ID   POLG_DEN27              Reviewed;        3391 AA.
AC   P29991;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   29-APR-2008, entry version 74.
DE   Genome polyprotein [Contains: Protein C (Core protein) (Capsid
DE   protein); prM; Peptide pr; Small envelope protein M (Matrix protein);
DE   Envelope protein E; Non-structural protein 1 (NS1); Non-structural
DE   protein 2A (NS2A); Non-structural protein 2A-alpha (NS2A-alpha);
DE   Serine protease subunit NS2B (Non-structural protein 2B); Serine
DE   protease subunit NS3 (EC 3.4.21.91) (Non-structural protein 3); Non-
DE   structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B
DE   (NS4B); RNA-directed RNA polymerase NS5 (EC 2.7.7.48) (EC 2.1.1.56)
DE   (Non-structural protein 5)].
OS   Dengue virus type 2 (strain 16681-PDK53) (DENV-2).
OC   Viruses; ssRNA positive-strand viruses, no DNA stage; Flaviviridae;
OC   Flavivirus; Dengue virus group.
OX   NCBI_TaxID=31635;
OH   NCBI_TaxID=7159; Aedes aegypti (Yellowfever mosquito).
OH   NCBI_TaxID=299627; Aedes furcifer.
OH   NCBI_TaxID=299628; Aedes taylori.
OH   NCBI_TaxID=9538; Erythrocebus patas (Red guenon) (Cercopithecus patas).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   MEDLINE=92188532; PubMed=1312269; DOI=10.1016/0042-6822(92)90460-7;
RA   Blok J., McWilliam S.M., Butler H.C., Gibbs A.J., Weiller G.,
RA   Herring B.L., Hemsley A.C., Aaskov J.G., Yoksan S., Bhamarapravati N.;
RT   "Comparison of a dengue-2 virus and its candidate vaccine derivative:
RT   sequence relationships with the flaviviruses and other viruses.";
RL   Virology 187:573-590(1992).
CC   -!- FUNCTION: Protein C packages viral RNA to form a viral
CC       nucleocapsid, and promotes virion budding (By similarity).
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 (By similarity).
CC   -!- FUNCTION: Envelope protein E binds cell surface receptor and is
CC       involved in membrane fusion between virion and target cell.
CC       Synthesized as an 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 (By
CC       similarity).
CC   -!- FUNCTION: Non-structural protein 1 is slowly secreted from
CC       mammalian cells, but not from mosquito cells. Secreted form
CC       elicits protective immune response and plays an essential role in
CC       RNA replication. Soluble and membrane-associated NS1 may activate
CC       human complement and induce host vascular leakage. This effect
CC       might explain the clinical manifestations of dengue hemorrhagic
CC       fever and dengue shock syndrome (By similarity).
CC   -!- FUNCTION: Non-structural protein 2B is a required cofactor for the
CC       serine protease function of NS3 (By similarity).
CC   -!- FUNCTION: Serine protease NS3 displays three enzymatic activities:
CC       serine protease, NTPase and RNA helicase. NS3 serine protease, in
CC       association with NS2B, cleaves the polyprotein at dibasic sites in
CC       the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and
CC       NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3'
CC       to 5' direction (By similarity).
CC   -!- FUNCTION: Non-structural protein 4A plays a role in RNA
CC       replication. Enhances inhibition of cell antiviral response by
CC       non-structural protein 4B (By similarity).
CC   -!- FUNCTION: Non-structural protein 4B prevent the establishment of
CC       cellular antiviral state by blocking the interferon-alpha/beta
CC       (IFN-alpha/beta) and IFN-gamma signaling pathways (By similarity).
CC   -!- FUNCTION: RNA-directed RNA polymerase NS5 replicates the viral (+)
CC       and (-) genome, and assure the capping of genomes in the
CC       cytoplasm. May be involved in methylation of 5'RNA cap structure
CC       (By similarity).
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).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S-
CC       adenosyl-L-homocysteine + m(7)G(5')pppR-RNA.
CC   -!- SUBUNIT: prM and envelope protein E form heterodimers in the
CC       endoplasmic reticulum and Golgi. Envelope protein E forms
CC       homodimers. NS1 forms homodimers as well as homohexamers when
CC       secreted. NS1 may interact with NS4A. NS3 and NS2B form an
CC       heterodimer. NS3 interacts with unphosphorylated NS5 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Note=The virion is assembled in the
CC       endoplasmic reticulum lumen, transported by vesicles to the Golgi,
CC       then transported again to the cell membrane where it is released
CC       outside the cell.
CC   -!- SUBCELLULAR LOCATION: Protein C: Virion (By similarity).
CC   -!- SUBCELLULAR LOCATION: Peptide pr: Secreted (By similarity).
CC   -!- SUBCELLULAR LOCATION: Small envelope protein M: Virion membrane;
CC       Single-pass type I membrane protein (By similarity).
CC   -!- SUBCELLULAR LOCATION: Envelope protein E: Virion membrane; Single-
CC       pass type I membrane protein (By similarity).
CC   -!- SUBCELLULAR LOCATION: Non-structural protein 1: Secreted.
CC       Endoplasmic reticulum membrane; Peripheral membrane protein;
CC       Lumenal side (By similarity).
CC   -!- SUBCELLULAR LOCATION: Non-structural protein 2A-alpha: Endoplasmic
CC       reticulum membrane (By similarity).
CC   -!- SUBCELLULAR LOCATION: Non-structural protein 2A: Endoplasmic
CC       reticulum membrane (By similarity).
CC   -!- SUBCELLULAR LOCATION: Serine protease subunit NS2B: Endoplasmic
CC       reticulum membrane; Peripheral membrane protein; Cytoplasmic side
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Serine protease subunit NS3: Endoplasmic
CC       reticulum membrane; Peripheral membrane protein; Cytoplasmic side
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Non-structural protein 4A: Endoplasmic
CC       reticulum membrane; Peripheral membrane protein; Cytoplasmic side
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Non-structural protein 4B: Endoplasmic
CC       reticulum membrane; Multi-pass membrane protein (By similarity).
CC       Note=The C-terminal transmembrane domain of non-structural protein
CC       4B is presumably reoriented after cleavage on the lumenal side (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase NS5: Endoplasmic
CC       reticulum; Cytoplasmic side. Nucleus (By similarity).
CC   -!- DOMAIN: Transmembrane domains of the small envelope protein M and
CC       envelope protein E contains an endoplasmic reticulum retention
CC       signals (By similarity).
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 (By similarity).
CC   -!- PTM: RNA-directed RNA polymerase NS5 is phosphorylated on serines
CC       residues. This phosphorylation may trigger NS5 nuclear
CC       localization (By similarity).
CC   -!- PTM: Envelope protein E and non-structural protein 1 are N-
CC       glycosylated (By similarity).
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 peptidase S7 domain.
CC   -!- SIMILARITY: Contains 1 RdRp catalytic domain.
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DR   EMBL; M84728; AAA73186.1; -; Genomic_RNA.
DR   EMBL; M84727; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   PIR; B42451; GNWV26.
DR   HSSP; Q88653; 1OKE.
DR   GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:EC.
DR   InterPro; IPR014001; DEAD-like_N.
DR   InterPro; IPR011492; DEAD_Flavivir.
DR   InterPro; IPR001650; DNA/RNA_helicase_C.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR011999; Flav_glyE_cen_dm.
DR   InterPro; IPR013754; Flav_glyE_dim.
DR   InterPro; IPR001122; Flavi_capsidC.
DR   InterPro; IPR000069; Flavi_M.
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; Flv_glyE_Ig-like.
DR   InterPro; IPR014412; Gen_Poly_FLV.
DR   InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd.
DR   InterPro; IPR001850; Peptidase_S7.
DR   InterPro; IPR000208; RNA_pol_flaviviral.
DR   InterPro; IPR007094; RNA_pol_PSvir.
DR   InterPro; IPR002877; RrmJFtsJ_MeTrfase.
DR   Gene3D; G3DSA:2.60.98.10; Flav_glyE_dim; 1.
DR   Gene3D; G3DSA:2.60.40.350; Flv_glyE_Ig-like; 1.
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   ProDom; PD001496; Flavi_NS1; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; FALSE_NEG.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; FALSE_NEG.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Capsid protein; Cleavage on pair of basic residues;
KW   Complete proteome; Endoplasmic reticulum; Envelope protein;
KW   Glycoprotein; Helicase; Hydrolase; Membrane; Metal-binding;
KW   Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase;
KW   Nucleus; Phosphoprotein; Protease; Ribonucleoprotein; RNA replication;
KW   RNA-binding; RNA-directed RNA polymerase; Secreted; Serine protease;
KW   Transcription; Transcription regulation; Transferase; Transmembrane;
KW   Viral nucleoprotein; Virion.
FT   CHAIN         1    100       Protein C (By similarity).
FT                                /FTId=PRO_0000037936.
FT   PROPEP      101    114       ER anchor for the protein C, removed in
FT                                mature form by serine protease NS3 (By
FT                                similarity).
FT                                /FTId=PRO_0000037937.
FT   CHAIN       115    280       prM (By similarity).
FT                                /FTId=PRO_0000308279.
FT   CHAIN       115    205       Peptide pr (By similarity).
FT                                /FTId=PRO_0000308280.
FT   CHAIN       206    280       Small envelope protein M (By similarity).
FT                                /FTId=PRO_0000037938.
FT   CHAIN       281    775       Envelope protein E (By similarity).
FT                                /FTId=PRO_0000037939.
FT   CHAIN       776   1127       Non-structural protein 1 (By similarity).
FT                                /FTId=PRO_0000037940.
FT   CHAIN      1128   1345       Non-structural protein 2A (By
FT                                similarity).
FT                                /FTId=PRO_0000037941.
FT   CHAIN      1128   1315       Non-structural protein 2A-alpha (By
FT                                similarity).
FT                                /FTId=PRO_0000037942.
FT   CHAIN      1346   1475       Serine protease subunit NS2B (By
FT                                similarity).
FT                                /FTId=PRO_0000037943.
FT   CHAIN      1476   2093       Serine protease subunit NS3 (By
FT                                similarity).
FT                                /FTId=PRO_0000308465.
FT   CHAIN      2094   2220       Non-structural protein 4A (By
FT                                similarity).
FT                                /FTId=PRO_0000037944.
FT   PEPTIDE    2221   2243       Peptide 2k (By similarity).
FT                                /FTId=PRO_0000308281.
FT   CHAIN      2244   2491       Non-structural protein 4B (By
FT                                similarity).
FT                                /FTId=PRO_0000037945.
FT   CHAIN      2492   3391       RNA-directed RNA polymerase NS5 (By
FT                                similarity).
FT                                /FTId=PRO_0000037946.
FT   TOPO_DOM      1    101       Cytoplasmic (Potential).
FT   TRANSMEM    102    122       Potential.
FT   TOPO_DOM    123    238       Extracellular (Potential).
FT   TRANSMEM    239    259       Potential.
FT   TOPO_DOM    260    265       Cytoplasmic (Potential).
FT   TRANSMEM    266    286       Potential.
FT   TOPO_DOM    287    725       Extracellular (Potential).
FT   TRANSMEM    726    746       Potential.
FT   TOPO_DOM    747    752       Cytoplasmic (Potential).
FT   TRANSMEM    753    773       Potential.
FT   TOPO_DOM    774   1156       Extracellular (Potential).
FT   TRANSMEM   1157   1177       Potential.
FT   TOPO_DOM   1178   1447       Cytoplasmic (Potential).
FT   TRANSMEM   1448   1468       Potential.
FT   TOPO_DOM   1469   2192       Lumenal (Potential).
FT   TRANSMEM   2193   2213       Potential.
FT   TOPO_DOM   2214   2220       Cytoplasmic (Potential).
FT   TRANSMEM   2221   2240       Potential.
FT   TRANSMEM   2348   2368       Potential.
FT   TOPO_DOM   2369   2413       Cytoplasmic (Potential).
FT   TRANSMEM   2414   2434       Potential.
FT   TOPO_DOM   2435   2459       Lumenal (Potential).
FT   TRANSMEM   2460   2480       Potential.
FT   TOPO_DOM   2481   3391       Cytoplasmic (Potential).
FT   DOMAIN     1655   1811       Helicase ATP-binding.
FT   DOMAIN     1821   1988       Helicase C-terminal.
FT   DOMAIN     3020   3169       RdRp catalytic.
FT   NP_BIND    1668   1675       ATP (Potential).
FT   MOTIF      1759   1762       DEAH box (By similarity).
FT   ACT_SITE   1526   1526       Charge relay system; for serine protease
FT                                NS3 activity (By similarity).
FT   ACT_SITE   1550   1550       Charge relay system; for serine protease
FT                                NS3 activity (By similarity).
FT   ACT_SITE   1610   1610       Charge relay system; for serine protease
FT                                NS3 activity (By similarity).
FT   SITE        100    101       Cleavage; by serine protease NS3 (By
FT                                similarity).
FT   SITE        114    115       Cleavage; by host signal peptidase (By
FT                                similarity).
FT   SITE        205    206       Cleavage; by host furin (By similarity).
FT   SITE        280    281       Cleavage; by host signal peptidase (By
FT                                similarity).
FT   SITE        775    776       Cleavage; by host signal peptidase (By
FT                                similarity).
FT   SITE       1127   1128       Cleavage; by host (By similarity).
FT   SITE       1315   1316       Cleavage; by serine protease NS3 (By
FT                                similarity).
FT   SITE       1345   1346       Cleavage; by serine protease NS3 (By
FT                                similarity).
FT   SITE       1475   1476       Cleavage; by serine protease NS3 (By
FT                                similarity).
FT   SITE       2093   2094       Cleavage; by serine protease NS3 (By
FT                                similarity).
FT   SITE       2220   2221       Cleavage; by host signal peptidase (By
FT                                similarity).
FT   SITE       2243   2244       Cleavage; by serine protease NS3 (By
FT                                similarity).
FT   SITE       2491   2492       Cleavage; by serine protease NS3 (By
FT                                similarity).
FT   CARBOHYD    183    183       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    347    347       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    433    433       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    905    905       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    982    982       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1134   1134       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2301   2301       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2305   2305       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2457   2457       N-linked (GlcNAc...) (Potential).
FT   DISULFID    283    310       By similarity.
FT   DISULFID    340    401       By similarity.
FT   DISULFID    354    385       By similarity.
FT   DISULFID    372    396       By similarity.
FT   DISULFID    465    565       By similarity.
FT   DISULFID    582    613       By similarity.
SQ   SEQUENCE   3391 AA;  379884 MW;  5EE11A74081C5177 CRC64;
     MNDQRKEAKN TPFNMLKRER NRVSTVQQLT KRFSLGMLQG RGPLKLYMAL VAFLRFLTIP
     PTAGILKRWG TIKKSKAINV LRGFRKEIGR MLNILNRRRR SAGMIIMLIP TVMAFHLTTR
     NGEPHMIVSR QEKGKSLLFK TEVGVNMCTL MAMDLGELCE DTITYKCPLL RQNEPEDIDC
     WCNSTSTWVT YGTCTTMGEH RREKRSVALV PHVGMGLETR TETWMSSEGA WKHVQRIETW
     ILRHPGFTMM AAILAYTIGT THFQRALILI LLTAVTPSMT MRCIGMSNRD FVEGVSGGSW
     VDIVLEHGSC VTTMAKNKPT LDFELIKTEA KQPATLRKYC IEAKLTNTTT ESRCPTQGEP
     SLNEEQDKRF VCKHSMVDRG WGNGCGLFGK GGIVTCAMFR CKKNMEGKVV QPENLEYTIV
     ITPHSGEEHA VGNDTGKHGK EIKITPQSSI TEAELTGYGT ITMECSPRTG LDFNEIVLLQ
     MENKAWLVHR QWFLDLPLPW LPGADTQGSN WIQKETLVTF KNPHAKKQDV VVLGSQEGAM
     HTALTGATEI QMSSGNLLFT GHLKCRLRMD KLQLKGMSYS MCTGKFKVVK EIAETQHGTI
     VIRVQYEGDG SPCKIPFEIM DLEKRHVLGR LITVNPIVTE KDSPVNIEAE PPFGDSYIII
     GVEPGQLKLN WFKKGSSIGQ MFETTMRGAK RMAILGDTAW DFGSLGGVFT SIGKALHQVF
     GAIYGAAFSG VSWTMKILIG VIITWIGMNS RSTSLSVTLV LVGIVTLYLG VMVQADSGCV
     VSWKNKELKC GSGIFITDNV HTWTEQYKFQ PESPSKLASA IQKAHEEDIC GIRSVTRLEN
     LMWKQITPEL NHILSENEVK LTIMTGDIKG IMQAGKRSLR PQPTELKYSW KTWGKAKMLS
     TESHNQTFFI DGPETAECPN TNRAWNSLEV EDYGFGVFTT NIWLKLKEKQ DVFCDSKLMS
     AAIKDNRAVH ADMGYWIESA LNDTWKIEKA SFIEVKNCHW PKSHTLWSNG VLESEMIIPK
     NLAGPVSKHN YRPGYHTQIT GPWHLGKLEM DFDFCDGTTV VVTEDCGNRG PSLRTTTASG
     KLITEWCCRS CTLPPLRYRG EDGCWYGMEI RPLKEKEENL VNSLVTAGHG QVDNFSLGVL
     GMALFLEEML RTRVGTKHAI LLVAVSFVTL IIGNRSFRDL GRVMVMVGAT MTDDIGMGVT
     YLALLAAFKV RPTFAAGLLL RKLTSKELMM TTIGIVLSSQ STIPETILEL TDALALGMMV
     LKMVRNMEKY QLAVTIMAIL CVPNAVILQN AWKVSCTILA VVSVSPLFLT SSQQKTDWIP
     LALTIKGLNP TAIFLTTLSR TSKKRSWPLN EAIMAVGMVS ILASSLLKND IPMTGPLVAG
     GLLTVCYVLT GRSADLELER AADVKWEDQA EISGSSPILS ITISEDGSMS IKNEEEEQTL
     TILIRRGLLV ISGLFPVSIP ITAAAWYLWE VKKQRAGVLW DVPSPPPMGK AELEDGAYRI
     KQKGILGYSQ IGAGVYKEGT FHTMWHVTRG AVLMHKGKRI EPSWADVKKD LISYGGGWKL
     EGEWKEGEEV QVLALDPGKN PRAVQTKPGL FKTNAGTIGA VSLDFSPGTS GSPIIDKKGK
     VVGLYGNGVV TRSGAYVSAI AQTEKSIEDN PEIEDDIFRK RRLTIMDLHP GAGKTKRYLP
     AIVREAIKRG LRTLILAPTR VVAAEMEEAL RGLPIRYQTP AIRAEHTGRE IVDLMCHATF
     TMRLLSPVRV PNYNLIIMDE AHFTDPASIA ARGYISTRVE MGEAAGIFMT ATPPGSRDPF
     PQSNAPIIDE EREIPERSWN SGHEWVTDFK GKTVWFVPSI KAGNDIAACL RKNGKKVIQL
     SRKTFDSEYV KTRTNDWDFV VTTDISEMGA NFKAERVIDP RRCMKPVILT DGEERVILAG
     PMPVTHSSAA QRRGRIGRNP KNENDQYIYM GEPLENDEDC AHWKEAKMLL DNINTPEGII
     PSMFEPEREK VDAIDGEYRL RGEARTTFVD LMRRGDLPVW LAYRVAAEGI NYADRRWCFD
     GVKNNQILEE NVEVEIWTKE GERKKLKPRW LDARIYSDPL ALKEFKEFAA GRKSLTLNLI
     TEMGRLPTFM TQKARNALDN LAVLHTAEAG GRAYNHALSE LPETLETLLL LTLLATVTGG
     IFLFLMSARG IGKMTLGMCC IITASILLWY AQIQPHWIAA SIILEFFLIV LLIPEPEKQR
     TPQDNQLTYV VIAILTVVAA TMANEMGFLE KTKKDLGLGS IATQQPESNI LDIDLRPASA
     WTLYAVATTF VTPMLRHSIE NSSVNVSLTA IANQATVLMG LGKGWPLSKM DIGVPLLAIG
     CYSQVNPTTL TAALFLLVAH YAIIGPALQA KASREAQKRA AAGIMKNPTV DGITVIDLDP
     IPYDPKFEKQ LGQVMLLVLC VTQVLMMRTT WALCEALTLA TGPISTLSEG NPGRFWNTTI
     AVSMANIFRG SYLAGAGLLF SIMKNTTNTR RVTGNIGETL GEKWKSRLNA LGKSEFQIYK
     KSGIQEVDRT LAKEGIKRGE TDHHAVSRGS AKLRWFVERN MVTPEGKVVD LGCGRGGWSY
     YCGGLKNVRE VKGLTKGGPG HEEPIPMSTY GWNLVRLQSG VDVFFIPPEK CDTLLCDIGE
     SSPNPTVEAG RTLRVLNLVE NWLNNNTQFC IKVLNPYMPS VIEKMEALQR KYGGALVRNP
     LSRNSTHEMY WVSNASGNIV SSVNMISRML INRFTMRYKK ATYEPDVDLG SGTRNIGIES
     EIPNLDIIGK RIEKIKQEHE TSWHYDQDHP YKTWAYHGSY ETKQTGSASS MVNGVFRLLT
     KPWDVVPMVT QMAMTDTTPF GQQRVFKEKV DTRTQEPKEG TKKLMKITAE WLWKELGKKK
     TPRMCTREEF TRKVRSNAAL GAIFTDENKW KSAREAVEDS RFWELVDKER NLHLEGKCET
     CVYNIMGKRE KKLGEFGKAK GSRAIWYMWL GARFLEFEAL GFLNEDHWFS RENSLSGVEG
     EGLHKLGYIL RDVSKKEGGA MYADDTAGWD TRITLEDLKN EEMVTNHMEG EHKKLAEAIF
     KLTYQNKVVR VQRPTPRGTV MDIISRRDQR GSGQVGTYGL NTFTNMEAQL IRQMEGEGVF
     KSIQHLTITE EIAVQNWLAR VGRERLSRMA ISGDDCVVKP LDDRLPSALT ALNDMGKIRK
     DIQQWEPSRG WNDWTQVPFC SHHFHELIMK DGRVLVVPCR NQDELIGRAR ISQGAGWSLR
     ETACLGKSYA QMWSLMYFHR RDLRLAANAI CSAVPSHWVP TSRTTWSIHA KHEWMTTEDM
     LTVWNRVWIQ ENPWMEDKTP VESWEEIPYL GKREDQWCGS LIGLTSRATW AKNIQAAINQ
     VRSLIGNEEY TDYMPSMKRF RREEEEAGVL W
//