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Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Non-structural protein 2A-alpha (NS2A-alpha); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]

 POLG_YEFVA              Reviewed;        3411 AA.
Q6DV88; Q89278;
28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
16-AUG-2004, sequence version 1.
20-JUN-2018, entry version 113.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Capsid protein C;
AltName: Full=Core protein;
Contains:
RecName: Full=Protein prM;
Contains:
RecName: Full=Peptide pr;
Contains:
RecName: Full=Small envelope protein M;
AltName: Full=Matrix protein;
Contains:
RecName: Full=Envelope protein E;
Contains:
RecName: Full=Non-structural protein 1;
Short=NS1;
Contains:
RecName: Full=Non-structural protein 2A;
Short=NS2A;
Contains:
RecName: Full=Non-structural protein 2A-alpha;
Short=NS2A-alpha;
Contains:
RecName: Full=Serine protease subunit NS2B;
AltName: Full=Flavivirin protease NS2B regulatory subunit;
AltName: Full=Non-structural protein 2B;
Contains:
RecName: Full=Serine protease NS3;
EC=3.4.21.91;
EC=3.6.1.15 {ECO:0000250|UniProtKB:Q9Q6P4};
EC=3.6.4.13 {ECO:0000250|UniProtKB:Q9Q6P4};
AltName: Full=Flavivirin protease NS3 catalytic subunit;
AltName: Full=Non-structural protein 3;
Contains:
RecName: Full=Non-structural protein 4A;
Short=NS4A;
Contains:
RecName: Full=Peptide 2k;
Contains:
RecName: Full=Non-structural protein 4B;
Short=NS4B;
Contains:
RecName: Full=RNA-directed RNA polymerase NS5;
EC=2.1.1.56 {ECO:0000255|PROSITE-ProRule:PRU00924};
EC=2.1.1.57 {ECO:0000255|PROSITE-ProRule:PRU00924};
EC=2.7.7.48 {ECO:0000255|PROSITE-ProRule:PRU00539};
AltName: Full=Non-structural protein 5;
Yellow fever virus (strain Ghana/Asibi/1927) (YFV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Flavivirus.
NCBI_TaxID=407134;
NCBI_TaxID=7159; Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
NCBI_TaxID=299629; Aedes luteocephalus (Mosquito).
NCBI_TaxID=7161; Aedes simpsoni.
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=314293; Simiiformes.
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate Senegal/French viscerotropic virus FVV/27;
PubMed=7595382; DOI=10.1099/0022-1317-76-11-2749;
Wang E., Ryman K.D., Jennings A.D., Wood D.J., Taffs F., Minor P.D.,
Sanders P.G., Barrett A.D.;
"Comparison of the genomes of the wild-type French viscerotropic
strain of yellow fever virus with its vaccine derivative French
neurotropic vaccine.";
J. Gen. Virol. 76:2749-2755(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=15914853; DOI=10.1099/vir.0.80746-0;
McElroy K.L., Tsetsarkin K.A., Vanlandingham D.L., Higgs S.;
"Characterization of an infectious clone of the wild-type yellow fever
virus Asibi strain that is able to infect and disseminate in
mosquitoes.";
J. Gen. Virol. 86:1747-1751(2005).
[3]
STRUCTURE BY NMR OF 573-683.
PubMed=19818466; DOI=10.1016/j.virol.2009.09.001;
Volk D.E., May F.J., Gandham S.H., Anderson A., Von Lindern J.J.,
Beasley D.W., Barrett A.D., Gorenstein D.G.;
"Structure of yellow fever virus envelope protein domain III.";
Virology 394:12-18(2009).
-!- FUNCTION: Capsid protein C: Plays a role in virus budding by
binding to the cell membrane and gathering the viral RNA into a
nucleocapsid that forms the core of a mature virus particle.
During virus entry, may induce genome penetration into the host
cytoplasm after hemifusion induced by the surface proteins. Can
migrate to the cell nucleus where it modulates host functions.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Capsid protein C: Inhibits RNA silencing by interfering
with host Dicer. {ECO:0000250|UniProtKB:P03314}.
-!- FUNCTION: Peptide pr: Prevents premature fusion activity of
envelope proteins in trans-Golgi by binding to envelope protein E
at pH6.0. After virion release in extracellular space, gets
dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Protein prM: Acts as a chaperone for envelope protein E
during intracellular virion assembly by masking and inactivating
envelope protein E fusion peptide. prM is the only viral peptide
matured by host furin in the trans-Golgi network probably to avoid
catastrophic activation of the viral fusion activity in acidic
Golgi compartment prior to virion release. prM-E cleavage is
inefficient, and many virions are only partially matured. These
uncleaved prM would play a role in immune evasion.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Small envelope protein M: May play a role in virus
budding. Exerts cytotoxic effects by activating a mitochondrial
apoptotic pathway through M ectodomain. May display a viroporin
activity. {ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Envelope protein E: Binds to host cell surface receptor
and mediates fusion between viral and cellular membranes. Envelope
protein is synthesized in the endoplasmic reticulum in the form of
heterodimer with protein prM. They play a role in virion budding
in the ER, and the newly formed immature particle is covered with
60 spikes composed of heterodimer between precursor prM and
envelope protein E. The virion is transported to the Golgi
apparatus where the low pH causes dissociation of PrM-E
heterodimers and formation of E homodimers. prM-E cleavage is
inefficient, and many virions are only partially matured. These
uncleaved prM would play a role in immune evasion.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Non-structural protein 1: Involved in immune evasion,
pathogenesis and viral replication. Once cleaved off the
polyprotein, is targeted to three destinations: the viral
replication cycle, the plasma membrane and the extracellular
compartment. Essential for viral replication. Required for
formation of the replication complex and recruitment of other non-
structural proteins to the ER-derived membrane structures.
Excreted as a hexameric lipoparticle that plays a role against
host immune response. Antagonizing the complement function. Binds
to the host macrophages and dendritic cells. Inhibits signal
transduction originating from Toll-like receptor 3 (TLR3).
{ECO:0000250|UniProtKB:Q9Q6P4}.
-!- FUNCTION: Non-structural protein 2A: Component of the viral RNA
replication complex that functions in virion assembly and
antagonizes the host immune response.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Serine protease subunit NS2B: Required cofactor for the
serine protease function of NS3. May have membrane-destabilizing
activity and form viroporins (By similarity).
{ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-
ProRule:PRU00859}.
-!- FUNCTION: Serine protease NS3: Displays three enzymatic
activities: serine protease, NTPase and RNA helicase. NS3 serine
protease, in association with NS2B, performs its autocleavage and
cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM,
NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA
helicase binds RNA and unwinds dsRNA in the 3' to 5' direction.
Also plays a role in virus assembly (By similarity).
{ECO:0000250|UniProtKB:P03314, ECO:0000255|PROSITE-
ProRule:PRU00860}.
-!- FUNCTION: Non-structural protein 4A: Regulates the ATPase activity
of the NS3 helicase activity. NS4A allows NS3 helicase to conserve
energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}.
-!- FUNCTION: Peptide 2k: Functions as a signal peptide for NS4B and
is required for the interferon antagonism activity of the latter.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Non-structural protein 4B: Induces the formation of ER-
derived membrane vesicles where the viral replication takes place.
Inhibits interferon (IFN)-induced host STAT1 phosphorylation and
nuclear translocation, thereby preventing the establishment of
cellular antiviral state by blocking the IFN-alpha/beta pathway.
{ECO:0000250|UniProtKB:Q9Q6P4}.
-!- FUNCTION: RNA-directed RNA polymerase NS5: Replicates the viral
(+) and (-) RNA genome, and performs the capping of genomes in the
cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose
2'-O positions (By similarity). Besides its role in RNA genome
replication, also prevents the establishment of cellular antiviral
state by blocking the interferon-alpha/beta (IFN-alpha/beta)
signaling pathway. IFN-I induces binding of NS5 to host IFN-
activated transcription factor STAT2, preventing its
transcriptional activity. Host TRIM23 is the E3 ligase that
interacts with and polyubiquitinates NS5 to promote its binding to
STAT2 and trigger IFN-I signaling inhibition.
{ECO:0000250|UniProtKB:P03314}.
-!- CATALYTIC ACTIVITY: Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds
in which each of the Xaa can be either Arg or Lys and Yaa can be
either Ser or Ala.
-!- 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.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S-
adenosyl-L-homocysteine + m(7)G(5')pppR-RNA. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + a 5'-(N(7)-methyl
5'-triphosphoguanosine)-(purine-ribonucleotide)-[mRNA] = S-
adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-
triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-[mRNA].
{ECO:0000255|PROSITE-ProRule:PRU00924}.
-!- SUBUNIT: Capsid protein C: Homodimer. Interacts (via N-terminus)
with host EXOC1 (via C-terminus); this interaction results in
EXOC1 degradation through the proteasome degradation pathway.
Protein prM: Forms heterodimers with envelope protein E in the
endoplasmic reticulum and Golgi. Envelope protein E: Homodimer; in
the endoplasmic reticulum and Golgi. Interacts with protein prM.
Interacts with non-structural protein 1. Non-structural protein 1:
Homodimer; Homohexamer when secreted. Interacts with envelope
protein E. Non-structural protein 2A: Interacts (via N-terminus)
with serine protease NS3. Non-structural protein 2B: Forms a
heterodimer with serine protease NS3. May form homooligomers.
Serine protease NS3: Forms a heterodimer with NS2B. Interacts with
non-structural protein 2A (via N-terminus). Interacts with NS4B.
Interacts with unphosphorylated RNA-directed RNA polymerase NS5;
this interaction stimulates RNA-directed RNA polymerase NS5
guanylyltransferase activity. NS3 interacts with host PDCD6IP;
this interaction contributes to virion release. Non-structural
protein 4B: Interacts with serine protease NS3. RNA-directed RNA
polymerase NS5: Homodimer. Interacts with host STAT2; this
interaction prevents the establishment of cellular antiviral
state. Interacts with host TRIM23; this interaction leads to NS5
ubiquitination. {ECO:0000250|UniProtKB:P03314}.
-!- SUBCELLULAR LOCATION: Capsid protein C: Virion
{ECO:0000250|UniProtKB:P17763}. Host nucleus
{ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear
region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Peptide pr: Secreted
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Small envelope protein M: Virion membrane
{ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum
membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane
protein {ECO:0000255}. Note=ER membrane retention is mediated by
the transmembrane domains. {ECO:0000250|UniProtKB:P03314}.
-!- SUBCELLULAR LOCATION: Envelope protein E: Virion membrane
{ECO:0000305}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum
membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane
protein {ECO:0000255}. Note=ER membrane retention is mediated by
the transmembrane domains. {ECO:0000250|UniProtKB:P03314}.
-!- SUBCELLULAR LOCATION: Non-structural protein 1: Secreted
{ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum
membrane; Peripheral membrane protein; Lumenal side
{ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived
vesicles hosting the replication complex.
{ECO:0000250|UniProtKB:Q9Q6P4}.
-!- SUBCELLULAR LOCATION: Non-structural protein 2A: Host endoplasmic
reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass
membrane protein {ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Serine protease subunit NS2B: Host
endoplasmic reticulum membrane; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Serine protease NS3: Host endoplasmic
reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860};
Peripheral membrane protein {ECO:0000255|PROSITE-
ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-
ProRule:PRU00860}. Note=Remains non-covalently associated to
serine protease subunit NS2B. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
-!- SUBCELLULAR LOCATION: Non-structural protein 4A: Host endoplasmic
reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass
membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in
RE-associated vesicles hosting the replication complex.
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Non-structural protein 4B: Host endoplasmic
reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass
membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in
RE-derived vesicles hosting the replication complex.
{ECO:0000250|UniProtKB:Q9Q6P4}.
-!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase NS5: Host
endoplasmic reticulum membrane; Peripheral membrane protein;
Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P17763}.
Note=Located in RE-associated vesicles hosting the replication
complex. NS5 protein is mainly localized in the nucleus rather
than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
-!- DOMAIN: The transmembrane domains of the small envelope protein M
and envelope protein E contain an endoplasmic reticulum retention
signal. {ECO:0000250|UniProtKB:P17763}.
-!- PTM: Genome polyprotein: Specific enzymatic cleavages in vivo
yield mature proteins. The nascent capsid protein C contains a C-
terminal hydrophobic domain that act as a signal sequence for
translocation of prM into the lumen of the ER. Mature capsid
protein C is cleaved at a site upstream of this hydrophobic domain
by NS3. prM is cleaved in post-Golgi vesicles by a host furin,
releasing the mature small envelope protein M, and peptide pr.
Non-structural protein 2A-alpha, a C-terminally truncated form of
non-structural protein 2A, results from partial cleavage by NS3.
Specific enzymatic cleavages in vivo yield mature proteins peptide
2K acts as a signal sequence and is removed from the N-terminus of
NS4B by the host signal peptidase in the ER lumen. Signal cleavage
at the 2K-4B site requires a prior NS3 protease-mediated cleavage
at the 4A-2K site. {ECO:0000250|UniProtKB:P03314}.
-!- PTM: Protein prM: Cleaved in post-Golgi vesicles by a host furin,
releasing the mature small envelope protein M, and peptide pr.
This cleavage is incomplete as up to 30% of viral particles still
carry uncleaved prM. {ECO:0000250|UniProtKB:P17763}.
-!- PTM: Envelope protein E: N-glycosylated.
{ECO:0000250|UniProtKB:P17763}.
-!- PTM: Non-structural protein 1: N-glycosylated. The excreted form
is glycosylated and this is required for efficient secretion of
the protein from infected cells. {ECO:0000250|UniProtKB:P17763}.
-!- PTM: Polyubiquitinated; ubiquitination is probably mediated by
host TRIM23 and is prerequisite for NS5-STAT2 interaction. NS5 is
not ISGylated or sumoylated. {ECO:0000250|UniProtKB:P03314}.
-!- PTM: RNA-directed RNA polymerase NS5: Phosphorylated on serines
residues. This phosphorylation may trigger NS5 nuclear
localization. {ECO:0000250|UniProtKB:P17763}.
-!- SIMILARITY: In the N-terminal section; belongs to the class I-like
SAM-binding methyltransferase superfamily. mRNA cap 0-1 NS5-type
methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU00924}.
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EMBL; U21056; AAA99713.1; -; Genomic_RNA.
EMBL; AY640589; AAT58050.1; -; Genomic_RNA.
PDB; 2JQM; NMR; -; A=573-683.
PDB; 2JV6; NMR; -; A=573-683.
PDBsum; 2JQM; -.
PDBsum; 2JV6; -.
ProteinModelPortal; Q6DV88; -.
SMR; Q6DV88; -.
PRIDE; Q6DV88; -.
OrthoDB; VOG0900007N; -.
EvolutionaryTrace; Q6DV88; -.
Proteomes; UP000008603; Genome.
Proteomes; UP000174416; Genome.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0044167; C:host cell endoplasmic reticulum 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; 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:0003725; F:double-stranded RNA binding; IEA:InterPro.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
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:0005198; F:structural molecule activity; 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:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0039564; P:suppression by virus of host STAT2 activity; IEA:UniProtKB-KW.
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:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
CDD; cd12149; Flavi_E_C; 1.
CDD; cd00079; HELICc; 1.
CDD; cd06174; MFS; 1.
Gene3D; 1.10.8.970; -; 1.
Gene3D; 1.20.1280.260; -; 1.
Gene3D; 2.60.260.50; -; 1.
Gene3D; 2.60.40.350; -; 1.
Gene3D; 2.60.98.10; -; 3.
Gene3D; 3.30.387.10; -; 2.
Gene3D; 3.30.67.10; -; 4.
InterPro; IPR011492; DEAD_Flavivir.
InterPro; IPR000069; Env_glycoprot_M_flavivir.
InterPro; IPR038302; Env_glycoprot_M_sf_flavivir.
InterPro; IPR013755; Flav_gly_cen_dom_subdom1.
InterPro; IPR001122; Flavi_capsidC.
InterPro; IPR027287; Flavi_E_Ig-like.
InterPro; IPR026470; Flavi_E_Stem/Anchor_dom.
InterPro; IPR038345; Flavi_E_Stem/Anchor_dom_sf.
InterPro; IPR001157; Flavi_NS1.
InterPro; IPR000752; Flavi_NS2A.
InterPro; IPR000487; Flavi_NS2B.
InterPro; IPR000404; Flavi_NS4A.
InterPro; IPR001528; Flavi_NS4B.
InterPro; IPR002535; Flavi_propep.
InterPro; IPR038688; Flavi_propep_sf.
InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
InterPro; IPR001850; Flavivirus_NS3_S7.
InterPro; IPR014412; Gen_Poly_FLV.
InterPro; IPR011998; Glycoprot_cen/dimer.
InterPro; IPR036253; Glycoprot_cen/dimer_sf.
InterPro; IPR038055; Glycoprot_E_dimer_dom.
InterPro; IPR013756; GlyE_cen_dom_subdom2.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR020846; MFS_dom.
InterPro; IPR026490; mRNA_cap_0/1_MeTrfase.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR000208; RNA-dir_pol_flavivirus.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom.
InterPro; IPR029063; SAM-dependent_MTases.
Pfam; PF01003; Flavi_capsid; 1.
Pfam; PF07652; Flavi_DEAD; 1.
Pfam; PF02832; Flavi_glycop_C; 1.
Pfam; PF00869; Flavi_glycoprot; 1.
Pfam; PF01004; Flavi_M; 1.
Pfam; PF00948; Flavi_NS1; 1.
Pfam; PF01005; Flavi_NS2A; 1.
Pfam; PF01002; Flavi_NS2B; 1.
Pfam; PF01350; Flavi_NS4A; 1.
Pfam; PF01349; Flavi_NS4B; 1.
Pfam; PF00972; Flavi_NS5; 1.
Pfam; PF01570; Flavi_propep; 1.
Pfam; PF01728; FtsJ; 1.
Pfam; PF00949; Peptidase_S7; 1.
PIRSF; PIRSF003817; Gen_Poly_FLV; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF53335; SSF53335; 1.
SUPFAM; SSF56983; SSF56983; 1.
SUPFAM; SSF81296; SSF81296; 1.
TIGRFAMs; TIGR04240; flavi_E_stem; 1.
PROSITE; PS51527; FLAVIVIRUS_NS2B; 1.
PROSITE; PS51528; FLAVIVIRUS_NS3PRO; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS51591; RNA_CAP01_NS5_MT; 1.
1: Evidence at protein level;
3D-structure; Activation of host autophagy by virus; ATP-binding;
Capsid protein; Clathrin-mediated endocytosis of virus by host;
Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane; Glycoprotein;
GTP-binding; Helicase; Host cytoplasm; Host endoplasmic reticulum;
Host membrane; 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 STAT2 by virus; Membrane; Metal-binding;
Methyltransferase; mRNA capping; mRNA processing;
Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase;
Phosphoprotein; Protease; RNA-binding; RNA-directed RNA polymerase;
S-adenosyl-L-methionine; Secreted; Serine protease;
Suppressor of RNA silencing; Transcription; Transcription regulation;
Transferase; Transmembrane; Transmembrane helix; Ubl conjugation;
Viral attachment to host cell; Viral envelope protein;
Viral immunoevasion; Viral penetration into host cytoplasm;
Viral RNA replication; Virion; Virus endocytosis by host;
Virus entry into host cell; Zinc.
CHAIN 1 3411 Genome polyprotein.
/FTId=PRO_0000405155.
CHAIN 1 101 Capsid protein C.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000261455.
PROPEP 102 121 ER anchor for the capsid protein C,
removed in mature form by serine protease
NS3. {ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000261456.
CHAIN 122 285 Protein prM.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000261457.
CHAIN 122 210 Peptide pr.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000261458.
CHAIN 211 285 Small envelope protein M.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000261459.
CHAIN 286 778 Envelope protein E.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000261460.
CHAIN 779 1130 Non-structural protein 1.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000261461.
CHAIN 1131 1354 Non-structural protein 2A.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000261462.
CHAIN 1131 1320 Non-structural protein 2A-alpha.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000261463.
CHAIN 1355 1484 Serine protease subunit NS2B.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000261464.
CHAIN 1485 2107 Serine protease NS3.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000261465.
CHAIN 2108 2233 Non-structural protein 4A.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000261466.
PEPTIDE 2234 2256 Peptide 2k.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000261467.
CHAIN 2257 2506 Non-structural protein 4B.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000261468.
CHAIN 2507 3411 RNA-directed RNA polymerase NS5.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000261469.
TOPO_DOM 1 104 Cytoplasmic. {ECO:0000255}.
TRANSMEM 105 125 Helical. {ECO:0000255}.
TOPO_DOM 126 244 Extracellular. {ECO:0000255}.
TRANSMEM 245 265 Helical. {ECO:0000255}.
TOPO_DOM 266 270 Cytoplasmic. {ECO:0000255}.
TRANSMEM 271 285 Helical. {ECO:0000305}.
TOPO_DOM 286 730 Extracellular. {ECO:0000255}.
TRANSMEM 731 751 Helical. {ECO:0000255}.
TOPO_DOM 752 757 Extracellular. {ECO:0000255}.
TRANSMEM 758 778 Helical. {ECO:0000250|UniProtKB:P03314}.
TOPO_DOM 779 1132 Extracellular.
{ECO:0000250|UniProtKB:P03314}.
TRANSMEM 1133 1153 Helical. {ECO:0000250|UniProtKB:P03314}.
TOPO_DOM 1154 1201 Cytoplasmic.
{ECO:0000250|UniProtKB:P03314}.
TRANSMEM 1202 1222 Helical. {ECO:0000250|UniProtKB:P03314}.
TOPO_DOM 1223 1287 Lumenal. {ECO:0000250|UniProtKB:P03314}.
TRANSMEM 1288 1308 Helical. {ECO:0000250|UniProtKB:P03314}.
TOPO_DOM 1309 1355 Cytoplasmic.
{ECO:0000250|UniProtKB:P03314}.
TRANSMEM 1356 1376 Helical. {ECO:0000250|UniProtKB:P03314}.
TOPO_DOM 1377 1378 Lumenal. {ECO:0000250|UniProtKB:P03314}.
TRANSMEM 1379 1399 Helical. {ECO:0000255}.
TOPO_DOM 1400 1456 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1457 1477 Helical. {ECO:0000255}.
TOPO_DOM 1478 2157 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2158 2178 Helical. {ECO:0000255}.
TOPO_DOM 2179 2186 Lumenal. {ECO:0000255}.
INTRAMEM 2187 2207 Helical. {ECO:0000255}.
TOPO_DOM 2208 2209 Lumenal. {ECO:0000255}.
TRANSMEM 2210 2230 Helical. {ECO:0000255}.
TOPO_DOM 2231 2241 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2242 2262 Helical; Note=Signal for NS4B.
{ECO:0000255}.
TOPO_DOM 2263 2293 Lumenal. {ECO:0000255}.
INTRAMEM 2294 2314 Helical. {ECO:0000255}.
TOPO_DOM 2315 2360 Lumenal. {ECO:0000255}.
TRANSMEM 2361 2380 Helical. {ECO:0000255}.
TOPO_DOM 2381 2421 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2422 2442 Helical. {ECO:0000255}.
TOPO_DOM 2443 2445 Lumenal. {ECO:0000255}.
TRANSMEM 2446 2466 Helical. {ECO:0000255}.
TOPO_DOM 2467 3411 Cytoplasmic. {ECO:0000255}.
DOMAIN 1485 1665 Peptidase S7. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
DOMAIN 1669 1825 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 1820 1997 Helicase C-terminal.
DOMAIN 2507 2771 mRNA cap 0-1 NS5-type MT.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
DOMAIN 3035 3187 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1682 1689 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
REGION 38 72 Hydrophobic; homodimerization of capsid
protein C.
{ECO:0000250|UniProtKB:P29990}.
REGION 383 396 Fusion peptide.
{ECO:0000250|UniProtKB:P14336}.
REGION 1407 1446 Interacts with and activates NS3
protease. {ECO:0000255|PROSITE-
ProRule:PRU00859}.
REGION 1673 1676 Important for RNA-binding.
{ECO:0000250|UniProtKB:P14340}.
MOTIF 1773 1776 DEAH box. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
MOTIF 2878 2911 Nuclear localization signal.
{ECO:0000250}.
COMPBIAS 2656 2660 Poly-Ser.
ACT_SITE 1537 1537 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1561 1561 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1622 1622 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 2567 2567 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2652 2652 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2688 2688 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2724 2724 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
METAL 2945 2945 Zinc 1. {ECO:0000250|UniProtKB:P14335}.
METAL 2949 2949 Zinc 1; via tele nitrogen.
{ECO:0000250|UniProtKB:P14335}.
METAL 2954 2954 Zinc 1. {ECO:0000250|UniProtKB:P14335}.
METAL 2957 2957 Zinc 1. {ECO:0000250|UniProtKB:P14335}.
METAL 3222 3222 Zinc 2; via tele nitrogen.
{ECO:0000250|UniProtKB:P14335}.
METAL 3238 3238 Zinc 2. {ECO:0000250|UniProtKB:P14335}.
METAL 3357 3357 Zinc 2. {ECO:0000250|UniProtKB:P14335}.
BINDING 2519 2519 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2522 2522 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2523 2523 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2525 2525 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2534 2534 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2562 2562 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2592 2592 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2593 2593 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2610 2610 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2611 2611 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2637 2637 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2638 2638 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2656 2656 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2719 2719 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2721 2721 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2726 2726 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 101 102 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P03314}.
SITE 121 122 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P03314}.
SITE 210 211 Cleavage; by host furin.
{ECO:0000250|UniProtKB:P29990}.
SITE 285 286 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P29990}.
SITE 778 779 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P03314}.
SITE 1130 1131 Cleavage; by host.
{ECO:0000250|UniProtKB:P29990}.
SITE 1354 1355 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P29990}.
SITE 1484 1485 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:P03314}.
SITE 1945 1945 Involved in NS3 ATPase and RTPase
activities.
{ECO:0000250|UniProtKB:P14335}.
SITE 1948 1948 Involved in NS3 ATPase and RTPase
activities.
{ECO:0000250|UniProtKB:P14335}.
SITE 2107 2108 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:P03314}.
SITE 2233 2234 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P29990}.
SITE 2256 2257 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P29990}.
SITE 2506 2507 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P03314}.
SITE 2530 2530 mRNA cap binding. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2567 2567 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2652 2652 Essential for 2'-O-methyltransferase and
N-7 methyltransferase activity.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 2653 2653 S-adenosyl-L-methionine binding.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 2688 2688 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2724 2724 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
MOD_RES 2562 2562 Phosphoserine.
{ECO:0000250|UniProtKB:P03314}.
CARBOHYD 134 134 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 150 150 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 908 908 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 986 986 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 288 315 {ECO:0000250|UniProtKB:P17763}.
DISULFID 345 406 {ECO:0000250|UniProtKB:P17763}.
DISULFID 345 401 {ECO:0000250}.
DISULFID 359 390 {ECO:0000250|UniProtKB:P17763}.
DISULFID 377 406 {ECO:0000250}.
DISULFID 377 401 {ECO:0000250|UniProtKB:P17763}.
DISULFID 467 568 {ECO:0000250|UniProtKB:P17763}.
DISULFID 585 615
DISULFID 782 793 {ECO:0000250|UniProtKB:P17763}.
DISULFID 833 921 {ECO:0000250|UniProtKB:P17763}.
DISULFID 957 1002 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1058 1107 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1069 1091 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1090 1094 {ECO:0000250|UniProtKB:P17763}.
VARIANT 512 512 E -> G (in strain: Isolate Senegal/French
viscerotropic virus FVV/27).
VARIANT 616 616 K -> R (in strain: Isolate Senegal/French
viscerotropic virus FVV/27).
VARIANT 692 692 A -> V (in strain: Isolate Senegal/French
viscerotropic virus FVV/27).
VARIANT 1006 1006 L -> P (in strain: Isolate Senegal/French
viscerotropic virus FVV/27).
VARIANT 1509 1509 Y -> S (in strain: Isolate Senegal/French
viscerotropic virus FVV/27).
VARIANT 1764 1764 V -> I (in strain: Isolate Senegal/French
viscerotropic virus FVV/27).
VARIANT 2502 2502 K -> E (in strain: Isolate Senegal/French
viscerotropic virus FVV/27).
VARIANT 2508 2508 S -> R (in strain: Isolate Senegal/French
viscerotropic virus FVV/27).
TURN 578 580 {ECO:0000244|PDB:2JQM}.
STRAND 590 597 {ECO:0000244|PDB:2JQM}.
STRAND 599 601 {ECO:0000244|PDB:2JQM}.
STRAND 603 608 {ECO:0000244|PDB:2JQM}.
STRAND 619 624 {ECO:0000244|PDB:2JQM}.
STRAND 633 636 {ECO:0000244|PDB:2JQM}.
STRAND 640 643 {ECO:0000244|PDB:2JV6}.
STRAND 649 653 {ECO:0000244|PDB:2JQM}.
STRAND 656 663 {ECO:0000244|PDB:2JQM}.
STRAND 670 676 {ECO:0000244|PDB:2JQM}.
TURN 679 681 {ECO:0000244|PDB:2JQM}.
SEQUENCE 3411 AA; 379169 MW; 02230DA20066E9A3 CRC64;
MSGRKAQGKT LGVNMVRRGV RSLSNKIKQK TKQIGNRPGP SRGVQGFIFF FLFNILTGKK
ITAHLKRLWK MLDPRQGLAV LRKVKRVVAS LMRGLSSRKR RSHDVLTVQF LILGMLLMTG
GVTLVRKNRW LLLNVTSEDL GKTFSVGTGN CTTNILEAKY WCPDSMEYNC PNLSPREEPD
DIDCWCYGVE NVRVAYGKCD SAGRSRRSRR AIDLPTHENH GLKTRQEKWM TGRMGERQLQ
KIERWLVRNP FFAVTALTIA YLVGSNMTQR VVIALLVLAV GPAYSAHCIG ITDRDFIEGV
HGGTWVSATL EQDKCVTVMA PDKPSLDISL ETVAIDGPAE ARKVCYNAVL THVKINDKCP
STGEAHLAEE NEGDNACKRT YSDRGWGNGC GLFGKGSIVA CAKFTCAKSM SLFEVDQTKI
QYVIRAQLHV GAKQENWNTD IKTLKFDALS GSQEAEFTGY GKATLECQVQ TAVDFGNSYI
AEMEKESWIV DRQWAQDLTL PWQSGSGGVW REMHHLVEFE PPHAATIRVL ALGNQEGSLK
TALTGAMRVT KDTNDNNLYK LHGGHVSCRV KLSALTLKGT SYKMCTDKMS FVKNPTDTGH
GTVVMQVKVP KGAPCKIPVI VADDLTAAIN KGILVTVNPI ASTNDDEVLI EVNPPFGDSY
IIVGTGDSRL TYQWHKEGSS IGKLFTQTMK GAERLAVMGD AAWDFSSAGG FFTSVGKGIH
TVFGSAFQGL FGGLNWITKV IMGAVLIWVG INTRNMTMSM SMILVGVIMM FLSLGVGADQ
GCAINFGKRE LKCGDGIFIF RDSDDWLNKY SYYPEDPVKL ASIVKASFEE GKCGLNSVDS
LEHEMWRSRA DEINAILEEN EVDISVVVQD PKNVYQRGTH PFSRIRDGLQ YGWKTWGKNL
VFSPGRKNGS FIIDGKSRKE CPFSNRVWNS FQIEEFGTGV FTTRVYMDAV FEYTIDCDGS
ILGAAVNGKK SAHGSPTFWM GSHEVNGTWM IHTLEALDYK ECEWPLTHTI GTSVEESEMF
MPRSIGGPVS SHNHIPGYKV QTNGPWMQVP LEVKREACPG TSVIIDGNCD GRGKSTRSTT
DSGKIIPEWC CRSCTMPPVS FHGSDGCWYP MEIRPRKTHE SHLVRSWVTA GEIHAVPFGL
VSMMIAMEVV LRKRQGPKQM LVGGVVLLGA MLVGQVTLLD LLKLTVAVGL HFHEMNNGGD
AMYMALIAAF SIRPGLLIGF GLRTLWSPRE RLVLTLGAAM VEIALGGMMG GLWKYLNAVS
LCILTINAVA SRKASNTILP LMALLTPVTM AEVRLATMLF CTVVIIGVLH QNSKDTSMQK
TIPLVALTLT SYLGLTQPFL GLCAFLATRI FGRRSIPVNE ALAAAGLVGV LAGLAFQEME
NFLGPIAVGG ILMMLVSVAG RVDGLELKKL GEVSWEEEAE ISGSSARYDV ALSEQGEFKL
LSEEKVPWDQ VVMTSLALVG AAIHPFALLL VLAGWLFHVR GARRSGDVLW DIPTPKIIEE
CEHLEDGIYG IFQSTFLGAS QRGVGVAQGG VFHTMWHVTR GAFLVRNGKK LIPSWASVKE
DLVAYGGSWK LEGRWDGEEE VQLIAAVPGK NVVNVQTKPS LFKVRNGGEI GAVALDYPSG
TSGSPIVNRN GEVIGLYGNG ILVGDNSFVS AISQTEVKEE GKEELQEIPT MLKKGMTTIL
DFHPGAGKTR RFLPQILAEC ARRRLRTLVL APTRVVLSEM KEAFHGLDVK FHTQAFSAHG
SGREVIDAMC HATLTYRMLE PTRVVNWEVI IMDEAHFLDP ASIAARGWAA HRARANESAT
ILMTATPPGT SDEFPHSNGE IEDVQTDIPS EPWNTGHDWI LADKRPTAWF LPSIRAANVM
AASLRKAGKS VVVLNRKTFE REYPTIKQKK PDFILATDIA EMGANLCVER VLDCRTAFKP
VLVDEGRKVA IKGPLRISAS SAAQRRGRIG RNPNRDGDSY YYSEPTSEDN AHHVCWLEAS
MLLDNMEVRG GMVAPLYGVE GTKTPVSPGE MRLRDDQRKV FRELVRNCDL PVWLSWQVAK
AGLKTNDRKW CFEGPEEHEI LNDSGETVKC RAPGGAKKPL RPRWCDERVS SDQSALSEFI
KFAEGRRGAA EVLVVLSELP DFLAKKGGEA MDTISVFLHS EEGSRAYRNA LSMMPEAMTI
VMLFILAGLL TSGMVIFFMS PKGISRMSMA MGTMAGCGYL MFLGGVKPTH ISYIMLIFFV
LMVVVIPEPG QQRSIQDNQV AYLIIGILTL VSVVAANELG MLEKTKEDLF GKKNLIPSSA
SPWSWPDLDL KPGAAWTVYV GIVTMLSPML HHWIKVEYGN LSLSGIAQSA SVLSFMDKGI
PFMKMNISVI ILLVSGWNSI TVMPLLCGIG CAMLHWSLIL PGIKAQQSKL AQRRVFHGVA
KNPVVDGNPT VDIEEAPEMP ALYEKKLALY LLLALSLASV AMCRTPFSLA EGIVLASAAL
GPLIEGNTSL LWNGPMAVSM TGVMRGNYYA FVGVMYNLWK MKTGRRGSAN GKTLGEVWKR
ELNLLDKQQF ELYKRTDIVE VDRDTARRHL AEGKVDTGVA VSRGTAKLRW FHERGYVKLE
GRVIDLGCGR GGWCYYAAAQ KEVSGVKGFT LGRDGHEKPM NVQSLGWNII TFKDKTDIHR
LEPVKCDTLL CDIGESSSSS VTEGERTVRV LDTVEKWLAC GVDNFCVKVL APYMPDVLEK
LELLQRRFGG TVIRNPLSRN STHEMYYVSG ARSNVTFTVN QTSRLLMRRM RRPTGKVTLE
ADVILPIGTR SVETDKGPLD KEAIEERVER IKSEYMTSWF YDNDNPYRTW HYCGSYVTKT
SGSAASMVNG VIKILTYPWD RIEEVTRMAM TDTTPFGQQR VFKEKVDTRA KDPPAGTRKI
MKVVNRWLFR HLAREKNPRL CTKEEFIAKV RSHAAIGAYL EEQEQWKTAN EAVQDPKFWE
LVDEERKLHQ QGRCRTCVYN MMGKREKKLS EFGKAKGSRA IWYMWLGARY LEFEALGFLN
EDHWASRENS GGGVEGIGLQ YLGYVIRDLA AMDGGGFYAD DTAGWDTRIT EADLDDEQEI
LNYMSPHHKK LAQAVMEMTY KNKVVKVLRP APGGKAYMDV ISRRDQRGSG QVVTYALNTI
TNLKVQLIRM AEAEMVIHHQ HVQDCDESVL TRLEAWLTEH GCNRLKRMAV SGDDCVVRPI
DDRFGLALSH LNAMSKVRKD ISEWQPSKGW NDWENVPFCS HHFHELQLKD GRRIVVPCRE
QDELIGRGRV SPGNGWMIKE TACLSKAYAN MWSLMYFHKR DMRLLSLAVS SAVPTSWVPQ
GRTTWSIHGK GEWMTTEDML EVWNRVWITN NPHMQDKTMV KEWRDVPYLT KRQDKLCGSL
IGMTNRATWA SHIHLVIHRI RTLIGQEKYT DYLTVMDRYS VDADLQPGEL I


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EIAAB38761 CAPE,Chromosome-associated protein E,hCAP-E,Homo sapiens,Human,PRO0324,SMC protein 2,SMC2,SMC-2,SMC2L1,Structural maintenance of chromosomes protein 2,XCAP-E homolog
EIAAB38770 Kiaa0594,MLZ-453,Mouse,mSMC5,Mus musculus,Protein expressed in male leptotene and zygotene spermatocytes 453,SMC protein 5,Smc5,SMC-5,Smc5l1,Structural maintenance of chromosomes protein 5
OBT1774 SMC2 (Structural Maintenance of Chromosomes 2), SMC2L1 (Structural Maintenance of Chromosomes 2_like 1), CAPE, CAP_E, hCAP_E (Human Chromosome _Associated Protein E), Rabbit anti_Human, Mouse; WB_IP_I 0.1 mg.
OBT1774 SMC2 (Structural Maintenance of Chromosomes 2), SMC2L1 (Structural Maintenance of Chromosomes 2_like 1), CAPE, CAP_E, hCAP_E (Human Chromosome _Associated Protein E), Rabbit anti_Human, Mouse; WB_IP_I 0.1 mg.
EIAAB38756 DXS423E,Homo sapiens,Human,KIAA0178,Sb1.8,SB1.8,SMC protein 1A,SMC1,SMC1A,SMC-1A,SMC-1-alpha,SMC1L1,Structural maintenance of chromosomes protein 1A
29-258 Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structural 0.1 mg
29-220 Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structural 0.1 mg
29-222 Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structural 0.05 mg
29-259 Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structural 0.1 mg


 

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