ID C6EN30_9ENTO Unreviewed; 2208 AA. AC C6EN30; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 26-FEB-2020, entry version 76. DE RecName: Full=Genome polyprotein {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=P3 {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Protein 3AB {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=P2 {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=P1 {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Capsid protein VP0 {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=VP4-VP2 {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Capsid protein VP4 {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=P1A {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=Virion protein 4 {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Capsid protein VP2 {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=P1B {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=Virion protein 2 {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Capsid protein VP3 {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=P1C {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=Virion protein 3 {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Capsid protein VP1 {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=P1D {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=Virion protein 1 {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Protease 2A {ECO:0000256|RuleBase:RU364118}; DE Short=P2A {ECO:0000256|RuleBase:RU364118}; DE EC=3.4.22.29 {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=Picornain 2A {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=Protein 2A {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Protein 2B {ECO:0000256|RuleBase:RU364118}; DE Short=P2B {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Protein 2C {ECO:0000256|RuleBase:RU364118}; DE Short=P2C {ECO:0000256|RuleBase:RU364118}; DE EC=3.6.1.15 {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Protein 3A {ECO:0000256|RuleBase:RU364118}; DE Short=P3A {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Viral protein genome-linked {ECO:0000256|RuleBase:RU364118}; DE Short=VPg {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=Protein 3B {ECO:0000256|RuleBase:RU364118}; DE Short=P3B {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Protein 3CD {ECO:0000256|RuleBase:RU364118}; DE EC=3.4.22.28 {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Protease 3C {ECO:0000256|RuleBase:RU364118}; DE Short=P3C {ECO:0000256|RuleBase:RU364118}; DE EC=3.4.22.28 {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=RNA-directed RNA polymerase {ECO:0000256|RuleBase:RU364118}; DE Short=RdRp {ECO:0000256|RuleBase:RU364118}; DE EC=2.7.7.48 {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=3D polymerase {ECO:0000256|RuleBase:RU364118}; DE Short=3Dpol {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=Protein 3D {ECO:0000256|RuleBase:RU364118}; DE Short=3D {ECO:0000256|RuleBase:RU364118}; OS Coxsackievirus A20. OC Viruses; Riboviria; Picornavirales; Picornaviridae; Enterovirus; OC Enterovirus C. OX NCBI_TaxID=42782 {ECO:0000313|EMBL:ABM54527.1, ECO:0000313|Proteomes:UP000126220}; RN [1] {ECO:0000313|EMBL:ABM54527.1, ECO:0000313|Proteomes:UP000126220} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BAN00-10538 {ECO:0000313|EMBL:ABM54527.1}; RX PubMed=19264596; DOI=10.1099/vir.0.008540-0; RA Brown B.A., Maher K., Flemister M.R., Naraghi-Arani P., Uddin M., RA Oberste M.S., Pallansch M.A.; RT "Resolving ambiguities in genetic typing of human enterovirus species C RT clinical isolates and identification of enterovirus 96, 99 and 102."; RL J. Gen. Virol. 90:1713-1723(2009). CC -!- FUNCTION: Capsid protein VP0: Component of immature procapsids, which CC is cleaved into capsid proteins VP4 and VP2 after maturation. Allows CC the capsid to remain inactive before the maturation step. CC {ECO:0000256|RuleBase:RU364118}. CC -!- FUNCTION: Capsid protein VP1: Forms an icosahedral capsid of pseudo T=3 CC symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms CC in diameter, composed of 60 copies of each capsid protein and enclosing CC the viral positive strand RNA genome. Capsid protein VP1 mainly forms CC the vertices of the capsid. Capsid protein VP1 interacts with host cell CC receptor to provide virion attachment to target host cells. This CC attachment induces virion internalization. Tyrosine kinases are CC probably involved in the entry process. After binding to its receptor, CC the capsid undergoes conformational changes. Capsid protein VP1 N- CC terminus (that contains an amphipathic alpha-helix) and capsid protein CC VP4 are externalized. Together, they shape a pore in the host membrane CC through which viral genome is translocated to host cell cytoplasm. CC After genome has been released, the channel shrinks. CC {ECO:0000256|RuleBase:RU364118}. CC -!- FUNCTION: Capsid protein VP2: Forms an icosahedral capsid of pseudo T=3 CC symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms CC in diameter, composed of 60 copies of each capsid protein and enclosing CC the viral positive strand RNA genome. {ECO:0000256|RuleBase:RU364118}. CC -!- FUNCTION: Capsid protein VP3: Forms an icosahedral capsid of pseudo T=3 CC symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms CC in diameter, composed of 60 copies of each capsid protein and enclosing CC the viral positive strand RNA genome. {ECO:0000256|RuleBase:RU364118}. CC -!- FUNCTION: Capsid protein VP4: Lies on the inner surface of the capsid CC shell. After binding to the host receptor, the capsid undergoes CC conformational changes. Capsid protein VP4 is released, Capsid protein CC VP1 N-terminus is externalized, and together, they shape a pore in the CC host membrane through which the viral genome is translocated into the CC host cell cytoplasm. After genome has been released, the channel CC shrinks. {ECO:0000256|RuleBase:RU364118}. CC -!- FUNCTION: Protease 2A: Cysteine protease that cleaves viral polyprotein CC and specific host proteins. {ECO:0000256|RuleBase:RU364118}. CC -!- FUNCTION: Protease 3C: cleaves host DDX58/RIG-I and thus contributes to CC the inhibition of type I interferon production. Cleaves also host CC PABPC1. {ECO:0000256|RuleBase:RU364118}. CC -!- FUNCTION: Protein 2B: Plays an essential role in the virus replication CC cycle by acting as a viroporin. Creates a pore in the host reticulum CC endoplasmic and as a consequence releases Ca2+ in the cytoplasm of CC infected cell. In turn, high levels of cytoplasmic calcium may trigger CC membrane trafficking and transport of viral ER-associated proteins to CC viroplasms, sites of viral genome replication. CC {ECO:0000256|RuleBase:RU364118}. CC -!- FUNCTION: Protein 2C: Induces and associates with structural CC rearrangements of intracellular membranes. Displays RNA-binding, CC nucleotide binding and NTPase activities. May play a role in virion CC morphogenesis and viral RNA encapsidation by interacting with the CC capsid protein VP3. {ECO:0000256|RuleBase:RU364118}. CC -!- FUNCTION: Protein 3A: Localizes the viral replication complex to the CC surface of membranous vesicles. It inhibits host cell endoplasmic CC reticulum-to-Golgi apparatus transport and causes the dissassembly of CC the Golgi complex, possibly through GBF1 interaction. This would result CC in depletion of MHC, trail receptors and IFN receptors at the host cell CC surface. {ECO:0000256|RuleBase:RU364118}. CC -!- FUNCTION: Protein 3AB: Localizes the viral replication complex to the CC surface of membranous vesicles. Together with protein 3CD binds the CC Cis-Active RNA Element (CRE) which is involved in RNA synthesis CC initiation. Acts as a cofactor to stimulate the activity of 3D CC polymerase, maybe through a nucleid acid chaperone activity. CC {ECO:0000256|RuleBase:RU364118}. CC -!- FUNCTION: Protein 3CD: Is involved in the viral replication complex and CC viral polypeptide maturation. It exhibits protease activity with a CC specificity and catalytic efficiency that is different from protease CC 3C. Protein 3CD lacks polymerase activity. The 3C domain in the context CC of protein 3CD may have an RNA binding activity. CC {ECO:0000256|RuleBase:RU364118}. CC -!- FUNCTION: RNA-directed RNA polymerase: Replicates the viral genomic RNA CC on the surface of intracellular membranes. May form linear arrays of CC subunits that propagate along a strong head-to-tail interaction called CC interface-I. Covalently attaches UMP to a tyrosine of VPg, which is CC used to prime RNA synthesis. The positive stranded RNA genome is first CC replicated at virus induced membranous vesicles, creating a dsRNA CC genomic replication form. This dsRNA is then used as template to CC synthesize positive stranded RNA genomes. ss(+)RNA genomes are either CC translated, replicated or encapsidated. CC {ECO:0000256|RuleBase:RU364118}. CC -!- FUNCTION: Viral protein genome-linked: acts as a primer for viral RNA CC replication and remains covalently bound to viral genomic RNA. VPg is CC uridylylated prior to priming replication into VPg-pUpU. The oriI viral CC genomic sequence may act as a template for this. The VPg-pUpU is then CC used as primer on the genomic RNA poly(A) by the RNA-dependent RNA CC polymerase to replicate the viral genome. VPg may be removed in the CC cytoplasm by an unknown enzyme termed "unlinkase". VPg is not cleaved CC off virion genomes because replicated genomic RNA are encapsidated at CC the site of replication. {ECO:0000256|RuleBase:RU364118}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Selective cleavage of Gln-|-Gly bond in the poliovirus CC polyprotein. In other picornavirus reactions Glu may be substituted CC for Gln, and Ser or Thr for Gly.; EC=3.4.22.28; CC Evidence={ECO:0000256|RuleBase:RU364118, CC ECO:0000256|SAAS:SAAS01116669}; CC -!- CATALYTIC ACTIVITY: CC Reaction=Selective cleavage of Tyr-|-Gly bond in the picornavirus CC polyprotein.; EC=3.4.22.29; Evidence={ECO:0000256|RuleBase:RU364118}; 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|RuleBase:RU364118}; 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|RuleBase:RU364118, CC ECO:0000256|SAAS:SAAS01198479}; CC -!- SUBUNIT: Capsid protein VP1: Interacts with capsid protein VP0, and CC capsid protein VP3 to form heterotrimeric protomers. Five protomers CC subsequently associate to form pentamers which serve as building blocks CC for the capsid. Interacts with capsid protein VP4 in the mature capsid CC (By similarity). Capsid protein VP0: interacts with capsid protein VP1 CC and capsid protein VP3 to form heterotrimeric protomers. Five protomers CC subsequently associate to form pentamers which serve as building blocks CC for the capsid. Capsid protein VP2: Interacts with capsid protein VP1 CC and capsid protein VP3 in the mature capsid (By similarity). Capsid CC protein VP3: interacts with capsid protein VP0 and capsid protein VP1 CC to form heterotrimeric protomers. Five protomers subsequently associate CC to form pentamers which serve as building blocks for the capsid. CC Interacts with capsid protein VP4 in the mature capsid (By similarity). CC Capsid protein VP4: Interacts with capsid protein VP1 and capsid CC protein VP3 (By similarity). Protein 2C: interacts with capsid protein CC VP3; this interaction may be important for virion morphogenesis (By CC similarity). Protein 3AB: interacts with protein 3CD (By similarity). CC Viral protein genome-linked: interacts with RNA-directed RNA polymerase CC (By similarity). Protein 3CD: interacts with protein 3AB and with RNA- CC directed RNA polymerase. RNA-directed RNA polymerase: interacts with CC viral protein genome-linked and with protein 3CD. CC {ECO:0000256|RuleBase:RU364118}. CC -!- SUBCELLULAR LOCATION: Host cytoplasmic vesicle membrane CC {ECO:0000256|SAAS:SAAS00711512}; Peripheral membrane protein CC {ECO:0000256|SAAS:SAAS00711512}; Cytoplasmic side CC {ECO:0000256|SAAS:SAAS00711512}. Virion CC {ECO:0000256|SAAS:SAAS01196568}. CC -!- SIMILARITY: Belongs to the picornaviruses polyprotein family. CC {ECO:0000256|RuleBase:RU364118}. 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; EF015018; ABM54527.1; -; Genomic_RNA. DR MEROPS; C03.020; -. DR Proteomes; UP000126220; Genome. 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:0039618; C:T=pseudo3 icosahedral 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 5'-3' RNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-KW. DR GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW. 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 complex oligomerization; IEA:UniProtKB-KW. DR GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW. DR GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW. DR GO; GO:0039522; P:suppression by virus of host mRNA export from nucleus; IEA:UniProtKB-KW. DR GO; GO:0039540; P:suppression by virus of host RIG-I activity; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro. 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; cd00205; rhv_like; 3. DR Gene3D; 1.10.10.870; -; 1. DR Gene3D; 2.60.120.20; -; 3. 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; IPR036203; P3A_soluble_dom. DR InterPro; IPR000081; Peptidase_C3. DR InterPro; IPR000199; Peptidase_C3A/C3B_picornavir. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR003138; Pico_P1A. DR InterPro; IPR002527; Pico_P2B. DR InterPro; IPR001676; Picornavirus_capsid. DR InterPro; IPR033703; Rhv-like. DR InterPro; IPR001205; RNA-dir_pol_C. DR InterPro; IPR007094; RNA-dir_pol_PSvirus. DR InterPro; IPR029053; Viral_coat. 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 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 3: Inferred from homology; KW Activation of host autophagy by virus {ECO:0000256|RuleBase:RU364118}; KW ATP-binding {ECO:0000256|RuleBase:RU364118, ECO:0000256|SAAS:SAAS01198603}; KW Capsid protein {ECO:0000256|RuleBase:RU364118, KW ECO:0000256|SAAS:SAAS01196445}; KW Covalent protein-RNA linkage {ECO:0000256|RuleBase:RU364118}; KW Eukaryotic host gene expression shutoff by virus KW {ECO:0000256|RuleBase:RU364118}; KW Eukaryotic host translation shutoff by virus KW {ECO:0000256|RuleBase:RU364118}; KW Helicase {ECO:0000256|RuleBase:RU364118, ECO:0000256|SAAS:SAAS01199809}; KW Host cytoplasm {ECO:0000256|RuleBase:RU364118, KW ECO:0000256|SAAS:SAAS00711571}; KW Host cytoplasmic vesicle {ECO:0000256|RuleBase:RU364118, KW ECO:0000256|SAAS:SAAS00711589}; KW Host gene expression shutoff by virus {ECO:0000256|RuleBase:RU364118}; KW Host membrane {ECO:0000256|RuleBase:RU364118, KW ECO:0000256|SAAS:SAAS00795395}; KW Host mRNA suppression by virus {ECO:0000256|RuleBase:RU364118}; KW Host-virus interaction {ECO:0000256|RuleBase:RU364118, KW ECO:0000256|SAAS:SAAS00711757}; KW Hydrolase {ECO:0000256|RuleBase:RU364118, ECO:0000256|SAAS:SAAS01198589}; KW Inhibition of host innate immune response by virus KW {ECO:0000256|RuleBase:RU364118}; KW Inhibition of host mRNA nuclear export by virus KW {ECO:0000256|RuleBase:RU364118}; KW Inhibition of host RIG-I by virus {ECO:0000256|RuleBase:RU364118}; KW Inhibition of host RLR pathway by virus {ECO:0000256|RuleBase:RU364118}; KW Ion channel {ECO:0000256|RuleBase:RU364118, ECO:0000256|SAAS:SAAS00711528}; KW Ion transport {ECO:0000256|RuleBase:RU364118, KW ECO:0000256|SAAS:SAAS00711758}; KW Lipoprotein {ECO:0000256|RuleBase:RU364118}; KW Membrane {ECO:0000256|RuleBase:RU364118, ECO:0000256|SAAS:SAAS00795440}; KW Myristate {ECO:0000256|RuleBase:RU364118}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU364118, KW ECO:0000256|SAAS:SAAS01198580}; KW Nucleotidyltransferase {ECO:0000256|RuleBase:RU364118, KW ECO:0000256|SAAS:SAAS01198562}; KW Pore-mediated penetration of viral genome into host cell KW {ECO:0000256|RuleBase:RU364118}; KW Protease {ECO:0000256|RuleBase:RU364118, ECO:0000256|SAAS:SAAS01199734}; KW Repeat {ECO:0000256|RuleBase:RU364118}; KW RNA-binding {ECO:0000256|RuleBase:RU364118, ECO:0000256|SAAS:SAAS00711776}; KW RNA-directed RNA polymerase {ECO:0000256|RuleBase:RU364118, KW ECO:0000256|SAAS:SAAS01198530}; KW T=pseudo3 icosahedral capsid protein {ECO:0000256|RuleBase:RU364118, KW ECO:0000256|SAAS:SAAS01130245}; KW Thiol protease {ECO:0000256|SAAS:SAAS01199735}; KW Transferase {ECO:0000256|RuleBase:RU364118, ECO:0000256|SAAS:SAAS01198537}; KW Transport {ECO:0000256|RuleBase:RU364118, ECO:0000256|SAAS:SAAS00711554}; KW Viral attachment to host cell {ECO:0000256|RuleBase:RU364118, KW ECO:0000256|SAAS:SAAS00711583}; KW Viral immunoevasion {ECO:0000256|RuleBase:RU364118}; KW Viral ion channel {ECO:0000256|RuleBase:RU364118, KW ECO:0000256|SAAS:SAAS00711569}; KW Viral penetration into host cytoplasm {ECO:0000256|RuleBase:RU364118}; KW Viral RNA replication {ECO:0000256|RuleBase:RU364118, KW ECO:0000256|SAAS:SAAS01198628}; KW Virion {ECO:0000256|RuleBase:RU364118, ECO:0000256|SAAS:SAAS01196585}; KW Virus endocytosis by host {ECO:0000256|RuleBase:RU364118}; KW Virus entry into host cell {ECO:0000256|RuleBase:RU364118, KW ECO:0000256|SAAS:SAAS00711553}. FT DOMAIN 1231..1387 FT /note="SF3 helicase" FT /evidence="ECO:0000259|PROSITE:PS51218" FT DOMAIN 1974..2089 FT /note="RdRp catalytic" FT /evidence="ECO:0000259|PROSITE:PS50507" FT REGION 1..21 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 594..616 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 2208 AA; 245950 MW; 01BBCC27F10EC582 CRC64; MGAQVSSQKV GAHENTNVAT GGSTVNYTTI NYYKDSASNA ASKQDFSQDP SKFTEPVKDI MLKSAPALNS PNVEACGYSD RVLQLTLGNS TITTQEAANS VVGYGQWPTY LNAKDANPVD QPTEPDVSAC RFYTLQSVEW KTESKGWWWK LPDALKDMGL FGQNMYYHYL GRSGYTVHVQ CNASKFHQGA LGVFAVPEYC LAGDSDVKNS YTTYKNANPG EAGGVFVDSF TATTQATRKF CPIDYLFGCG VLTGNAFVFP HQIINLRTNN SATLVLPYVN SLAIDCMAKH NNWGLAIIPL SKLQFPDTSS TEIPITVTIA PMCCEFNGLR NITIPSTQGL PVMNTPGSNQ YLTSDNFQSP CALPEFDVTQ AINIPGEVKN IMEIAEIDTM IPLNLSADRK NSMDMYRVPV STSANLNDPI LCLSLSPASD ERLSYTMLGE ILNYYTHWAG SIKYTFLFCG SMMATGKLLV AYAPPGAKPP RSRKEAMLGT HVIWDVGLQS SCTMVVPWIS NTAYRRTVKD DFTEGGYISM FYQTKIVVPA STPTNMDVLG FVSACNDFSV RLLRDTTHIS QKAMPQGIEE LISEVASNAL KLSQPKPNTQ QSLPNTSSSE PTHSQEVPAL TAVETGATSS VVPADLVQTR HVIQTRSRSE STVESFFARG ACVTIMSVEN YNEAASISNS KLFAKWNITY TDTVQLRRKL EMFTYSRFDI EFTFVVTERY YTANSGHALN QVYQIMYVPP GAPVPQKWDD YTWQTSSNPS VFYTYGTAPA RISIPYVGIA NAYSHFYDGF AKVPIEGETT DPGDAYYGAT SINDFGILAV RVVNEHNPVQ VSSKIRVYMK PKHVRVWCPR PPRAVPYFGP GVDYKGDSLT PLSQKNLTTY GFGHQNKAVY TAGYKICNYH LATQEDLQNA VSIMWNRDLI VVESKAQGTD SIARCNCNTG VYYCESRRKY YPVSFVGPTF QYMEANDYYP ARYQSHMLIG HGFASPGDCG GILRCQHGVI GIVTAGGEGL VAFSDIRDLY AYEEEAMEQG ISNYIESLGA AFGSGFTQQI GDKISELTNM VTSTITEKLL KNLIKIISSL VIITRNYEDT TTVLATLALL GCDISPWQWL KKKACDILEI PYVTRQGDSW LKKFTEACNA AKGLEWVSNK ISKFIDWLKD KIIPQARDKL EFVTKLKQLE MLENQISTIH QSCPSQEHQE ILFNNVRWLS IQSKRFAPLY AVEAKRIQKL EHTINNYIQF KSKHRIEPVC LLVHGSPGTG KSVATNLIAR AIAEKENTST YSLPPDPSHF DGYKQQGVVI MDDLNQNPDG ADMKLFCQMV STVEFIPPMA SLEEKGILFT SNYVLASTNS SRITPPTVAH SDALARRFAF DMDIQVMGEY SRDGKLNMAM ATEMCKNCHQ PANFKRCCPL VCGKAIQLMD KSSRVRYSID QMTTMIINER NRRSNIGNCM EALFQGPLQY KDLKIDIKTT PPPECINDLL QAVDSQEVRD YCEKKGWLVN ISSQVQLERN INRAMTILQA VTTFAAVAGV VYVMYKLFAG HQGAYTGLPN KKPNIPTIRT AKVQGPGFDY AVAMAKRNIV TATTSKGEFT MLGVHDNVAV LPTHSSPGET IVIDGKDVEV LDARALEDQA GTNLEITIVT LKRNEKFRDI RPHIPTQITE TNDGVLIVNT SKYPNMYVPV GAVTEQGYLN LGGRQTARTL MYNFPTRAGQ CGGIITCTGK VIGMHVGGNG SHGFAAALKR SYFTQSQGEI QWMRPSKEVG YPVINAPSKT KLEPSAFHYI FEGVKEPAVL TKNDPRLKTD FEEAIFSKYV GNKITEVDEY MREAVDHYAG QLMSLDINTE QMCLEDAMYG TDGLEALDLT TSAGYPYVAL GKKKRDILNK QTRDTKEMQR LLDTYGINLP LVTYVKDELR SKSKVEQGKS RLIEASSLND SVAMRMAFGN LYAAFHKNPG VITGSAVGCD PDLFWSKIPV LMEERLFAFD YTGYDASLSP AWFEALKMVL EKIGFGDRVD YIDYLNHSHH LYKNKTYCVK GGMPSGCSGT SIFNSMINNL IIRTLLLKTY KGIDLDHLKM IAYGDDVIAS YPHEVDASLL AQSGKDYGLT MTPADKSATF EKVTWENVTF LKRFFRADEK YPFLVHPVMP MKEIHESIRW TKDPRNTQDH VRSLCLLAWH NGEEEYNKFL AKIRSVPIGR ALLLPEYSTL YRRWLDSF //