ID POLG_EC11G Reviewed; 2195 AA. AC P29813; Q66785; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 19-MAR-2014, entry version 130. DE RecName: Full=Genome polyprotein; DE Contains: DE RecName: Full=Protein VP0; DE AltName: Full=VP4-VP2; DE Contains: DE RecName: Full=Protein VP4; DE AltName: Full=P1A; DE AltName: Full=Virion protein 4; DE Contains: DE RecName: Full=Protein VP2; DE AltName: Full=P1B; DE AltName: Full=Virion protein 2; DE Contains: DE RecName: Full=Protein VP3; DE AltName: Full=P1C; DE AltName: Full=Virion protein 3; DE Contains: DE RecName: Full=Protein VP1; DE AltName: Full=P1D; DE AltName: Full=Virion protein 1; DE Contains: DE RecName: Full=Protease 2A; DE Short=P2A; DE EC=3.4.22.29; DE AltName: Full=Protein 2A; DE Contains: DE RecName: Full=Protein 2B; DE Short=P2B; DE Contains: DE RecName: Full=Protein 2C; DE Short=P2C; DE EC=3.6.1.15; DE Contains: DE RecName: Full=Protein 3A; DE Short=P3A; DE Contains: DE RecName: Full=Protein 3B; DE Short=P3B; DE AltName: Full=VPg; DE Contains: DE RecName: Full=Protease 3C; DE Short=P3C; DE EC=3.4.22.28; DE AltName: Full=Picornain 3C; DE Contains: DE RecName: Full=RNA-directed RNA polymerase 3D-POL; DE Short=P3D-POL; DE EC=2.7.7.48; OS Echovirus 11 (strain Gregory). OC Viruses; ssRNA positive-strand viruses, no DNA stage; Picornavirales; OC Picornaviridae; Enterovirus; Enterovirus B. OX NCBI_TaxID=31705; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=7762294; DOI=10.1016/0168-1702(94)00104-K; RA Dahllund L., Nissinen L., Pulli T., Hyttinen V.P., Stanway G., RA Hyypiae T.; RT "The genome of echovirus 11."; RL Virus Res. 35:215-222(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 822-2195. RX PubMed=2170575; RA Auvinen P., Hyypiae T.; RT "Echoviruses include genetically distinct serotypes."; RL J. Gen. Virol. 71:2133-2139(1990). RN [3] RP INTERACTION WITH HOST CD55. RX PubMed=7517044; DOI=10.1073/pnas.91.13.6245; RA Bergelson J.M., Chan M., Solomon K.R., St John N.F., Lin H., RA Finberg R.W.; RT "Decay-accelerating factor (CD55), a glycosylphosphatidylinositol- RT anchored complement regulatory protein, is a receptor for several RT echoviruses."; RL Proc. Natl. Acad. Sci. U.S.A. 91:6245-6248(1994). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-859. RC STRAIN=Isolate clinical EV11-207; RX PubMed=12097583; DOI=10.1128/JVI.76.15.7694-7704.2002; RA Stuart A.D., McKee T.A., Williams P.A., Harley C., Shen S., RA Stuart D.I., Brown T.D., Lea S.M.; RT "Determination of the structure of a decay accelerating factor-binding RT clinical isolate of echovirus 11 allows mapping of mutants with RT altered receptor requirements for infection."; RL J. Virol. 76:7694-7704(2002). CC -!- FUNCTION: Protein VP1: Forms, together with VP2 and VP3, an CC icosahedral capsid (pseudo T=3), 300 Angstroms in diameter, CC composed of 60 copies of each capsid protein and enclosing the CC viral positive strand RNA genome. Protein VP1 mainly forms the CC vertices of the capsid. VP1 interacts with host cell receptor to CC provide virion attachment to target cell. After binding to its CC receptor, the capsid undergoes conformational changes. VP1 N- CC terminus (that contains an amphipathic alpha-helix) is CC externalized, VP4 is released and together, they shape a virion- CC cell connecting channel and a pore in the host membrane through CC which RNase-protected transfer of the viral genome takes place. CC After genome has been released, the channel shrinks (By CC similarity). CC -!- FUNCTION: Protein VP2: Forms, together with VP1 and VP3, an CC icosahedral capsid (pseudo T=3), 300 Angstroms in diameter, CC composed of 60 copies of each capsid protein and enclosing the CC viral positive strand RNA genome (By similarity). CC -!- FUNCTION: Protein VP3: Forms, together with VP1 and VP2, an CC icosahedral capsid (pseudo T=3), 300 Angstroms in diameter, CC composed of 60 copies of each capsid protein and enclosing the CC viral positive strand RNA genome (By similarity). CC -!- FUNCTION: Protein VP4: Lies on the inner surface of the capsid CC shell. After binding to the host receptor, the capsid undergoes CC conformational changes. VP4 is released, VP1 N-terminus is CC externalized, and together, they shape a virion-cell connecting CC channel and a pore in the host membrane through which RNase- CC protected transfer of the viral genome takes place. After genome CC has been released, the channel shrinks (By similarity). CC -!- FUNCTION: Protein VP0: Protein VP0: VP0 precursor is a component CC of immature procapsids, which gives rise to VP4 and VP2 after CC maturation. Allows the capsid to remain inactive before the CC maturation step (By similarity). CC -!- FUNCTION: Protease 2A: cysteine protease that is responsible for CC the cleavage between the P1 and P2 regions. It cleaves the host CC translation initiation factor EIF4G1, in order to shut off the CC capped cellular mRNA transcription (By similarity). CC -!- FUNCTION: Protein 2B: Affects membrane integrity and cause an CC increase in membrane permeability (By similarity). CC -!- FUNCTION: Protein 2C: Associates with and induces structural CC rearrangements of intracellular membranes. It displays RNA- CC binding, nucleotide binding and NTPase activities (By similarity). CC -!- FUNCTION: Protein 3A, via its hydrophobic domain, serves as CC membrane anchor. It also inhibits endoplasmic reticulum-to-Golgi CC transport (By similarity). CC -!- FUNCTION: Protease 3C: cysteine protease that generates mature CC viral proteins from the precursor polyprotein. In addition to its CC proteolytic activity, it binds to viral RNA, and thus influences CC viral genome replication. RNA and substrate bind cooperatively to CC the protease (By similarity). CC -!- FUNCTION: RNA-directed RNA polymerase 3D-POL replicates genomic CC and antigenomic RNA by recognizing replications specific signals CC (By similarity). CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). CC -!- CATALYTIC ACTIVITY: Selective cleavage of Tyr-|-Gly bond in the CC picornavirus polyprotein. CC -!- CATALYTIC ACTIVITY: Selective cleavage of Gln-|-Gly bond in the CC poliovirus polyprotein. In other picornavirus reactions Glu may be CC substituted for Gln, and Ser or Thr for Gly. CC -!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate. CC -!- SUBUNIT: Capsid proteins interact with host CD55. CC -!- SUBCELLULAR LOCATION: Protein VP2: Virion. Host cytoplasm CC (Potential). CC -!- SUBCELLULAR LOCATION: Protein VP3: Virion. Host cytoplasm CC (Potential). CC -!- SUBCELLULAR LOCATION: Protein VP1: Virion. Host cytoplasm CC (Potential). CC -!- SUBCELLULAR LOCATION: Protein 2B: Host cytoplasmic vesicle CC membrane; Peripheral membrane protein; Cytoplasmic side CC (Potential). Note=Probably localizes to the surface of CC intracellular membrane vesicles that are induced after virus CC infection as the site for viral RNA replication. These vesicles CC are derived from the endoplasmic reticulum (By similarity). CC -!- SUBCELLULAR LOCATION: Protein 2C: Host cytoplasmic vesicle CC membrane; Peripheral membrane protein; Cytoplasmic side CC (Potential). Note=Probably localizes to the surface of CC intracellular membrane vesicles that are induced after virus CC infection as the site for viral RNA replication. These vesicles CC are derived from the endoplasmic reticulum (By similarity). CC -!- SUBCELLULAR LOCATION: Protein 3A: Host cytoplasmic vesicle CC membrane; Peripheral membrane protein; Cytoplasmic side CC (Potential). Note=Probably localizes to the surface of CC intracellular membrane vesicles that are induced after virus CC infection as the site for viral RNA replication. These vesicles CC are derived from the endoplasmic reticulum (By similarity). CC -!- SUBCELLULAR LOCATION: Protein 3B: Virion (Potential). CC -!- SUBCELLULAR LOCATION: Protease 3C: Host cytoplasm (Potential). CC -!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase 3D-POL: Host CC cytoplasmic vesicle membrane; Peripheral membrane protein; CC Cytoplasmic side (Potential). Note=Probably localizes to the CC surface of intracellular membrane vesicles that are induced after CC virus infection as the site for viral RNA replication. These CC vesicles are derived from the endoplasmic reticulum (By CC similarity). CC -!- PTM: Specific enzymatic cleavages in vivo by the viral proteases CC yield a variety of precursors and mature proteins. Polyprotein CC processing intermediates such as VP0 which is a VP4-VP2 precursor CC are produced. During virion maturation, non-infectious particles CC are rendered infectious following cleavage of VP0. This maturation CC cleavage is followed by a conformational change of the particle CC (By similarity). CC -!- PTM: VPg is uridylylated by the polymerase and is covalently CC linked to the 5'-end of genomic RNA. This uridylylated form acts CC as a nucleotide-peptide primer for the polymerase (By similarity). CC -!- PTM: Myristoylation of VP4 is required during RNA encapsidation CC and formation of the mature virus particle (By similarity). CC -!- SIMILARITY: Belongs to the picornaviruses polyprotein family. CC -!- SIMILARITY: Contains 2 peptidase C3 domains. CC -!- SIMILARITY: Contains 1 RdRp catalytic domain. CC -!- SIMILARITY: Contains 1 SF3 helicase domain. CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral CC capsid structure; CC URL="http://viperdb.scripps.edu/info_page.php?VDB=1h8t"; 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; X80059; CAA56365.1; -; Genomic_RNA. DR EMBL; D10582; BAA01439.1; -; Genomic_RNA. DR PIR; A36642; GNNYEC. DR PDB; 2C8I; EM; 14.00 A; A=570-857, B=79-328, C=332-569, D=2-69. DR PDBsum; 2C8I; -. DR ProteinModelPortal; P29813; -. DR SMR; P29813; 2-69, 79-330, 332-858, 862-1011, 1551-2195. DR MEROPS; C03.011; -. DR PRIDE; P29813; -. DR EvolutionaryTrace; P29813; -. DR GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. 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:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW. DR GO; GO:0034220; P:ion transmembrane transport; IEA:GOC. DR GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW. DR GO; GO:0044694; P:pore-mediated entry of viral genome into host cell; IEA:UniProtKB-KW. DR GO; GO:0051259; P:protein oligomerization; IEA:UniProtKB-KW. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW. DR GO; GO:0039540; P:suppression by virus of host RIG-I activity; IEA:UniProtKB-KW. DR GO; GO:0039604; P:suppression by virus of host translation; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro. DR GO; GO:0001172; P:transcription, RNA-templated; IEA:GOC. DR GO; GO:0019079; P:viral genome replication; IEA:InterPro. DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW. DR Gene3D; 4.10.80.10; -; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir. DR InterPro; IPR014759; Helicase_SF3_ssRNA_vir. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR014838; P3A. DR InterPro; IPR000081; Peptidase_C3. DR InterPro; IPR000199; Peptidase_C3A/C3B_picornavir. DR InterPro; IPR003138; Pico_P1A. DR InterPro; IPR002527; Pico_P2B. DR InterPro; IPR001676; Picornavirus_capsid. DR InterPro; IPR001205; RNA-dir_pol_C. DR InterPro; IPR007094; RNA-dir_pol_PSvirus. DR InterPro; IPR009003; Trypsin-like_Pept_dom. DR Pfam; PF08727; P3A; 1. DR Pfam; PF00548; Peptidase_C3; 1. DR Pfam; PF02226; Pico_P1A; 1. DR Pfam; PF00947; Pico_P2A; 1. DR Pfam; PF01552; Pico_P2B; 1. DR Pfam; PF00680; RdRP_1; 1. DR Pfam; PF00073; Rhv; 3. DR Pfam; PF00910; RNA_helicase; 1. DR ProDom; PD001306; Peptidase_C3; 1. DR ProDom; PD649346; Pico_P2B; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF50494; SSF50494; 2. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF89043; SSF89043; 1. DR PROSITE; PS50507; RDRP_SSRNA_POS; 1. DR PROSITE; PS51218; SF3_HELICASE_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Activation of host autophagy by virus; ATP-binding; KW Capsid protein; Complete proteome; Covalent protein-RNA linkage; KW Helicase; Host cytoplasm; Host cytoplasmic vesicle; KW Host gene expression shutoff by virus; Host membrane; KW Host translation shutoff by virus; Host-virus interaction; Hydrolase; KW Inhibition of host innate immune response by virus; KW Inhibition of host RIG-I by virus; KW Inhibition of host RLR pathway by virus; Ion channel; Ion transport; KW Lipoprotein; Membrane; Myristate; Nucleotide-binding; KW Nucleotidyltransferase; Phosphoprotein; KW Pore-mediated penetration of viral genome into host cell; Protease; KW RNA-binding; RNA-directed RNA polymerase; Thiol protease; Transferase; KW Transport; Viral attachment to host cell; Viral immunoevasion; KW Viral ion channel; Viral penetration into host cytoplasm; KW Viral RNA replication; Virion; Virus entry into host cell. FT INIT_MET 1 1 Removed; by host (By similarity). FT CHAIN 2 331 Protein VP0 (Potential). FT /FTId=PRO_0000311058. FT CHAIN 2 69 Protein VP4 (Potential). FT /FTId=PRO_0000039703. FT CHAIN 70 331 Protein VP2 (Potential). FT /FTId=PRO_0000039704. FT CHAIN 332 569 Protein VP3 (Potential). FT /FTId=PRO_0000039705. FT CHAIN 570 861 Protein VP1 (Potential). FT /FTId=PRO_0000039706. FT CHAIN 862 1011 Protease 2A (Potential). FT /FTId=PRO_0000039707. FT CHAIN 1012 1110 Protein 2B (Potential). FT /FTId=PRO_0000039708. FT CHAIN 1111 1439 Protein 2C (Potential). FT /FTId=PRO_0000039709. FT CHAIN 1440 1528 Protein 3A (Potential). FT /FTId=PRO_0000039710. FT CHAIN 1529 1550 Protein 3B (Potential). FT /FTId=PRO_0000039711. FT CHAIN 1551 1733 Protease 3C (Potential). FT /FTId=PRO_0000039712. FT CHAIN 1734 2195 RNA-directed RNA polymerase 3D-POL FT (Potential). FT /FTId=PRO_0000039713. FT TOPO_DOM 2 1505 Cytoplasmic (Potential). FT INTRAMEM 1506 1521 Potential. FT TOPO_DOM 1522 2195 Cytoplasmic (Potential). FT DOMAIN 1215 1371 SF3 helicase. FT DOMAIN 1960 2076 RdRp catalytic. FT NP_BIND 1239 1246 ATP (Potential). FT ACT_SITE 882 882 For protease 2A activity (By similarity). FT ACT_SITE 900 900 For protease 2A activity (By similarity). FT ACT_SITE 971 971 For protease 2A activity (By similarity). FT ACT_SITE 1590 1590 For protease 3C activity (Potential). FT ACT_SITE 1621 1621 For protease 3C activity (Potential). FT ACT_SITE 1697 1697 For protease 3C activity (By similarity). FT SITE 69 70 Cleavage (Potential). FT SITE 331 332 Cleavage; by protease 3C (Potential). FT SITE 861 862 Cleavage; by protease 2A (Potential). FT SITE 1011 1012 Cleavage; by protease 3C (Potential). FT SITE 1110 1111 Cleavage; by protease 3C (Potential). FT SITE 1439 1440 Cleavage; by protease 3C (Potential). FT SITE 1528 1529 Cleavage; by protease 3C (Potential). FT SITE 1550 1551 Cleavage; by protease 3C (Potential). FT SITE 1733 1734 Cleavage; by protease 3C (Potential). FT MOD_RES 1531 1531 O-(5'-phospho-RNA)-tyrosine (By FT similarity). FT LIPID 2 2 N-myristoyl glycine; by host (By FT similarity). FT CONFLICT 823 827 RLCQY -> SYANT (in Ref. 2; BAA01439). FT STRAND 4 7 FT STRAND 25 29 FT HELIX 36 38 FT HELIX 50 52 FT STRAND 57 59 FT STRAND 63 65 FT STRAND 83 87 FT STRAND 90 96 FT STRAND 100 102 FT TURN 113 115 FT HELIX 126 128 FT STRAND 138 140 FT STRAND 147 152 FT HELIX 159 167 FT STRAND 168 180 FT STRAND 188 197 FT STRAND 203 205 FT HELIX 212 215 FT STRAND 218 220 FT STRAND 225 227 FT STRAND 231 235 FT HELIX 239 241 FT TURN 242 244 FT HELIX 248 253 FT STRAND 254 260 FT TURN 261 263 FT STRAND 265 271 FT STRAND 276 278 FT TURN 282 284 FT STRAND 288 299 FT STRAND 308 324 FT TURN 339 342 FT STRAND 354 356 FT HELIX 374 378 FT HELIX 396 399 FT STRAND 401 407 FT STRAND 414 417 FT TURN 420 422 FT HELIX 424 427 FT HELIX 430 435 FT STRAND 438 442 FT STRAND 445 451 FT STRAND 458 466 FT STRAND 468 470 FT HELIX 476 479 FT STRAND 482 488 FT STRAND 490 492 FT STRAND 494 499 FT STRAND 504 506 FT STRAND 508 511 FT STRAND 520 530 FT STRAND 537 547 FT STRAND 552 556 FT STRAND 565 567 FT HELIX 603 605 FT HELIX 613 616 FT HELIX 629 631 FT HELIX 633 637 FT STRAND 641 651 FT STRAND 653 655 FT HELIX 656 658 FT STRAND 659 663 FT HELIX 670 676 FT STRAND 679 696 FT STRAND 710 716 FT HELIX 729 732 FT STRAND 734 736 FT STRAND 738 742 FT STRAND 749 752 FT STRAND 757 763 FT STRAND 767 770 FT HELIX 779 782 FT STRAND 787 794 FT STRAND 801 819 FT STRAND 854 856 SQ SEQUENCE 2195 AA; 245407 MW; 1CFC5DF288831AF0 CRC64; MGAQVSTQKT GAHETGLNAS GSSIIHYTNI NYYKDAASNS ANRQEFSQDP GKFTEPVKDI MVKSLPALNS PSAEECGYSD RVRSITLGNS TITTQESANV VVGYGRWPEY LKDNEATAED QPTQPDVATC RFYTLESVTW ERDSPGWWWK FPDALKDMGL FGQNMYYHYL GRAGYTLHVQ CNASKFHQGC LLVVCVPEAE MGCSQVDGTV NEHGLSEGET AKKFSSTSTN GTNTVQTIVT NAGMGVGVGN LTIYPHQWIN LRTNNCATIV MPYINNVPMD NMFRHHNFTL MIIPFVPLDY SSDSSTYVPI TVTVAPMCAE YNGLRLSTSL QGLPVMNTPG SNQFLTSDDF QSPSAMPQFD VTPELNIPGE VQNLMEIAEV DSVVPVNNVE GKLDTMEVYR IPVQSGNHQS DQVFGFQVQP GLDSVFKHTL LGEILNYFAH WSGSIKLTFV FCGSAMATGK FLLAYAPPGA NAPKNRKDAM LGTHIIWDVG LQSSCVLCVP WISQTHYRLV QQDEYTSAGN VTCWYQTGIV VPAGTPTSCS IMCFVSACND FSVRLLKDTP FIEQTALLQG DVVEAVENAV ARVADTIGSG PSNSQAVPAL TAVETGHTSQ VTPSDTMQTR HVKNYHSRSE SSIENFLSRS ACVYMGGYHT TNTDQTKLFA SWTISARRMV QMRRKLEIFT YVRFDVEVTF VITSKQDQGS RLGQDMPPLT HQIMYIPPGG PIPKSVTDYA WQTSTNPSIF WTEGNAPPRM SIPFISIGNA YSNFYDGWSH FSQNGVYGYN TLNHMGQIYV RHVNGSSPLP MTSTVRMYFK PKHVKAWVPR PPRLCQYKNA STVNFTPTNV TDKRTSINYI PETVKPDLSN YGAFGYQSGA VYVVNYRVVN RHLATHTDWQ NCVWEDYNRD LLISTTTAHG CDVIARCRCS TGVYYCQSKG KHYPVNFEGP GLVEVQESEY YPKRYQSHVL LAAGFSEPGD CGGILRCEHG VIGIVTMGGE GVVGFADVRD LLWLEDDAME QGVKDYVEQL GNAFGSGFTN QICEQVNLLK ESLVGQDSIL EKSLKALVKI ISALVIVVRN HDDLITVTAT LALIGCTSSP WRWLKQKVSQ YYGIPMAERQ NNGWLKKFTE MTNSCKGMEW ISIKIQKFIE WLKVKILPEV REKHEFLNRL KQLPLLESQI ATIEQSAPSQ SDQEQLFSNV QYFAHYCRKY APLYASEAKR VFSLEKKMSN YIQFKSKCRI EPVCLLLHGS PGAGKSVATN LIGRSLAEKL NSSVYTLPPD PDHFDGYKQQ AVVIVDDLCQ NPDGKDVSLF CQMVSSVDFV PPMAALEEKG ILFTSLFVLA STNAGSINAP TVSDSRALAR RFHFDMNIEV ISMYSQNGKI NMPMSEKTCD EECCPVNFKR CCPLVCGKAI QFIDRRTQVR YSLDMLVTEM FREYNHRHSV GATLEALFQG PPIYREIKIS VAPETPPPPA IADLLKSVDS EAVREYCKEK GWLVPEVNST LQIEKHVSRA FICLQALTTF VSVAGIIYII YKLFAGFQGA YTGMPNQKPK VPTLRQAKVQ GPAFEFAVAM MKRNSSTVKT EYREFTMLGI YDRWAVLPRH AKPGPTILMN NQEVGVLDAK ELVDKDGTNL ELTLLKLNRN EKFRDIRGFL AKEEVEANQA VLAINTSKFP NMYIPVGQVT DYGFLNLGGT PTKRMLMSNF PTRAGQCGGV LMSTGKVLGI HVGGNGHQGF SAALLKHYFN DEQGEIEFIE SSKDAGFPII NTPSKTKLEP SVFHQVFEGD KEPAVLRNGD PRLKANFEEA IFSKYIGNVN THVDEYMLEA VDHYAGQLAT LDISTEPMRL EDAVYGTEGL EALDLTTSAG YPYVALGIKK RDILSRRTRD LTKLKECMDK YGLNLPMVTY VKDELRSADK VAKGKSRLIE ASSLNDSVAM RQTFGNLYRT FHLNPGIVTG SAVGCDPDLF WSKIPVMLDG HLIAFDYSGY DASLSPVWFA CLKLLLEKLG YTHKETNYID YLCNSHHLYR DKHYFERGGM PSGYSGTSMF NSMINNIIIR TLMLKVYKGI DLDQFRMIAY GDDVIASYPW PIDASLLAET GKGYGLIMTP ADKGECFNEV TWTNVTFLKR YFRADEQYPF LVHPVMPMKD IHESIRWTKD PKNTQDHVRS LCLLAWHNGE HEYEEFIRKI RSVPVGRCLT LPAFSTLRRK WLDSF //