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 R1AB_IBVM               Reviewed;        6631 AA.
P0C6Y3; Q0GNB9; Q0GNC0; Q5I5Y0; Q5I5Y1;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
25-OCT-2017, entry version 74.
RecName: Full=Replicase polyprotein 1ab;
Short=pp1ab;
AltName: Full=ORF1ab polyprotein;
Contains:
RecName: Full=Non-structural protein 2;
Short=nsp2;
AltName: Full=p87;
Contains:
RecName: Full=Non-structural protein 3;
Short=nsp3;
EC=3.4.22.-;
AltName: Full=Papain-like proteinase;
Short=PL-PRO;
AltName: Full=p195;
Contains:
RecName: Full=Non-structural protein 4;
Short=nsp4;
AltName: Full=Peptide HD2;
AltName: Full=p41;
Contains:
RecName: Full=3C-like proteinase;
Short=3CL-PRO;
Short=3CLp;
EC=3.4.22.-;
AltName: Full=M-PRO;
AltName: Full=nsp5;
AltName: Full=p33;
Contains:
RecName: Full=Non-structural protein 6;
Short=nsp6;
AltName: Full=p34;
Contains:
RecName: Full=Non-structural protein 7;
Short=nsp7;
AltName: Full=p9;
Contains:
RecName: Full=Non-structural protein 8;
Short=nsp8;
AltName: Full=p24;
Contains:
RecName: Full=Non-structural protein 9;
Short=nsp9;
AltName: Full=p10;
Contains:
RecName: Full=Non-structural protein 10;
Short=nsp10;
AltName: Full=Growth factor-like peptide;
Short=GFL;
AltName: Full=p16;
Contains:
RecName: Full=RNA-directed RNA polymerase;
Short=Pol;
Short=RdRp;
EC=2.7.7.48;
AltName: Full=nsp12;
AltName: Full=p100;
Contains:
RecName: Full=Helicase;
Short=Hel;
EC=3.6.4.12;
EC=3.6.4.13;
AltName: Full=nsp13;
AltName: Full=p68;
Contains:
RecName: Full=Exoribonuclease;
Short=ExoN;
EC=3.1.13.-;
AltName: Full=nsp14;
AltName: Full=p58;
Contains:
RecName: Full=Uridylate-specific endoribonuclease;
EC=3.1.-.-;
AltName: Full=NendoU;
AltName: Full=nsp15;
AltName: Full=p39;
Contains:
RecName: Full=Putative 2'-O-methyl transferase;
EC=2.1.1.-;
AltName: Full=nsp16;
AltName: Full=p35;
Name=rep; ORFNames=1a-1b;
Avian infectious bronchitis virus (strain M41) (IBV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Gammacoronavirus.
NCBI_TaxID=11127;
NCBI_TaxID=9031; Gallus gallus (Chicken).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Mondal S.P., Buckles E.L.;
"Avian infectious bronchitis virus strain M41.";
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=16934878; DOI=10.1016/j.jviromet.2006.07.018;
Callison S.A., Hilt D.A., Boynton T.O., Sample B.F., Robison R.,
Swayne D.E., Jackwood M.W.;
"Development and evaluation of a real-time Taqman RT-PCR assay for the
detection of infectious bronchitis virus from infected chickens.";
J. Virol. Methods 138:60-65(2006).
-!- 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.
-!- FUNCTION: The papain-like proteinase (PL-PRO) is responsible for
the cleavages located at the N-terminus of replicase polyprotein.
Activity of PL-PRO is dependent on zinc (By similarity).
{ECO:0000250}.
-!- FUNCTION: The main proteinase 3CL-PRO is responsible for the
majority of cleavages as it cleaves the C-terminus of replicase
polyprotein at 11 sites. Recognizes substrates containing the core
sequence [ILMVF]-Q-|-[SGACN]. Inhibited by the substrate-analog
Cbz-Val-Asn-Ser-Thr-Leu-Gln-CMK. Also contains an ADP-ribose-1''-
phosphate (ADRP)-binding function (By similarity).
{ECO:0000255|PROSITE-ProRule:PRU00772}.
-!- FUNCTION: The peptide p16 might be involved in the EGF signaling
pathway. {ECO:0000250}.
-!- FUNCTION: The helicase which contains a zinc finger structure
displays RNA and DNA duplex-unwinding activities with 5' to 3'
polarity. Its ATPase activity is strongly stimulated by poly(U),
poly(dT), poly(C), poly(dA), but not by poly(G) (By similarity).
{ECO:0000250}.
-!- FUNCTION: The exoribonuclease acts on both ssRNA and dsRNA in a 3'
to 5' direction. {ECO:0000250}.
-!- FUNCTION: Nsp7-nsp8 hexadecamer may possibly confer processivity
to the polymerase, maybe by binding to dsRNA or by producing
primers utilized by the latter. {ECO:0000250}.
-!- FUNCTION: Nsp9 is a ssRNA-binding protein. {ECO:0000250}.
-!- FUNCTION: NendoU is a Mn(2+)-dependent, uridylate-specific enzyme,
which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond.
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- SUBUNIT: 3CL-PRO exists as monomer and homodimer. The three
peptides nsp2, nsp3 and nsp4 may form a complex. Nsp9 is a dimer.
Eight copies of nsp7 and eight copies of nsp8 assemble to form a
heterohexadecamer. Nsp10 forms a dodecamer (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Non-structural protein 3: Host membrane
{ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Non-structural protein 4: Host membrane
{ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- 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=P0C6Y3-1; Sequence=Displayed;
Note=Produced by -1 ribosomal frameshifting at the 1a-1b genes
boundary.;
Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
IsoId=P0C6V5-1; Sequence=External;
Note=Produced by conventional translation.;
-!- 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}.
-!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAW33784.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAW33785.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=ABI26421.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=ABI26422.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; DQ834384; ABI26421.1; ALT_SEQ; Genomic_RNA.
EMBL; DQ834384; ABI26422.1; ALT_SEQ; Genomic_RNA.
EMBL; AY851295; AAW33784.1; ALT_SEQ; Genomic_RNA.
EMBL; AY851295; AAW33785.1; ALT_SEQ; Genomic_RNA.
PDB; 2Q6D; X-ray; 2.35 A; A/B/C=2783-3088.
PDB; 2Q6F; X-ray; 2.00 A; A/B=2783-3088.
PDB; 5C94; X-ray; 2.44 A; A=3675-3785.
PDBsum; 2Q6D; -.
PDBsum; 2Q6F; -.
PDBsum; 5C94; -.
ProteinModelPortal; P0C6Y3; -.
SMR; P0C6Y3; -.
MEROPS; C30.002; -.
PRIDE; P0C6Y3; -.
OrthoDB; VOG09000000; -.
EvolutionaryTrace; P0C6Y3; -.
Proteomes; UP000007642; Genome.
Proteomes; UP000096468; 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:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
GO; GO:0016896; F:exoribonuclease activity, producing 5'-phosphomonoesters; IEA:InterPro.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
GO; GO:0008242; F:omega peptidase activity; IEA:InterPro.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0039520; P:induction by virus of host autophagy; 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.
Gene3D; 2.40.10.250; -; 1.
InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
InterPro; IPR032505; Corona_NSP4_C.
InterPro; IPR009461; Coronavirus_NSP16.
InterPro; IPR027352; CV_ZBD.
InterPro; IPR037227; EndoU-like.
InterPro; IPR002589; Macro_dom.
InterPro; IPR036333; NSP10_sf.
InterPro; IPR009466; NSP11.
InterPro; IPR014828; NSP7.
InterPro; IPR037204; NSP7_sf.
InterPro; IPR014829; NSP8.
InterPro; IPR037230; NSP8_sf.
InterPro; IPR014822; NSP9.
InterPro; IPR036499; NSP9_sf.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR008740; Peptidase_C30.
InterPro; IPR013016; Peptidase_C30/C16.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001205; RNA-dir_pol_C.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR009469; RNA_pol_N_coronovir.
InterPro; IPR018995; RNA_synth_NSP10_coronavirus.
InterPro; IPR029063; SAM-dependent_MTases.
InterPro; IPR014827; Viral_protease.
Pfam; PF16348; Corona_NSP4_C; 1.
Pfam; PF06478; Corona_RPol_N; 1.
Pfam; PF01661; Macro; 1.
Pfam; PF09401; NSP10; 1.
Pfam; PF06471; NSP11; 1.
Pfam; PF06460; NSP13; 1.
Pfam; PF08716; nsp7; 1.
Pfam; PF08717; nsp8; 1.
Pfam; PF08710; nsp9; 1.
Pfam; PF05409; Peptidase_C30; 1.
Pfam; PF00680; RdRP_1; 1.
Pfam; PF01443; Viral_helicase1; 1.
Pfam; PF08715; Viral_protease; 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; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF53335; SSF53335; 1.
PROSITE; PS51653; CV_ZBD; 1.
PROSITE; PS51442; M_PRO; 1.
PROSITE; PS51154; MACRO; 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;
Complete proteome; Endonuclease; Exonuclease; Helicase;
Host cytoplasm; Host membrane; Host-virus interaction; Hydrolase;
Membrane; Metal-binding; Methyltransferase; Nuclease;
Nucleotide-binding; Nucleotidyltransferase; Protease; Repeat;
Ribosomal frameshifting; RNA-binding; RNA-directed RNA polymerase;
Thiol protease; Transferase; Transmembrane; Transmembrane helix;
Viral RNA replication; Zinc; Zinc-finger.
CHAIN 1 673 Non-structural protein 2. {ECO:0000250}.
/FTId=PRO_0000283889.
CHAIN 674 2267 Non-structural protein 3. {ECO:0000250}.
/FTId=PRO_0000283890.
CHAIN 2268 2781 Non-structural protein 4. {ECO:0000250}.
/FTId=PRO_0000283891.
CHAIN 2782 3088 3C-like proteinase. {ECO:0000250}.
/FTId=PRO_0000283892.
CHAIN 3089 3381 Non-structural protein 6. {ECO:0000250}.
/FTId=PRO_0000283893.
CHAIN 3382 3464 Non-structural protein 7. {ECO:0000250}.
/FTId=PRO_0000283894.
CHAIN 3465 3674 Non-structural protein 8. {ECO:0000250}.
/FTId=PRO_0000283895.
CHAIN 3675 3785 Non-structural protein 9. {ECO:0000250}.
/FTId=PRO_0000283896.
CHAIN 3786 3930 Non-structural protein 10. {ECO:0000250}.
/FTId=PRO_0000283897.
CHAIN 3931 4870 RNA-directed RNA polymerase.
{ECO:0000250}.
/FTId=PRO_0000283898.
CHAIN 4871 5470 Helicase. {ECO:0000250}.
/FTId=PRO_0000283899.
CHAIN 5471 5991 Exoribonuclease. {ECO:0000250}.
/FTId=PRO_0000283900.
CHAIN 5992 6329 Uridylate-specific endoribonuclease.
{ECO:0000250}.
/FTId=PRO_0000283901.
CHAIN 6330 6631 Putative 2'-O-methyl transferase.
{ECO:0000250}.
/FTId=PRO_0000283902.
TRANSMEM 1723 1743 Helical. {ECO:0000255}.
TRANSMEM 1753 1773 Helical. {ECO:0000255}.
TRANSMEM 1846 1866 Helical. {ECO:0000255}.
TRANSMEM 1889 1909 Helical. {ECO:0000255}.
TRANSMEM 2283 2303 Helical. {ECO:0000255}.
TRANSMEM 2373 2393 Helical. {ECO:0000255}.
TRANSMEM 2562 2582 Helical. {ECO:0000255}.
TRANSMEM 2591 2611 Helical. {ECO:0000255}.
TRANSMEM 2614 2634 Helical. {ECO:0000255}.
TRANSMEM 2646 2666 Helical. {ECO:0000255}.
TRANSMEM 3103 3123 Helical. {ECO:0000255}.
TRANSMEM 3124 3144 Helical. {ECO:0000255}.
TRANSMEM 3154 3174 Helical. {ECO:0000255}.
TRANSMEM 3191 3211 Helical. {ECO:0000255}.
TRANSMEM 3222 3242 Helical. {ECO:0000255}.
TRANSMEM 3260 3280 Helical. {ECO:0000255}.
TRANSMEM 3299 3319 Helical. {ECO:0000255}.
DOMAIN 1005 1181 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1238 1499 Peptidase C16. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 2782 3088 Peptidase C30. {ECO:0000255|PROSITE-
ProRule:PRU00772}.
DOMAIN 4550 4712 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
DOMAIN 4871 4954 CV ZBD. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
DOMAIN 5127 5307 (+)RNA virus helicase ATP-binding.
DOMAIN 5308 5479 (+)RNA virus helicase C-terminal.
ZN_FING 1355 1392 C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 3860 3880 {ECO:0000250}.
ZN_FING 3906 3919 {ECO:0000250}.
NP_BIND 5152 5159 ATP. {ECO:0000250}.
REGION 1723 1909 HD1. {ECO:0000250}.
REGION 2283 2666 HD2. {ECO:0000250}.
REGION 2887 3319 HD3. {ECO:0000250}.
COMPBIAS 1729 1734 Poly-Phe.
ACT_SITE 1276 1276 For PL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1439 1439 For PL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 2822 2822 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
ACT_SITE 2924 2924 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
METAL 4875 4875 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 4878 4878 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 4886 4886 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 4889 4889 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 4896 4896 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 4899 4899 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 4903 4903 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 4909 4909 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 4920 4920 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 4925 4925 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 4942 4942 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 4945 4945 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
SITE 673 674 Cleavage; by PL-PRO. {ECO:0000250}.
SITE 2267 2268 Cleavage; by PL-PRO. {ECO:0000250}.
SITE 2781 2782 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3088 3089 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3381 3382 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3464 3465 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3674 3675 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3785 3786 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3930 3931 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4870 4871 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 5470 5471 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 5991 5992 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 6329 6330 Cleavage; by 3CL-PRO. {ECO:0000250}.
VARIANT 807 807 L -> S.
VARIANT 1618 1618 S -> F.
VARIANT 1739 1739 S -> A.
VARIANT 2631 2631 M -> L.
VARIANT 2774 2774 S -> P.
VARIANT 4230 4230 D -> G.
VARIANT 4692 4692 S -> P.
VARIANT 4859 4859 Y -> C.
VARIANT 5104 5104 S -> P.
VARIANT 6033 6033 V -> A.
VARIANT 6080 6080 T -> M.
VARIANT 6314 6314 A -> T.
HELIX 2792 2795 {ECO:0000244|PDB:2Q6D}.
STRAND 2798 2802 {ECO:0000244|PDB:2Q6D}.
STRAND 2807 2813 {ECO:0000244|PDB:2Q6D}.
STRAND 2816 2820 {ECO:0000244|PDB:2Q6D}.
HELIX 2821 2824 {ECO:0000244|PDB:2Q6D}.
TURN 2829 2831 {ECO:0000244|PDB:2Q6D}.
HELIX 2832 2838 {ECO:0000244|PDB:2Q6D}.
HELIX 2841 2843 {ECO:0000244|PDB:2Q6D}.
STRAND 2845 2847 {ECO:0000244|PDB:2Q6D}.
STRAND 2856 2862 {ECO:0000244|PDB:2Q6D}.
STRAND 2865 2872 {ECO:0000244|PDB:2Q6D}.
STRAND 2879 2882 {ECO:0000244|PDB:2Q6D}.
STRAND 2890 2897 {ECO:0000244|PDB:2Q6D}.
STRAND 2900 2908 {ECO:0000244|PDB:2Q6D}.
STRAND 2927 2932 {ECO:0000244|PDB:2Q6D}.
STRAND 2935 2945 {ECO:0000244|PDB:2Q6D}.
STRAND 2950 2954 {ECO:0000244|PDB:2Q6D}.
HELIX 2961 2963 {ECO:0000244|PDB:2Q6D}.
STRAND 2966 2969 {ECO:0000244|PDB:2Q6D}.
HELIX 2980 2993 {ECO:0000244|PDB:2Q6D}.
HELIX 3012 3019 {ECO:0000244|PDB:2Q6D}.
TURN 3020 3023 {ECO:0000244|PDB:2Q6D}.
HELIX 3031 3039 {ECO:0000244|PDB:2Q6D}.
HELIX 3044 3056 {ECO:0000244|PDB:2Q6D}.
STRAND 3066 3068 {ECO:0000244|PDB:2Q6D}.
HELIX 3075 3080 {ECO:0000244|PDB:2Q6D}.
STRAND 3681 3693 {ECO:0000244|PDB:5C94}.
HELIX 3694 3696 {ECO:0000244|PDB:5C94}.
STRAND 3699 3708 {ECO:0000244|PDB:5C94}.
STRAND 3711 3720 {ECO:0000244|PDB:5C94}.
STRAND 3726 3730 {ECO:0000244|PDB:5C94}.
STRAND 3736 3741 {ECO:0000244|PDB:5C94}.
STRAND 3745 3751 {ECO:0000244|PDB:5C94}.
STRAND 3754 3763 {ECO:0000244|PDB:5C94}.
HELIX 3768 3778 {ECO:0000244|PDB:5C94}.
HELIX 3779 3781 {ECO:0000244|PDB:5C94}.
STRAND 3782 3784 {ECO:0000244|PDB:5C94}.
SEQUENCE 6631 AA; 744412 MW; CB222611D8C1B9E2 CRC64;
MASSLKQGVS PKLRDVILVS KDIPEQLCDA LFFYTSHNPK DYADAFAVRQ KFDRNLQTGK
QFKFETVCGL FLLKGVDKIT PGVPAKVLKA TSKLADLEDI FGVSPFARKY RELLKTACQW
SLTVETLDAR AQTLDEIFDP TEILWLQVAA KIQVSAMAMR RLVGEVTAKV MDALGSNMSA
LFQIFKQQIV RIFQKALAIF ENVSELPQRI AALKMAFAKC AKSITVVVME RTLVVREFAG
TCLASINGAV AKFFEELPNG FMGAKIFTTL AFFREAAVKI VDNIPNAPRG TKGFEVVGNA
KGTQVVVRGM RNDLTLLDQK AEIPVESEGW SAILGGHLCY VFKSGDRFYA APLSGNFALH
DVHCCERVVC LSDGVTPEIN DGLILAAIYS SFSVAELVAA IKRGEPFKFL GHKFVYAKDA
AVSFTLAKAA TIADVLKLFQ SARVKVEDVW SSLTEKSFEF WRLAYGKVRN LEEFVKTCFC
KAQMAIVILA TVLGEGIWHL VSQVIYKVGG LFTKVVDFCE KYWKGFCAQL KRAKLIVTET
LCVLKGVAQH CFQLLLDAIQ FMYKSFKKCA LGRIHGDLLF WKGGVHKIIQ EGDEIWFDAI
DSIDVEDLGV VQEKLIDFDV CDNVTLPENQ PGHMVQIEDD GKNYMFFRFK KDENIYYTPM
SQLGAINVVC KAGGKTVTFG ETTVQEIPPP DVVFIKVSIE CCGEPWNTIF KKAYKEPIEV
ETDLTVEQLL SVVYEKMCDD LKLFPEAPEP PPFENVTLVD KNGKDLDCIK SCHLIYRDYE
SDDDIEEEDA EECDTDSGDA EECDTNLECE EEDEDTKVLA LIQDPASNKY PLPLDDDYSV
YNGCIVHKDA LDVVNLPSGE ETFVVNNCFE GAVKALPQKV IDVLGDWGEA VDAQEQLCQQ
ESTRVISEKS VEGFTGSCDA MAEQAIVEEQ EIVPVVEQSQ DVVVFTPADL EVVKETAEEV
DEFILISAVP KEEVVSQEKE EPQVEQEPTL VVKAQREKKA KKFKVKPATC EKPKFLEYKT
CVGDLAVVIA KALDEFKEFC IVNAANEHMS HGGGVAKAIA DFCGPDFVEY CADYVKKHGP
QQKLVTPSFV KGIQCVNNVV GPRHGDSNLR EKLVAAYKSV LVGGVVNYVV PVLSSGIFGV
DFKISIDAMR EAFKGCAIRV LLFSLSQEHI DYFDATCKQK TIYLTEDGVK YRSVVLKPGD
SLGQFGQVFA RNKVVFSADD VEDKEILFIP TTDKTILEYY GLDAQKYVTY LQTLAQKWDV
QYRDNFVILE WRDGNCWISS AIVLLQAAKI RFKGFLAEAW AKLLGGDPTD FVAWCYASCN
AKVGDFSDAN WLLANLAEHF DADYTNALLK KCVSCNCGVK SYELRGLEAC IQPVRAPNLL
HFKTQYSNCP TCGASSTDEV IEASLPYLLL FATDGPATVD CDENAVGTVV FIGSTNSGHC
YTQADGKAFD NLAKDRKFGR KSPYITAMYT RFSLRSENPL LVVEHSKGKA KVVKEDVSNL
ATSSKASFDD LTDFEQWYDS NIYESLKVQE TPDNLDEYVS FTTKEDSKLP LTLKVRGIKS
VVDFRSKDGF TYKLTPDTDE NSKTPVYYPV LDSISLRAIW VEGSANFVVG HPNYYSKSLR
IPTFWENAES FVKMGYKIDG VTMGLWRAEH LNKPNLERIF NIAKKAIVGS SVVTTQCGKI
LVKAATYVAD KVGDGVVRNI TDRIKGLCGF TRGHFEKKMS LQFLKTLVFF FFYFLKASSK
SLVSSYKIVL CKVVFATLLI VWFIYTSNPV VFTGIRVLDF LFEGSLCGPY NDYGKDSFDV
LRYCAGDFTC RVCLHDRDSL HLYKHAYSVE QIYKDAASGI NFNWNWLYLV FLILFVKPVA
GFVIICYCVK YLVLSSTVLQ TGVGFLDWFV KTVFTHFNFM GAGFYFWLFY KIYVQVHHIL
YCKDVTCEVC KRVARSNRQE VSVVVGGRKQ IVHVYTNSGY NFCKRHNWYC RNCDDYGHQN
TFMSPEVAGE LSEKLKRHVK PTAYAYHVVY EACVVDDFVN LKYKAAIPGK DNASSAVKCF
SVTDFLKKAV FLKEALKCEQ ISNDGFIVCN TQSAHALEEA KNAAVYYAQY LCKPILILDQ
ALYEQLIVEP VSKSVIDKVC SILSNIISVD TAALNYKAGT LRDALLSITK DEEAVDMAIF
CHNHEVEYTG DGFTNVIPSY GMDTDKLTPR DRGFLINADA SIANLRVKNA PPVVWKFSDL
IKLSDSCLKY LISATVKSGG RFFITKSGAK QVISCHTQKL LVEKKAGGVI NNTFKWFMSC
FKWLFVFYIL FTACCLGYYY MEMNKSFVHP MYDVNSTLHV EGFKVIDKGV IREIVSEDNC
FSNKFVNFDA FWGKSYENNK NCPIVTVVID GDGTVAVGVP GFVSWVMDGV MFVHMTQTDR
RPWYIPTWFN REIVGYTQDS IITEGSFYTS IALFSARCLY LTASNTPQLY CFNGDNDAPG
ALPFGSIIPH RVYFQPNGVR LIVPQQILHT PYIVKFVSDS YCRGSVCEYT KPGYCVSLDS
QWVLFNDEYI SKPGVFCGST VRELMFNMVS TFFTGVNPNI YIQLATMFLI LVVIVLIFAM
VIKFQGVFKA YATIVFTIML VWVINAFVLC VHSYNSVLAV ILLVLYCYAS MVTSRNTAII
MHCWLVFTFG LIVPTWLACC YLGFILYMYT PLVFWCYGTT KNTRKLYDGN EFVGNYDLAA
KSTFVIRGTE FVKLTNEIGD KFEAYLSAYA RLKYYSGTGS EQDYLQACRA WLAYALDQYR
NSGVEVVYTP PRYSIGVSRL QAGFKKLVSP SSAVEKCIVS VSYRGNNLNG LWLGDSIYCP
RHVLGKFSGD QWGDVLNLAN NHEFEVVTQN GVTLNVVSRR LKGAVLILQT AVANAETPKY
KFVKANCGDS FTIACSYGGT VIGLYPVTMR SNGTIRASFL AGACGSVGFN IEKGVVNFFY
MHHLELPNAL HTGTDLMGEF YGGYVDEEVA QRVPPDNLVT NNIVAWLYAA IISVKESSFS
QPKWLESTTV SIEDYNRWAS DNGFTPFSTS TAITKLSAIT GVDVCKLLRT IMVKSAQWGS
DPILGQYNFE DELTPESVFN QVGGVRLQSS FVRKATSWFW SRCVLACFLF VLCAIVLFTA
VPLKFYVHAA VILLMAVLFI SFTVKHVMAY MDTFLLPTLI TVIIGVCAEV PFIYNTLISQ
VVIFLSQWYD PVVFDTMVPW MLLPLVLYTA FKCVQGCYMN SFNTSLLMLY QFMKLGFVIY
TSSNTLTAYT EGNWELFFEL VHTIVLANVS SNSLIGLIVF KCAKWMLYYC NATYFNNYVL
MAVMVNGIGW LCTCYFGLYW WVNKVFGLTL GKYNFKVSVD QYRYMCLHKV NPPKTVWEVF
TTNILIQGIG GDRVLPIATV QSKLSDVKCT TVVLMQLLTK LNVEANSKMH AYLVELHNKI
LASDDVGECM DNLLGMLITL FCIDSTIDLG EYCDDILKRS TVLQSVTQEF SHIPSYAEYE
RAKSIYEKVL ADSKNGGVTQ QELAAYRKAA NIAKSVFDRD LAVQKKLDSM AERAMTTMYK
EARVTDRRAK LVSSLHALLF SMLKKIDSEK LNVLFDQANS GVVPLATVPI VCSNKLTLVI
PDPETWVKCV EGVHVTYSTV VWNIDCVTDA DGTELHPTST GSGLTYCISG DNIAWPLKVN
LTRNGHNKVD VALQNNELMP HGVKTKACVA GVDQAHCSVE SKCYYTSISG SSVVAAITSS
NPNLKVASFL NEAGNQIYVD LDPPCKFGMK VGDKVEVVYL YFIKNTRSIV RGMVLGAISN
VVVLQSKGHE TEEVDAVGIL SLCSFAVDPA DTYCKYVAAG NQPLGNCVKM LTVHNGSGFA
ITSKPSPTPD QDSYGGASVC LYCRAHIAHP GGAGNLDGRC QFKGSFVQIP TTEKDPVGFC
LRNKVCTVCQ CWIGYGCQCD SLRQPKPSVQ SVAVASGFDK NYLNRVRGSS EARLIPLANG
CDPDVVKRAF DVCNKESAGM FQNLKRNCAR FQEVRDTEDG NLEYCDSYFV VKQTTPSNYE
HEKACYEDLK SEVTADHDFF VFNKNIYNIS RQRLTKYTMM DFCYALRHFD PKDCEVLKEI
LVTYGCIEDY HPKWFEENKD WYDPIENPKY YAMLAKMGPI VRRALLNAIE FGNLMVEKGY
VGVITLDNQD LNGKFYDFGD FQKTAPGAGV PVFDTYYSYM MPIIAMTDAL APERYFEYDV
HKGYKSYDLL KYDYTEEKQD LFQKYFKYWD QEYHPNCRDC SDDRCLIHCA NFNILFSTLV
PQTSFGNLCR KVFVDGVPFI ATCGYHSKEL GVIMNQDNTM SFSKMGLSQL MQFVGDPALL
VGTSNKLVDL RTSCFSVCAL ASGITHQTVK PGHFNKDFYD FAEKAGMFKE GSSIPLKHFF
YPQTGNAAIN DYDYYRYNRP TMFDIRQLLF CLEVTSKYFE CYEGGCIPAS QVVVNNLDKS
AGYPFNKFGK ARLYYEMSLE EQDQLFESTK KNVLPTITQM NLKYAISAKN RARTVAGVSI
LSTMTNRQFH QKILKSIVNT RNAPVVIGTT KFYGGWDNML RNLIQGVEDP ILMGWDYPKC
DRAMPNLLRI AASLVLARKH TNCCTWSERV YRLYNECAQV LSETVLATGG IYVKPGGTSS
GDATTAYANS VFNIIQATSA NVARLLSVIT RDIVYDDIKS LQYELYQQVY RRVNFDPAFV
EKFYSYLCKN FSLMILSDDG VVCYNNTLAK QGLVADISGF REVLYYQNNV FMADSKCWVE
PDLEKGPHEF CSQHTMLVEV DGEPRYLPYP DPSRILCACV FVDDLDKTES VAVMERYIAL
AIDAYPLVHH ENEEYKKVFF VLLSYIRKLY QELSQNMLMD YSFVMDIDKG SKFWEQEFYE
NMYRAPTTLQ SCGVCVVCNS QTILRCGNCI RKPFLCCKCC YDHVMHTDHK NVLSINPYIC
SQPGCGEADV TKLYLGGMSY FCGNHKPKLS IPLVSNGTVF GIYRANCAGS ENVDDFNQLA
TTNWSTVEPY ILANRCVDSL RRFAAETVKA TEELHKQQFA SAEVREVLSD RELILSWEPG
KTRPPLNRNY VFTGFHFTRT SKVQLGDFTF EKGEGKDVVY YRATSTAKLS VGDIFVLTSH
NVVSLIAPTL CPQQTFSRFV NLRPNVMVPA CFVNNIPLYH LVGKQKRTTV QGPPGSGKSH
FAIGLAAYFS NARVVFTACS HAAVDALCEK AFKFLKVDDC TRIVPQRTTI DCFSKFKAND
TGKKYIFSTI NALPEVSCDI LLVDEVSMLT NYELSFINGK INYQYVVYVG DPAQLPAPRT
LLNGSLSPKD YNVVTNLMVC VKPDIFLAKC YRCPKEIVDT VSTLVYDGKF IANNPESRQC
FKVIVNNGNS DVGHESGSAY NITQLEFVKD FVCRNKEWRE ATFISPYNAM NQRAYRMLGL
NVQTVDSSQG SEYDYVIFCV TADSQHALNI NRFNVALTRA KRGILVVMRQ RDELYSALKF
IELDSVASLQ GTGLFKICNK EFSGVHPAYA VTTKALAATY KVNDELAALV NVEAGSEITY
KHLISLLGFK MSVNVEGCHN MFITRDEAIR NVRGWVGFDV EATHACGTNI GTNLPFQVGF
STGADFVVTP EGLVDTSIGN NFEPVNSKAP PGEQFNHLRA LFKSAKPWHV VRPRIVQMLA
DNLCNVSDCV VFVTWCHGLE LTTLRYFVKI GKDQVCSCGS RATTFNSHTQ AYACWKHCLG
FDFVYNPLLV DIQQWGYSGN LQFNHDLHCN VHGHAHVASA DAIMTRCLAI NNAFCQDVNW
DLTYPHIANE DEVNSSCRYL QRMYLNACVD ALKVNVVYDI GNPKGIKCVR RGDLNFRFYD
KNPIVPNVKQ FEYDYNQHKD KFADGLCMFW NCNVDCYPDN SLVCRYDTRN LSVFNLPGCN
GGSLYVNKHA FHTPKFDRTS FRNLKAMPFF FYDSSPCETI QLDGVAQDLV SLATKDCITK
CNIGGAVCKK HAQMYADFVT SYNAAVTAGF TFWVTNNFNP YNLWKSFSAL QSIDNIAYNM
YKGGHYDAIA GEMPTIVTGD KVFVIDQGVE KAVFFNQTIL PTSVAFELYA KRNIRTLPNN
RILKGLGVDV TNGFVIWDYT NQTPLYRNTV KVCAYTDIEP NGLIVLYDDR YGDYQSFLAA
DNAVLVSTQC YKRYSYVEIP SNLLVQNGIP LKDGANLYVY KRVNGAFVTL PNTLNTQGRS
YETFEPRSDV ERDFLDMSEE SFVEKYGKEL GLQHILYGEV DKPQLGGLHT VIGMCRLLRA
NKLNAKSVTN SDSDVMQNYF VLADNGSYKQ VCTVVDLLLD DFLELLRNIL KEYGTNKSKV
VTVSIDYHSI NFMAWFEDGI IKTCYPQLQS AWTCGYNMPE LYKVQNCVME PCNIPNYGVG
IALPSGIMMN VAKYTQLCQY LSKTTMCVPH NMRVMHFGAG SDKGVAPGST VLKQWLPEGT
LLVDNDIVDY VSDAHVSVLS DCNKYKTEHK FDLVISDMYT DNDSKRKHEG VIANNGNDDV
FIYLSSFLRN NLALGGSFAV KVTETSWHEV LYDIAQDCAW WTMFCTAVNA SSSEAFLVGV
NYLGASEKVK VSGKTLHANY IFWRNCNYLQ TSAYSIFDVA KFDLRLKATP VVNLKTEQKT
DLVFNLIKCG KLLVRDVGNT SFTSDSFVCT M


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