ID C8XPB1_ZIKV Unreviewed; 3417 AA. AC C8XPB1; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 11-DEC-2019, entry version 85. DE RecName: Full=Genome polyprotein {ECO:0000256|SAAS:SAAS01197934}; OS Zika virus (ZIKV). OC Viruses; Riboviria; Flaviviridae; Flavivirus. OX NCBI_TaxID=64320 {ECO:0000313|EMBL:ABI54475.1, ECO:0000313|Proteomes:UP000180703}; OH NCBI_TaxID=7159; Aedes aegypti (Yellowfever mosquito) (Culex aegypti). OH NCBI_TaxID=7160; Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta). OH NCBI_TaxID=9606; Homo sapiens (Human). OH NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque). RN [1] {ECO:0000313|EMBL:ABI54475.1, ECO:0000313|Proteomes:UP000180703} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MR 766 {ECO:0000313|EMBL:ABI54475.1}; RX PubMed=19741066; DOI=10.1099/vir.0.014506-0; RA Grard G., Moureau G., Charrel R.N., Holmes E.C., Gould E.A., RA de Lamballerie X.; RT "Genomics and evolution of Aedes-borne flaviviruses."; RL J. Gen. Virol. 91:87-94(2010). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; CC Evidence={ECO:0000256|SAAS:SAAS01122357}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'- CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; CC Evidence={ECO:0000256|SAAS:SAAS01122355}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA- CC COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:83400; CC EC=2.7.7.48; Evidence={ECO:0000256|SAAS:SAAS01198479}; CC -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum CC {ECO:0000256|SAAS:SAAS01209087}. Virion membrane CC {ECO:0000256|SAAS:SAAS01195842}; Multi-pass membrane protein CC {ECO:0000256|SAAS:SAAS01195842}. 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; DQ859059; ABI54475.1; -; Genomic_RNA. DR MEROPS; S07.003; -. DR Proteomes; UP000180703; Genome. DR GO; GO:0044165; C:host cell endoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-KW. 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:InterPro. DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 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:InterPro. DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:InterPro. DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro. DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC. DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. 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:0039503; P:suppression by virus of host innate immune response; 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; 1.10.10.930; -; 1. DR Gene3D; 1.10.8.970; -; 1. DR Gene3D; 1.20.1280.260; -; 1. DR Gene3D; 2.60.260.50; -; 1. DR Gene3D; 2.60.40.350; -; 1. DR Gene3D; 2.60.98.10; -; 1. DR Gene3D; 3.30.387.10; -; 1. DR Gene3D; 3.30.67.10; -; 1. DR InterPro; IPR011492; DEAD_Flavivir. DR InterPro; IPR000069; Env_glycoprot_M_flavivir. DR InterPro; IPR038302; Env_glycoprot_M_sf_flavivir. DR InterPro; IPR013755; Flav_gly_cen_dom_subdom1. DR InterPro; IPR001122; Flavi_capsidC. DR InterPro; IPR037172; Flavi_capsidC_sf. DR InterPro; IPR027287; Flavi_E_Ig-like. DR InterPro; IPR026470; Flavi_E_Stem/Anchor_dom. DR InterPro; IPR038345; Flavi_E_Stem/Anchor_dom_sf. 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; IPR038688; Flavi_propep_sf. DR InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf. DR InterPro; IPR001850; Flavivirus_NS3_S7. DR InterPro; IPR014412; Gen_Poly_FLV. DR InterPro; IPR011998; Glycoprot_cen/dimer. DR InterPro; IPR036253; Glycoprot_cen/dimer_sf. DR InterPro; IPR038055; Glycoprot_E_dimer_dom. DR InterPro; IPR013756; GlyE_cen_dom_subdom2. 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; SSF101257; SSF101257; 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 4: Predicted; KW Activation of host autophagy by virus {ECO:0000256|SAAS:SAAS00291633}; KW ATP-binding {ECO:0000256|SAAS:SAAS01198603}; KW Capsid protein {ECO:0000256|SAAS:SAAS01208933}; KW Disulfide bond {ECO:0000256|PIRSR:PIRSR003817-3, KW ECO:0000256|SAAS:SAAS01200326}; KW Fusion of virus membrane with host endosomal membrane KW {ECO:0000256|SAAS:SAAS01200298}; KW Fusion of virus membrane with host membrane KW {ECO:0000256|SAAS:SAAS01200343}; Helicase {ECO:0000256|SAAS:SAAS01209034}; KW Host membrane {ECO:0000256|SAAS:SAAS00291629}; KW Host-virus interaction {ECO:0000256|SAAS:SAAS00291630}; KW Hydrolase {ECO:0000256|SAAS:SAAS01198589}; KW Inhibition of host innate immune response by virus KW {ECO:0000256|SAAS:SAAS00910833}; KW Membrane {ECO:0000256|SAAS:SAAS00291489, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR003817-4, KW ECO:0000256|SAAS:SAAS01198594}; KW Methyltransferase {ECO:0000256|SAAS:SAAS01198504}; KW mRNA capping {ECO:0000256|SAAS:SAAS01198443}; KW mRNA processing {ECO:0000256|SAAS:SAAS01198505}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS01198580}; KW Nucleotidyltransferase {ECO:0000256|SAAS:SAAS01198562}; KW Protease {ECO:0000256|SAAS:SAAS01200356}; KW RNA-binding {ECO:0000256|SAAS:SAAS01198501}; KW RNA-directed RNA polymerase {ECO:0000256|SAAS:SAAS01198530}; KW S-adenosyl-L-methionine {ECO:0000256|SAAS:SAAS01198586}; KW Serine protease {ECO:0000256|SAAS:SAAS01200312}; KW Transferase {ECO:0000256|SAAS:SAAS01198537}; KW Transmembrane {ECO:0000256|SAAS:SAAS00291514, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00291474, KW ECO:0000256|SAM:Phobius}; KW Viral attachment to host cell {ECO:0000256|SAAS:SAAS00291492}; KW Viral immunoevasion {ECO:0000256|SAAS:SAAS00910833}; KW Viral penetration into host cytoplasm {ECO:0000256|SAAS:SAAS01200338}; KW Viral RNA replication {ECO:0000256|SAAS:SAAS01198628}; KW Virion {ECO:0000256|SAAS:SAAS01197947}; KW Virus entry into host cell {ECO:0000256|SAAS:SAAS00291600}; KW Zinc {ECO:0000256|PIRSR:PIRSR003817-4}. FT TRANSMEM 250..269 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 275..295 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 740..761 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 767..792 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1172..1191 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1267..1284 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1337..1360 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1372..1388 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1394..1411 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1467..1490 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2168..2187 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2194..2210 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2216..2233 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2245..2263 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2300..2321 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2328..2347 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2367..2386 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2436..2456 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1367..1496 FT /note="FLAVIVIRUS_NS2B" FT /evidence="ECO:0000259|PROSITE:PS51527" FT DOMAIN 1497..1674 FT /note="Peptidase S7" FT /evidence="ECO:0000259|PROSITE:PS51528" FT DOMAIN 1677..1833 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51192" FT DOMAIN 1828..2007 FT /note="Helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51194" FT DOMAIN 2515..2779 FT /note="MRNA cap 0-1 NS5-type MT" FT /evidence="ECO:0000259|PROSITE:PS51591" FT DOMAIN 3043..3193 FT /note="RdRp catalytic" FT /evidence="ECO:0000259|PROSITE:PS50507" FT ACT_SITE 1547 FT /note="Charge relay system; for serine protease NS3 FT activity" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1" FT ACT_SITE 1571 FT /note="Charge relay system; for serine protease NS3 FT activity" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1" FT ACT_SITE 1631 FT /note="Charge relay system; for serine protease NS3 FT activity" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1" FT METAL 2953 FT /note="Zinc 1" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT METAL 2957 FT /note="Zinc 1; via tele nitrogen" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT METAL 2962 FT /note="Zinc 1" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT METAL 2965 FT /note="Zinc 1" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT METAL 3228 FT /note="Zinc 2; via tele nitrogen" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT METAL 3244 FT /note="Zinc 2" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT METAL 3363 FT /note="Zinc 2" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT BINDING 2570 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2600 FT /note="S-adenosyl-L-methionine; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2601 FT /note="S-adenosyl-L-methionine; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2618 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2619 FT /note="S-adenosyl-L-methionine; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2645 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2646 FT /note="S-adenosyl-L-methionine; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2734 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT DISULFID 293..320 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" FT DISULFID 350..406 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" FT DISULFID 364..395 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" FT DISULFID 382..411 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" FT DISULFID 474..575 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" FT DISULFID 592..623 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" SQ SEQUENCE 3417 AA; 378191 MW; 3B9B8F66DAA096F9 CRC64; MKNPKKKSGG FRIVNMLKRG VARVNPLGGL KRLPAGLLLG HGPIRMVLAI LAFLRFTAIK PSLGLINRWG TVGKKEAMEI IKKFKKDLAA MLRIINARKE RKRRGADTSI GIVGLLLTTA MAAEITRRGS AYYMYLDRSD AGKAISFATT LGVNKCHVQI MDLGHMCDAT MSYECPMLDE GVEPDDVDCW CNTTSTWVVY GTCHHKKGEA RRSRRAVTLP SHSTRKLQTR SQTWLESREY TKHLIKVENW IFRNPGFTLV AVAIAWLLGS STSQKVIYLV MILLIAPAYS IRCIGVSNRD FVEGMSGGTW VDVVLEHGGC VTVMAQDKPT VDIELVTTTV SNMAEVRSYC YEASISDMAS DSRCPTQGEA YLDKQSDTQY VCKRTLVDRG WGNGCGLFGK GSLVTCAKFT CSKKMTGKSI QPENLEYRIM LSVHGSQHSG MIVNDENRAK VEVTPNSPRA EATLGGFGSL GLDCEPRTGL DFSDLYYLTM NNKHWLVHKE WFHDIPLPWH AGADTGTPHW NNKEALVEFK DAHAKRQTVV VLGSQEGAVH TALAGALEAE MDGAKGRLFS GHLKCRLKMD KLRLKGVSYS LCTAAFTFTK VPAETLHGTV TVEVQYAGTD GPCKVPAQMA VDMQTLTPVG RLITANPVIT ESTENSKMML ELDPPFGDSY IVIGVGDKKI THHWHRSGST IGKAFEATVR GAKRMAVLGD TAWDFGSVGG VFNSLGKGIH QIFGAAFKSL FGGMSWFSQI LIGTLLVWLG LNTKNGSISL TCLALGGVMI FLSTAVSADV GCSVDFSKKE TRCGTGVFVY NDVEAWRDRY KYHPDSPRRL AAAVKQAWEE GICGISSVSR MENIMWKSVE GELNAILEEN GVQLTVVVGS VKNPMWRGPQ RLPVPVNELP HGWKAWGKSY FVRAAKTNNS FVVDGDTLKE CPLKHRAWNS FLVEDHGFGV FHTSVWLKVR EDYSLECDPA VIGTAVKGKE AAHSDLGYWI ESEKNDTWRL KRAHLIEMKT CEWPKSHTLW TDGVEESDLI IPKSLAGPLS HHNTREGYRT QVKGPWHSEE LEIRFEECPG TKVHVEETCG TRGPSLRSTT ASGRVIEEWC CRECTMPPLS FRAKDGCWYG MEIRPRKEPE SNLVRSMVTA GSTDHMDHFS LGVLVILLMV QEGLKKRMTT KIIMSTSMAV LVAMILGGFS MSDLAKLVIL MGATFAEMNT GGDVAHLALV AAFKVRPALL VSFIFRANWT PRESMLLALA SCLLQTAISA LEGDLMVLVN GFALAWLAIR AMAVPRTDNI ALAILAALTP LARGTLLVAW RAGLATCGGF MLLSLKGKGS VKKNLPFVAA LGLTAVRIVD PINVVGLLLL TRSGKRSWPP SEVLTAVGLI CALAGGFAKA DIEMAGPMAA VGLLIVSYVV SGKSVDMYIE RAGDITWEKD AEVTGNSPRL DVALDESGDF SLVEEDGPPM REIILKVVLM AICGMNPIAI PFAAGAWYVY VKTGKRSGAL WDVPAPKEVK KGETTDGVYR VMTRRLLGST QVGVGVMQEG VFHTMWHVTK GAALRSGEGR LDPYWGDVKQ DLVSYCGPWK LDAAWDGVSE VQLLAVPPGE RARNIQTLPG IFKTKDGDIG AVALDYPAGT SGSPILDKCG RVIGLYGNGV VIKNGSYVSA ITQGKREEET PVECFEPSML KKKQLTVLDL HPGAGKTRRV LPEIVREAIK KRLRTVILAP TRVVAAEMEE ALRGLPVRYM TTAVKVTHSG TEIVDLMCHA TFTSRLLQPI RVPNYNLYIM DEAHFTDPSS IAARGYISTR VEMGEAAAIF MTATPPGTRD AFPDSNSPIM DTEVEVPERA WSSGFDWVTD HSGKTVWFVP SVRNGNEIAA CLTKAGKRVI QLSRKTFETE FQKTKNQEWD FVITTDISEM GANFKADRVI DSRRCLKPVI LDGERVILAG PMPVTHASAA QRRGRIGRNP NKPGDEYMYG GGCAETDEDH AHWLEARMLL DNIYLQDGLI ASLYRPEADK VAAIEGEFKL RTEQRKTFVE LMKRGDLPVW LAYQVASAGI TYTDRRWCFD GTTNNTIMED SVPAEVWTKY GEKRVLKPRW MDARVCSDHA ALKSFKEFAA GKRGAALGVM EALGTLPGHM TERFQEAIDN LAVLMRAETG SRPYKAAAAQ LPETLETIML LGLLGTVSLG IFFVLMRNKG IGKMGFEMVT LGASAWLMWL SEIEPARIAC VLIVVFLLLV VLIPEPEKQR SPQDNQMAII IMVAVGLLGL ITANELGWLE RTKNDIAHLM GKREEGTTVG FSMDIDLRPA SAWAIYAALT TLITPAVQHA VTTSYNNYSL MAMATQAGVL FGMGKGMPFY AWDLGVPLLM MGCYSQLTPL TLIVAIILLV AHYMYLIPGL QAAAARAAQK RTAAGIMKNP VVDGIVVTDI DTMTIDPQVE KKMGQVLLIA VAVSSAVLLR TAWGWGEAGA LITAATSTLW EGSPNKYWNS STATSLCNIF RGSYLAGASL IYTVTRNAGL VKRRGGGTGE TLGEKWKARL NQMSALEFYS YKKSGITEVC REEARRALKD GVATGGHAVS RGSAKLRWLV ERGYLQPYGK VVDLGCGRGG WSYYAATIRK VQEVRGYTKG GPGHEEPMLV QSYGWNIIRL KSGVDVFHMA AESCDTLLCD IGESSSSPEV EETRTLRVLS MVGDWLEKRP GAFCIKVLCP YTSTMMETME RLQRRYGGGL VRVPLSRNST HEMYWVSGAK SNIIKSVSTT SQLLLGRMDG PRRPVKYEED VNLGSGTRAV ASCAEAPNMK VIGRRIERIR SEHAETWFFD ENHPYRTWAY HGSYEAPTQG SASSLVNGVV RLLSKPWDVV TGVTGIAMTD TTPYGQQRVF KEKVDTRVPD PQEGTRQVMN MVASWLWKEL GKRKRPRVCT KEEFINKVRS NAALGAIFEE EKEWKTAVEA VNDPRFWALV DKEREHHLRG ECHSCVYNMM GKREKKQGEF GKAKGSRAIW YMWLGARFLE FEALGFLNED HWMGRENSGG GVEGLGLQRL GYVLEEMSRA PGGKMYADDT AGWDTRISKF DLENEALITN QMDEGHRTLA LAVIKYTYQN KVVKVLRPAE GGKTVMDIIS RQDQRGSGQV VTYALNTFTN LVVQLIRNME AEEVLEMQDL WLLRKPEKVT RWLQSSGWDR LKRMAVSGDD CVVKPIDDRF AHALRFLNDM GKVRKDTQEW KPSTGWSNWE EVPFCSHHFN KLHLKDGRSI VVPCRHQDEL IGRARVSPGA GWSIRETACL AKSYAQMWQL LYFHRRDLRL MANAICSAVP VDWVPTGRTT WSIHGKGEWM TTEDMLMVWN RVWIEENDHM EDKTPVTKWT DIPYLGKRED LWCGSLIGHR PRTTWAENIK DTVSMVRRII GDEEKYMDYL STQVRYLGEE GSTPGVL //