:3UB0"
FT   STRAND          3697..3702
FT                   /evidence="ECO:0007829|PDB:3UB0"
FT   STRAND          3709..3714
FT                   /evidence="ECO:0007829|PDB:3UB0"
FT   HELIX           3717..3723
FT                   /evidence="ECO:0007829|PDB:3UB0"
FT   STRAND          3728..3731
FT                   /evidence="ECO:0007829|PDB:3UB0"
FT   STRAND          3734..3742
FT                   /evidence="ECO:0007829|PDB:3UB0"
FT   HELIX           3751..3753
FT                   /evidence="ECO:0007829|PDB:3UB0"
FT   HELIX           3756..3761
FT                   /evidence="ECO:0007829|PDB:3UB0"
FT   STRAND          3766..3772
FT                   /evidence="ECO:0007829|PDB:3UB0"
SQ   SEQUENCE   6709 AA;  751196 MW;  F26AC0FFF5FE27F9 CRC64;
     MSSKQFKILV NEDYQVNVPS LPFRDALQEI KYCYRNGFDG YVFVPEYRRD LVDCNRKDHY
     VIGVLGNGIS DLKPVLLTEP SVMLQGFIVR ANCNGVLEDF DLKFARTGNG AIYVDQYMCG
     ADGKPVIEGE FKDYFGDEDV IIYEGEEYHC AWLTVRDEKP LWQQTLLTIR EIQYNLDIPH
     KLPNCAIREV APPVKKNSKV VLSEEYRKLY DIFGSPFMGN GDSLNTCFDS LHFIAATLKC
     PCGAESSGVG DWTGFKTACC GLHGKVKGVT LGAVKPGDAI VTSMSAGKGV KFFANSVLQY
     AGDVENVSVW KVIKTFTVNE TVCTTDFEGE LNDFIRPEST SPVSCSIKRA FITGEVDDAV
     HDCIIAGKLD LSTNLFGSAN LLFKKMPWFV QKCGAIFADA WKVVEELLCS LKLTYKQIYD
     VVASLCTSAF TIMDYKPVFV VSSNSVKDLV DKCVKILVKA FDVFTQTITI AGVEAKCFVL
     GSKYLLFNNA LVKLVSVKIL GKRQKGLDSA FFATNLIGAT VNVTPQRTES AYISLNKVDD
     VVTPGGGHIV IIGDMAFYKS EEYYFMMASP DSVLVNNVFK AARVPSYNIV YDVNDDTKSK
     MVVKIGTSFD FDGDLDAAIA KVNDLLIEFR QEKLCFRALK DGENILVEAY LKKYKMPVCL
     KNHVGLWDII RQDSGKKGFL DTFNHLNELE DVKDIKIQTI KNIICPDLLL ELDFGAIWYR
     CMPACSDKSI LGNVKIMLGN GVKVVCDGCH SFANRLTINY NKLCDTARKD IEIGGIPFST
     FKTPSSSFID MKDAIYSVVE YGEALSFKTA SVPVTNSGII TTDDWSDPIL LEPADYVEPK
     DNGDVIVIAG YTFYKDEDDH FYPYGSGMVV QKMYNKMGGG DKSVSFSDNV NVREIEPVTR
     VRLEFEFDNE VVTQVLEKVI GTKYKFIGTT WEEFEDSISE KLDKIFDTLA EQGVELEGYF
     IYDTCGGFDI NNPDGVMISQ YDLNTAADDK SDSDASVEDI SLISDNEDVE QIEEDNTSTD
     DAEDVSSVEG ETVSVVDVED FVEQVSLVEE NNVLTPAVNP DEQLSSVEKK DEVSAKNDPW
     AAAVDEQEAE QPKPSLTPFK TTNLNGKIIL KQQDNNCWIN ACCYQLQAFD FFNHDLWDGF
     KKDDVMPFVD FCYAALTLKQ GDSGDAEYLL ETMLNDYSTA KVTLSAKCGC GVKEIVLERT
     VFKLTPLRNE FKYGVCGDCK QINMCKFASV EGSGVFVHDR IEKQTPVSQF IVTPTMHAVY
     TGTTQSGHYM IEDCIHDYCV DGMGIKPRKH KFYTSTLFLN ANVMTAKSKT MVEPPVPVED
     KCVEDCQSPK DLILPFYKAG KVSFYQGDLD VLINFLEPDV LVNAANGDLR HVGGVARAID
     VFTGGKLTKR SKEYLKSSKA IAPGNAVLFE NVLEHLSVLN AVGPRNGDSR VEGKLCNVYK
     AIAKCDGKIL TPLISVGIFK VKLEVSLQCL LKTVTDRDLN VFVYTDQERV TIENFFNGTI
     PIKVTEDTVN QKRVSVALDK TYGEQLKGTV VIKDKDVTNQ LPSVSDVGEK VVKALDVDWN
     AYYGFPNAAA FSASSHDAYE FDVVTHNNFI VHKQTDNNCW VNAICLALQR LKPTWKFPGV
     KSLWDAFLTR KTAGFVHMLY HISGLTKGQP GDAELTLHKL VDLMSSDSAV TVTHTTACDK
     CAKVETFTGP VVAAPLLVCG TDEICVHGVH VNVKVTSIRG TVAITSLIGP VVGDVIDATG
     YICYTGLNSR GHYTYYDNRN GLMVDADKAY HFEKNLLQVT TAIASNFVAN TPKKEIMPKT
     QAKESKAKES NTARVFSEVE ENPKNIVRKE KLLAIESGVD YTITTLGKYA DVFFMAGDKI
     LRFLLEVFKY LLVVFMCLRK SKMPKVKVKP PHVFRNLGAK VRTLNYVRQL NKPALWRYIK
     LVLLLIALYH FFYLFVSIPV VHKLACSGSV QAYSNSSFVK SEVCGNSILC KACLASYDEL
     ADFDHLQVSW DYKSDPLWNR VIQLSYFIFL AVFGNNYVRC LLMYFVSQYL NLWLSYFGYV
     KYSWFLHVVN FESISVEFVI IVVVFKAVLA LKHIFLPCNN PSCKTCSKIA RQTRIPIQVV
     VNGSMKTVYV HANGTGKLCK KHNFYCKNCD SYGFDHTFIC DEIVRDLSNS IKQTVYATDR
     SYQEVTKVEC TDGFYRFYVG EEFTAYDYDV KHKKYSSQEV LKTMFLLDDF IVYNPSGSSL
     ASVRNVCVYF SQLIGRPIKI VNSELLEDLS VDFKGALFNA KKNVIKNSFN VDVSECKNLE
     ECYKLCNLDV TFSTFEMAIN NAHRFGILIT DRSFNNFWPS KIKPGSSGVS AMDIGKCMTF
     DAKIVNAKVL TQRGKSVVWL SQDFSTLSST AQKVLVKTFV EEGVNFSLTF NAVGSDEDLP
     YERFTESVSA KSGSGFFDVL KQLKQLFWCL VLFITLYGLC SVYSVATQSY IDSAEGYDYM
     VIKNGVVQSF DDSINCVHNT YKGFAVWFKA KHGFVPTFDK SCPIVLGTVF DLGNMRPIPD
     VPAYVALVGR SLVFAINAAF GVTNVCYDHT GAAVSKNSYF DTCVFNSACT TLTGIGGTVV
     YCAKQGLVEG AKLYSELLPD YYYEHASGNM VKIPAIIRSF GLRFVKTQAT TYCRVGECTE
     SQAGFCFGGD NWFVYDKEFG DGYICGSSTL GFFKNVFALF NSNMSVVATS GAMLANIVIA
     CLAIAVCYGV LKFKKIFGDC TLLVVMIIVT LVVNNVSYFV TQNTFFMIVY AIIYYFTTRK
     LAYPGVLDAG FIIAYLNMAP WYVLVLYIMV FLYDSLPSLF KLKVTTNLFE GDKFVGSFES
     AAMGTFVIDM RSYETLVNST SLDRIKSYAN SFNKYKYYTG SMGEADYRMA CYAHLGKALM
     DYSVSRNDML YTPPTVSVNS TLQSGLRKMA QPSGVVEPCI VRVAYGNNVL NGLWLGDEVI
     CPRHVIASDT SRVINYENEL SSVRLHNFSI AKNNAFLGVV SAKYKGVNLV LKVNQVNPNT
     PEHKFKSVRP GESFNILACY EGCPGSVYGV NMRSQGTIKG SFIAGTCGSV GYVLENGTLY
     FVYMHHLELG NGSHVGSNLE GEMYGGYEDQ PSMQLEGTNV MSSDNVVAFL YAALINGERW
     FVTNTSMTLE SYNAWAKTNS FTEIVSTDAF NMLAAKTGYS VEKLLECIVR LNKGFGGRTI
     LSYGSLCDEF TPTEVIRQMY GVNLQSGKVK SIFYPMMTAI AILFAFWLEF FMYTPFTWIN
     PTFVSVVLAI TTLVSVLLVA GIKHKMLFFM SFVMPSVILA TAHNVVWDMT YYESLQVLVE
     NVNTTFLPVD MQGVMLALFC VVVFVICTIR FFTCKQSWFS LFATTIFVMF NIVKLLGMIG
     EPWTDDHFLL CLVNMLTMLI SLTTKDWFVV FASYKVAYYI VVYVMQPAFV QDFGFVKCVS
     IIYMACGYLF CCYYGILYWV NRFTCMTCGV YQFTVSPAEL KYMTANNLSA PKTAYDAMIL
     SFKLMGIGGG RNIKISTVQS KLTEMKCTNV VLLGLLSKMH VESNSKEWNY CVGLHNEINL
     CDDPDAVLEK LLALIAFFLS KHNTCDLSDL IESYFENTTI LQSVASAYAA LPSWIAYEKA
     RADLEEAKKN DVSPQLLKQL TKACNIAKSE FEREASVQKK LDKMAEQAAA SMYKEARAVD
     RKSKIVSAMH SLLFGMLKKL DMSSVNTIIE QARNGVLPLS IIPAASATRL IVVTPNLEVL
     SKVRQENNVH YAGAIWSIVE VKDANGAQVH LKEVTAANEL NITWPLSITC ERTTKLQNNE
     ILPGKLKEKA VKASATIDGD AYGSGKALMA SEGGKSFIYA FIASDSNLKY VKWESNNDVI
     PIELEAPLRF YVDGVNGPEV KYLYFVKSLN TLRRGAVLGY IGATVRLQAG KPTEHPSNSG
     LLTLCAFAPD PAKAYVDAVK RGMQPVTNCV KMLSNGAGNG MAITNGVESN TQQDSYGGAS
     VCIYCRCHVE HPAIDGLCRF KGKFVQVPTG TQDPIRFCIE NEVCVVCGCW LTNGCMCDRT
     SIQGTTIDQS YLNECGVLVQ LDLEPCNGTD PDHVSRAFDI YNKDVACIGK FLKTNCSRFR
     NLDKHDAYYV VKRCTKSVMD HEQVCYNDLK DSGVVAEHDF FLYKEGRCEF GNVARKDLTK
     YTMMDLCYAI RNFDEKNCEV LKEILVTLGA CNESFFENKD WFDPVENEAI HEVYARLGPI
     VANAMLKCVA FCDAIVEKGY IGIITLDNQD LNGNFYDFGD FVKTTPGFGC ACVTSYYSYM
     MPLMGMTSCL ESENFVKSDI YGADYKQYDL LAYDFTDHKE KLFHKYFKHW DRTYHPNCSD
     CTSDECIIHC ANFNTLFSMT IPSTAFGPLV RKVHIDGVPV VVTAGYHFKQ LGIVWNLDVK
     LDTMKLSMTD LLRFVTDPTL LVASSPALLD QRTVCFSIAA LSTGVTYQTV KPGHFNKDFY
     DFITERGFFE EGSELTLKHF FFAQGGEAAM TDFNYYRYNR VTVLDICQAQ FVYKIVGKYF
     ECYDGGCINA REVVVTNYDK SAGYPLNKFG KARLYYETLS YEEQDALFAL TKRNVLPTMT
     QMNLKYAISG KARARTVGGV SLLSTMTTRQ YHQKHLKSIA ATRNATVVIG STKFYGGWDN
     MLKNLMRDVD NGCLMGWDYP KCDRALPNMI RMASAMILGS KHVGCCTHSD RFYRLSNELA
     QVLTEVVHCT GGFYFKPGGT TSGDGTTAYA NSAFNIFQAV SANVNKLLGV DSNACNNVTV
     KSIQRKIYDN CYRSSSIDEE FVVEYFSYLR KHFSMMILSD DGVVCYNKDY ADLGYVADIN
     AFKATLYYQN NVFMSTSKCW VEPDLSVGPH EFCSQHTLQI VGPDGDYYLP YPDPSRILSA
     GVFVDDIVKT DNVIMLERYV SLAIDAYPLT KHPKPAYQKV FYTLLDWVKH LQKNLNAGVL
     DSFSVTMLEE GQDKFWSEEF YASLYEKSTV LQAAGMCVVC GSQTVLRCGD CLRRPLLCTK
     CAYDHVMGTK HKFIMSITPY VCSFNGCNVN DVTKLFLGGL SYYCMDHKPQ LSFPLCANGN
     VFGLYKSSAV GSEDVEDFNK LAVSDWTNVE DYKLANNVKE SLKIFAAETV KAKEESVKSE
     YAYAILKEVI GPKEIVLQWE ASKTKPPLNR NSVFTCFQIS KDTKIQLGEF VFEQSEYGSD
     SVYYKSTSTY KLTPGMIFVL TSHNVSPLKA TILVNQEKYN TISKLYPVFN IAEAYNTLVP
     YYQMIGKQKF TTIQGPPGSG KSHCVIGLGL YYPQARIVYT ACSHAAVDAL CEKAAKNFNV
     DRCSRIIPQR IRVDCYTGFK PNNTNAQYLF CTVNALPEAS CDIVVVDEVS MCTNYDLSVI
     NSRLSYKHIV YVGDPQQLPA PRTLINKGVL QPQDYNVVTQ RVCTLGPDVF LHKCYRCPAE
     IVKTVSALVY ENKFVPVNPE SKQCFKMFVK GQVQIESNSS INNKQLEVVK AFLAHNPKWR
     KAVFISPYNS QNYVARRLLG LQTQTVDSAQ GSEYDYVIYT QTSDTQHATN VNRFNVAITR
     AKVGILCIMC DRTMYENLDF YELKDSKIGL QAKPETCGLF KDCSKSEQYI PPAYATTYMS
     LSDNFKTSDG LAVNIGTKDV KYANVISYMG FRFEANIPGY HTLFCTRDFA MRNVRAWLGF
     DVEGAHVCGD NVGTNVPLQL GFSNGVDFVV QTEGCVVTEK GNSIEVVKAR APPGEQFAHL
     IPLMRKGQPW HIVRRRIVQM VCDYFDGLSD ILIFVLWAGG LELTTMRYFV KIGRPQKCEC
     GKSATCYSSS QCVYACFKHA LGCDYLYNPY CIDIQQWGYT GSLSMNHHEV CNIHRNEHVA
     SGDAIMTRCL AIHDCFVKRV DWSIVYPFID NEEKINKAGR IVQSHVMKAA LKIFNPAAIH
     DVGNPKGIRC ATTPIPWFCY DRDPINNNVR CLEYDYMVHG QMNGLMLFWN CNVDMYPEFS
     IVCRFDTRTR SKLSLEGCNG GALYVNNHAF HTPAYDRRAF AKLKPMPFFY YDDSNCELVD
     GQPNYVPLKS NVCITKCNIG GAVCKKHAAL YRAYVEDYNM FMQAGFTIWC PQNFDTYMLW
     HGFVNSKALQ SLENVAFNVV KKGAFTGLKG DLPTAVIADK IMVRDGPTDK CIFTNKTSLP
     TNVAFELYAK RKLGLTPPLT ILRNLGVVAT YKFVLWDYEA ECPFSNFTKQ VCSYTDLDSE
     VVTCFDNSIA GSFERFTTTK DAVLISNNAV KGLSAIKLQY GFLNDLPVST VGNKPVTWYI
     YVRKNGEYVE QIDSYYTHGR TFETFKPRST MEEDFLSMDT TLFIQKYGLE DYGFEHVVFG
     DVSKTTIGGM HLLISQVRLA KMGLFSVQEF MTNSDSTLKS CCITYADDPS SKNVCTYMDI
     LLDDFVTIIK SLDLNVVSKV VDVIVDCKAW RWMLWCENSQ IKTFYPQLQS AEWNPGYSMP
     TLYKIQRMCL ERCNLYNYGA QVRLPDGITT NVVKYTQLCQ YLNTTTVCVP HKMRVLHLGA
     AGASGVAPGS TVLRRWLPDD AILVDNDLRD YVSDADFSVT GDCTSLYIED KFDLLISDLY
     DGSTKSIDGE NTSKDGFFTY INGFIKEKLS LGGSAAIKIT EFSWNKDLYE LIQRFEYWTV
     FCTSVNTSSS EGFLIGINYL GPYCDKAIVD GNIMHANYIF WRNSTIMALS HNSVLDTPKF
     KCRCNNALIV NLKEKELNEM VVGLLRKGKL LIRNNGKLLN FGNHLVNVP
 
 
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