ID E2I7G4_9FLAV Unreviewed; 3415 AA.
AC E2I7G4;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
OS Powassan virus.
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Orthoflavivirus;
OC Orthoflavivirus powassanense.
OX NCBI_TaxID=11083 {ECO:0000313|EMBL:ADK37753.1, ECO:0000313|Proteomes:UP000096423};
RN [1] {ECO:0000313|EMBL:ADK37753.1, ECO:0000313|Proteomes:UP000096423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NFS001 {ECO:0000313|EMBL:ADK37753.1};
RX PubMed=20631087; DOI=10.1099/vir.0.024232-0;
RA Pesko K.N., Torres-Perez F., Hjelle B.L., Ebel G.D.;
RT "Molecular epidemiology of Powassan virus in North America.";
RL J. Gen. Virol. 91:2698-2705(2010).
CC -!- FUNCTION: Functions as a signal peptide for NS4B and is required for
CC the interferon antagonism activity of the latter.
CC {ECO:0000256|ARBA:ARBA00003504}.
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|ARBA:ARBA00001556};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of
CC the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.;
CC EC=3.4.21.91; Evidence={ECO:0000256|ARBA:ARBA00024468};
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|ARBA:ARBA00001491};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004397}. Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004367}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004367}; Lumenal side
CC {ECO:0000256|ARBA:ARBA00004367}. Host endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004153}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004153}. Host endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004461}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004461}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004461}. Host endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00023443}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00023443}; Lumenal side
CC {ECO:0000256|ARBA:ARBA00023443}. Host nucleus
CC {ECO:0000256|ARBA:ARBA00004147}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613}. Virion membrane
CC {ECO:0000256|ARBA:ARBA00004385}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004385}.
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DR EMBL; HM440559; ADK37753.1; -; Genomic_RNA.
DR Proteomes; UP000096423; Genome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
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:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0004482; F:mRNA 5'-cap (guanine-N7-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003968; F:RNA-dependent 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:0039564; P:disruption by virus of host JAK-STAT cascade via inhibition of STAT2 activity; IEA:UniProtKB-KW.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; 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; cd20761; capping_2-OMTase_Flaviviridae; 1.
DR CDD; cd12149; Flavi_E_C; 1.
DR CDD; cd17038; Flavi_M; 1.
DR CDD; cd23204; Flavivirus_RdRp; 1.
DR Gene3D; 1.10.260.90; -; 1.
DR Gene3D; 1.20.1280.260; -; 1.
DR Gene3D; 2.40.10.120; -; 1.
DR Gene3D; 2.60.40.350; -; 1.
DR Gene3D; 1.10.8.970; Flavivirus envelope glycoprotein M-like; 1.
DR Gene3D; 2.60.260.50; Flavivirus polyprotein propeptide domain; 1.
DR Gene3D; 3.30.70.2840; Flavivirus RNA-directed RNA polymerase, thumb domain; 3.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 2.60.98.10; Tick-borne Encephalitis virus Glycoprotein, domain 1; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR Gene3D; 3.30.67.10; Viral Envelope Glycoprotein, domain 2; 1.
DR Gene3D; 3.30.387.10; Viral Envelope Glycoprotein, domain 3; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
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; IPR011492; Flavi_DEAD.
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; IPR011998; Flavi_Glycoprot_E_cen/dimer.
DR InterPro; IPR001157; Flavi_NS1.
DR InterPro; IPR000752; Flavi_NS2A.
DR InterPro; IPR000487; Flavi_NS2B.
DR InterPro; IPR001850; Flavi_NS3_S7.
DR InterPro; IPR000404; Flavi_NS4A.
DR InterPro; IPR001528; Flavi_NS4B.
DR InterPro; IPR046811; Flavi_NS5_thumb.
DR InterPro; IPR002535; Flavi_propep.
DR InterPro; IPR038688; Flavi_propep_sf.
DR InterPro; IPR047530; Flavi_RdRp.
DR InterPro; IPR000208; Flavi_RdRp_fingers/palm.
DR InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
DR InterPro; IPR014412; Gen_Poly_FLV.
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; IPR049486; NS3-hel_C_flaviviridae.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR04240; flavi_E_stem; 1.
DR Pfam; PF20907; Flav_NS3-hel_C; 1.
DR Pfam; PF01003; Flavi_capsid; 1.
DR Pfam; PF07652; Flavi_DEAD; 1.
DR Pfam; PF21659; Flavi_E_stem; 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; PF01350; Flavi_NS4A; 1.
DR Pfam; PF01349; Flavi_NS4B; 1.
DR Pfam; PF00972; Flavi_NS5; 1.
DR Pfam; PF20483; Flavi_NS5_thumb; 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; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR SUPFAM; SSF56983; Viral glycoprotein, central and dimerisation domains; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Capsid protein {ECO:0000256|ARBA:ARBA00022561};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR003817-3};
KW Fusion of virus membrane with host endosomal membrane
KW {ECO:0000256|ARBA:ARBA00022510};
KW Fusion of virus membrane with host membrane
KW {ECO:0000256|ARBA:ARBA00022506};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Host endoplasmic reticulum {ECO:0000256|ARBA:ARBA00023184};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW Host nucleus {ECO:0000256|ARBA:ARBA00022562};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Inhibition of host innate immune response by virus
KW {ECO:0000256|ARBA:ARBA00022632};
KW Inhibition of host interferon signaling pathway by virus
KW {ECO:0000256|ARBA:ARBA00022830};
KW Inhibition of host STAT2 by virus {ECO:0000256|ARBA:ARBA00022883};
KW Interferon antiviral system evasion {ECO:0000256|ARBA:ARBA00022883};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR003817-4};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW mRNA capping {ECO:0000256|ARBA:ARBA00023042};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
KW Viral immunoevasion {ECO:0000256|ARBA:ARBA00023280};
KW Viral penetration into host cytoplasm {ECO:0000256|ARBA:ARBA00022595};
KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953};
KW Virion {ECO:0000256|ARBA:ARBA00022844};
KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296};
KW Zinc {ECO:0000256|PIRSR:PIRSR003817-4}.
FT TRANSMEM 99..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 727..748
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 755..775
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1132..1153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1160..1181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1294..1316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1328..1348
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1385..1402
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1453..1481
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2161..2184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2191..2208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2243..2260
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2347..2364
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2370..2388
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2434..2455
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1357..1487
FT /note="Flavivirus NS2B"
FT /evidence="ECO:0000259|PROSITE:PS51527"
FT DOMAIN 1486..1669
FT /note="Peptidase S7"
FT /evidence="ECO:0000259|PROSITE:PS51528"
FT DOMAIN 1675..1832
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1842..2001
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 2513..2777
FT /note="MRNA cap 0-1 NS5-type MT"
FT /evidence="ECO:0000259|PROSITE:PS51591"
FT DOMAIN 3041..3190
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1543
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1"
FT ACT_SITE 1567
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1"
FT ACT_SITE 1627
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1"
FT BINDING 2951
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT BINDING 2955
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT BINDING 2960
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT BINDING 2963
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT BINDING 3225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT BINDING 3241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT BINDING 3360
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT DISULFID 281..308
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
FT DISULFID 338..394
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
FT DISULFID 352..383
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
FT DISULFID 370..399
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
FT DISULFID 464..568
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
FT DISULFID 585..617
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
SQ SEQUENCE 3415 AA; 378388 MW; B91C5272768E1F16 CRC64;
MVTTSKGKGG GPPKRKLKVT ANKSRPATSP MPKGFVLSRM LGILWHAMTG TARTPVLKMF
WKTVPLRQAE SALKKIKRVI GNLMQSLHMR GRRRSGVDWT WTFLVMALMA MAMATSIHRD
KEGYMVMRAS GRDAASQVRV QNGTCVILAT DMGEWCEDSI TYSCVTIDQE EEPVDVDCFC
RGVDRVKLEY GRCGRQAGFR GRRSVVIPTH AQKDMVGRGH AWLKGDNIRD HVTRVEGWMW
KNKLLTVAVV ALAWLMLDSW MARVTVILLA LSLGPVYATR CTHLENRDFV TGVQGTTRVS
LVLELGGCVT ITAEGKPSID VWLEDIFQES PAETREYCLH AKLSNTKVEA RCPTTGPATL
PEEHQANMVC KRDQSDRGWG NHCGFFGKGS IVACAKFECE EAKKAVGHVY DSTKITYVVK
VEPHTGDYQA ANETNENRKT AQFTVASEKV ILNLGDYGDV SLTCKVASGI DVAQTVVMSL
GSSKDHLPSA WQVHRDWFED LALPWKHKDN QDWNSVEKLV EFGPPHAVKM DIFNLGDQTA
VLLKSLAGVP LASVDNQKYH LKSGHVTCDV GLEKLKLKGT TYSMCDKTKF KWKRVPVDSG
HDTVVMEVSY TGSDKPCRIP VRAVAHGVPT INVAMLITPN PTIETSGGGF IEMQLPPGDN
IIYVGDLSQQ WFQKGSTIGR MLEKTRKGLE RLSVVGEHAW DFGSVGGILS SVGKAVHTVL
GGAFNTLFGG VGFIPKMLLG VALVWLGLNA RNPTMSMTFL AVGVLTLMMT MGVGADYGCA
VDPERMEIRC GEGLVVWKEV SEWYDGYAYH PESPDTLAQA LREAFERGIC GVVPQNRLEM
AMWRSTAPEL NLVLSEGEAN LTIVVDKTDP ADYRGGTPMA LKKTGKESKV SWKSWGKSIL
WSVPESPRRM MMGVDGAGEC PLHKRATGVF TVAEFGVGLR TKVFLDLRGE ASKECDTGVM
GAAVKNGKAI HTDQSMWMSS FRNDTGTYIQ ELILTDLRNC TWPASHTIDN DGVLDSRLFL
PVTLAGPRSK YNRIPGYSEQ TKGPWDQTPL RVVRDHCPGT SVKIDSQCDK RGASVRSTTE
SGKIIPEWCC RACELPPVTF RSGTDCWYAM EIRPVHSQGG LVRSMVMADN GAMLSEGGTP
GLVAVFVLME FLLRRRPGSV TSILWGGILM LGLLVTGLVR VEEIVRYIIA VGITFHLELG
PEIMALVMLQ AVFSMRTCYL IGFLAKRVIT TREVVTVYFL LLVLEMGIPE MNFGHLWEWA
DSLAMGLLII KASSMEDRKG LGFLLAGLMT QRHLTAVHHG LIVFLTVALA VVGRSIYNGQ
KERKGLSFTI PLASLLGGPG SGLRMLALWE CLGGRGRRSL SEPLTVVGVM LAMASGLLRH
SSQEALLVLS AGSFLILMLI LGTRRLQLTA EWAGLAEWNP ELVNEGGEVS LKVRQDAMGN
LHLTEVEREE RRLALWLAFG LLASAFHWSG ILVTMGAWTL YELFSSARRT DLVFSGQSSD
HGEKRPFDIK DGVYRIYAPG LVWGHRQIGV GYGTKGVLHT MWHVTRGAAL SVEGAVSGPY
WADVREDVVC YGGAWSLEGK WGGEVVQVHA FPPDSGHKVH QCQPGKLNLE GGRVMGAIPI
DLPRGTSGSP IINAQGVVLG LYGNGLKSND VYISSIAQGS VEKSRPEMPL AIQGGRWTSK
GSITVLDMHP GSGKTHRVLP ELIRECIDKR LRTVVLAPTR VVLKEMERAL QGKRVKFHSA
AVDNTSSSLG AIVDVMCHAT YVNRRLLPQG RQNWEVAIMD EAHWTDPHSI AARGHLYSLA
KENRCAFVLM TATPPGKSEA FPESKGAIVS EERPIPDGEW RDGFDWITEF EGRTAWFVSS
IAKGGAIART LRQKGKSVIC LNSKTFDKDY GRVREEKPDF VVTTDISEMG ANLDVNRVID
GRTNIKPEEI DGRVELAGTR RVTTASAAQR RGRVGRHEGR TDTYVYSGQC DDDDSSLVQW
KEAQILLDNI TTVRGPVATF YGPEQGKMLE VAGHFRLTEE KRKHFRHLLT NCDFTPWLAW
HVAANTTCVT DRKWTWEGPE ENAIDGPDGE LVTFRSPNGA ERKLKPVWKD SRMFREGRDV
ADFLQYASGR RSAMDIFTGL GGVPDLLRLR CTAAWDVVYT LLNETPGSRA MKMAERDAPE
AMLTLLEVAV LGIATLGVVW CFIVRTSVSR MVLGTVVLVV ALILLWLGGM DYGTMAGVAL
IFYLLLTVLQ PEPGKQRSGE DNRLAFLLIG LGSVIGLLAA NELGYLERTK ADIAGLFRYD
TQGDRVWDTW TNIDIQPARS WGTYVFIVSL FTPYMLHQLQ TKIQRLVNSS VAAGTQAMKD
LGGGTPFFGV AGHVVALGVT SLVGATPTSL ALGVALAILH LAVVTSGLEA ELTQRAHRAF
FSAMVKNPMV DGEVINPIPD GEPKPALYER KMSLLLAVGL CIAAVALNRT AAAMTEAGAV
AVAALGQLLR PGEESWWTMP MACGMAGLVR GSLWGLLPVL HRIWLRTQGA RRGGAEGSTL
GDIWKQRLNS CTKEEFFAYR RTGVMETNRD QARELLRRGE TNMGLAVSRG CAKLAWLEER
GYATLKGEVV DLGCGRGGWS YYAASRPSVM AVKAYTIGGK GHEAPRLVTS LGWNLIKFRS
GMDVFSMPAT RVDTILCDIG ESNPDPEKEG TRSRRVILLM EQWKARNPDA AAVFKVLAPY
RPEVLEALHR FQLQWGGGLV RVPFSRNSTH EMYYSTAVTG NLVNSVNVLS RKLLARFGET
RGPIQVPEID LGTGTRCVTL AEDKVKPSDV MERIGALKEQ YSESWHEDKE HPYRTWQYWG
SYRTPATGSA ASLINGVVKL LSWPWNARED VTRMAMTDTT AFGQQRVFKE KVDTKAQEPQ
PGTRVIMRAV SDWLLEHLHS RARVRMCTRD EFIAKVRSNA ALGAWSDEQN KWSSAKEAVE
DPEFWNLVDE ERSRHLKGQC RHCVYNMMGK REKKLGEFGV AKGSRAIWYM WLGSRFLEFE
VLGFLNEEHW ASRVVSGAGV EGTSLNYLGW LLRELGAKDG GRLYADDTAG WDTRITNADL
EDEEQILRYM EGEHHVLAKT ILEKAYHAKV VKVARPSPQG GCVMDVITRR DQRGSGQVVT
YALNTITNMK VQLIRMMEGE GVIGPADSQD PRLKRVEAWL REHGAERLGR MLVSGDDCVV
KPIDDRFGKA LYFLNDMAKT RKDVGEWEPS VGFTAWEEVP FCSHHFHELV MKDGRSLIVP
CRDQDELVGR ARVSPGCGWS VRETACLSKA YGQMWLLNYF HRRDLRTLGL AICSAVPVNW
VPMGRTTWSI HASGEWMTTE DMLRIWNKVW ILDNPHMENK QMVDEWRDIP YLPKTQDLVC
SSLVGRKERA EWAKNIWGSV EKVRKLIGAE EYRDYLANMD RHDLHWELKL ESSII
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