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Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]

 POLG_HCVJF              Reviewed;        3033 AA.
Q99IB8;
10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
30-AUG-2017, entry version 139.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Core protein p21;
AltName: Full=Capsid protein C;
AltName: Full=p21;
Contains:
RecName: Full=Core protein p19;
Contains:
RecName: Full=Envelope glycoprotein E1;
AltName: Full=gp32;
AltName: Full=gp35;
Contains:
RecName: Full=Envelope glycoprotein E2;
AltName: Full=NS1;
AltName: Full=gp68;
AltName: Full=gp70;
Contains:
RecName: Full=p7;
Contains:
RecName: Full=Protease NS2-3;
Short=p23;
EC=3.4.22.-;
Contains:
RecName: Full=Serine protease NS3;
EC=3.4.21.98;
EC=3.6.1.15;
EC=3.6.4.13;
AltName: Full=Hepacivirin;
AltName: Full=NS3P;
AltName: Full=p70;
Contains:
RecName: Full=Non-structural protein 4A;
Short=NS4A;
AltName: Full=p8;
Contains:
RecName: Full=Non-structural protein 4B;
Short=NS4B;
AltName: Full=p27;
Contains:
RecName: Full=Non-structural protein 5A;
Short=NS5A;
AltName: Full=p56;
Contains:
RecName: Full=RNA-directed RNA polymerase;
EC=2.7.7.48;
AltName: Full=NS5B;
AltName: Full=p68;
Hepatitis C virus genotype 2a (isolate JFH-1) (HCV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Hepacivirus.
NCBI_TaxID=356411;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=11424123; DOI=10.1002/jmv.1055;
Kato T., Furusaka A., Miyamoto M., Date T., Yasui K., Hiramoto J.,
Nagayama K., Tanaka T., Wakita T.;
"Sequence analysis of hepatitis C virus isolated from a fulminant
hepatitis patient.";
J. Med. Virol. 64:334-339(2001).
[2]
SUBCELLULAR LOCATION OF P7.
PubMed=17170445; DOI=10.1099/vir.0.82049-0;
Haqshenas G., Mackenzie J.M., Dong X., Gowans E.J.;
"Hepatitis C virus p7 protein is localized in the endoplasmic
reticulum when it is encoded by a replication-competent genome.";
J. Gen. Virol. 88:134-142(2007).
[3]
REVIEW.
PubMed=10718937; DOI=10.1046/j.1365-2893.2000.00201.x;
McLauchlan J.;
"Properties of the hepatitis C virus core protein: a structural
protein that modulates cellular processes.";
J. Viral Hepat. 7:2-14(2000).
[4]
REVIEW, AND SUBCELLULAR LOCATION.
PubMed=14752815; DOI=10.1002/hep.20032;
Penin F., Dubuisson J., Rey F.A., Moradpour D., Pawlotsky J.-M.;
"Structural biology of hepatitis C virus.";
Hepatology 39:5-19(2004).
[5]
INTERACTION WITH HNRNPA1 AND SEPT6.
PubMed=17229681; DOI=10.1128/JVI.01311-06;
Kim C.S., Seol S.K., Song O.-K., Park J.H., Jang S.K.;
"An RNA-binding protein, hnRNP A1, and a scaffold protein, septin 6,
facilitate hepatitis C virus replication.";
J. Virol. 81:3852-3865(2007).
-!- FUNCTION: Core protein packages viral RNA to form a viral
nucleocapsid, and promotes virion budding. Modulates viral
translation initiation by interacting with HCV IRES and 40S
ribosomal subunit. Also regulates many host cellular functions
such as signaling pathways and apoptosis. Prevents the
establishment of cellular antiviral state by blocking the
interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling
pathways and by inducing human STAT1 degradation. Thought to play
a role in virus-mediated cell transformation leading to
hepatocellular carcinomas. Interacts with, and activates STAT3
leading to cellular transformation. May repress the promoter of
p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the
cytoplasm. Also represses cell cycle negative regulating factor
CDKN1A, thereby interrupting an important check point of normal
cell cycle regulation. Targets transcription factors involved in
the regulation of inflammatory responses and in the immune
response: suppresses NK-kappaB activation, and activates AP-1.
Could mediate apoptotic pathways through association with TNF-type
receptors TNFRSF1A and LTBR, although its effect on death
receptor-induced apoptosis remains controversial. Enhances TRAIL
mediated apoptosis, suggesting that it might play a role in
immune-mediated liver cell injury. Seric core protein is able to
bind C1QR1 at the T-cell surface, resulting in down-regulation of
T-lymphocytes proliferation. May transactivate human MYC, Rous
sarcoma virus LTR, and SV40 promoters. May suppress the human FOS
and HIV-1 LTR activity. Alters lipid metabolism by interacting
with hepatocellular proteins involved in lipid accumulation and
storage. Core protein induces up-regulation of FAS promoter
activity, and thereby probably contributes to the increased
triglyceride accumulation in hepatocytes (steatosis) (By
similarity). {ECO:0000250}.
-!- FUNCTION: E1 and E2 glycoproteins form a heterodimer that is
involved in virus attachment to the host cell, virion
internalization through clathrin-dependent endocytosis and fusion
with host membrane. E1/E2 heterodimer binds to human LDLR, CD81
and SCARB1/SR-BI receptors, but this binding is not sufficient for
infection, some additional liver specific cofactors may be needed.
The fusion function may possibly be carried by E1. E2 inhibits
human EIF2AK2/PKR activation, preventing the establishment of an
antiviral state. E2 is a viral ligand for CD209/DC-SIGN and
CLEC4M/DC-SIGNR, which are respectively found on dendritic cells
(DCs), and on liver sinusoidal endothelial cells and macrophage-
like cells of lymph node sinuses. These interactions allow capture
of circulating HCV particles by these cells and subsequent
transmission to permissive cells. DCs act as sentinels in various
tissues where they entrap pathogens and convey them to local
lymphoid tissue or lymph node for establishment of immunity.
Capture of circulating HCV particles by these SIGN+ cells may
facilitate virus infection of proximal hepatocytes and lymphocyte
subpopulations and may be essential for the establishment of
persistent infection (By similarity). {ECO:0000250}.
-!- FUNCTION: P7 seems to be a heptameric ion channel protein
(viroporin) and is inhibited by the antiviral drug amantadine.
Also inhibited by long-alkyl-chain iminosugar derivatives.
Essential for infectivity (By similarity). {ECO:0000250}.
-!- FUNCTION: Protease NS2-3 is a cysteine protease responsible for
the autocatalytic cleavage of NS2-NS3. Seems to undergo self-
inactivation following maturation (By similarity). {ECO:0000250}.
-!- FUNCTION: NS3 displays three enzymatic activities: serine
protease, NTPase and RNA helicase. NS3 serine protease, in
association with NS4A, is responsible for the cleavages of NS3-
NS4A, NS4A-NS4B, NS4B-NS5A and NS5A-NS5B. NS3/NS4A complex also
prevents phosphorylation of human IRF3, thus preventing the
establishment of dsRNA induced antiviral state. NS3 RNA helicase
binds to RNA and unwinds dsRNA in the 3' to 5' direction, and
likely RNA stable secondary structure in the template strand.
Cleaves and inhibits the host antiviral protein MAVS (By
similarity). {ECO:0000250}.
-!- FUNCTION: NS4B induces a specific membrane alteration that serves
as a scaffold for the virus replication complex. This membrane
alteration gives rise to the so-called ER-derived membranous web
that contains the replication complex (By similarity).
{ECO:0000250}.
-!- FUNCTION: NS5A is a component of the replication complex involved
in RNA-binding. Its interaction with Human VAPB may target the
viral replication complex to vesicles. Down-regulates viral IRES
translation initiation. Mediates interferon resistance, presumably
by interacting with and inhibiting human EIF2AK2/PKR. Seems to
inhibit apoptosis by interacting with BIN1 and FKBP8. The
hyperphosphorylated form of NS5A is an inhibitor of viral
replication (By similarity). {ECO:0000250}.
-!- FUNCTION: NS5B is an RNA-dependent RNA polymerase that plays an
essential role in the virus replication. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Hydrolysis of four peptide bonds in the viral
precursor polyprotein, commonly with Asp or Glu in the P6
position, Cys or Thr in P1 and Ser or Ala in P1'.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per NS3 protease domain. {ECO:0000250};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per NS5A N-terminal domain. {ECO:0000250};
-!- ENZYME REGULATION: Activity of auto-protease NS2-3 is dependent on
zinc ions and completely inhibited by EDTA. Serine protease NS3 is
also activated by zinc ions (By similarity). {ECO:0000250}.
-!- SUBUNIT: Core protein is a homomultimer that binds the C-terminal
part of E1 and interacts with numerous cellular proteins.
Interaction with human STAT1 SH2 domain seems to result in
decreased STAT1 phosphorylation, leading to decreased IFN-
stimulated gene transcription. In addition to blocking the
formation of phosphorylated STAT1, the core protein also promotes
ubiquitin-mediated proteasome-dependent degradation of STAT1.
Interacts with, and constitutively activates human STAT3.
Associates with human LTBR and TNFRSF1A receptors and possibly
induces apoptosis. Binds to human SP110 isoform 3/Sp110b, HNRPK,
C1QR1, YWHAE, UBE3A/E6AP, DDX3X, APOA2 and RXRA proteins.
Interacts with human CREB3 nuclear transcription protein,
triggering cell transformation. May interact with human p53. Also
binds human cytokeratins KRT8, KRT18, KRT19 and VIM (vimentin). E1
and E2 glycoproteins form a heterodimer that binds to human LDLR,
CLDN1, CD81 and SCARB1 receptors. E2 binds and inhibits human
EIF2AK2/PKR. Also binds human CD209/DC-SIGN and CLEC4M/DC-SIGNR.
p7 forms a homoheptamer in vitro. NS2 forms a homodimer containing
a pair of composite active sites at the dimerization interface.
NS2 seems to interact with all other non-structural (NS) proteins.
NS4A interacts with NS3 serine protease and stabilizes its
folding. NS3-NS4A complex is essential for the activation of the
latter and allows membrane anchorage of NS3. NS3 interacts with
human TANK-binding kinase TBK1 and MAVS. NS4B and NS5A form
homodimers and seem to interact with all other non-structural (NS)
proteins. NS5A also interacts with human EIF2AK2/PKR, FKBP8, GRB2,
BIN1, PIK3R1, SRCAP, VAPB and with most Src-family kinases. NS5B
is a homooligomer and interacts with human VAPB, HNRNPA1 and SEPT6
(By similarity). {ECO:0000250}.
-!- INTERACTION:
P27958:- (xeno); NbExp=3; IntAct=EBI-6858513, EBI-8753518;
P55265:ADAR (xeno); NbExp=3; IntAct=EBI-6858501, EBI-2462104;
P02771:AFP (xeno); NbExp=2; IntAct=EBI-6901449, EBI-722498;
P07355:ANXA2 (xeno); NbExp=5; IntAct=EBI-6927873, EBI-352622;
P60033:CD81 (xeno); NbExp=2; IntAct=EBI-6901449, EBI-712921;
O43169:CYB5B (xeno); NbExp=5; IntAct=EBI-6928570, EBI-1058710;
O00571:DDX3X (xeno); NbExp=9; IntAct=EBI-6674379, EBI-353779;
O75907:DGAT1 (xeno); NbExp=2; IntAct=EBI-6927873, EBI-3906527;
P49327:FASN (xeno); NbExp=6; IntAct=EBI-6927928, EBI-356658;
P02751:FN1 (xeno); NbExp=3; IntAct=EBI-6927928, EBI-1220319;
Q9H8Y8:GORASP2 (xeno); NbExp=3; IntAct=EBI-6927928, EBI-739467;
Q9P035:HACD3 (xeno); NbExp=2; IntAct=EBI-6927873, EBI-359013;
P11142:HSPA8 (xeno); NbExp=3; IntAct=EBI-6927928, EBI-351896;
Q16584:MAP3K11 (xeno); NbExp=5; IntAct=EBI-6927873, EBI-49961;
O75592:MYCBP2 (xeno); NbExp=3; IntAct=EBI-6927928, EBI-1043774;
Q02818:NUCB1 (xeno); NbExp=3; IntAct=EBI-6927928, EBI-2622179;
Q96CV9:OPTN (xeno); NbExp=3; IntAct=EBI-6858501, EBI-748974;
P42356:PI4KA (xeno); NbExp=5; IntAct=EBI-6927873, EBI-723050;
P53350:PLK1 (xeno); NbExp=4; IntAct=EBI-6927873, EBI-476768;
P62937:PPIA (xeno); NbExp=2; IntAct=EBI-6927873, EBI-437708;
O60260:PRKN (xeno); NbExp=3; IntAct=EBI-6858513, EBI-716346;
Q9BRP8:PYM1 (xeno); NbExp=4; IntAct=EBI-6858513, EBI-2352802;
Q9NP72:RAB18 (xeno); NbExp=5; IntAct=EBI-6927873, EBI-722247;
Q13129:RLF (xeno); NbExp=2; IntAct=EBI-6927928, EBI-958266;
Q8WXG1:RSAD2 (xeno); NbExp=3; IntAct=EBI-12737359, EBI-12736320;
Q14683:SMC1A (xeno); NbExp=3; IntAct=EBI-6927928, EBI-80690;
Q9Y6A9:SPCS1 (xeno); NbExp=7; IntAct=EBI-6901421, EBI-8852196;
P05455:SSB (xeno); NbExp=2; IntAct=EBI-6858501, EBI-358037;
P36897:TGFBR1 (xeno); NbExp=5; IntAct=EBI-6858501, EBI-1027557;
Q86WV6:TMEM173 (xeno); NbExp=5; IntAct=EBI-6928570, EBI-2800345;
Q9P0L0:VAPA (xeno); NbExp=3; IntAct=EBI-9096996, EBI-1059156;
O95292:VAPB (xeno); NbExp=2; IntAct=EBI-9096996, EBI-1188298;
Q9Y2W2:WBP11 (xeno); NbExp=3; IntAct=EBI-6927928, EBI-714455;
-!- SUBCELLULAR LOCATION: Core protein p21: Host endoplasmic reticulum
membrane {ECO:0000250}; Single-pass membrane protein
{ECO:0000250}. Host mitochondrion membrane {ECO:0000250}; Single-
pass type I membrane protein {ECO:0000250}. Host lipid droplet
{ECO:0000250}. Note=The C-terminal transmembrane domain of core
protein p21 contains an ER signal leading the nascent polyprotein
to the ER membrane. Only a minor proportion of core protein is
present in the nucleus and an unknown proportion is secreted.
-!- SUBCELLULAR LOCATION: Core protein p19: Virion {ECO:0000250}. Host
cytoplasm {ECO:0000250}. Host nucleus {ECO:0000250}. Secreted
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Envelope glycoprotein E1: Virion membrane
{ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Host endoplasmic reticulum membrane {ECO:0000250}; Single-pass
type I membrane protein {ECO:0000250}. Note=The C-terminal
transmembrane domain acts as a signal sequence and forms a hairpin
structure before cleavage by host signal peptidase. After
cleavage, the membrane sequence is retained at the C-terminus of
the protein, serving as ER membrane anchor. A reorientation of the
second hydrophobic stretch occurs after cleavage producing a
single reoriented transmembrane domain. These events explain the
final topology of the protein. ER retention of E1 is leaky and, in
overexpression conditions, only a small fraction reaches the
plasma membrane.
-!- SUBCELLULAR LOCATION: Envelope glycoprotein E2: Virion membrane
{ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Host endoplasmic reticulum membrane {ECO:0000250}; Single-pass
type I membrane protein {ECO:0000250}. Note=The C-terminal
transmembrane domain acts as a signal sequence and forms a hairpin
structure before cleavage by host signal peptidase. After
cleavage, the membrane sequence is retained at the C-terminus of
the protein, serving as ER membrane anchor. A reorientation of the
second hydrophobic stretch occurs after cleavage producing a
single reoriented transmembrane domain. These events explain the
final topology of the protein. ER retention of E2 is leaky and, in
overexpression conditions, only a small fraction reaches the
plasma membrane.
-!- SUBCELLULAR LOCATION: p7: Host endoplasmic reticulum membrane
{ECO:0000269|PubMed:17170445}; Multi-pass membrane protein
{ECO:0000269|PubMed:17170445}. Host cell membrane
{ECO:0000269|PubMed:17170445}. Note=The C-terminus of p7 membrane
domain acts as a signal sequence. After cleavage by host signal
peptidase, the membrane sequence is retained at the C-terminus of
the protein, serving as ER membrane anchor. Only a fraction
localizes to the plasma membrane.
-!- SUBCELLULAR LOCATION: Protease NS2-3: Host endoplasmic reticulum
membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Serine protease NS3: Host endoplasmic
reticulum membrane {ECO:0000305}; Peripheral membrane protein
{ECO:0000305}. Note=NS3 is associated to the ER membrane through
its binding to NS4A.
-!- SUBCELLULAR LOCATION: Non-structural protein 4A: Host endoplasmic
reticulum membrane {ECO:0000305}; Single-pass type I membrane
protein {ECO:0000305}. Note=Host membrane insertion occurs after
processing by the NS3 protease.
-!- SUBCELLULAR LOCATION: Non-structural protein 4B: Host endoplasmic
reticulum membrane {ECO:0000250}; Multi-pass membrane protein
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Non-structural protein 5A: Host endoplasmic
reticulum membrane {ECO:0000250}; Peripheral membrane protein
{ECO:0000250}. Host cytoplasm, host perinuclear region
{ECO:0000250}. Host mitochondrion {ECO:0000250}. Note=Host
membrane insertion occurs after processing by the NS3 protease.
-!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase: Host
endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I
membrane protein {ECO:0000305}. Note=Host membrane insertion
occurs after processing by the NS3 protease.
-!- DOMAIN: The transmembrane regions of envelope E1 and E2
glycoproteins are involved in heterodimer formation, ER
localization, and assembly of these proteins. Envelope E2
glycoprotein contain a highly variable region called hypervariable
region 1 (HVR1). E2 also contains two segments involved in CD81-
binding. HVR1 is implicated in the SCARB1-mediated cell entry.
CD81-binding regions may be involved in sensitivity and/or
resistance to IFN-alpha therapy (By similarity). {ECO:0000250}.
-!- DOMAIN: The N-terminus of NS5A acts as membrane anchor. The
central part of NS5A seems to be intrinsically disordered and
interacts with NS5B and host PKR (By similarity). {ECO:0000250}.
-!- DOMAIN: The SH3-binding domain of NS5A is involved in the
interaction with human Bin1, GRB2 and Src-family kinases.
{ECO:0000250}.
-!- DOMAIN: The N-terminal one-third of serine protease NS3 contains
the protease activity. This region contains a zinc atom that does
not belong to the active site, but may play a structural rather
than a catalytic role. This region is essential for the activity
of protease NS2-3, maybe by contributing to the folding of the
latter. The helicase activity is located in the C-terminus of NS3
(By similarity). {ECO:0000250}.
-!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
The structural proteins, core, E1, E2 and p7 are produced by
proteolytic processing by host signal peptidases. The core protein
is synthesized as a 21 kDa precursor which is retained in the ER
membrane through the hydrophobic signal peptide. Cleavage by the
signal peptidase releases the 19 kDa mature core protein. The
other proteins (p7, NS2-3, NS3, NS4A, NS4B, NS5A and NS5B) are
cleaved by the viral proteases (By similarity). {ECO:0000250}.
-!- PTM: Envelope E1 and E2 glycoproteins are highly N-glycosylated.
{ECO:0000250}.
-!- PTM: Core protein is phosphorylated by host PKC and PKA.
{ECO:0000250}.
-!- PTM: NS5A is phosphorylated in a basal form termed p56. p58 is a
hyperphosphorylated form of p56. p56 and p58 coexist in the cell
in roughly equivalent amounts. Hyperphosphorylation is dependent
on the presence of NS4A. Human AKT1, RPS6KB1/p70S6K, MAP2K1/MEK1,
MAP2K6/MKK6 and CSNK1A1/CKI-alpha kinases may be responsible for
NS5A phosphorylation (By similarity). {ECO:0000250}.
-!- PTM: NS4B is palmitoylated. This modification may play a role in
its polymerization or in protein-protein interactions (By
similarity). {ECO:0000250}.
-!- PTM: The N-terminus of a fraction of NS4B molecules seems to be
relocated post-translationally from the cytoplasm to the ER lumen,
with a 5th transmembrane segment. The C-terminus of NS2 may be
lumenal with a fourth transmembrane segment (By similarity).
{ECO:0000250}.
-!- PTM: Core protein is ubiquitinated; mediated by UBE3A and leading
to core protein subsequent proteasomal degradation. {ECO:0000250}.
-!- MISCELLANEOUS: Cell culture adaptation of the virus leads to
mutations in NS5A, reducing its inhibitory effect on replication.
{ECO:0000250}.
-!- MISCELLANEOUS: Core protein exerts viral interference on hepatitis
B virus when HCV and HBV coinfect the same cell, by suppressing
HBV gene expression, RNA encapsidation and budding. {ECO:0000250}.
-!- SIMILARITY: Belongs to the hepacivirus polyprotein family.
{ECO:0000305}.
-!- CAUTION: The core gene probably also codes for alternative reading
frame proteins (ARFPs). Many functions depicted for the core
protein might belong to the ARFPs. {ECO:0000305}.
-!- WEB RESOURCE: Name=Virus Pathogen Resource;
URL="http://www.viprbrc.org/brc/home.spg?decorator=flavi_hcv";
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EMBL; AB047639; BAB32872.1; -; Genomic_RNA.
PDB; 2KZQ; NMR; -; A=684-719.
PDB; 2LIF; NMR; -; A=171-195.
PDB; 2LVG; NMR; -; A=1716-1755.
PDB; 2XXD; X-ray; 1.88 A; A=2443-3005.
PDB; 2XYM; X-ray; 1.77 A; A=2443-3005.
PDB; 3I5K; X-ray; 2.20 A; A/B/C/D=2443-3007.
PDB; 4AEP; X-ray; 1.80 A; A=2443-3013.
PDB; 4AEX; X-ray; 2.41 A; A/B=2443-3013.
PDB; 4E76; X-ray; 2.50 A; A=2443-2885, A=2896-3012.
PDB; 4E78; X-ray; 2.90 A; A=2443-2885, A=2896-3012.
PDB; 4E7A; X-ray; 3.00 A; A=2443-2885, A=2896-3012.
PDB; 4J1V; X-ray; 1.95 A; E/F/G/H=2284-2303.
PDB; 4OBC; X-ray; 2.50 A; A=2443-3012.
PDB; 4WT9; X-ray; 2.50 A; A=2443-2885, A=2896-3012.
PDB; 4WTA; X-ray; 2.80 A; A=2443-2885, A=2896-3012.
PDB; 4WTC; X-ray; 2.75 A; A=2443-2885, A=2896-3012.
PDB; 4WTD; X-ray; 2.70 A; A=2443-2885, A=2896-3012.
PDB; 4WTE; X-ray; 2.90 A; A=2443-2885, A=2896-3012.
PDB; 4WTF; X-ray; 2.65 A; A=2443-2885, A=2896-3012.
PDB; 4WTG; X-ray; 2.90 A; A=2443-2885, A=2896-3012.
PDB; 4WTI; X-ray; 2.80 A; A=2443-3012.
PDB; 4WTJ; X-ray; 2.20 A; A=2443-3012.
PDB; 4WTK; X-ray; 2.50 A; A=2443-3012.
PDB; 4WTL; X-ray; 2.00 A; A=2443-3012.
PDB; 4WTM; X-ray; 2.15 A; A=2443-3012.
PDB; 5NPJ; X-ray; 1.90 A; D/E=531-542.
PDB; 5TWM; X-ray; 1.97 A; A=2443-3015.
PDB; 5UJ2; X-ray; 2.90 A; A=2443-3012.
PDBsum; 2KZQ; -.
PDBsum; 2LIF; -.
PDBsum; 2LVG; -.
PDBsum; 2XXD; -.
PDBsum; 2XYM; -.
PDBsum; 3I5K; -.
PDBsum; 4AEP; -.
PDBsum; 4AEX; -.
PDBsum; 4E76; -.
PDBsum; 4E78; -.
PDBsum; 4E7A; -.
PDBsum; 4J1V; -.
PDBsum; 4OBC; -.
PDBsum; 4WT9; -.
PDBsum; 4WTA; -.
PDBsum; 4WTC; -.
PDBsum; 4WTD; -.
PDBsum; 4WTE; -.
PDBsum; 4WTF; -.
PDBsum; 4WTG; -.
PDBsum; 4WTI; -.
PDBsum; 4WTJ; -.
PDBsum; 4WTK; -.
PDBsum; 4WTL; -.
PDBsum; 4WTM; -.
PDBsum; 5NPJ; -.
PDBsum; 5TWM; -.
PDBsum; 5UJ2; -.
DisProt; DP01031; -.
ProteinModelPortal; Q99IB8; -.
SMR; Q99IB8; -.
DIP; DIP-48925N; -.
IntAct; Q99IB8; 346.
MINT; MINT-8361175; -.
BindingDB; Q99IB8; -.
euHCVdb; AB047639; -.
OrthoDB; VOG09000032; -.
Reactome; R-HSA-5621480; Dectin-2 family.
EvolutionaryTrace; Q99IB8; -.
Proteomes; UP000008096; Genome.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0030430; C:host cell cytoplasm; IDA:AgBase.
GO; GO:0044165; C:host cell endoplasmic reticulum; IDA:AgBase.
GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0044186; C:host cell lipid particle; IEA:UniProtKB-SubCell.
GO; GO:0044191; C:host cell mitochondrial membrane; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; TAS:Reactome.
GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
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:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0005160; F:transforming growth factor beta receptor binding; IPI:AgBase.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:AgBase.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
GO; GO:0039614; P:induction by virus of host protein phosphorylation; IDA:AgBase.
GO; GO:0039645; P:modulation by virus of host G1/S transition checkpoint; IEA:UniProtKB-KW.
GO; GO:1990214; P:negative regulation by symbiont of host protein levels; IDA:AgBase.
GO; GO:1902902; P:negative regulation of autophagosome assembly; IDA:AgBase.
GO; GO:0010507; P:negative regulation of autophagy; IDA:AgBase.
GO; GO:0032715; P:negative regulation of interleukin-6 production; IDA:AgBase.
GO; GO:1903147; P:negative regulation of mitophagy; IDA:AgBase.
GO; GO:1903637; P:negative regulation of protein import into mitochondrial outer membrane; IDA:AgBase.
GO; GO:1903215; P:negative regulation of protein targeting to mitochondrion; IDA:AgBase.
GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:AgBase.
GO; GO:0034136; P:negative regulation of toll-like receptor 2 signaling pathway; IDA:AgBase.
GO; GO:0034144; P:negative regulation of toll-like receptor 4 signaling pathway; IDA:AgBase.
GO; GO:0034156; P:negative regulation of toll-like receptor 7 signaling pathway; IDA:AgBase.
GO; GO:0034164; P:negative regulation of toll-like receptor 9 signaling pathway; IDA:AgBase.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0052369; P:positive regulation by symbiont of defense-related host reactive oxygen species production; IDA:AgBase.
GO; GO:1990219; P:positive regulation by symbiont of host protein levels; IDA:AgBase.
GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IDA:AgBase.
GO; GO:0032914; P:positive regulation of transforming growth factor beta1 production; IDA:AgBase.
GO; GO:1901397; P:positive regulation of transforming growth factor beta2 activation; IDA:AgBase.
GO; GO:0051259; P:protein oligomerization; IEA:UniProtKB-KW.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0039545; P:suppression by virus of host MAVS activity; IEA:UniProtKB-KW.
GO; GO:0039563; P:suppression by virus of host STAT1 activity; IEA:UniProtKB-KW.
GO; GO:0039547; P:suppression by virus of host TRAF activity; IEA:UniProtKB-KW.
GO; GO:0039653; P:suppression by virus of host transcription; IDA:AgBase.
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:UniProtKB-KW.
GO; GO:0019087; P:transformation of host cell by virus; IEA:InterPro.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
InterPro; IPR011492; DEAD_Flavivir.
InterPro; IPR002521; HCV_core_C.
InterPro; IPR002522; HCV_core_N.
InterPro; IPR002519; HCV_env.
InterPro; IPR002531; HCV_NS1.
InterPro; IPR002518; HCV_NS2.
InterPro; IPR000745; HCV_NS4a.
InterPro; IPR001490; HCV_NS4b.
InterPro; IPR002868; HCV_NS5a.
InterPro; IPR013193; HCV_NS5a_1B_dom.
InterPro; IPR024350; HCV_NS5a_C.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR013192; NS5A_1a.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR004109; Peptidase_S29.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR002166; RNA_pol_HCV.
Pfam; PF07652; Flavi_DEAD; 1.
Pfam; PF01543; HCV_capsid; 1.
Pfam; PF01542; HCV_core; 1.
Pfam; PF01539; HCV_env; 1.
Pfam; PF01560; HCV_NS1; 1.
Pfam; PF01538; HCV_NS2; 1.
Pfam; PF01006; HCV_NS4a; 1.
Pfam; PF01001; HCV_NS4b; 1.
Pfam; PF01506; HCV_NS5a; 1.
Pfam; PF08300; HCV_NS5a_1a; 1.
Pfam; PF08301; HCV_NS5a_1b; 1.
Pfam; PF12941; HCV_NS5a_C; 1.
Pfam; PF02907; Peptidase_S29; 1.
Pfam; PF00998; RdRP_3; 1.
ProDom; PD001388; HCV_env; 1.
SMART; SM00487; DEXDc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS51693; HCV_NS2_PRO; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51822; HV_PV_NS3_PRO; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activation of host autophagy by virus;
Apoptosis; ATP-binding; Capsid protein;
Clathrin-mediated endocytosis of virus by host; Complete proteome;
Disulfide bond; Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane;
G1/S host cell cycle checkpoint dysregulation by virus; Glycoprotein;
Helicase; Host cell membrane; Host cytoplasm;
Host endoplasmic reticulum; Host lipid droplet; Host membrane;
Host mitochondrion; Host nucleus; Host-virus interaction; Hydrolase;
Inhibition of host innate immune response by virus;
Inhibition of host interferon signaling pathway by virus;
Inhibition of host MAVS by virus;
Inhibition of host RLR pathway by virus;
Inhibition of host STAT1 by virus; Inhibition of host TRAFs by virus;
Interferon antiviral system evasion; Ion channel; Ion transport;
Lipoprotein; Membrane; Metal-binding;
Modulation of host cell cycle by virus; Multifunctional enzyme;
Nucleotide-binding; Nucleotidyltransferase; Oncogene; Palmitate;
Phosphoprotein; Protease; Ribonucleoprotein; RNA-binding;
RNA-directed RNA polymerase; Secreted; Serine protease; SH3-binding;
Thiol protease; Transcription; Transcription regulation; Transferase;
Transmembrane; Transmembrane helix; Transport; Ubl conjugation;
Viral attachment to host cell; Viral envelope protein;
Viral immunoevasion; Viral ion channel; Viral nucleoprotein;
Viral penetration into host cytoplasm; Viral RNA replication; Virion;
Virus endocytosis by host; Virus entry into host cell; Zinc.
INIT_MET 1 1 Removed; by host. {ECO:0000250}.
CHAIN 2 191 Core protein p21. {ECO:0000255}.
/FTId=PRO_0000045592.
CHAIN 2 177 Core protein p19. {ECO:0000250}.
/FTId=PRO_0000045593.
PROPEP 178 191 ER anchor for the core protein, removed
in mature form by host signal peptidase.
{ECO:0000250}.
/FTId=PRO_0000045594.
CHAIN 192 383 Envelope glycoprotein E1. {ECO:0000255}.
/FTId=PRO_0000045595.
CHAIN 384 750 Envelope glycoprotein E2. {ECO:0000255}.
/FTId=PRO_0000045596.
CHAIN 751 813 p7. {ECO:0000250}.
/FTId=PRO_0000045597.
CHAIN 814 1030 Protease NS2-3. {ECO:0000255|PROSITE-
ProRule:PRU01030}.
/FTId=PRO_0000045598.
CHAIN 1031 1661 Serine protease NS3. {ECO:0000255}.
/FTId=PRO_0000045599.
CHAIN 1662 1715 Non-structural protein 4A. {ECO:0000255}.
/FTId=PRO_0000045600.
CHAIN 1716 1976 Non-structural protein 4B. {ECO:0000255}.
/FTId=PRO_0000045601.
CHAIN 1977 2442 Non-structural protein 5A. {ECO:0000255}.
/FTId=PRO_0000045602.
CHAIN 2443 3033 RNA-directed RNA polymerase.
{ECO:0000255}.
/FTId=PRO_0000045603.
TOPO_DOM 2 168 Cytoplasmic. {ECO:0000255}.
TRANSMEM 169 189 Helical. {ECO:0000255}.
TOPO_DOM 190 358 Lumenal. {ECO:0000255}.
TRANSMEM 359 379 Helical. {ECO:0000255}.
TOPO_DOM 380 729 Lumenal. {ECO:0000255}.
TRANSMEM 730 750 Helical. {ECO:0000255}.
TOPO_DOM 751 761 Lumenal. {ECO:0000255}.
TRANSMEM 762 782 Helical. {ECO:0000255}.
TOPO_DOM 783 786 Cytoplasmic. {ECO:0000255}.
TRANSMEM 787 807 Helical. {ECO:0000255}.
TOPO_DOM 808 817 Lumenal. {ECO:0000255}.
TRANSMEM 818 838 Helical. {ECO:0000255}.
TOPO_DOM 839 885 Cytoplasmic. {ECO:0000255}.
TRANSMEM 886 906 Helical. {ECO:0000255}.
TOPO_DOM 907 932 Lumenal. {ECO:0000255}.
TRANSMEM 933 953 Helical. {ECO:0000255}.
TOPO_DOM 954 1661 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1662 1682 Helical. {ECO:0000255}.
TOPO_DOM 1683 1809 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1810 1830 Helical. {ECO:0000255}.
TOPO_DOM 1831 1832 Lumenal. {ECO:0000255}.
TRANSMEM 1833 1853 Helical. {ECO:0000255}.
TOPO_DOM 1854 1854 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1855 1875 Helical. {ECO:0000255}.
TOPO_DOM 1876 1885 Lumenal. {ECO:0000255}.
TRANSMEM 1886 1906 Helical. {ECO:0000255}.
TOPO_DOM 1907 1976 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1977 2006 {ECO:0000250}.
TOPO_DOM 2007 3012 Cytoplasmic. {ECO:0000255}.
TRANSMEM 3013 3033 Helical. {ECO:0000250}.
DOMAIN 907 1030 Peptidase C18. {ECO:0000255|PROSITE-
ProRule:PRU01030}.
DOMAIN 1031 1212 Peptidase S29. {ECO:0000255|PROSITE-
ProRule:PRU01166}.
DOMAIN 1221 1373 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 2656 2774 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1234 1241 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
REGION 2 59 Interaction with DDX3X. {ECO:0000250}.
REGION 2 23 Interaction with STAT1. {ECO:0000250}.
REGION 122 173 Interaction with APOA2. {ECO:0000250}.
REGION 150 159 Mitochondrial targeting signal.
{ECO:0000250}.
REGION 164 167 Important for lipid droplets
localization. {ECO:0000250}.
REGION 265 296 Fusion peptide. {ECO:0000255}.
REGION 385 411 HVR1. {ECO:0000250}.
REGION 484 496 CD81-binding 1. {ECO:0000255}.
REGION 524 555 CD81-binding 2. {ECO:0000255}.
REGION 664 675 PKR/eIF2-alpha phosphorylation homology
domain (PePHD). {ECO:0000250}.
REGION 1683 1694 NS3-binding (by NS4A). {ECO:0000255}.
REGION 2124 2332 Transcriptional activation.
{ECO:0000255}.
REGION 2124 2212 FKBP8-binding. {ECO:0000255}.
REGION 2204 2250 Basal phosphorylation. {ECO:0000250}.
REGION 2214 2275 PKR-binding. {ECO:0000255}.
REGION 2249 2306 NS4B-binding. {ECO:0000255}.
REGION 2351 2442 Basal phosphorylation. {ECO:0000250}.
MOTIF 5 13 Nuclear localization signal.
{ECO:0000255}.
MOTIF 38 43 Nuclear localization signal.
{ECO:0000255}.
MOTIF 58 64 Nuclear localization signal.
{ECO:0000255}.
MOTIF 66 71 Nuclear localization signal.
{ECO:0000255}.
MOTIF 1320 1323 DECH box. {ECO:0000250}.
MOTIF 2322 2325 SH3-binding. {ECO:0000255}.
MOTIF 2327 2335 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 1436 1439 Poly-Val.
COMPBIAS 2277 2327 Pro-rich.
COMPBIAS 2328 2331 Poly-Arg.
COMPBIAS 3018 3021 Poly-Leu.
ACT_SITE 956 956 For protease NS2-3 activity; shared with
dimeric partner. {ECO:0000255|PROSITE-
ProRule:PRU01030}.
ACT_SITE 976 976 For protease NS2-3 activity; shared with
dimeric partner. {ECO:0000255|PROSITE-
ProRule:PRU01030}.
ACT_SITE 997 997 For protease NS2-3 activity; shared with
dimeric partner. {ECO:0000255|PROSITE-
ProRule:PRU01030}.
ACT_SITE 1087 1087 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU01166}.
ACT_SITE 1111 1111 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU01166}.
ACT_SITE 1169 1169 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU01166}.
METAL 1127 1127 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01166}.
METAL 1129 1129 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01166}.
METAL 1175 1175 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01166}.
METAL 1179 1179 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01166}.
METAL 2015 2015 Zinc. {ECO:0000250}.
METAL 2033 2033 Zinc. {ECO:0000250}.
METAL 2035 2035 Zinc. {ECO:0000250}.
METAL 2056 2056 Zinc. {ECO:0000250}.
SITE 177 178 Cleavage; by host signal peptidase.
{ECO:0000250}.
SITE 191 192 Cleavage; by host signal peptidase.
{ECO:0000255}.
SITE 383 384 Cleavage; by host signal peptidase.
{ECO:0000255}.
SITE 750 751 Cleavage; by host signal peptidase.
{ECO:0000250}.
SITE 813 814 Cleavage; by host signal peptidase.
{ECO:0000250}.
SITE 1030 1031 Cleavage; by protease NS2-3.
{ECO:0000255|PROSITE-ProRule:PRU01030}.
SITE 1661 1662 Cleavage; by serine protease NS3.
{ECO:0000255}.
SITE 1715 1716 Cleavage; by serine protease NS3.
{ECO:0000255}.
SITE 1976 1977 Cleavage; by serine protease NS3.
{ECO:0000255}.
SITE 2442 2443 Cleavage; by serine protease NS3.
{ECO:0000255}.
MOD_RES 2 2 N-acetylserine; by host. {ECO:0000250}.
MOD_RES 53 53 Phosphoserine; by host. {ECO:0000250}.
MOD_RES 99 99 Phosphoserine; by host. {ECO:0000250}.
MOD_RES 116 116 Phosphoserine; by host PKA.
{ECO:0000250}.
MOD_RES 2198 2198 Phosphoserine; by host; in p56.
{ECO:0000250}.
MOD_RES 2201 2201 Phosphoserine; by host; in p58.
{ECO:0000250}.
MOD_RES 2205 2205 Phosphoserine; by host; in p58.
{ECO:0000250}.
MOD_RES 2208 2208 Phosphoserine; by host; in p58.
{ECO:0000250}.
LIPID 1972 1972 S-palmitoyl cysteine; by host.
{ECO:0000250}.
LIPID 1976 1976 S-palmitoyl cysteine; by host.
{ECO:0000250}.
CARBOHYD 196 196 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 209 209 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 234 234 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 305 305 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 417 417 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 423 423 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 430 430 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 448 448 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 477 477 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 534 534 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 542 542 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 558 558 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 578 578 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 627 627 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 649 649 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 2118 2166 {ECO:0000250}.
HELIX 175 185 {ECO:0000244|PDB:2LIF}.
HELIX 189 194 {ECO:0000244|PDB:2LIF}.
HELIX 692 701 {ECO:0000244|PDB:2KZQ}.
TURN 702 706 {ECO:0000244|PDB:2KZQ}.
HELIX 710 714 {ECO:0000244|PDB:2KZQ}.
TURN 715 718 {ECO:0000244|PDB:2KZQ}.
HELIX 1719 1748 {ECO:0000244|PDB:2LVG}.
STRAND 2444 2448 {ECO:0000244|PDB:2XYM}.
HELIX 2467 2470 {ECO:0000244|PDB:2XYM}.
HELIX 2476 2478 {ECO:0000244|PDB:2XYM}.
STRAND 2479 2481 {ECO:0000244|PDB:2XYM}.
HELIX 2484 2486 {ECO:0000244|PDB:2XYM}.
HELIX 2487 2494 {ECO:0000244|PDB:2XYM}.
HELIX 2504 2517 {ECO:0000244|PDB:2XYM}.
HELIX 2527 2532 {ECO:0000244|PDB:2XYM}.
TURN 2542 2544 {ECO:0000244|PDB:4AEX}.
HELIX 2547 2552 {ECO:0000244|PDB:2XYM}.
HELIX 2557 2570 {ECO:0000244|PDB:2XYM}.
STRAND 2572 2574 {ECO:0000244|PDB:2XXD}.
STRAND 2578 2582 {ECO:0000244|PDB:2XYM}.
STRAND 2586 2588 {ECO:0000244|PDB:2XYM}.
HELIX 2591 2593 {ECO:0000244|PDB:2XYM}.
STRAND 2601 2604 {ECO:0000244|PDB:2XYM}.
HELIX 2607 2629 {ECO:0000244|PDB:2XYM}.
HELIX 2630 2632 {ECO:0000244|PDB:2XYM}.
HELIX 2634 2636 {ECO:0000244|PDB:2XYM}.
HELIX 2639 2651 {ECO:0000244|PDB:2XYM}.
STRAND 2653 2663 {ECO:0000244|PDB:2XYM}.
HELIX 2666 2669 {ECO:0000244|PDB:2XYM}.
HELIX 2672 2684 {ECO:0000244|PDB:2XYM}.
HELIX 2689 2701 {ECO:0000244|PDB:2XYM}.
TURN 2702 2704 {ECO:0000244|PDB:2XYM}.
STRAND 2706 2709 {ECO:0000244|PDB:2XYM}.
STRAND 2715 2719 {ECO:0000244|PDB:2XYM}.
HELIX 2729 2748 {ECO:0000244|PDB:2XYM}.
STRAND 2754 2758 {ECO:0000244|PDB:2XYM}.
STRAND 2761 2767 {ECO:0000244|PDB:2XYM}.
HELIX 2771 2787 {ECO:0000244|PDB:2XYM}.
STRAND 2792 2794 {ECO:0000244|PDB:2XYM}.
STRAND 2799 2801 {ECO:0000244|PDB:2XYM}.
HELIX 2802 2804 {ECO:0000244|PDB:2XYM}.
STRAND 2810 2816 {ECO:0000244|PDB:2XYM}.
HELIX 2818 2820 {ECO:0000244|PDB:2XYM}.
STRAND 2822 2828 {ECO:0000244|PDB:2XYM}.
HELIX 2831 2842 {ECO:0000244|PDB:2XYM}.
STRAND 2846 2849 {ECO:0000244|PDB:2XYM}.
HELIX 2850 2856 {ECO:0000244|PDB:2XYM}.
TURN 2857 2859 {ECO:0000244|PDB:2XYM}.
HELIX 2861 2865 {ECO:0000244|PDB:2XYM}.
HELIX 2867 2878 {ECO:0000244|PDB:2XYM}.
STRAND 2881 2883 {ECO:0000244|PDB:4E76}.
STRAND 2885 2889 {ECO:0000244|PDB:2XYM}.
STRAND 2892 2896 {ECO:0000244|PDB:2XYM}.
HELIX 2898 2900 {ECO:0000244|PDB:2XYM}.
HELIX 2901 2909 {ECO:0000244|PDB:2XYM}.
HELIX 2911 2914 {ECO:0000244|PDB:2XYM}.
HELIX 2921 2934 {ECO:0000244|PDB:2XYM}.
HELIX 2939 2955 {ECO:0000244|PDB:2XYM}.
HELIX 2958 2967 {ECO:0000244|PDB:2XYM}.
HELIX 2969 2971 {ECO:0000244|PDB:2XYM}.
STRAND 2972 2974 {ECO:0000244|PDB:4WTL}.
HELIX 2982 2986 {ECO:0000244|PDB:2XYM}.
HELIX 2992 2996 {ECO:0000244|PDB:2XYM}.
HELIX 2998 3000 {ECO:0000244|PDB:4AEP}.
STRAND 3003 3005 {ECO:0000244|PDB:3I5K}.
SEQUENCE 3033 AA; 328828 MW; 7E5BEA79702AF95B CRC64;
MSTNPKPQRK TKRNTNRRPE DVKFPGGGQI VGGVYLLPRR GPRLGVRTTR KTSERSQPRG
RRQPIPKDRR STGKAWGKPG RPWPLYGNEG LGWAGWLLSP RGSRPSWGPT DPRHRSRNVG
KVIDTLTCGF ADLMGYIPVV GAPLSGAARA VAHGVRVLED GVNYATGNLP GFPFSIFLLA
LLSCITVPVS AAQVKNTSSS YMVTNDCSND SITWQLEAAV LHVPGCVPCE RVGNTSRCWV
PVSPNMAVRQ PGALTQGLRT HIDMVVMSAT FCSALYVGDL CGGVMLAAQV FIVSPQYHWF
VQECNCSIYP GTITGHRMAW DMMMNWSPTA TMILAYVMRV PEVIIDIVSG AHWGVMFGLA
YFSMQGAWAK VIVILLLAAG VDAGTTTVGG AVARSTNVIA GVFSHGPQQN IQLINTNGSW
HINRTALNCN DSLNTGFLAA LFYTNRFNSS GCPGRLSACR NIEAFRIGWG TLQYEDNVTN
PEDMRPYCWH YPPKPCGVVP ARSVCGPVYC FTPSPVVVGT TDRRGVPTYT WGENETDVFL
LNSTRPPQGS WFGCTWMNST GFTKTCGAPP CRTRADFNAS TDLLCPTDCF RKHPDATYIK
CGSGPWLTPK CLVHYPYRLW HYPCTVNFTI FKIRMYVGGV EHRLTAACNF TRGDRCDLED
RDRSQLSPLL HSTTEWAILP CTYSDLPALS TGLLHLHQNI VDVQYMYGLS PAITKYVVRW
EWVVLLFLLL ADARVCACLW MLILLGQAEA ALEKLVVLHA ASAANCHGLL YFAIFFVAAW
HIRGRVVPLT TYCLTGLWPF CLLLMALPRQ AYAYDAPVHG QIGVGLLILI TLFTLTPGYK
TLLGQCLWWL CYLLTLGEAM IQEWVPPMQV RGGRDGIAWA VTIFCPGVVF DITKWLLALL
GPAYLLRAAL THVPYFVRAH ALIRVCALVK QLAGGRYVQV ALLALGRWTG TYIYDHLTPM
SDWAASGLRD LAVAVEPIIF SPMEKKVIVW GAETAACGDI LHGLPVSARL GQEILLGPAD
GYTSKGWKLL APITAYAQQT RGLLGAIVVS MTGRDRTEQA GEVQILSTVS QSFLGTTISG
VLWTVYHGAG NKTLAGLRGP VTQMYSSAEG DLVGWPSPPG TKSLEPCKCG AVDLYLVTRN
ADVIPARRRG DKRGALLSPR PISTLKGSSG GPVLCPRGHV VGLFRAAVCS RGVAKSIDFI
PVETLDVVTR SPTFSDNSTP PAVPQTYQVG YLHAPTGSGK STKVPVAYAA QGYKVLVLNP
SVAATLGFGA YLSKAHGINP NIRTGVRTVM TGEAITYSTY GKFLADGGCA SGAYDIIICD
ECHAVDATSI LGIGTVLDQA ETAGVRLTVL ATATPPGSVT TPHPDIEEVG LGREGEIPFY
GRAIPLSCIK GGRHLIFCHS KKKCDELAAA LRGMGLNAVA YYRGLDVSII PAQGDVVVVA
TDALMTGYTG DFDSVIDCNV AVTQAVDFSL DPTFTITTQT VPQDAVSRSQ RRGRTGRGRQ
GTYRYVSTGE RASGMFDSVV LCECYDAGAA WYDLTPAETT VRLRAYFNTP GLPVCQDHLE
FWEAVFTGLT HIDAHFLSQT KQAGENFAYL VAYQATVCAR AKAPPPSWDA MWKCLARLKP
TLAGPTPLLY RLGPITNEVT LTHPGTKYIA TCMQADLEVM TSTWVLAGGV LAAVAAYCLA
TGCVSIIGRL HVNQRVVVAP DKEVLYEAFD EMEECASRAA LIEEGQRIAE MLKSKIQGLL
QQASKQAQDI QPAMQASWPK VEQFWARHMW NFISGIQYLA GLSTLPGNPA VASMMAFSAA
LTSPLSTSTT ILLNIMGGWL ASQIAPPAGA TGFVVSGLVG AAVGSIGLGK VLVDILAGYG
AGISGALVAF KIMSGEKPSM EDVINLLPGI LSPGALVVGV ICAAILRRHV GPGEGAVQWM
NRLIAFASRG NHVAPTHYVT ESDASQRVTQ LLGSLTITSL LRRLHNWITE DCPIPCSGSW
LRDVWDWVCT ILTDFKNWLT SKLFPKLPGL PFISCQKGYK GVWAGTGIMT TRCPCGANIS
GNVRLGSMRI TGPKTCMNTW QGTFPINCYT EGQCAPKPPT NYKTAIWRVA ASEYAEVTQH
GSYSYVTGLT TDNLKIPCQL PSPEFFSWVD GVQIHRFAPT PKPFFRDEVS FCVGLNSYAV
GSQLPCEPEP DADVLRSMLT DPPHITAETA ARRLARGSPP SEASSSVSQL SAPSLRATCT
THSNTYDVDM VDANLLMEGG VAQTEPESRV PVLDFLEPMA EEESDLEPSI PSECMLPRSG
FPRALPAWAR PDYNPPLVES WRRPDYQPPT VAGCALPPPK KAPTPPPRRR RTVGLSESTI
SEALQQLAIK TFGQPPSSGD AGSSTGAGAA ESGGPTSPGE PAPSETGSAS SMPPLEGEPG
DPDLESDQVE LQPPPQGGGV APGSGSGSWS TCSEEDDTTV CCSMSYSWTG ALITPCSPEE
EKLPINPLSN SLLRYHNKVY CTTSKSASQR AKKVTFDRTQ VLDAHYDSVL KDIKLAASKV
SARLLTLEEA CQLTPPHSAR SKYGFGAKEV RSLSGRAVNH IKSVWKDLLE DPQTPIPTTI
MAKNEVFCVD PAKGGKKPAR LIVYPDLGVR VCEKMALYDI TQKLPQAVMG ASYGFQYSPA
QRVEYLLKAW AEKKDPMGFS YDTRCFDSTV TERDIRTEES IYQACSLPEE ARTAIHSLTE
RLYVGGPMFN SKGQTCGYRR CRASGVLTTS MGNTITCYVK ALAACKAAGI VAPTMLVCGD
DLVVISESQG TEEDERNLRA FTEAMTRYSA PPGDPPRPEY DLELITSCSS NVSVALGPRG
RRRYYLTRDP TTPLARAAWE TVRHSPINSW LGNIIQYAPT IWVRMVLMTH FFSILMVQDT
LDQNLNFEMY GSVYSVNPLD LPAIIERLHG LDAFSMHTYS HHELTRVASA LRKLGAPPLR
VWKSRARAVR ASLISRGGKA AVCGRYLFNW AVKTKLKLTP LPEARLLDLS SWFTVGAGGG
DIFHSVSRAR PRSLLFGLLL LFVGVGLFLL PAR


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