ID POLG_YEFVC Reviewed; 3411 AA. AC Q6J3P1; Q6PX46; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 09-JAN-2007, entry version 16. 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 Yellow fever virus (isolate Ivory Coast/1999) (YFV). OC Viruses; ssRNA positive-strand viruses, no DNA stage; Flaviviridae; OC Flavivirus; Yellow fever virus group. OX NCBI_TaxID=407136; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RC STRAIN=Isolate Gambia/2001, and Isolate Ivory Coast/1999; RX PubMed=16036176; DOI=10.1016/j.jcv.2004.12.001; RA Bae H.-G., Drosten C., Emmerich P., Colebunders R., Hantson P., RA Pest S., Parent M., Schmitz H., Warnat M.-A., Niedrig M.; RT "Analysis of two imported cases of yellow fever infection from Ivory RT Coast and The Gambia to Germany and Belgium."; RL J. Clin. Virol. 33:274-280(2005). 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 heterodimers are dissociated (By CC 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. The secreted form CC elicits protective immune response and plays an essential role in CC RNA replication (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 (By similarity). CC -!- FUNCTION: Non-structural protein 4B plays a role in RNA CC replication (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: Protein C: Virion. Peptide pr: Secreted CC protein. Small envelope protein M: Virion; virion membrane; CC single-pass type I membrane protein. Envelope protein E: Virion; CC virion membrane; single-pass type I membrane protein. Non- CC structural protein 1: Secreted protein. Endoplasmic reticulum; CC endoplasmic reticulum membrane; peripheral membrane protein; CC lumenal side. Non-structural protein 2A-alpha: Endoplasmic CC reticulum; endoplasmic reticulum membrane. Non-structural protein CC 2A: Endoplasmic reticulum; endoplasmic reticulum membrane. Serine CC protease subunit NS2B: Endoplasmic reticulum; endoplasmic CC reticulum membrane; peripheral membrane protein; cytoplasmic side. CC Serine protease subunit NS3: Endoplasmic reticulum; endoplasmic CC reticulum membrane; peripheral membrane protein; cytoplasmic side. CC Non-structural protein 4A: Endoplasmic reticulum; endoplasmic CC reticulum membrane; peripheral membrane protein; cytoplasmic side. CC Non-structural protein 4B: Endoplasmic reticulum; endoplasmic CC reticulum membrane; peripheral membrane protein; cytoplasmic side. CC RNA-directed RNA polymerase NS5: Endoplasmic reticulum; CC cytoplasmic side. Nucleus. 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. The C-terminal transmembrane domains of non- CC structural protein 4B is presumably reoriented after cleavage on CC the lumenal side (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. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY603338; AAT12476.1; -; Genomic_RNA. DR EMBL; AY572535; AAS78199.1; -; Genomic_RNA. DR HSSP; Q9Q4T1; 1BEF. DR SMR; Q6J3P1; 1671-2107. DR GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:EC. DR InterPro; IPR014001; DEAD-like_N. DR InterPro; IPR011999; Flav_glyE_cen_dm. DR InterPro; IPR013754; Flav_glyE_dim. DR InterPro; IPR001122; Flavi_capsidC. DR InterPro; IPR011492; Flavi_DEAD. 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; IPR000208; Flavi_NS5. DR InterPro; IPR002535; Flavi_propep. DR InterPro; IPR000336; Flv_glyE_Ig-like. DR InterPro; IPR014021; Helic_SF1/SF2_ATP_bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR001850; Peptidase_S7. DR InterPro; IPR001865; Ribosomal_S2. DR InterPro; IPR007094; RNA_pol_PSvir. DR InterPro; IPR002877; RrmJFtsJ_mtfrase. DR InterPro; IPR011998; Vrl_glyE_cen_dim. 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; PF00271; Helicase_C; 1. DR Pfam; PF00949; Peptidase_S7; 1. DR ProDom; PD001496; Flavi_NS1; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS50507; RDRP_SSRNA_POS; 1. KW ATP-binding; Capsid protein; Endoplasmic reticulum; Envelope protein; KW Glycoprotein; Helicase; Hydrolase; Membrane; Metal-binding; KW Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase; KW Phosphorylation; Protease; Ribonucleoprotein; RNA replication; KW RNA-binding; RNA-directed RNA polymerase; Serine protease; KW Transferase; Transmembrane; Viral nucleoprotein; Virion protein. FT CHAIN 1 101 Protein C. FT /FTId=PRO_0000261500. FT INIT_MET 1 1 Removed from protein C by the cellular FT aminopeptidase. FT PROPEP 102 121 ER anchor for the protein C, removed in FT mature form by serine protease NS3. FT /FTId=PRO_0000261501. FT CHAIN 122 285 prM. FT /FTId=PRO_0000261502. FT CHAIN 122 210 Peptide pr. FT /FTId=PRO_0000261503. FT CHAIN 211 285 Small envelope protein M. FT /FTId=PRO_0000261504. FT CHAIN 286 778 Envelope protein E. FT /FTId=PRO_0000261505. FT CHAIN 779 1130 Non-structural protein 1. FT /FTId=PRO_0000261506. FT CHAIN 1131 1354 Non-structural protein 2A. FT /FTId=PRO_0000261507. FT CHAIN 1131 1320 Non-structural protein 2A-alpha. FT /FTId=PRO_0000261508. FT CHAIN 1355 1484 Serine protease subunit NS2B. FT /FTId=PRO_0000261509. FT CHAIN 1485 2107 Serine protease subunit NS3. FT /FTId=PRO_0000261510. FT CHAIN 2108 2233 Non-structural protein 4A. FT /FTId=PRO_0000261511. FT PEPTIDE 2234 2256 Peptide 2k. FT /FTId=PRO_0000261512. FT CHAIN 2257 2506 Non-structural protein 4B. FT /FTId=PRO_0000261513. FT CHAIN 2507 3411 RNA-directed RNA polymerase NS5. FT /FTId=PRO_0000261514. FT TOPO_DOM 1 101 Cytoplasmic (Potential). FT TRANSMEM 102 121 Potential. FT TOPO_DOM 122 244 Extracellular (Potential). FT TRANSMEM 245 265 Potential. FT TOPO_DOM 266 269 Cytoplasmic (Potential). FT TRANSMEM 270 287 Potential. FT TOPO_DOM 288 730 Extracellular (Potential). FT TRANSMEM 731 751 Potential. FT TOPO_DOM 752 757 Cytoplasmic (Potential). FT TRANSMEM 758 778 Potential. FT TOPO_DOM 779 1130 Extracellular (Potential). FT TRANSMEM 1131 1151 Potential. FT TOPO_DOM 1152 1160 Cytoplasmic (Potential). FT TRANSMEM 1161 1181 Potential. FT TOPO_DOM 1182 1201 Lumenal (Potential). FT TRANSMEM 1202 1222 Potential. FT TOPO_DOM 1223 1231 Cytoplasmic (Potential). FT TRANSMEM 1232 1252 Potential. FT TOPO_DOM 1253 1262 Lumenal (Potential). FT TRANSMEM 1263 1285 Potential. FT TOPO_DOM 1286 1287 Cytoplasmic (Potential). FT TRANSMEM 1288 1308 Potential. FT TOPO_DOM 1309 1321 Lumenal (Potential). FT TRANSMEM 1322 1342 Potential. FT TOPO_DOM 1343 2186 Cytoplasmic (Potential). FT TRANSMEM 2187 2207 Potential. FT TOPO_DOM 2208 2209 Lumenal (Potential). FT TRANSMEM 2210 2230 Potential. FT TOPO_DOM 2231 2233 Cytoplasmic (Potential). FT TRANSMEM 2234 2256 Potential. FT TOPO_DOM 2257 2359 Lumenal (Potential). FT TRANSMEM 2360 2380 Potential. FT TOPO_DOM 2381 2421 Cytoplasmic (Potential). FT TRANSMEM 2422 2442 Potential. FT TOPO_DOM 2443 2445 Lumenal (Potential). FT TRANSMEM 2446 2466 Potential. FT TOPO_DOM 2467 3411 Cytoplasmic (Potential). FT DOMAIN 1492 1666 Peptidase S7. FT DOMAIN 1669 1825 Helicase ATP-binding. FT DOMAIN 1820 1997 Helicase C-terminal. FT DOMAIN 3035 3187 RdRp catalytic. FT NP_BIND 1682 1689 ATP (Potential). FT REGION 383 396 Involved in fusion (By similarity). FT REGION 2878 2911 Nuclear localization signal (By FT similarity). FT MOTIF 1773 1776 DEAH box (By similarity). FT ACT_SITE 1537 1537 Charge relay system; for serine protease FT NS3 activity (By similarity). FT ACT_SITE 1561 1561 Charge relay system; for serine protease FT NS3 activity (By similarity). FT ACT_SITE 1622 1622 Charge relay system; for serine protease FT NS3 activity (By similarity). FT SITE 101 102 Cleavage (by serine protease NS3) (By FT similarity). FT SITE 121 122 Cleavage (by host signal peptidase) (By FT similarity). FT SITE 210 211 Cleavage (by host furin) (By similarity). FT SITE 285 286 Cleavage (by host signal peptidase) (By FT similarity). FT SITE 778 779 Cleavage (by host signal peptidase) (By FT similarity). FT SITE 1130 1131 Cleavage (by host) (By similarity). FT SITE 1320 1321 Cleavage (by serine protease NS3) (By FT similarity). FT SITE 1354 1355 Cleavage (by serine protease NS3) (By FT similarity). FT SITE 1484 1485 Cleavage (by serine protease NS3) (By FT similarity). FT SITE 2107 2108 Cleavage (by serine protease NS3) (By FT similarity). FT SITE 2233 2234 Cleavage (by host signal peptidase) (By FT similarity). FT SITE 2256 2257 Cleavage (by serine protease NS3) (By FT similarity). FT SITE 2506 2507 Cleavage (by serine protease NS3) (By FT similarity). FT CARBOHYD 134 134 N-linked (GlcNAc...) (Potential). FT CARBOHYD 150 150 N-linked (GlcNAc...) (Potential). FT CARBOHYD 908 908 N-linked (GlcNAc...) (Potential). FT CARBOHYD 986 986 N-linked (GlcNAc...) (Potential). FT DISULFID 288 315 By similarity. FT DISULFID 345 401 By similarity. FT DISULFID 359 390 By similarity. FT DISULFID 377 406 By similarity. FT DISULFID 467 568 By similarity. FT DISULFID 585 615 By similarity. FT VARIANT 107 107 A -> T (in strain: Isolate Gambia 2001). FT VARIANT 110 110 F -> L (in strain: Isolate Gambia 2001). FT VARIANT 116 116 L -> I (in strain: Isolate Gambia 2001). FT VARIANT 148 148 A -> T (in strain: Isolate Gambia 2001). FT VARIANT 712 712 L -> F (in strain: Isolate Gambia 2001). FT VARIANT 899 899 N -> S (in strain: Isolate Gambia 2001). FT VARIANT 1185 1185 T -> I (in strain: Isolate Gambia 2001). FT VARIANT 1297 1297 A -> T (in strain: Isolate Gambia 2001). FT VARIANT 1433 1433 S -> N (in strain: Isolate Gambia 2001). FT VARIANT 2056 2056 D -> E (in strain: Isolate Gambia 2001). FT VARIANT 2161 2161 A -> V (in strain: Isolate Gambia 2001). FT VARIANT 2373 2373 M -> T (in strain: Isolate Gambia 2001). FT VARIANT 2438 2438 A -> S (in strain: Isolate Gambia 2001). FT VARIANT 2644 2644 M -> V (in strain: Isolate Gambia 2001). SQ SEQUENCE 3411 AA; 378956 MW; C121A19ABEA92218 CRC64; MSGRKAQGKT LGVNMVRRGV RSLSNKIKQK TKQIGNRPGP SRGVQGFIFF FLFNILTGKK ITAHLKRLWK MLDPRQGLAV LRKVKRVVAS LMRGLSSRKR RSHDALAVQF LILGMLLMAG GVTLVRKNRW LLLNVTSEDL GKTFSVGAGN 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 FLTSVGKGIH TVFGSAFQGL FGGLSWITKV 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 LEVRREACPG TSVIIDGNCD GRGKSTRSTT DSGKIIPEWC CRSCTMPPVS FHGSDGCWYP MEIRPRKTHE SHLVRSWVTA GEIHAVPFGL VSMMIAMEVV LRKRQGPKQM LVGGVVLLGA MLVGQVTLLD LLKLTVAVGL HFHEMNNGGD AMYMALIAAF SIRPGLLIGF GLRTLWSPRE RLVLTLGAAM VEIALGGMMG GLWKYLNAVS LCILTINAVA SRKASNTILP LMALLTPVTM AEVRLAAMLF CTVVIIGVLH QNSKDTSMQK TIPLVALTLT SYLGLTQPFL GLCAFLATRL FGRRSIPVNE ALAAAGLVGV LAGLAFQEME NFLGPIAVGG ILMMLVSVAG RVDGLELRKL GEVSWEEEAE ISGSSARYDV ALSEQGEFKL LSEEKVPWDQ VVMTSLALVG AAIHPFALLL VLAGWLFHVK 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 PTRIVNWEVI 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 FRELVRNCDQ PVWLSWQVAK AGLKTNDRKW CFEGPDEHEI LNDSGETVKC RAPGGAKKPL RPRWCDERVS SDQSALADFI KFAEGRRGAA EVLVVLSELP DFLAKKGGEA MDTISVFLHS EEGSRAYRNA LSMMPEAMTI AMLFILAGLL TSGMVIFFMS PKGISRMSMA MGTMAGCGYL MFLGGVKPTH ISYIMLIFFV LMVVVIPEPG QQRSIQDNQV AYLIIGILTL VSVVAANELG MLEKTKEDLF GKKDLIPSSA SPWSWPDLDL KPGAAWTVYV GIVTMLSPML HHWIKVEYGN LSLSGIAQSA SVLSFMDKGI PFMKMNISVI ILLVSGWNSI TVMPLLCGIG CAMLHWSLIL PGIKAQQSKL AQRRVFHGVA KNPVVDGNPT VDIEEAPEMP ALYEKKLALY LLLALSLASV AMCRTPFSLA EGIVLASAAL GPLIEGNTSL LWNGPMAVSM TGVMRGNYYA FVGVMYNLWK MKTGRRGRAN GKTLGEVWKR ELNLLDKQQF ELYKRTDIVE VDRDTARRHL AEGKVDTGVA VSRGTAKLRW FHERGYVKLE GRVTDLGCGR GGWCYYAAAQ KEVSGVKGFT LGRDGHEKPM NVQSLGWNII TFKDKTDIHR LEPMKCDTLL CDIGESSSSS VTEGERTMRV LDTVEKWLAC GVDNFCVKVL APYMPDVLEK LELLQRRFGG TVIRNPLSRN STHEMYYVSG ARSNVTFTVN QTSRLLMRRM RRPTGKVTLE ADVILPIGTR SVETDKGPLD REAIEERVER IKSEYMTTWF 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 HVQDCDESAL ARLEAWLTEH GCDRLKRMAV SGDDCVVRPI DDRFGLALSH LNAMSKVRKD ISEWQPSKGW NDWENVPFCS HHFHELHLKD GRRIVVPCRE QDELIGRGRV SPGNGWMIKE TACLSKAYAN MWSLMYFHKR DMRLLSLAVS SAVPTSWVPQ GRTTWSIHGK GEWMTTEDML GVWNRVWITN NPHMQDKTVV KEWRDVPYLT KRQDKLCGSL IGMTNRATWA SHIHLVIHRI RTLIGQEKYT DYLTVMDRYS VDADLQPGEL I //