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Replicase polyprotein 1ab (pp1ab) (ORF1ab polyprotein) [Cleaved into: Host translation inhibitor nsp1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Papain-like proteinase (PL-PRO) (EC 3.4.19.12) (EC 3.4.22.69) (Non-structural protein 3) (nsp3); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (nsp12); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (nsp13); Guanine-N7 methyltransferase (ExoN) (EC 2.1.1.-) (EC 3.1.13.-) (nsp14); Uridylate-specific endoribonuclease (EC 3.1.-.-) (NendoU) (nsp15); 2'-O-methyltransferase (EC 2.1.1.-) (nsp16)]

 R1AB_MERS1              Reviewed;        7078 AA.
K9N7C7;
29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
06-MAR-2013, sequence version 1.
07-APR-2021, entry version 55.
RecName: Full=Replicase polyprotein 1ab;
Short=pp1ab;
AltName: Full=ORF1ab polyprotein;
Contains:
RecName: Full=Host translation inhibitor nsp1;
Short=nsp1;
AltName: Full=Leader protein;
Contains:
RecName: Full=Non-structural protein 2;
Short=nsp2;
AltName: Full=p65 homolog;
Contains:
RecName: Full=Papain-like proteinase;
Short=PL-PRO;
EC=3.4.19.12;
EC=3.4.22.69;
AltName: Full=Non-structural protein 3;
Short=nsp3;
Contains:
RecName: Full=Non-structural protein 4;
Short=nsp4;
Contains:
RecName: Full=3C-like proteinase;
Short=3CL-PRO;
Short=3CLp;
EC=3.4.22.-;
AltName: Full=nsp5;
Contains:
RecName: Full=Non-structural protein 6;
Short=nsp6;
Contains:
RecName: Full=Non-structural protein 7;
Short=nsp7;
Contains:
RecName: Full=Non-structural protein 8;
Short=nsp8;
Contains:
RecName: Full=Non-structural protein 9;
Short=nsp9;
Contains:
RecName: Full=Non-structural protein 10;
Short=nsp10;
AltName: Full=Growth factor-like peptide;
Short=GFL;
Contains:
RecName: Full=RNA-directed RNA polymerase;
Short=Pol;
Short=RdRp;
EC=2.7.7.48;
AltName: Full=nsp12;
Contains:
RecName: Full=Helicase;
Short=Hel;
EC=3.6.4.12;
EC=3.6.4.13;
AltName: Full=nsp13;
Contains:
RecName: Full=Guanine-N7 methyltransferase;
Short=ExoN;
EC=2.1.1.-;
EC=3.1.13.-;
AltName: Full=nsp14;
Contains:
RecName: Full=Uridylate-specific endoribonuclease;
EC=3.1.-.-;
AltName: Full=NendoU;
AltName: Full=nsp15;
Contains:
RecName: Full=2'-O-methyltransferase;
EC=2.1.1.-;
AltName: Full=nsp16;
Name=rep; ORFNames=1a-1b;
Middle East respiratory syndrome-related coronavirus (isolate United
Kingdom/H123990006/2012) (MERS-CoV) (Betacoronavirus England 1).
Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
Betacoronavirus; Merbecovirus.
NCBI_TaxID=1263720;
NCBI_TaxID=9838; Camelus dromedarius (Dromedary) (Arabian camel).
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=23078800;
Bermingham A., Chand M.A., Brown C.S., Aarons E., Tong C., Langrish C.,
Hoschler K., Brown K., Galiano M., Myers R., Pebody R.G., Green H.K.,
Boddington N.L., Gopal R., Price N., Newsholme W., Drosten C.,
Fouchier R.A., Zambon M.;
"Severe respiratory illness caused by a novel coronavirus, in a patient
transferred to the United Kingdom from the Middle East, September 2012.";
Eurosurveillance 17:20290-20290(2012).
[2]
FUNCTION (PAPAIN-LIKE PROTEINASE).
PubMed=25142582; DOI=10.1128/jvi.01294-14;
Baez-Santos Y.M., Mielech A.M., Deng X., Baker S., Mesecar A.D.;
"Catalytic function and substrate specificity of the papain-like protease
domain of nsp3 from the Middle East respiratory syndrome coronavirus.";
J. Virol. 88:12511-12527(2014).
[3]
FUNCTION (NSP1).
PubMed=26311885; DOI=10.1128/jvi.01352-15;
Lokugamage K.G., Narayanan K., Nakagawa K., Terasaki K., Ramirez S.I.,
Tseng C.T., Makino S.;
"Middle east respiratory syndrome coronavirus nsp1 inhibits host gene
expression by selectively targeting mRNAs transcribed in the nucleus while
sparing mRNAs of cytoplasmic origin.";
J. Virol. 89:10970-10981(2015).
-!- FUNCTION: The replicase polyprotein of coronaviruses is a
multifunctional protein: it contains the activities necessary for the
transcription of negative stranded RNA, leader RNA, subgenomic mRNAs
and progeny virion RNA as well as proteinases responsible for the
cleavage of the polyprotein into functional products.
{ECO:0000250|UniProtKB:P0C6X7}.
-!- FUNCTION: [Host translation inhibitor nsp1]: Promotes the degradation
of host mRNAs by inducing an endonucleolytic RNA cleavage in template
mRNAs, and inhibits of host mRNA translation, a function that is
separable from its RNA cleavage activity. By suppressing host gene
expression, nsp1 facilitates efficient viral gene expression in
infected cells and evasion from host immune response.
{ECO:0000269|PubMed:26311885}.
-!- FUNCTION: [Non-structural protein 2]: May play a role in the modulation
of host cell survival signaling pathway by interacting with host PHB
and PHB2. Indeed, these two proteins play a role in maintaining the
functional integrity of the mitochondria and protecting cells from
various stresses. {ECO:0000250|UniProtKB:P0C6X7}.
-!- FUNCTION: [Papain-like proteinase]: Responsible for the cleavages
located at the N-terminus of the replicase polyprotein. In addition,
PL-PRO possesses a deubiquitinating/deISGylating activity and processes
both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular
substrates. Participates, together with nsp4, in the assembly of
virally induced cytoplasmic double-membrane vesicles necessary for
viral replication. Antagonizes innate immune induction of type I
interferon by blocking the phosphorylation, dimerization and subsequent
nuclear translocation of host IRF3. Prevents also host NF-kappa-B.
signaling. {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:25142582}.
-!- FUNCTION: [Non-structural protein 4]: Participates in the assembly of
virally-induced cytoplasmic double-membrane vesicles necessary for
viral replication. {ECO:0000250|UniProtKB:P0C6X7}.
-!- FUNCTION: [3C-like proteinase]: Cleaves the C-terminus of replicase
polyprotein at 11 sites. Recognizes substrates containing the core
sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''-
phosphate (ADRP). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000255|PROSITE-
ProRule:PRU00772}.
-!- FUNCTION: [Non-structural protein 6]: Plays a role in the initial
induction of autophagosomes from host reticulum endoplasmic. Later,
limits the expansion of these phagosomes that are no longer able to
deliver viral components to lysosomes. {ECO:0000250|UniProtKB:P0C6X7}.
-!- FUNCTION: [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8
subunits of each) that may participate in viral replication by acting
as a primase. Alternatively, may synthesize substantially longer
products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}.
-!- FUNCTION: [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8
subunits of each) that may participate in viral replication by acting
as a primase. Alternatively, may synthesize substantially longer
products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}.
-!- FUNCTION: [Non-structural protein 9]: May participate in viral
replication by acting as a ssRNA-binding protein.
{ECO:0000250|UniProtKB:P0C6X7}.
-!- FUNCTION: [Non-structural protein 10]: Plays a pivotal role in viral
transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16
2'-O-methyltransferase activities. Therefore plays an essential role in
viral mRNAs cap methylation. {ECO:0000250|UniProtKB:P0C6X7}.
-!- FUNCTION: [RNA-directed RNA polymerase]: Responsible for replication
and transcription of the viral RNA genome.
{ECO:0000250|UniProtKB:P0C6X7}.
-!- FUNCTION: [Helicase]: Multi-functional protein with a zinc-binding
domain in N-terminus displaying RNA and DNA duplex-unwinding activities
with 5' to 3' polarity. Activity of helicase is dependent on magnesium.
{ECO:0000250|UniProtKB:P0C6X7}.
-!- FUNCTION: [Guanine-N7 methyltransferase]: Enzyme possessing two
different activities: an exoribonuclease activity acting on both ssRNA
and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase
activity. {ECO:0000250|UniProtKB:P0C6X7}.
-!- FUNCTION: [Uridylate-specific endoribonuclease]: Mn(2+)-dependent,
uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to
the cleaved bond. {ECO:0000250|UniProtKB:P0C6X7}.
-!- FUNCTION: [2'-O-methyltransferase]: Methyltransferase that mediates
mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral
mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16.
Therefore plays an essential role in viral mRNAs cap methylation which
is essential to evade immune system. {ECO:0000250|UniProtKB:P0C6X7}.
-!- CATALYTIC ACTIVITY:
Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA-
COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:83400;
EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
-!- CATALYTIC ACTIVITY:
Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
-!- CATALYTIC ACTIVITY:
Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
-!- CATALYTIC ACTIVITY:
Reaction=TSAVLQ-|-SGFRK-NH(2) and SGVTFQ-|-GKFKK the two peptides
corresponding to the two self-cleavage sites of the SARS 3C-like
proteinase are the two most reactive peptide substrates. The enzyme
exhibits a strong preference for substrates containing Gln at P1
position and Leu at P2 position.; EC=3.4.22.69;
-!- CATALYTIC ACTIVITY:
Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
residue protein attached to proteins as an intracellular targeting
signal).; EC=3.4.19.12;
-!- SUBUNIT: Nsp2 interacts with host PHB and PHB2. 3CL-PRO exists as
monomer and homodimer. Nsp4 interacts with PL-PRO and nsp6. Only the
homodimer shows catalytic activity. Eight copies of nsp7 and eight
copies of nsp8 assemble to form a heterohexadecamer dsRNA-encircling
ring structure. Nsp9 is a dimer. Nsp10 forms a dodecamer and interacts
with nsp14 and nsp16; these interactions enhance nsp14 and nsp16
enzymatic activities. Nsp14 interacts (via N-terminus) with DDX1.
{ECO:0000250|UniProtKB:P0C6X7}.
-!- INTERACTION:
PRO_0000422441; Q96PM5: RCHY1; Xeno; NbExp=2; IntAct=EBI-25592237, EBI-947779;
PRO_0000422446; PRO_0000422452 [K9N7C7]: rep; NbExp=2; IntAct=EBI-25592080, EBI-25592093;
PRO_0000422452; PRO_0000422452 [K9N7C7]: rep; NbExp=2; IntAct=EBI-25592093, EBI-25592093;
-!- SUBCELLULAR LOCATION: [Papain-like proteinase]: Host membrane; Multi-
pass membrane protein. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}.
-!- SUBCELLULAR LOCATION: [Non-structural protein 4]: Host membrane; Multi-
pass membrane protein. Host cytoplasm. Note=Localizes in virally-
induced cytoplasmic double-membrane vesicles.
{ECO:0000250|UniProtKB:P0C6X7}.
-!- SUBCELLULAR LOCATION: [Non-structural protein 6]: Host membrane
{ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: [Non-structural protein 7]: Host cytoplasm, host
perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are
localized in cytoplasmic foci, largely perinuclear. Late in infection,
they merge into confluent complexes (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: [Non-structural protein 8]: Host cytoplasm, host
perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are
localized in cytoplasmic foci, largely perinuclear. Late in infection,
they merge into confluent complexes (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: [Non-structural protein 9]: Host cytoplasm, host
perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are
localized in cytoplasmic foci, largely perinuclear. Late in infection,
they merge into confluent complexes (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: [Non-structural protein 10]: Host cytoplasm, host
perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are
localized in cytoplasmic foci, largely perinuclear. Late in infection,
they merge into confluent complexes (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: [Helicase]: Host endoplasmic reticulum-Golgi
intermediate compartment {ECO:0000305}. Note=The helicase interacts
with the N protein in membranous complexes and colocalizes with sites
of synthesis of new viral RNA. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: [Uridylate-specific endoribonuclease]: Host
cytoplasm, host perinuclear region {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=2;
Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
IsoId=K9N7C7-1; Sequence=Displayed;
Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
IsoId=K9N638-1; Sequence=External;
-!- DOMAIN: The hydrophobic domains (HD) could mediate the membrane
association of the replication complex and thereby alter the
architecture of the host cell membrane.
-!- PTM: Specific enzymatic cleavages in vivo by its own proteases yield
mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically
processed (By similarity). {ECO:0000250}.
-!- MISCELLANEOUS: [Isoform Replicase polyprotein 1ab]: Produced by -1
ribosomal frameshifting at the 1a-1b genes boundary.
-!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
{ECO:0000305}.
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EMBL; KC164505; AFY13306.1; -; Genomic_RNA.
PDB; 4WUR; X-ray; 3.16 A; A=1482-1801.
PDB; 5HOL; X-ray; 1.59 A; A=1109-1275.
PDB; 5KO3; X-ray; 1.95 A; A=1544-1800.
PDBsum; 4WUR; -.
PDBsum; 5HOL; -.
PDBsum; 5KO3; -.
SMR; K9N7C7; -.
BioGRID; 4383886; 4.
BioGRID; 4383887; 27.
BioGRID; 4383888; 4.
BioGRID; 4383889; 8.
BioGRID; 4383890; 17.
BioGRID; 4383891; 2.
BioGRID; 4383892; 20.
BioGRID; 4383893; 36.
BioGRID; 4383894; 12.
BioGRID; 4383895; 3.
BioGRID; 4383897; 29.
BioGRID; 4383898; 10.
BioGRID; 4383899; 3.
BioGRID; 4383900; 18.
ComplexPortal; CPX-5746; MERS-CoV primase complex.
ComplexPortal; CPX-5772; MERS-CoV NSP3-NSP4 complex.
ComplexPortal; CPX-5777; MERS-CoV main protease complex.
ComplexPortal; CPX-5778; MERS-CoV NSP9 complex.
ComplexPortal; CPX-5779; MERS-CoV polymerase complex.
ComplexPortal; CPX-5783; MERS-CoV 3'-5' exoribonuclease proof-reading complex.
ComplexPortal; CPX-5784; MERS-CoV NSP10-NSP16 2'-O-methyltransferase complex.
ComplexPortal; CPX-5785; MERS-CoV NSP15 complex.
IntAct; K9N7C7; 188.
BindingDB; K9N7C7; -.
ChEMBL; CHEMBL4295557; -.
DrugBank; DB15797; GC-373.
DrugBank; DB15796; GC-376 free acid.
DrugBank; DB14761; Remdesivir.
SABIO-RK; K9N7C7; -.
Proteomes; UP000139997; Genome.
GO; GO:0044172; C:host cell endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
GO; GO:0004532; F:exoribonuclease activity; IEA:InterPro.
GO; GO:0002151; F:G-quadruplex RNA binding; IEA:InterPro.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0003727; F:single-stranded RNA binding; IEA:InterPro.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IEA:UniProtKB-EC.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0039595; P:induction by virus of catabolism of host mRNA; IEA:UniProtKB-KW.
GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
GO; GO:0039648; P:modulation by virus of host protein ubiquitination; IEA:UniProtKB-KW.
GO; GO:0071108; P:protein K48-linked deubiquitination; IDA:UniProtKB.
GO; GO:0070536; P:protein K63-linked deubiquitination; IDA:UniProtKB.
GO; GO:0039503; P:suppression by virus of host innate immune response; IDA:UniProtKB.
GO; GO:0039579; P:suppression by virus of host ISG15 activity; IDA:UniProtKB.
GO; GO:0039644; P:suppression by virus of host NF-kappaB transcription factor activity; IEA:UniProtKB-KW.
GO; GO:0039653; P:suppression by virus of host transcription; IDA:UniProtKB.
GO; GO:0039604; P:suppression by virus of host translation; IDA:UniProtKB.
GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0019082; P:viral protein processing; IEA:InterPro.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
CDD; cd21409; 1B_cv_Nsp13-like; 1.
CDD; cd21560; betaCoV-Nsp6; 1.
CDD; cd21659; betaCoV_Nsp14; 1.
CDD; cd21666; betaCoV_Nsp5_Mpro; 1.
CDD; cd20762; capping_2-OMTase_Nidovirales; 1.
CDD; cd21517; cv_beta_Nsp2_MERS-like; 1.
CDD; cd21473; cv_Nsp4_TM; 1.
CDD; cd21165; M_cv-Nsp15-like; 1.
CDD; cd21563; Macro_cv_SUD-M_Nsp3-like; 1.
CDD; cd21557; Macro_X_Nsp3-like; 1.
CDD; cd21592; MERS-CoV-like_RdRp; 1.
CDD; cd21161; NendoU_cv_Nsp15-like; 1.
CDD; cd21171; NTD_alpha_beta_cv_Nsp15-like; 1.
CDD; cd21523; SUD_C_MERS-CoV_Nsp3; 1.
CDD; cd21467; Ubl1_cv_Nsp3_N-like; 1.
CDD; cd21466; Ubl2_cv_PLpro_N_Nsp3-like; 1.
CDD; cd21401; ZBD_cv_Nsp13-like; 1.
Gene3D; 1.10.150.420; -; 1.
Gene3D; 1.10.1840.10; -; 1.
Gene3D; 1.10.8.1190; -; 1.
Gene3D; 1.10.8.370; -; 1.
Gene3D; 2.20.25.360; -; 1.
Gene3D; 2.40.10.10; -; 2.
Gene3D; 2.40.10.250; -; 1.
Gene3D; 2.40.10.290; -; 1.
Gene3D; 3.10.20.350; -; 1.
Gene3D; 3.10.20.540; -; 1.
Gene3D; 3.40.220.10; -; 1.
Gene3D; 3.40.220.20; -; 1.
Gene3D; 3.40.50.11020; -; 1.
Gene3D; 3.40.50.11580; -; 1.
Gene3D; 3.90.70.90; -; 1.
InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
InterPro; IPR043608; CoV_NSP15_M.
InterPro; IPR043606; CoV_NSP15_N.
InterPro; IPR043613; CoV_NSP2_C.
InterPro; IPR043611; CoV_NSP3_C.
InterPro; IPR043612; CoV_NSP4_N.
InterPro; IPR043502; DNA/RNA_pol_sf.
InterPro; IPR041679; DNA2/NAM7-like_C.
InterPro; IPR037227; EndoU-like.
InterPro; IPR002589; Macro_dom.
InterPro; IPR043472; Macro_dom-like.
InterPro; IPR044371; Macro_X_NSP3-like.
InterPro; IPR042570; NAR_sf.
InterPro; IPR043609; NendoU_nidovirus.
InterPro; IPR036333; NSP10_sf_CoV.
InterPro; IPR044343; NSP13_1B_dom_CoV.
InterPro; IPR027352; NSP13_ZBD_CoV-like.
InterPro; IPR044315; NSP14_betaCoV.
InterPro; IPR009466; NSP14_CoV.
InterPro; IPR044330; NSP15_alpha_betaCoV_N.
InterPro; IPR044327; NSP15_M_betaCoV.
InterPro; IPR043174; NSP15_middle_sf.
InterPro; IPR042515; NSP15_N_CoV.
InterPro; IPR044401; NSP15_NendoU_CoV.
InterPro; IPR009461; NSP16_CoV-like.
InterPro; IPR021590; NSP1_bCoV.
InterPro; IPR044388; NSP2_MERS-like.
InterPro; IPR043615; NSP2_N_CoV.
InterPro; IPR024375; NSP3_bCoV.
InterPro; IPR032592; NSP3_NAR_bCoV.
InterPro; IPR038400; NSP3_SUD-M_sf_bCoV.
InterPro; IPR044382; NSP3_SUD_C_MERS-CoV.
InterPro; IPR044357; NSP3_Ubl1_dom_CoV.
InterPro; IPR044353; Nsp3_Ubl2_dom_CoV.
InterPro; IPR038083; NSP3A-like.
InterPro; IPR032505; NSP4_C_CoV.
InterPro; IPR038123; NSP4_C_sf_CoV.
InterPro; IPR044367; NSP6_betaCoV.
InterPro; IPR043610; NSP6_CoV.
InterPro; IPR014828; NSP7_CoV.
InterPro; IPR037204; NSP7_sf_CoV.
InterPro; IPR014829; NSP8_CoV-like.
InterPro; IPR037230; NSP8_sf_CoV.
InterPro; IPR014822; NSP9_CoV.
InterPro; IPR036499; NSP9_sf_CoV.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR013016; Peptidase_C16_CoV.
InterPro; IPR008740; Peptidase_C30_CoV.
InterPro; IPR043477; Peptidase_C30_dom3_CoV.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
InterPro; IPR043177; PLpro_N_sf_CoV.
InterPro; IPR043503; PLpro_palm_finger_dom_CoV.
InterPro; IPR043178; PLpro_thumb_sf_CoV.
InterPro; IPR044350; RdRp_MERS-CoV-like.
InterPro; IPR001205; RNA-dir_pol_C.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR009469; RNA_pol_N_coronovir.
InterPro; IPR018995; RNA_synth_NSP10_CoV.
InterPro; IPR029063; SAM-dependent_MTases.
Pfam; PF13087; AAA_12; 1.
Pfam; PF16251; bCoV_NAR; 1.
Pfam; PF11501; bCoV_NSP1; 1.
Pfam; PF11633; bCoV_SUD_M; 1.
Pfam; PF06471; CoV_Methyltr_1; 1.
Pfam; PF06460; CoV_Methyltr_2; 1.
Pfam; PF09401; CoV_NSP10; 1.
Pfam; PF19215; CoV_NSP15_C; 1.
Pfam; PF19216; CoV_NSP15_M; 1.
Pfam; PF19219; CoV_NSP15_N; 1.
Pfam; PF19212; CoV_NSP2_C; 1.
Pfam; PF19211; CoV_NSP2_N; 1.
Pfam; PF19218; CoV_NSP3_C; 1.
Pfam; PF16348; CoV_NSP4_C; 1.
Pfam; PF19217; CoV_NSP4_N; 1.
Pfam; PF19213; CoV_NSP6; 1.
Pfam; PF08716; CoV_NSP7; 1.
Pfam; PF08717; CoV_NSP8; 1.
Pfam; PF08710; CoV_NSP9; 1.
Pfam; PF08715; CoV_peptidase; 1.
Pfam; PF06478; CoV_RPol_N; 1.
Pfam; PF01661; Macro; 1.
Pfam; PF05409; Peptidase_C30; 1.
Pfam; PF00680; RdRP_1; 1.
SMART; SM00506; A1pp; 1.
SUPFAM; SSF101816; SSF101816; 1.
SUPFAM; SSF140367; SSF140367; 1.
SUPFAM; SSF142877; SSF142877; 1.
SUPFAM; SSF143076; SSF143076; 1.
SUPFAM; SSF144246; SSF144246; 1.
SUPFAM; SSF159936; SSF159936; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF52949; SSF52949; 1.
SUPFAM; SSF53335; SSF53335; 1.
SUPFAM; SSF56672; SSF56672; 1.
PROSITE; PS51942; BCOV_NSP3C_C; 1.
PROSITE; PS51941; BCOV_NSP3C_M; 1.
PROSITE; PS51945; BCOV_NSP3E_NAB; 1.
PROSITE; PS51952; COV_EXON_MTASE_COACT; 1.
PROSITE; PS51954; COV_N7_MTASE; 1.
PROSITE; PS51948; COV_NSP12_RDRP; 1.
PROSITE; PS51943; COV_NSP3A_UBL; 1.
PROSITE; PS51944; COV_NSP3D_UBL; 1.
PROSITE; PS51946; COV_NSP4C; 1.
PROSITE; PS51949; COV_NSP7; 1.
PROSITE; PS51950; COV_NSP8; 1.
PROSITE; PS51951; COV_NSP9_SSRNA_BD; 1.
PROSITE; PS51653; CV_ZBD; 1.
PROSITE; PS51442; M_PRO; 1.
PROSITE; PS51154; MACRO; 1.
PROSITE; PS51947; NIRAN; 1.
PROSITE; PS51955; NIV_2_O_MTASE; 1.
PROSITE; PS51953; NIV_EXON; 1.
PROSITE; PS51124; PEPTIDASE_C16; 1.
PROSITE; PS51657; PSRV_HELICASE; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
1: Evidence at protein level;
3D-structure; Activation of host autophagy by virus; ATP-binding;
Decay of host mRNAs by virus; Endonuclease;
Eukaryotic host gene expression shutoff by virus;
Eukaryotic host translation shutoff by virus; Exonuclease; Helicase;
Host cytoplasm; Host gene expression shutoff by virus; Host membrane;
Host mRNA suppression by virus; Host-virus interaction; Hydrolase;
Inhibition of host innate immune response by virus;
Inhibition of host interferon signaling pathway by virus;
Inhibition of host ISG15 by virus; Inhibition of host NF-kappa-B by virus;
Membrane; Metal-binding; Methyltransferase;
Modulation of host ubiquitin pathway by viral deubiquitinase;
Modulation of host ubiquitin pathway by virus; Nuclease;
Nucleotide-binding; Nucleotidyltransferase; Protease; Repeat;
Ribosomal frameshifting; RNA-binding; RNA-directed RNA polymerase;
Thiol protease; Transferase; Transmembrane; Transmembrane helix;
Ubl conjugation pathway; Viral immunoevasion; Viral RNA replication; Zinc;
Zinc-finger.
CHAIN 1..193
/note="Host translation inhibitor nsp1"
/evidence="ECO:0000250|UniProtKB:P0C6X7"
/id="PRO_0000422439"
CHAIN 194..853
/note="Non-structural protein 2"
/evidence="ECO:0000250|UniProtKB:P0C6X7"
/id="PRO_0000422440"
CHAIN 854..2740
/note="Papain-like proteinase"
/evidence="ECO:0000250|UniProtKB:P0C6X7"
/id="PRO_0000422441"
CHAIN 2741..3247
/note="Non-structural protein 4"
/evidence="ECO:0000250|UniProtKB:P0C6X7"
/id="PRO_0000422442"
CHAIN 3248..3553
/note="3C-like proteinase"
/evidence="ECO:0000250|UniProtKB:P0C6X7"
/id="PRO_0000422443"
CHAIN 3554..3845
/note="Non-structural protein 6"
/evidence="ECO:0000250|UniProtKB:P0C6X7"
/id="PRO_0000422444"
CHAIN 3846..3928
/note="Non-structural protein 7"
/evidence="ECO:0000250|UniProtKB:P0C6X7"
/id="PRO_0000422445"
CHAIN 3929..4127
/note="Non-structural protein 8"
/evidence="ECO:0000250|UniProtKB:P0C6X7"
/id="PRO_0000422446"
CHAIN 4128..4237
/note="Non-structural protein 9"
/evidence="ECO:0000250|UniProtKB:P0C6X7"
/id="PRO_0000422447"
CHAIN 4238..4377
/note="Non-structural protein 10"
/evidence="ECO:0000250|UniProtKB:P0C6X7"
/id="PRO_0000422448"
CHAIN 4378..5310
/note="RNA-directed RNA polymerase"
/evidence="ECO:0000250|UniProtKB:P0C6X7"
/id="PRO_0000422449"
CHAIN 5311..5908
/note="Helicase"
/evidence="ECO:0000250|UniProtKB:P0C6X7"
/id="PRO_0000422450"
CHAIN 5909..6432
/note="Guanine-N7 methyltransferase"
/evidence="ECO:0000250, ECO:0000250|UniProtKB:P0C6X7"
/id="PRO_0000422451"
CHAIN 6433..6775
/note="Uridylate-specific endoribonuclease"
/evidence="ECO:0000250|UniProtKB:P0C6X7"
/id="PRO_0000422452"
CHAIN 6776..7078
/note="2'-O-methyltransferase"
/evidence="ECO:0000250|UniProtKB:P0C6X7"
/id="PRO_0000422453"
TRANSMEM 2105..2125
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 2177..2197
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 2281..2301
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 2305..2325
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 2330..2350
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 2757..2777
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 3028..3048
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 3062..3082
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 3104..3124
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 3125..3145
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 3559..3579
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 3593..3613
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 3618..3638
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 3664..3684
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 3691..3711
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 3740..3760
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 3765..3785
/note="Helical"
/evidence="ECO:0000255"
DOMAIN 856..966
/note="Ubiquitin-like 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
DOMAIN 1110..1276
/note="Macro 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
DOMAIN 1278..1404
/note="Macro 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
DOMAIN 1404..1477
/note="DPUP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01289"
DOMAIN 1482..1537
/note="Ubiquitin-like 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
DOMAIN 1552..1823
/note="Peptidase C16"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
DOMAIN 1837..1954
/note="Nucleic acid-binding"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01290"
DOMAIN 3151..3247
/note="Nsp4C"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01291"
DOMAIN 3248..3553
/note="Peptidase C30"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
DOMAIN 3846..3928
/note="RdRp Nsp7 cofactor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01294"
DOMAIN 3929..4127
/note="RdRp Nsp8 cofactor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01295"
DOMAIN 4128..4237
/note="Nsp9 ssRNA-binding"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01296"
DOMAIN 4238..4377
/note="ExoN/MTase coactivator"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
DOMAIN 4383..4639
/note="NiRAN"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01292"
DOMAIN 4743..5310
/note="Nsp12 RNA-dependent RNA polymerase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
DOMAIN 4990..5152
/note="RdRp catalytic"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
DOMAIN 5311..5394
/note="CV ZBD"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
DOMAIN 5980..6195
/note="ExoN"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
DOMAIN 6204..6432
/note="N7-MTase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
DOMAIN 6777..7071
/note="Nidovirus-type SAM-dependent 2'-O-MTase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
ZN_FING 1672..1709
/note="C4-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
ZN_FING 4311..4327
ZN_FING 4354..4367
NP_BIND 5592..5599
/note="ATP"
/evidence="ECO:0000250"
REGION 2040..2363
/note="HD1"
REGION 2761..3171
/note="HD2"
REGION 3571..3785
/note="HD3"
REGION 6239..6245
/note="SAM-binding"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
REGION 6318..6332
/note="GpppA-binding"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
ACT_SITE 1592
/note="For PL-PRO activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
ACT_SITE 1759
/note="For PL-PRO activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
ACT_SITE 3288
/note="For 3CL-PRO activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
ACT_SITE 3395
/note="For 3CL-PRO activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
ACT_SITE 5137
/evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
ACT_SITE 5138
/evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
ACT_SITE 5139
/evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
ACT_SITE 5998
/evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
ACT_SITE 6000
/evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
ACT_SITE 6099
/evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
ACT_SITE 6176
/evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
ACT_SITE 6181
/evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
ACT_SITE 6821
/evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
ACT_SITE 6905
/evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
ACT_SITE 6945
/evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
ACT_SITE 6978
/evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
METAL 4311
/note="Zinc"
METAL 4311
/note="Zinc 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
METAL 4314
/note="Zinc"
METAL 4314
/note="Zinc 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
METAL 4320
/note="Zinc"
METAL 4320
/note="Zinc 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
METAL 4327
/note="Zinc"
METAL 4327
/note="Zinc 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
METAL 4354
/note="Zinc"
METAL 4354
/note="Zinc 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
METAL 4357
/note="Zinc"
METAL 4357
/note="Zinc 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
METAL 4365
/note="Zinc"
METAL 4365
/note="Zinc 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
METAL 4367
/note="Zinc 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
METAL 5315
/note="Zinc 3"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
METAL 5318
/note="Zinc 3"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
METAL 5326
/note="Zinc 4"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
METAL 5329
/note="Zinc 3"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
METAL 5336
/note="Zinc 3"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
METAL 5339
/note="Zinc 4"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
METAL 5343
/note="Zinc 4"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
METAL 5349
/note="Zinc 4"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
METAL 5360
/note="Zinc 5"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
METAL 5365
/note="Zinc 5"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
METAL 5382
/note="Zinc 5"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
METAL 5385
/note="Zinc 5"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
METAL 6115
/note="Zinc 6"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
METAL 6118
/note="Zinc 6"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
METAL 6134
/note="Zinc 6"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
METAL 6137
/note="Zinc 6"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
METAL 6165
/note="Zinc 7"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
METAL 6169
/note="Zinc 7"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
METAL 6172
/note="Zinc 7"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
METAL 6187
/note="Zinc 7"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
METAL 6356
/note="Zinc 8"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
METAL 6378
/note="Zinc 8"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
METAL 6389
/note="Zinc 8"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
METAL 6392
/note="Zinc 8"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
SITE 193..194
/note="Cleavage"
/evidence="ECO:0000250"
SITE 853..854
/note="Cleavage; by PL-PRO"
/evidence="ECO:0000250"
SITE 2740..2741
/note="Cleavage; by PL-PRO"
/evidence="ECO:0000250"
SITE 3247..3248
/note="Cleavage; by 3CL-PRO"
/evidence="ECO:0000250"
SITE 3553..3554
/note="Cleavage; by 3CL-PRO"
/evidence="ECO:0000250"
SITE 3845..3846
/note="Cleavage; by 3CL-PRO"
/evidence="ECO:0000250"
SITE 3928..3929
/note="Cleavage; by 3CL-PRO"
/evidence="ECO:0000250"
SITE 4127..4128
/note="Cleavage; by 3CL-PRO"
/evidence="ECO:0000250"
SITE 4237..4238
/note="Cleavage; by 3CL-PRO"
/evidence="ECO:0000250"
SITE 4377..4378
/note="Cleavage; by 3CL-PRO"
/evidence="ECO:0000250"
SITE 5310..5311
/note="Cleavage; by 3CL-PRO"
/evidence="ECO:0000250"
SITE 5908..5909
/note="Cleavage; by 3CL-PRO"
/evidence="ECO:0000250"
SITE 6432..6433
/note="Cleavage; by 3CL-PRO"
/evidence="ECO:0000250"
SITE 6775..6776
/note="Cleavage; by 3CL-PRO"
/evidence="ECO:0000250"
HELIX 1110..1113
/evidence="ECO:0007744|PDB:5HOL"
STRAND 1116..1118
/evidence="ECO:0007744|PDB:5HOL"
STRAND 1120..1128
/evidence="ECO:0007744|PDB:5HOL"
HELIX 1130..1135
/evidence="ECO:0007744|PDB:5HOL"
STRAND 1141..1146
/evidence="ECO:0007744|PDB:5HOL"
HELIX 1156..1163
/evidence="ECO:0007744|PDB:5HOL"
TURN 1164..1166
/evidence="ECO:0007744|PDB:5HOL"
HELIX 1167..1179
/evidence="ECO:0007744|PDB:5HOL"
STRAND 1187..1191
/evidence="ECO:0007744|PDB:5HOL"
TURN 1193..1195
/evidence="ECO:0007744|PDB:5HOL"
STRAND 1196..1203
/evidence="ECO:0007744|PDB:5HOL"
HELIX 1207..1209
/evidence="ECO:0007744|PDB:5HOL"
HELIX 1213..1215
/evidence="ECO:0007744|PDB:5HOL"
HELIX 1216..1223
/evidence="ECO:0007744|PDB:5HOL"
STRAND 1226..1231
/evidence="ECO:0007744|PDB:5HOL"
HELIX 1243..1253
/evidence="ECO:0007744|PDB:5HOL"
STRAND 1256..1263
/evidence="ECO:0007744|PDB:5HOL"
HELIX 1265..1272
/evidence="ECO:0007744|PDB:5HOL"
STRAND 1485..1494
/evidence="ECO:0007744|PDB:4WUR"
STRAND 1496..1501
/evidence="ECO:0007744|PDB:4WUR"
STRAND 1503..1505
/evidence="ECO:0007744|PDB:4WUR"
HELIX 1507..1510
/evidence="ECO:0007744|PDB:4WUR"
STRAND 1513..1516
/evidence="ECO:0007744|PDB:4WUR"
HELIX 1528..1530
/evidence="ECO:0007744|PDB:4WUR"
STRAND 1534..1537
/evidence="ECO:0007744|PDB:4WUR"
HELIX 1545..1553
/evidence="ECO:0007744|PDB:5KO3"
HELIX 1560..1570
/evidence="ECO:0007744|PDB:5KO3"
HELIX 1571..1573
/evidence="ECO:0007744|PDB:5KO3"
STRAND 1576..1579
/evidence="ECO:0007744|PDB:5KO3"
STRAND 1582..1585
/evidence="ECO:0007744|PDB:5KO3"
TURN 1589..1591
/evidence="ECO:0007744|PDB:5KO3"
HELIX 1592..1601
/evidence="ECO:0007744|PDB:5KO3"
STRAND 1607..1611
/evidence="ECO:0007744|PDB:5KO3"
HELIX 1612..1622
/evidence="ECO:0007744|PDB:5KO3"
HELIX 1627..1636
/evidence="ECO:0007744|PDB:5KO3"
HELIX 1647..1655
/evidence="ECO:0007744|PDB:5KO3"
STRAND 1658..1662
/evidence="ECO:0007744|PDB:5KO3"
STRAND 1665..1672
/evidence="ECO:0007744|PDB:5KO3"
TURN 1673..1675
/evidence="ECO:0007744|PDB:5KO3"
STRAND 1676..1683
/evidence="ECO:0007744|PDB:5KO3"
HELIX 1684..1687
/evidence="ECO:0007744|PDB:5KO3"
STRAND 1688..1692
/evidence="ECO:0007744|PDB:5KO3"
HELIX 1696..1700
/evidence="ECO:0007744|PDB:5KO3"
STRAND 1703..1706
/evidence="ECO:0007744|PDB:5KO3"
STRAND 1708..1721
/evidence="ECO:0007744|PDB:5KO3"
STRAND 1723..1740
/evidence="ECO:0007744|PDB:5KO3"
STRAND 1745..1752
/evidence="ECO:0007744|PDB:5KO3"
STRAND 1759..1766
/evidence="ECO:0007744|PDB:5KO3"
STRAND 1769..1774
/evidence="ECO:0007744|PDB:5KO3"
STRAND 1777..1794
/evidence="ECO:0007744|PDB:5KO3"
STRAND 1797..1799
/evidence="ECO:0007744|PDB:5KO3"
SEQUENCE 7078 AA; 789563 MW; A944AF691D57A1E0 CRC64;
MSFVAGVTAQ GARGTYRAAL NSEKHQDHVS LTVPLCGSGN LVEKLSPWFM DGENAYEVVK
AMLLKKEPLL YVPIRLAGHT RHLPGPRVYL VERLIACENP FMVNQLAYSS SANGSLVGTT
LQGKPIGMFF PYDIELVTGK QNILLRKYGR GGYHYTPFHY ERDNTSCPEW MDDFEADPKG
KYAQNLLKKL IGGDVTPVDQ YMCGVDGKPI SAYAFLMAKD GITKLADVEA DVAARADDEG
FITLKNNLYR LVWHVERKDV PYPKQSIFTI NSVVQKDGVE NTPPHYFTLG CKILTLTPRN
KWSGVSDLSL KQKLLYTFYG KESLENPTYI YHSAFIECGS CGNDSWLTGN AIQGFACGCG
ASYTANDVEV QSSGMIKPNA LLCATCPFAK GDSCSSNCKH SVAQLVSYLS ERCNVIADSK
SFTLIFGGVA YAYFGCEEGT MYFVPRAKSV VSRIGDSIFT GCTGSWNKVT QIANMFLEQT
QHSLNFVGEF VVNDVVLAIL SGTTTNVDKI RQLLKGVTLD KLRDYLADYD VAVTAGPFMD
NAINVGGTGL QYAAITAPYV VLTGLGESFK KVATIPYKVC NSVKDTLTYY AHSVLYRVFP
YDMDSGVSSF SELLFDCVDL SVASTYFLVR LLQDKTGDFM STIITSCQTA VSKLLDTCFE
ATEATFNFLL DLAGLFRIFL RNAYVYTSQG FVVVNGKVST LVKQVLDLLN KGMQLLHTKV
SWAGSNISAV IYSGRESLIF PSGTYYCVTT KAKSVQQDLD VILPGEFSKK QLGLLQPTDN
STTVSVTVSS NMVETVVGQL EQTNMHSPDV IVGDYVIISE KLFVRSKEED GFAFYPACTN
GHAVPTLFRL KGGAPVKKVA FGGDQVHEVA AVRSVTVEYN IHAVLDTLLA SSSLRTFVVD
KSLSIEEFAD VVKEQVSDLL VKLLRGMPIP DFDLDDFIDA PCYCFNAEGD ASWSSTMIFS
LHPVECDEEC SEVEASDLEE GESECISETS TEQVDVSHEI SDDEWAAAVD EAFPLDEAED
VTESVQEEAQ PVEVPVEDIA QVVIADTLQE TPVVSDTVEV PPQVVKLPSE PQTIQPEVKE
VAPVYEADTE QTQSVTVKPK RLRKKRNVDP LSNFEHKVIT ECVTIVLGDA IQVAKCYGES
VLVNAANTHL KHGGGIAGAI NAASKGAVQK ESDEYILAKG PLQVGDSVLL QGHSLAKNIL
HVVGPDARAK QDVSLLSKCY KAMNAYPLVV TPLVSAGIFG VKPAVSFDYL IREAKTRVLV
VVNSQDVYKS LTIVDIPQSL TFSYDGLRGA IRKAKDYGFT VFVCTDNSAN TKVLRNKGVD
YTKKFLTVDG VQYYCYTSKD TLDDILQQAN KSVGIISMPL GYVSHGLDLI QAGSVVRRVN
VPYVCLLANK EQEAILMSED VKLNPSEDFI KHVRTNGGYN SWHLVEGELL VQDLRLNKLL
HWSDQTICYK DSVFYVVKNS TAFPFETLSA CRAYLDSRTT QQLTIEVLVT VDGVNFRTVV
LNNKNTYRSQ LGCVFFNGAD ISDTIPDEKQ NGHSLYLADN LTADETKALK ELYGPVDPTF
LHRFYSLKAA VHKWKMVVCD KVRSLKLSDN NCYLNAVIMT LDLLKDIKFV IPALQHAFMK
HKGGDSTDFI ALIMAYGNCT FGAPDDASRL LHTVLAKAEL CCSARMVWRE WCNVCGIKDV
VLQGLKACCY VGVQTVEDLR ARMTYVCQCG GERHRQIVEH TTPWLLLSGT PNEKLVTTST
APDFVAFNVF QGIETAVGHY VHARLKGGLI LKFDSGTVSK TSDWKCKVTD VLFPGQKYSS
DCNVVRYSLD GNFRTEVDPD LSAFYVKDGK YFTSEPPVTY SPATILAGSV YTNSCLVSSD
GQPGGDAISL SFNNLLGFDS SKPVTKKYTY SFLPKEDGDV LLAEFDTYDP IYKNGAMYKG
KPILWVNKAS YDTNLNKFNR ASLRQIFDVA PIELENKFTP LSVESTPVEP PTVDVVALQQ
EMTIVKCKGL NKPFVKDNVS FVADDSGTPV VEYLSKEDLH TLYVDPKYQV IVLKDNVLSS
MLRLHTVESG DINVVAASGS LTRKVKLLFR ASFYFKEFAT RTFTATTAVG SCIKSVVRHL
GVTKGILTGC FSFVKMLFML PLAYFSDSKL GTTEVKVSAL KTAGVVTGNV VKQCCTAAVD
LSMDKLRRVD WKSTLRLLLM LCTTMVLLSS VYHLYVFNQV LSSDVMFEDA QGLKKFYKEV
RAYLGISSAC DGLASAYRAN SFDVPTFCAN RSAMCNWCLI SQDSITHYPA LKMVQTHLSH
YVLNIDWLWF AFETGLAYML YTSAFNWLLL AGTLHYFFAQ TSIFVDWRSY NYAVSSAFWL
FTHIPMAGLV RMYNLLACLW LLRKFYQHVI NGCKDTACLL CYKRNRLTRV EASTVVCGGK
RTFYITANGG ISFCRRHNWN CVDCDTAGVG NTFICEEVAN DLTTALRRPI NATDRSHYYV
DSVTVKETVV QFNYRRDGQP FYERFPLCAF TNLDKLKFKE VCKTTTGIPE YNFIIYDSSD
RGQESLARSA CVYYSQVLCK SILLVDSSLV TSVGDSSEIA TKMFDSFVNS FVSLYNVTRD
KLEKLISTAR DGVRRGDNFH SVLTTFIDAA RGPAGVESDV ETNEIVDSVQ YAHKHDIQIT
NESYNNYVPS YVKPDSVSTS DLGSLIDCNA ASVNQIVLRN SNGACIWNAA AYMKLSDALK
RQIRIACRKC NLAFRLTTSK LRANDNILSV RFTANKIVGG APTWFNALRD FTLKGYVLAT
IIVFLCAVLM YLCLPTFSMV PVEFYEDRIL DFKVLDNGII RDVNPDDKCF ANKHRSFTQW
YHEHVGGVYD NSITCPLTVA VIAGVAGARI PDVPTTLAWV NNQIIFFVSR VFANTGSVCY
TPIDEIPYKS FSDSGCILPS ECTMFRDAEG RMTPYCHDPT VLPGAFAYSQ MRPHVRYDLY
DGNMFIKFPE VVFESTLRIT RTLSTQYCRF GSCEYAQEGV CITTNGSWAI FNDHHLNRPG
VYCGSDFIDI VRRLAVSLFQ PITYFQLTTS LVLGIGLCAF LTLLFYYINK VKRAFADYTQ
CAVIAVVAAV LNSLCICFVA SIPLCIVPYT ALYYYATFYF TNEPAFIMHV SWYIMFGPIV
PIWMTCVYTV AMCFRHFFWV LAYFSKKHVE VFTDGKLNCS FQDAASNIFV INKDTYAALR
NSLTNDAYSR FLGLFNKYKY FSGAMETAAY REAAACHLAK ALQTYSETGS DLLYQPPNCS
ITSGVLQSGL VKMSHPSGDV EACMVQVTCG SMTLNGLWLD NTVWCPRHVM CPADQLSDPN
YDALLISMTN HSFSVQKHIG APANLRVVGH AMQGTLLKLT VDVANPSTPA YTFTTVKPGA
AFSVLACYNG RPTGTFTVVM RPNYTIKGSF LCGSCGSVGY TKEGSVINFC YMHQMELANG
THTGSAFDGT MYGAFMDKQV HQVQLTDKYC SVNVVAWLYA AILNGCAWFV KPNRTSVVSF
NEWALANQFT EFVGTQSVDM LAVKTGVAIE QLLYAIQQLY TGFQGKQILG STMLEDEFTP
EDVNMQIMGV VMQSGVRKVT YGTAHWLFAT LVSTYVIILQ ATKFTLWNYL FETIPTQLFP
LLFVTMAFVM LLVKHKHTFL TLFLLPVAIC LTYANIVYEP TTPISSALIA VANWLAPTNA
YMRTTHTDIG VYISMSLVLV IVVKRLYNPS LSNFALALCS GVMWLYTYSI GEASSPIAYL
VFVTTLTSDY TITVFVTVNL AKVCTYAIFA YSPQLTLVFP EVKMILLLYT CLGFMCTCYF
GVFSLLNLKL RAPMGVYDFK VSTQEFRFMT ANNLTAPRNS WEAMALNFKL IGIGGTPCIK
VAAMQSKLTD LKCTSVVLLS VLQQLHLEAN SRAWAFCVKC HNDILAATDP SEAFEKFVSL
FATLMTFSGN VDLDALASDI FDTPSVLQAT LSEFSHLATF AELEAAQKAY QEAMDSGDTS
PQVLKALQKA VNIAKNAYEK DKAVARKLER MADQAMTSMY KQARAEDKKA KIVSAMQTML
FGMIKKLDND VLNGIISNAR NGCIPLSVIP LCASNKLRVV IPDFTVWNQV VTYPSLNYAG
ALWDITVINN VDNEIVKSSD VVDSNENLTW PLVLECTRAS TSAVKLQNNE IKPSGLKTMV
VSAGQEQTNC NTSSLAYYEP VQGRKMLMAL LSDNAYLKWA RVEGKDGFVS VELQPPCKFL
IAGPKGPEIR YLYFVKNLNN LHRGQVLGHI AATVRLQAGS NTEFASNSSV LSLVNFTVDP
QKAYLDFVNA GGAPLTNCVK MLTPKTGTGI AISVKPESTA DQETYGGASV CLYCRAHIEH
PDVSGVCKYK GKFVQIPAQC VRDPVGFCLS NTPCNVCQYW IGYGCNCDSL RQAALPQSKD
SNFLKRVRGS IVNARIEPCS SGLSTDVVFR AFDICNYKAK VAGIGKYYKT NTCRFVELDD
QGHHLDSYFV VKRHTMENYE LEKHCYDLLR DCDAVAPHDF FIFDVDKVKT PHIVRQRLTE
YTMMDLVYAL RHFDQNSEVL KAILVKYGCC DVTYFENKLW FDFVENPSVI GVYHKLGERV
RQAILNTVKF CDHMVKAGLV GVLTLDNQDL NGKWYDFGDF VITQPGSGVA IVDSYYSYLM
PVLSMTDCLA AETHRDCDFN KPLIEWPLTE YDFTDYKVQL FEKYFKYWDQ TYHANCVNCT
DDRCVLHCAN FNVLFAMTMP KTCFGPIVRK IFVDGVPFVV SCGYHYKELG LVMNMDVSLH
RHRLSLKELM MYAADPAMHI ASSNAFLDLR TSCFSVAALT TGLTFQTVRP GNFNQDFYDF
VVSKGFFKEG SSVTLKHFFF AQDGNAAITD YNYYSYNLPT MCDIKQMLFC MEVVNKYFEI
YDGGCLNASE VVVNNLDKSA GHPFNKFGKA RVYYESMSYQ EQDELFAMTK RNVIPTMTQM
NLKYAISAKN RARTVAGVSI LSTMTNRQYH QKMLKSMAAT RGATCVIGTT KFYGGWDFML
KTLYKDVDNP HLMGWDYPKC DRAMPNMCRI FASLILARKH GTCCTTRDRF YRLANECAQV
LSEYVLCGGG YYVKPGGTSS GDATTAYANS VFNILQATTA NVSALMGANG NKIVDKEVKD
MQFDLYVNVY RSTSPDPKFV DKYYAFLNKH FSMMILSDDG VVCYNSDYAA KGYIAGIQNF
KETLYYQNNV FMSEAKCWVE TDLKKGPHEF CSQHTLYIKD GDDGYFLPYP DPSRILSAGC
FVDDIVKTDG TLMVERFVSL AIDAYPLTKH EDIEYQNVFW VYLQYIEKLY KDLTGHMLDS
YSVMLCGDNS AKFWEEAFYR DLYSSPTTLQ AVGSCVVCHS QTSLRCGTCI RRPFLCCKCC
YDHVIATPHK MVLSVSPYVC NAPGCGVSDV TKLYLGGMSY FCVDHRPVCS FPLCANGLVF
GLYKNMCTGS PSIVEFNRLA TCDWTESGDY TLANTTTEPL KLFAAETLRA TEEASKQSYA
IATIKEIVGE RQLLLVWEAG KSKPPLNRNY VFTGYHITKN SKVQLGEYIF ERIDYSDAVS
YKSSTTYKLT VGDIFVLTSH SVATLTAPTI VNQERYVKIT GLYPTITVPE EFASHVANFQ
KSGYSKYVTV QGPPGTGKSH FAIGLAIYYP TARVVYTACS HAAVDALCEK AFKYLNIAKC
SRIIPAKARV ECYDRFKVNE TNSQYLFSTI NALPETSADI LVVDEVSMCT NYDLSIINAR
IKAKHIVYVG DPAQLPAPRT LLTRGTLEPE NFNSVTRLMC NLGPDIFLSM CYRCPKEIVS
TVSALVYNNK LLAKKELSGQ CFKILYKGNV THDASSAINR PQLTFVKNFI TANPAWSKAV
FISPYNSQNA VARSMLGLTT QTVDSSQGSE YQYVIFCQTA DTAHANNINR FNVAITRAQK
GILCVMTSQA LFESLEFTEL SFTNYKLQSQ IVTGLFKDCS RETSGLSPAY APTYVSVDDK
YKTSDELCVN LNLPANVPYS RVISRMGFKL DATVPGYPKL FITREEAVRQ VRSWIGFDVE
GAHASRNACG TNVPLQLGFS TGVNFVVQPV GVVDTEWGNM LTGIAARPPP GEQFKHLVPL
MHKGAAWPIV RRRIVQMLSD TLDKLSDYCT FVCWAHGFEL TSASYFCKIG KEQKCCMCNR
RAAAYSSPLQ SYACWTHSCG YDYVYNPFFV DVQQWGYVGN LATNHDRYCS VHQGAHVASN
DAIMTRCLAI HSCFIERVDW DIEYPYISHE KKLNSCCRIV ERNVVRAALL AGSFDKVYDI
GNPKGIPIVD DPVVDWHYFD AQPLTRKVQQ LFYTEDMASR FADGLCLFWN CNVPKYPNNA
IVCRFDTRVH SEFNLPGCDG GSLYVNKHAF HTPAYDVSAF RDLKPLPFFY YSTTPCEVHG
NGSMIEDIDY VPLKSAVCIT ACNLGGAVCR KHATEYREYM EAYNLVSASG FRLWCYKTFD
IYNLWSTFTK VQGLENIAFN FVKQGHFIGV EGELPVAVVN DKIFTKSGVN DICMFENKTT
LPTNIAFELY AKRAVRSHPD FKLLHNLQAD ICYKFVLWDY ERSNIYGTAT IGVCKYTDID
VNSALNICFD IRDNGSLEKF MSTPNAIFIS DRKIKKYPCM VGPDYAYFNG AIIRDSDVVK
QPVKFYLYKK VNNEFIDPTE CIYTQSRSCS DFLPLSDMEK DFLSFDSDVF IKKYGLENYA
FEHVVYGDFS HTTLGGLHLL IGLYKKQQEG HIIMEEMLKG SSTIHNYFIT ETNTAAFKAV
CSVIDLKLDD FVMILKSQDL GVVSKVVKVP IDLTMIEFML WCKDGQVQTF YPRLQASADW
KPGHAMPSLF KVQNVNLERC ELANYKQSIP MPRGVHMNIA KYMQLCQYLN TCTLAVPANM
RVIHFGAGSD KGIAPGTSVL RQWLPTDAII IDNDLNEFVS DADITLFGDC VTVRVGQQVD
LVISDMYDPT TKNVTGSNES KALFFTYLCN LINNNLALGG SVAIKITEHS WSVELYELMG
KFAWWTVFCT NANASSSEGF LLGINYLGTI KENIDGGAMH ANYIFWRNST PMNLSTYSLF
DLSKFQLKLK GTPVLQLKES QINELVISLL SQGKLLIRDN DTLSVSTDVL VNTYRKLR


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Pathways :