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MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | RecName: Full=Genome polyprotein; Contains: RecName: Full=Capsid protein C; AltName: Full=Core protein; Contains: RecName: Full=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; EC=3.6.4.13; 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; EC=2.1.1.57; EC=2.7.7.48; AltName: Full=Non-structural protein 5; |
 |
|
| MyHits synonyms | POLG_YEFVN , Q1X881 , DA9310F26DE41B95 |
 Legends: 1, TOPO_DOM Lumenal. {ECO:0000255}; 2, ACT_SITE Charge relay system; for serine protease NS3 activity. {ECO:0000255|PROSITE- ProRule:PRU00860}; 3, BINDING mRNA cap. {ECO:0000255|PROSITE- ProRule:PRU00924}; 4, BINDING mRNA cap; via carbonyl oxygen. {ECO:0000255|PROSITE-ProRule:PRU00924}; 5, BINDING S-adenosyl-L-methionine. {ECO:0000255|PROSITE-ProRule:PRU00924}; 6, BINDING S-adenosyl-L-methionine; via carbonyl oxygen. {ECO:0000255|PROSITE- ProRule:PRU00924}; 7, SITE mRNA cap binding. {ECO:0000255|PROSITE- ProRule:PRU00924}; 8, SITE Essential for 2'-O-methyltransferase activity. {ECO:0000255|PROSITE- ProRule:PRU00924}; 9, SITE Essential for 2'-O-methyltransferase and N-7 methyltransferase activity. {ECO:0000255|PROSITE-ProRule:PRU00924}; 10, SITE S-adenosyl-L-methionine binding. {ECO:0000255|PROSITE-ProRule:PRU00924}; 11, N-linked (GlcNAc...); by host. {ECO:0000255}; 12, CHAIN Capsid protein C. {ECO:0000250}; 13, PROPEP ER anchor for the protein C, removed in mature form by serine protease NS3; 14, CHAIN prM. {ECO:0000250}; 15, CHAIN Peptide pr. {ECO:0000250}; 16, CHAIN Small envelope protein M. {ECO:0000250}; 17, CHAIN Envelope protein E. {ECO:0000250}; 18, CHAIN Non-structural protein 1. {ECO:0000250}; 19, CHAIN Non-structural protein 2A. {ECO:0000250}; 20, CHAIN Non-structural protein 2A-alpha. {ECO:0000250}; 21, CHAIN Serine protease subunit NS2B. {ECO:0000250}; 22, CHAIN Serine protease NS3. {ECO:0000250}; 23, CHAIN Non-structural protein 4A. {ECO:0000250}; 24, PEPTIDE Peptide 2k; 25, CHAIN Non-structural protein 4B. {ECO:0000250}; 26, CHAIN RNA-directed RNA polymerase NS5. {ECO:0000250}; 27, TOPO_DOM Cytoplasmic. {ECO:0000255}; 28, TRANSMEM Helical. {ECO:0000255}; 29, TOPO_DOM Extracellular. {ECO:0000255}; 30, INTRAMEM Helical. {ECO:0000255}; 31, TRANSMEM Helical; Note=Signal for NS4B. {ECO:0000255}; 32, Peptidase S7. {ECO:0000255|PROSITE- ProRule:PRU00860}; 33, Helicase ATP-binding. {ECO:0000255|PROSITE-ProRule:PRU00541}; 34, Helicase C-terminal. {ECO:0000255|PROSITE-ProRule:PRU00542}; 35, mRNA cap 0-1 NS5-type MT. {ECO:0000255|PROSITE-ProRule:PRU00924}; 36, RdRp catalytic. {ECO:0000255|PROSITE- ProRule:PRU00539}; 37, NP_BIND ATP. {ECO:0000255|PROSITE- ProRule:PRU00541}; 38, REGION Hydrophobic; homodimerization of capsid protein C. {ECO:0000250}; 39, REGION Involved in fusion. {ECO:0000250}; 40, REGION Interacts with and activates NS3 protease. {ECO:0000255|PROSITE- ProRule:PRU00859}; 41, MOTIF DEAH box; 42, MOTIF Nuclear localization signal. {ECO:0000250}; 43, SITE Cleavage; by viral protease NS3. {ECO:0000255}; 44, SITE Cleavage; by host signal peptidase. {ECO:0000250}; 45, SITE Cleavage; by host furin. {ECO:0000255}; 46, SITE Cleavage; by host signal peptidase. {ECO:0000255}; 47, SITE Cleavage; by host. {ECO:0000255}; 48, SITE Cleavage; by autolysis. {ECO:0000255}; 49, ipfam:Flavi_DEAD [T]; 50, ismart:DEXDc [T]; 51, iprf:RDRP_SSRNA_POS [T]; 52, ipfam:Flavi_glycoprot [T]; 53, ipfam:Flavi_NS4B [T]; 54, iprf:RNA_CAP01_NS5_MT [T]; 55, ipfam:Flavi_glycop_C [T]; 56, ipfam:Peptidase_S7 [T]; 57, ipfam:Flavi_NS1 [T]; 58, ipfam:Flavi_NS4A [T]; 59, iprf:FLAVIVIRUS_NS3PRO [T]; 60, ipfam:Flavi_capsid [T]; 61, iprf:FLAVIVIRUS_NS2B [T]; 62, iprf:HELICASE_CTER [T]; 63, ipfam:Flavi_NS2A [T]; 64, ipfam:Flavi_NS2B [T]; 65, ipfam:Flavi_propep [T]; 66, ismart:HELICc [T]; 67, iprf:HELICASE_ATP_BIND_1 [T]; 68, ipfam:Flavi_M [T]; 69, ipfam:FtsJ [T].
| |
ID POLG_YEFVN Reviewed; 3412 AA.
AC Q1X881;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 02-NOV-2016, entry version 88.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=Capsid protein C;
DE AltName: Full=Core protein;
DE Contains:
DE RecName: Full=prM;
DE Contains:
DE RecName: Full=Peptide pr;
DE Contains:
DE RecName: Full=Small envelope protein M;
DE AltName: Full=Matrix protein;
DE Contains:
DE RecName: Full=Envelope protein E;
DE Contains:
DE RecName: Full=Non-structural protein 1;
DE Short=NS1;
DE Contains:
DE RecName: Full=Non-structural protein 2A;
DE Short=NS2A;
DE Contains:
DE RecName: Full=Non-structural protein 2A-alpha;
DE Short=NS2A-alpha;
DE Contains:
DE RecName: Full=Serine protease subunit NS2B;
DE AltName: Full=Flavivirin protease NS2B regulatory subunit;
DE AltName: Full=Non-structural protein 2B;
DE Contains:
DE RecName: Full=Serine protease NS3;
DE EC=3.4.21.91;
DE EC=3.6.1.15;
DE EC=3.6.4.13;
DE AltName: Full=Flavivirin protease NS3 catalytic subunit;
DE AltName: Full=Non-structural protein 3;
DE Contains:
DE RecName: Full=Non-structural protein 4A;
DE Short=NS4A;
DE Contains:
DE RecName: Full=Peptide 2k;
DE Contains:
DE RecName: Full=Non-structural protein 4B;
DE Short=NS4B;
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase NS5;
DE EC=2.1.1.56;
DE EC=2.1.1.57;
DE EC=2.7.7.48;
DE AltName: Full=Non-structural protein 5;
OS Yellow fever virus (isolate Angola/14FA/1971) (YFV).
OC Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
OC Flaviviridae; Flavivirus; Yellow fever virus group.
OX NCBI_TaxID=407140;
OH NCBI_TaxID=7159; Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OH NCBI_TaxID=299629; Aedes luteocephalus (Mosquito).
OH NCBI_TaxID=7161; Aedes simpsoni.
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=314293; Simiiformes.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16528039; DOI=10.1099/vir.0.81236-0;
RA von Lindern J.J., Aroner S., Barrett N.D., Wicker J.A., Davis C.T.,
RA Barrett A.D.;
RT "Genome analysis and phylogenetic relationships between east, central
RT and west African isolates of Yellow fever virus.";
RL J. Gen. Virol. 87:895-907(2006).
CC -!- FUNCTION: Capsid protein C self-assembles to form an icosahedral
CC capsid about 30 nm in diameter. The capsid encapsulates the
CC genomic RNA. {ECO:0000250}.
CC -!- FUNCTION: prM acts as a chaperone for envelope protein E during
CC intracellular virion assembly by masking and inactivating envelope
CC protein E fusion peptide. prM is matured in the last step of
CC virion assembly, presumably to avoid catastrophic activation of
CC the viral fusion peptide induced by the acidic pH of the trans-
CC Golgi network. After cleavage by host furin, the pr peptide is
CC released in the extracellular medium and small envelope protein M
CC and envelope protein E homodimers are dissociated. {ECO:0000250}.
CC -!- FUNCTION: Envelope protein E binding to host cell surface receptor
CC is followed by virus internalization through clathrin-mediated
CC endocytosis. Envelope protein E is subsequently involved in
CC membrane fusion between virion and host late endosomes.
CC Synthesized as a homodimer with prM which acts as a chaperone for
CC envelope protein E. After cleavage of prM, envelope protein E
CC dissociate from small envelope protein M and homodimerizes.
CC {ECO:0000250}.
CC -!- FUNCTION: Non-structural protein 1 is involved in virus
CC replication and regulation of the innate immune response.
CC {ECO:0000250}.
CC -!- FUNCTION: Non-structural protein 2A may be involved viral RNA
CC replication and capsid assembly. {ECO:0000305}.
CC -!- FUNCTION: Non-structural protein 2B is a required cofactor for the
CC serine protease function of NS3. {ECO:0000255|PROSITE-
CC ProRule:PRU00859}.
CC -!- FUNCTION: Serine protease NS3 displays three enzymatic activities:
CC serine protease, NTPase and RNA helicase. NS3 serine protease, in
CC association with NS2B, performs its autocleavage and cleaves the
CC polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B,
CC NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds
CC RNA and unwinds dsRNA in the 3' to 5' direction (By similarity).
CC {ECO:0000255|PROSITE-ProRule:PRU00860}.
CC -!- FUNCTION: Non-structural protein 4A induces host endoplasmic
CC reticulum membrane rearrangements leading to the formation of
CC virus-induced membranous vesicles hosting the dsRNA and
CC polymerase, functioning as a replication complex. NS4A might also
CC regulate the ATPase activity of the NS3 helicase. {ECO:0000250}.
CC -!- FUNCTION: Peptide 2k functions as a signal peptide for NS4B and is
CC required for the interferon antagonism activity of the latter.
CC {ECO:0000250}.
CC -!- FUNCTION: Non-structural protein 4B inhibits interferon (IFN)-
CC induced host STAT1 phosphorylation and nuclear translocation,
CC thereby preventing the establishment of cellular antiviral state
CC by blocking the IFN-alpha/beta pathway. {ECO:0000250}.
CC -!- FUNCTION: RNA-directed RNA polymerase NS5 replicates the viral (+)
CC and (-) genome, and performs the capping of genomes in the
CC cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose
CC 2'-O positions. Besides its role in genome replication, also
CC prevents the establishment of cellular antiviral state by blocking
CC the interferon-alpha/beta (IFN-alpha/beta) signaling pathway (By
CC similarity). {ECO:0000255|PROSITE-ProRule:PRU00539}.
CC -!- CATALYTIC ACTIVITY: Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds
CC in which each of the Xaa can be either Arg or Lys and Yaa can be
CC either Ser or Ala.
CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
CC + RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
CC -!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S-
CC adenosyl-L-homocysteine + m(7)G(5')pppR-RNA. {ECO:0000255|PROSITE-
CC ProRule:PRU00924}.
CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + a 5'-(N(7)-methyl
CC 5'-triphosphoguanosine)-(purine-ribonucleotide)-[mRNA] = S-
CC adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-
CC triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-[mRNA].
CC -!- SUBUNIT: Capsid protein C forms homodimers. prM and envelope
CC protein E form heterodimers in the endoplasmic reticulum and
CC Golgi. In immature particles, there are 60 icosaedrally organized
CC trimeric spikes on the surface. Each spike consists of three
CC heterodimers of envelope protein M precursor (prM) and envelope
CC protein E. NS1 forms homodimers as well as homohexamers when
CC secreted. NS1 may interact with NS4A. NS3 and NS2B form a
CC heterodimer. NS3 is the catalytic subunit, whereas NS2B strongly
CC stimulates the latter, acting as a cofactor. In the absence of the
CC NS2B, NS3 protease is unfolded and inactive. NS3 interacts with
CC unphosphorylated NS5; this interaction stimulates NS5
CC guanylyltransferase activity. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Capsid protein C: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Peptide pr: Secreted {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Small envelope protein M: Virion membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host
CC endoplasmic reticulum membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00860}; Multi-pass membrane protein {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Envelope protein E: Virion membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host
CC endoplasmic reticulum membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00860}; Multi-pass membrane protein {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Non-structural protein 1: Secreted. Host
CC endoplasmic reticulum membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00860}; Peripheral membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU00860}; Lumenal side
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Non-structural protein 2A-alpha: Host
CC endoplasmic reticulum membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00860}; Multi-pass membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Non-structural protein 2A: Host endoplasmic
CC reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Multi-
CC pass membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Serine protease subunit NS2B: Host
CC endoplasmic reticulum membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00860}; Peripheral membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side
CC {ECO:0000255|PROSITE-ProRule:PRU00860}.
CC -!- SUBCELLULAR LOCATION: Serine protease NS3: Host endoplasmic
CC reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860};
CC Peripheral membrane protein {ECO:0000255|PROSITE-
CC ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-
CC ProRule:PRU00860}. Note=Remains non-covalently associated to NS3
CC protease. {ECO:0000255|PROSITE-ProRule:PRU00860}.
CC -!- SUBCELLULAR LOCATION: Non-structural protein 4A: Host endoplasmic
CC reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Multi-
CC pass membrane protein {ECO:0000250}. Note=Located in RE-associated
CC vesicles hosting the replication complex.
CC -!- SUBCELLULAR LOCATION: Non-structural protein 4B: Host endoplasmic
CC reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Multi-
CC pass membrane protein {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase NS5: Host
CC endoplasmic reticulum membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00860}; Peripheral membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side
CC {ECO:0000255|PROSITE-ProRule:PRU00860}. Host nucleus
CC {ECO:0000250}. Note=Located in RE-associated vesicles hosting the
CC replication complex.
CC -!- DOMAIN: Transmembrane domains of the small envelope protein M and
CC envelope protein E contains an endoplasmic reticulum retention
CC signals. {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
CC The nascent protein C contains a C-terminal hydrophobic domain
CC that act as a signal sequence for translocation of prM into the
CC lumen of the ER. Mature protein C is cleaved at a site upstream of
CC this hydrophobic domain by NS3. prM is cleaved in post-Golgi
CC vesicles by a host furin, releasing the mature small envelope
CC protein M, and peptide pr. Non-structural protein 2A-alpha, a C-
CC terminally truncated form of non-structural protein 2A, results
CC from partial cleavage by NS3. Specific enzymatic cleavages in vivo
CC yield mature proteins Peptide 2K acts as a signal sequence and is
CC removed from the N-terminus of NS4B by the host signal peptidase
CC in the ER lumen. Signal cleavage at the 2K-4B site requires a
CC prior NS3 protease-mediated cleavage at the 4A-2K site.
CC {ECO:0000250}.
CC -!- PTM: RNA-directed RNA polymerase NS5 is phosphorylated on serines
CC residues. This phosphorylation may trigger NS5 nuclear
CC localization.
CC -!- PTM: Envelope protein E and non-structural protein 1 are N-
CC glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the class I-like
CC SAM-binding methyltransferase superfamily. mRNA cap 0-1 NS5-type
CC methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU00924}.
CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC {ECO:0000255|PROSITE-ProRule:PRU00541}.
CC -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC {ECO:0000255|PROSITE-ProRule:PRU00542}.
CC -!- SIMILARITY: Contains 1 mRNA cap 0-1 NS5-type MT domain.
CC {ECO:0000255|PROSITE-ProRule:PRU00924}.
CC -!- SIMILARITY: Contains 1 peptidase S7 domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00860}.
CC -!- SIMILARITY: Contains 1 RdRp catalytic domain.
CC {ECO:0000255|PROSITE-ProRule:PRU00539}.
DR EMBL; AY968064; AAY34247.1; -; Genomic_RNA.
DR ProteinModelPortal; Q1X881; -.
DR PRIDE; Q1X881; -.
DR Proteomes; UP000008607; Genome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0003968; F:RNA-directed RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0070008; F:serine-type exopeptidase activity; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR CDD; cd12149; Flavi_E_C; 1.
DR Gene3D; 2.60.40.350; -; 1.
DR Gene3D; 2.60.98.10; -; 2.
DR Gene3D; 3.30.387.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011492; DEAD_Flavivir.
DR InterPro; IPR000069; Env_glycoprot_M_flavivir.
DR InterPro; IPR013755; Flav_gly_cen_dom_subdom1.
DR InterPro; IPR001122; Flavi_capsidC.
DR InterPro; IPR027287; Flavi_E_Ig-like.
DR InterPro; IPR026470; Flavi_E_Stem/Anchor_dom.
DR InterPro; IPR001157; Flavi_NS1.
DR InterPro; IPR000752; Flavi_NS2A.
DR InterPro; IPR000487; Flavi_NS2B.
DR InterPro; IPR000404; Flavi_NS4A.
DR InterPro; IPR001528; Flavi_NS4B.
DR InterPro; IPR002535; Flavi_propep.
DR InterPro; IPR000336; Flavivir/Alphavir_Ig-like.
DR InterPro; IPR001850; Flavivirus_NS3_S7.
DR InterPro; IPR014412; Gen_Poly_FLV.
DR InterPro; IPR011998; Glycoprot_cen/dimer.
DR InterPro; IPR013754; GlyE_dim.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR026490; mRNA_cap_0/1_MeTrfase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR000208; RNA-dir_pol_flavivirus.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR029063; SAM-dependent_MTases.
DR Pfam; PF01003; Flavi_capsid; 1.
DR Pfam; PF07652; Flavi_DEAD; 1.
DR Pfam; PF02832; Flavi_glycop_C; 1.
DR Pfam; PF00869; Flavi_glycoprot; 1.
DR Pfam; PF01004; Flavi_M; 1.
DR Pfam; PF00948; Flavi_NS1; 1.
DR Pfam; PF01005; Flavi_NS2A; 1.
DR Pfam; PF01002; Flavi_NS2B; 1.
DR Pfam; PF01350; Flavi_NS4A; 1.
DR Pfam; PF01349; Flavi_NS4B; 1.
DR Pfam; PF00972; Flavi_NS5; 1.
DR Pfam; PF01570; Flavi_propep; 1.
DR Pfam; PF01728; FtsJ; 1.
DR Pfam; PF00949; Peptidase_S7; 1.
DR PIRSF; PIRSF003817; Gen_Poly_FLV; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF56983; SSF56983; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR TIGRFAMs; TIGR04240; flavi_E_stem; 1.
DR PROSITE; PS51527; FLAVIVIRUS_NS2B; 1.
DR PROSITE; PS51528; FLAVIVIRUS_NS3PRO; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS51591; RNA_CAP01_NS5_MT; 1.
PE 3: Inferred from homology;
KW Activation of host autophagy by virus; ATP-binding; Capsid protein;
KW Clathrin-mediated endocytosis of virus by host;
KW Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
KW Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein; Helicase;
KW Host endoplasmic reticulum; Host membrane; Host nucleus;
KW Host-virus interaction; Hydrolase;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host interferon signaling pathway by virus; Membrane;
KW Metal-binding; Methyltransferase; mRNA capping; mRNA processing;
KW Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase;
KW Phosphoprotein; Protease; RNA-binding; RNA-directed RNA polymerase;
KW S-adenosyl-L-methionine; Secreted; Serine protease; Transcription;
KW Transcription regulation; Transferase; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell;
KW Viral envelope protein; Viral immunoevasion;
KW Viral penetration into host cytoplasm; Viral RNA replication; Virion;
KW Virus endocytosis by host; Virus entry into host cell.
FT CHAIN 1 3412 Genome polyprotein.
FT /FTId=PRO_0000405161.
FT CHAIN 1 101 Capsid protein C. {ECO:0000250}.
FT /FTId=PRO_0000261545.
FT PROPEP 102 121 ER anchor for the protein C, removed in
FT mature form by serine protease NS3.
FT /FTId=PRO_0000261546.
FT CHAIN 122 285 prM. {ECO:0000250}.
FT /FTId=PRO_0000261547.
FT CHAIN 122 210 Peptide pr. {ECO:0000250}.
FT /FTId=PRO_0000261548.
FT CHAIN 211 285 Small envelope protein M. {ECO:0000250}.
FT /FTId=PRO_0000261549.
FT CHAIN 286 778 Envelope protein E. {ECO:0000250}.
FT /FTId=PRO_0000261550.
FT CHAIN 779 1130 Non-structural protein 1. {ECO:0000250}.
FT /FTId=PRO_0000261551.
FT CHAIN 1131 1354 Non-structural protein 2A. {ECO:0000250}.
FT /FTId=PRO_0000261552.
FT CHAIN 1131 1320 Non-structural protein 2A-alpha.
FT {ECO:0000250}.
FT /FTId=PRO_0000261553.
FT CHAIN 1355 1484 Serine protease subunit NS2B.
FT {ECO:0000250}.
FT /FTId=PRO_0000261554.
FT CHAIN 1485 2107 Serine protease NS3. {ECO:0000250}.
FT /FTId=PRO_0000261555.
FT CHAIN 2108 2233 Non-structural protein 4A. {ECO:0000250}.
FT /FTId=PRO_0000261556.
FT PEPTIDE 2234 2256 Peptide 2k.
FT /FTId=PRO_0000261557.
FT CHAIN 2257 2507 Non-structural protein 4B. {ECO:0000250}.
FT /FTId=PRO_0000261558.
FT CHAIN 2508 3412 RNA-directed RNA polymerase NS5.
FT {ECO:0000250}.
FT /FTId=PRO_0000261559.
FT TOPO_DOM 1 104 Cytoplasmic. {ECO:0000255}.
FT TRANSMEM 105 125 Helical. {ECO:0000255}.
FT TOPO_DOM 126 244 Extracellular. {ECO:0000255}.
FT TRANSMEM 245 265 Helical. {ECO:0000255}.
FT TOPO_DOM 266 270 Cytoplasmic. {ECO:0000255}.
FT TRANSMEM 271 285 Helical. {ECO:0000255}.
FT TOPO_DOM 286 730 Extracellular. {ECO:0000255}.
FT INTRAMEM 731 751 Helical. {ECO:0000255}.
FT TOPO_DOM 752 757 Extracellular. {ECO:0000255}.
FT INTRAMEM 758 778 Helical. {ECO:0000255}.
FT TOPO_DOM 779 1130 Extracellular. {ECO:0000255}.
FT TRANSMEM 1131 1151 Helical. {ECO:0000255}.
FT TOPO_DOM 1152 1160 Cytoplasmic. {ECO:0000255}.
FT TRANSMEM 1161 1181 Helical. {ECO:0000255}.
FT TOPO_DOM 1182 1201 Lumenal. {ECO:0000255}.
FT TRANSMEM 1202 1222 Helical. {ECO:0000255}.
FT TOPO_DOM 1223 1231 Cytoplasmic. {ECO:0000255}.
FT TRANSMEM 1232 1252 Helical. {ECO:0000255}.
FT TOPO_DOM 1253 1262 Lumenal. {ECO:0000255}.
FT TRANSMEM 1263 1285 Helical. {ECO:0000255}.
FT TOPO_DOM 1286 1355 Cytoplasmic. {ECO:0000255}.
FT TRANSMEM 1356 1376 Helical. {ECO:0000255}.
FT TOPO_DOM 1377 1378 Lumenal. {ECO:0000255}.
FT TRANSMEM 1379 1399 Helical. {ECO:0000255}.
FT TOPO_DOM 1400 1456 Cytoplasmic. {ECO:0000255}.
FT INTRAMEM 1457 1477 Helical. {ECO:0000255}.
FT TOPO_DOM 1478 2157 Cytoplasmic. {ECO:0000255}.
FT TRANSMEM 2158 2178 Helical. {ECO:0000255}.
FT TOPO_DOM 2179 2186 Lumenal. {ECO:0000255}.
FT INTRAMEM 2187 2207 Helical. {ECO:0000255}.
FT TOPO_DOM 2208 2209 Lumenal. {ECO:0000255}.
FT TRANSMEM 2210 2230 Helical. {ECO:0000255}.
FT TOPO_DOM 2231 2241 Cytoplasmic. {ECO:0000255}.
FT TRANSMEM 2242 2262 Helical; Note=Signal for NS4B.
FT {ECO:0000255}.
FT TOPO_DOM 2263 2293 Lumenal. {ECO:0000255}.
FT INTRAMEM 2294 2314 Helical. {ECO:0000255}.
FT TOPO_DOM 2315 2338 Lumenal. {ECO:0000255}.
FT INTRAMEM 2339 2359 Helical. {ECO:0000255}.
FT TOPO_DOM 2360 2360 Lumenal. {ECO:0000255}.
FT TRANSMEM 2361 2380 Helical. {ECO:0000255}.
FT TOPO_DOM 2381 2421 Cytoplasmic. {ECO:0000255}.
FT TRANSMEM 2422 2442 Helical. {ECO:0000255}.
FT TOPO_DOM 2443 2445 Lumenal. {ECO:0000255}.
FT TRANSMEM 2446 2466 Helical. {ECO:0000255}.
FT TOPO_DOM 2467 3411 Cytoplasmic. {ECO:0000255}.
FT DOMAIN 1485 1665 Peptidase S7. {ECO:0000255|PROSITE-
FT ProRule:PRU00860}.
FT DOMAIN 1669 1825 Helicase ATP-binding.
FT {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT DOMAIN 1836 1997 Helicase C-terminal.
FT {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT DOMAIN 2508 2772 mRNA cap 0-1 NS5-type MT.
FT {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT DOMAIN 3036 3188 RdRp catalytic. {ECO:0000255|PROSITE-
FT ProRule:PRU00539}.
FT NP_BIND 1682 1689 ATP. {ECO:0000255|PROSITE-
FT ProRule:PRU00541}.
FT REGION 30 74 Hydrophobic; homodimerization of capsid
FT protein C. {ECO:0000250}.
FT REGION 383 396 Involved in fusion. {ECO:0000250}.
FT REGION 1407 1446 Interacts with and activates NS3
FT protease. {ECO:0000255|PROSITE-
FT ProRule:PRU00859}.
FT MOTIF 1773 1776 DEAH box.
FT MOTIF 2879 2912 Nuclear localization signal.
FT {ECO:0000250}.
FT ACT_SITE 1537 1537 Charge relay system; for serine protease
FT NS3 activity. {ECO:0000255|PROSITE-
FT ProRule:PRU00860}.
FT ACT_SITE 1561 1561 Charge relay system; for serine protease
FT NS3 activity. {ECO:0000255|PROSITE-
FT ProRule:PRU00860}.
FT ACT_SITE 1622 1622 Charge relay system; for serine protease
FT NS3 activity. {ECO:0000255|PROSITE-
FT ProRule:PRU00860}.
FT BINDING 2520 2520 mRNA cap. {ECO:0000255|PROSITE-
FT ProRule:PRU00924}.
FT BINDING 2523 2523 mRNA cap; via carbonyl oxygen.
FT {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT BINDING 2524 2524 mRNA cap. {ECO:0000255|PROSITE-
FT ProRule:PRU00924}.
FT BINDING 2526 2526 mRNA cap; via carbonyl oxygen.
FT {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT BINDING 2535 2535 mRNA cap. {ECO:0000255|PROSITE-
FT ProRule:PRU00924}.
FT BINDING 2563 2563 S-adenosyl-L-methionine.
FT {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT BINDING 2593 2593 S-adenosyl-L-methionine; via carbonyl
FT oxygen. {ECO:0000255|PROSITE-
FT ProRule:PRU00924}.
FT BINDING 2594 2594 S-adenosyl-L-methionine; via carbonyl
FT oxygen. {ECO:0000255|PROSITE-
FT ProRule:PRU00924}.
FT BINDING 2611 2611 S-adenosyl-L-methionine.
FT {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT BINDING 2612 2612 S-adenosyl-L-methionine; via carbonyl
FT oxygen. {ECO:0000255|PROSITE-
FT ProRule:PRU00924}.
FT BINDING 2638 2638 S-adenosyl-L-methionine.
FT {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT BINDING 2639 2639 S-adenosyl-L-methionine; via carbonyl
FT oxygen. {ECO:0000255|PROSITE-
FT ProRule:PRU00924}.
FT BINDING 2657 2657 mRNA cap. {ECO:0000255|PROSITE-
FT ProRule:PRU00924}.
FT BINDING 2720 2720 mRNA cap. {ECO:0000255|PROSITE-
FT ProRule:PRU00924}.
FT BINDING 2722 2722 mRNA cap. {ECO:0000255|PROSITE-
FT ProRule:PRU00924}.
FT BINDING 2727 2727 S-adenosyl-L-methionine.
FT {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT SITE 101 102 Cleavage; by viral protease NS3.
FT {ECO:0000255}.
FT SITE 121 122 Cleavage; by host signal peptidase.
FT {ECO:0000250}.
FT SITE 210 211 Cleavage; by host furin. {ECO:0000255}.
FT SITE 285 286 Cleavage; by host signal peptidase.
FT {ECO:0000255}.
FT SITE 778 779 Cleavage; by host signal peptidase.
FT {ECO:0000255}.
FT SITE 1130 1131 Cleavage; by host. {ECO:0000255}.
FT SITE 1354 1355 Cleavage; by viral protease NS3.
FT {ECO:0000255}.
FT SITE 1484 1485 Cleavage; by autolysis. {ECO:0000255}.
FT SITE 2107 2108 Cleavage; by autolysis. {ECO:0000255}.
FT SITE 2233 2234 Cleavage; by viral protease NS3.
FT {ECO:0000255}.
FT SITE 2256 2257 Cleavage; by host signal peptidase.
FT {ECO:0000255}.
FT SITE 2507 2508 Cleavage; by viral protease NS3.
FT {ECO:0000255}.
FT SITE 2531 2531 mRNA cap binding. {ECO:0000255|PROSITE-
FT ProRule:PRU00924}.
FT SITE 2568 2568 Essential for 2'-O-methyltransferase
FT activity. {ECO:0000255|PROSITE-
FT ProRule:PRU00924}.
FT SITE 2653 2653 Essential for 2'-O-methyltransferase and
FT N-7 methyltransferase activity.
FT {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT SITE 2654 2654 S-adenosyl-L-methionine binding.
FT {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT SITE 2689 2689 Essential for 2'-O-methyltransferase
FT activity. {ECO:0000255|PROSITE-
FT ProRule:PRU00924}.
FT SITE 2725 2725 Essential for 2'-O-methyltransferase
FT activity. {ECO:0000255|PROSITE-
FT ProRule:PRU00924}.
FT CARBOHYD 134 134 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 150 150 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 908 908 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 986 986 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT DISULFID 288 315 {ECO:0000250}.
FT DISULFID 345 401 {ECO:0000250}.
FT DISULFID 359 390 {ECO:0000250}.
FT DISULFID 377 406 {ECO:0000250}.
FT DISULFID 467 568 {ECO:0000250}.
FT DISULFID 585 615 {ECO:0000250}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 1673 1818 ipfam:Flavi_DEAD [T]
FT MYHIT 1656 1839 ismart:DEXDc [T]
FT MYHIT 3036 3188 iprf:RDRP_SSRNA_POS [T]
FT MYHIT 287 579 ipfam:Flavi_glycoprot [T]
FT MYHIT 2759 3407 ipfam:Flavi_NS5 [T]
FT MYHIT 2257 2501 ipfam:Flavi_NS4B [T]
FT MYHIT 2508 2772 iprf:RNA_CAP01_NS5_MT [T]
FT MYHIT 581 676 ipfam:Flavi_glycop_C [T]
FT MYHIT 1503 1655 ipfam:Peptidase_S7 [T]
FT MYHIT 780 1132 ipfam:Flavi_NS1 [T]
FT MYHIT 2111 2254 ipfam:Flavi_NS4A [T]
FT MYHIT 1485 1665 iprf:FLAVIVIRUS_NS3PRO [T]
FT MYHIT 5 117 ipfam:Flavi_capsid [T]
FT MYHIT 1355 1484 iprf:FLAVIVIRUS_NS2B [T]
FT MYHIT 1836 1997 iprf:HELICASE_CTER [T]
FT MYHIT 1139 1323 ipfam:Flavi_NS2A [T]
FT MYHIT 1358 1484 ipfam:Flavi_NS2B [T]
FT MYHIT 126 209 ipfam:Flavi_propep [T]
FT MYHIT 1858 1953 ismart:HELICc [T]
FT MYHIT 1669 1825 iprf:HELICASE_ATP_BIND_1 [T]
FT MYHIT 212 285 ipfam:Flavi_M [T]
FT MYHIT 2562 2730 ipfam:FtsJ [T]
SQ SEQUENCE 3412 AA; 378939 MW; DA9310F26DE41B95 CRC64;
MSGRKAQGKT LGVNMVRRGV RSLSNKIKQK TKQIGNRPGP SRGVQGFIFF FLFNILTGKK
LTAHLKKLWR MLDPRQGLAV LRKVKRVVAS LMRGLSSRKR RSNEMALFPL LLLGLLALSG
GVTLVRKNRW LLLNVTAEDL GKTFSVGTGN CTTNILEAKY WCPDSMEYNC PNLSPREEPD
DIDCWCYGVE NVRVAYGRCD AVGRSKRSRR AIDLPTHENH GLKTRQEKWM TGRMGERQLQ
KIERWLVRNP FFAVTALAIA YLVGNNTTQR VVIALLVLAV GPAYSAHCIG ITDRDFIEGV
HGGTWVSATL EQDKCVTVMA PDKPSLDISL QTVAIDGPAE ARKVCYSAVL THVKINDKCP
STGEAHLAEE NDGDNACKRT YSDRGWGNGC GLFGKGSIVA CAKFTCAKSM SLFEVDQTKI
QYVIRAQLHV GAKQENWNTD IKTLKFDALS GSQEAEFTGY GKATLECQVQ TAVDFGNSYI
AEMEKDSWIV DRQWAQDLTL PWQSGSGGIW REMHHLVEFE PPHAATIRVL ALGNQEGSLK
TALTGAMRVT KDENDNNLYK LHGGHVSCRV KLSALTLKGT SYKMCTDKMS FVKNPTDTGH
GTVVMQVKVP KGAPCKIPVI VADDLTAAVN KGILVTVNPI ASTNDDEVLI EVNPPFGDSY
IIVGTGDSRL TYQWHKEGSS IGKLFTQTMK GAERLAVMGD AAWDFSSAGG FFTSVGKGIH
TVFGSAFQGL FGGLSWITKV IMGAVLIWVG INTRNMTMSM SMILVGVIMM FLSLGVGADQ
GCAVNFGKRE LKCGDGIFVF RDSDDWLTKY SYYPEDPVKL ASIIKASHEE GKCGLNSVDS
LEHEMWRSRA DEINAIFEEN EVDISVVVQD PKNIYQRGTH PFSRIRDGLQ YGWKTWGKNL
VFSPGRKNGS FIIDGKSRKE CPFSNRVWNS FQIEEFGMGV FTTRVFMDAT FDYSVDCDGA
ILGAAVNGKK SAHGSPTFWM GSHEVNGTWM IHTLETLDYK ECEWPLTHTI GTSVEESDMF
MPRSIGGPVS SHNRIPGYKV QTNGPWMQVP LEVKREVCPG TSVVVDSNCD GRGKSTRSTT
DSGKIIPEWC CRSCTMPPVS FHGSDGCWYP MEIRPMKTSD SHLVRSWVTA GEVHAVPFGL
VSMMIAMEVV LRRRQGPKQM LVGGVVLLGA MLVGQVTVLD LVKFVVAVGL HFHEINNGGD
AMYMALIASF SIRPGLLMGF GLRTLWSPRE RLVMAFGAAM VEIALGGMMG GLWQYLNAVS
LCVLTINAIS SRKASNMILP LMALMTPMTM HEVRMATMLF CTVVIIGVLH QNSKDTSMQK
TIPIVALTLT SYMGLTQPFL GLCAYMSTQV FGRRSIPVNE ALAAAGLVGV LAGLAFQDME
NFLGPIAVGG ILMMLVSVAG RVDGLELKKL GEISWEEEAE ISGSSSRYDV ALSEQGEFKL
LSEDKVPWDQ IVMTSLALVG AAIHPFALLL VLGGWILHIK GARRSGDVLW DIPTPKVIEE
CEHLEDGIYG IFQSTFLGAS QRGVGVAQGG VFHTMWHVTR GAFLLRNGKK LVPSWASVKE
DLVAYGGSWK LDGRWDGEEE VQLIAAVPGK SVVNVQTKPS LFRVKNGGEI GAVALDYPSG
TSGSPIVNRN GEVVGLYGNG ILVGDNSFVS AISQTELKEE SKEELQEIPT MLKKGMTTIL
DFHPGAGKTR RFLPQILAEC ARRRLRTLVL APTRVVLSEM KEAFQGLDVK FHTQAFSAHG
SGKEVIDAMC HATLTYRMLE PTRVVNWEVI IMDEAHFLDP ASIAARGWAA HRARANESAT
ILMTATPPGT SDEFPHSNGE IEDVQTDIPS EPWTAGHEWI LADKRPTAWF LPSIRAANVM
AASLRKAGKN VVVLNRKTFE KEYPTIKQKK PDFILATDIA EMGANLCVER VLDCRTAYKP
VLVDEGKKVA IKGPLRISAS SAAQRRGRIG RNPNRDGDSY YYSEPTSEDN AHHVCWLEAS
MLLDNMEVRG GMVAPLYGIE GTKTPVSPGE MRLRDDQRRV FRELVRGCDL PVWLAWQVAK
AGLKTNDRKW CFEGPEEHEI LNDNGETVKC RSPGGAKRAL RPRWCDERVS SDQSALADFI
KFAEGRRGAA EMLVILTELP DFLAKKGGEA MDTISVFLHS EEGSRAYRNA LSMMPEAMTI
VMLFLLAGLL TSGAVIFFMS PKGMSRMSMA MGTMAGSGYL MFLGGVKPTH ISYVMLIFFV
LMVVVIPEPG QQRTIQDNQV AYLIIGILTL LSVVAANELG MLEKTKEDFF GKRDITTPSG
AIPWSWPDLD LKPGAAWTVY VGIVTMLSPM LHHWIKVEYG NLSLSGIAQS ASVLSFMDKG
IPFMKMNISV VILLVSGWNS ITVIPLLCGI GGAMLHWTLI LPGIKAQQSK LAQKRVFHGV
AKNPVVDGNP TADIEEAPEM PALYEKKLAL YLLLALSLMS VAMCRTPFSL AEGIVLSSAA
LGPLIEGNTS LLWNGPMAVS MTGVMRGNYY AFVGVMYNLW KMKTERRGSA SGKTLGEVWK
RELNLLDKQQ FEMYKRTDII EVDRDMARRH LAEGKVDTGV AVSRGTAKLR WFHERGYVKL
EGRVTDLGCG RGGWCYYAAA QKEVSGVKGY TLGRDGHEKP MNVQSLGWNI VTFKDKTDVH
RLEPLKCETL LCDIGESSPS SATEGERTLR VLDTVEKWLA CGVDNFCIKV LAPYMPDVIE
KLELLQRRFG GTVIRNPLSR NSTHEMYYVS GARSNITFTV NQTSRLLMRR MRRPTGKVTL
EADVILPIGT RSVETDKGPL DKDAIEERVE RIKNEYATTW FYDNDNPYRT WHYCGSYVTK
TSGSAASMIN GVIKILTFPW DRIEEVTRMA MTDTTPFGQQ RVFKEKVDTR AKDPPAGTRK
IMKVVNRWLF RHLSREKNPR LCTKEEFIAK VRSHAAVGAF LEEQEQWKTA NEAVQDPKFW
EMVDAERKLH QQGRCQSCVY NMMGKREKKL SEFGKAKGSR AIWYMWLGAR FLEFEALGFL
NEDHWASREN SGGGVEGTGL QYLGYVIRDL SAKEGGGFYA DDTAGWDTRI TEADLDDEQE
IMSYMSPEQR KLAWAIMEMT YKNKVVKVLR PAPGGKAFMD IISRRDQRGS GQVVTYALNT
ITNLKVQLIR MAEAEMVINH QHVQECGENV LERLETWLAE NGCDRLSRMA VSGDDCVVRP
VDDRFGLALS HLNAMSKVRK DISEWQPSKG WTDWENVPFC SHHFHELVLK DGRKIVVPCR
DQDELIGRGR VSPGNGWMIK ETACLSKAYA NMWSLMYFHK RDMRLLSFAV SSAVPTAWVP
SGRTTWSVHG RGEWMTTEDM LDVWNRVWVL NNPHMTDKTT IKEWRDVPYL TKRQDKLCGS
LIGMTNRATW ASHIHLVIHR IRTLIGQEKF TDYLTVMDRY SVDADLQPGE LI
//
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