POLG_COSAA
ID POLG_COSAA Reviewed; 2124 AA.
AC B8XTP8;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=Capsid protein VP0;
DE AltName: Full=VP4-VP2;
DE Contains:
DE RecName: Full=Capsid protein VP4;
DE AltName: Full=P1A;
DE AltName: Full=Rho;
DE AltName: Full=Virion protein 4;
DE Contains:
DE RecName: Full=Capsid protein VP2;
DE AltName: Full=Beta;
DE AltName: Full=P1B;
DE AltName: Full=Virion protein 2;
DE Contains:
DE RecName: Full=Capsid protein VP3;
DE AltName: Full=Gamma;
DE AltName: Full=P1C;
DE AltName: Full=Virion protein 3;
DE Contains:
DE RecName: Full=Capsid protein VP1;
DE AltName: Full=Alpha;
DE AltName: Full=P1D;
DE AltName: Full=Virion protein 1;
DE Contains:
DE RecName: Full=Protein 2A;
DE Short=P2A;
DE AltName: Full=G;
DE Contains:
DE RecName: Full=Protein 2B;
DE Short=I;
DE Short=P2B;
DE Contains:
DE RecName: Full=Protein 2C;
DE Short=C;
DE Short=P2C;
DE EC=3.6.4.13;
DE Contains:
DE RecName: Full=Protein 3A;
DE Short=P3A;
DE Contains:
DE RecName: Full=VPg;
DE Short=P3B;
DE AltName: Full=H;
DE AltName: Full=Protein 3B;
DE Contains:
DE RecName: Full=Protease 3C;
DE Short=P3C;
DE EC=3.4.22.28 {ECO:0000250|UniProtKB:P12296};
DE AltName: Full=Picornain 3C;
DE AltName: Full=p22;
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase;
DE Short=RdRp;
DE EC=2.7.7.48 {ECO:0000255|PROSITE-ProRule:PRU00539};
DE AltName: Full=3D polymerase;
DE Short=3Dpol;
DE AltName: Full=Protein 3D;
DE Short=3D;
OS Cosavirus A (isolate Human/Pakistan/0553/-) (HCoSV-A).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Cosavirus.
OX NCBI_TaxID=1554483;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate Human/Pakistan/0553/-;
RX PubMed=19033469; DOI=10.1073/pnas.0807979105;
RA Kapoor A., Victoria J., Simmonds P., Slikas E., Chieochansin T., Naeem A.,
RA Shaukat S., Sharif S., Alam M.M., Angez M., Wang C., Shafer R.W., Zaidi S.,
RA Delwart E.;
RT "A highly prevalent and genetically diversified Picornaviridae genus in
RT South Asian children.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:20482-20487(2008).
CC -!- FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo
CC T=3 symmetry with capsid proteins VP2 and VP3. Together they form an
CC icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3,
CC with a diameter of approximately 300 Angstroms.VP4 lies on the inner
CC surface of the protein shell formed by VP1, VP2 and VP3. All the three
CC latter proteins contain a beta-sheet structure called beta-barrel jelly
CC roll. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are
CC located at the quasi-sixfold axes. {ECO:0000250|UniProtKB:P12296}.
CC -!- FUNCTION: [Capsid protein VP2]: Forms an icosahedral capsid of pseudo
CC T=3 symmetry with capsid proteins VP2 and VP3. Together they form an
CC icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3,
CC with a diameter of approximately 300 Angstroms.VP4 lies on the inner
CC surface of the protein shell formed by VP1, VP2 and VP3. All the three
CC latter proteins contain a beta-sheet structure called beta-barrel jelly
CC roll. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are
CC located at the quasi-sixfold axes. {ECO:0000250|UniProtKB:P12296}.
CC -!- FUNCTION: [Capsid protein VP3]: Forms an icosahedral capsid of pseudo
CC T=3 symmetry with capsid proteins VP2 and VP3. Together they form an
CC icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3,
CC with a diameter of approximately 300 Angstroms.VP4 lies on the inner
CC surface of the protein shell formed by VP1, VP2 and VP3. All the three
CC latter proteins contain a beta-sheet structure called beta-barrel jelly
CC roll. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are
CC located at the quasi-sixfold axes. {ECO:0000250|UniProtKB:P12296}.
CC -!- FUNCTION: [Capsid protein VP4]: Lies on the inner surface of the capsid
CC shell (By similarity). After binding to the host receptor, the capsid
CC undergoes conformational changes (By similarity). Capsid protein VP4 is
CC released, capsid protein VP1 N-terminus is externalized, and together,
CC they shape a pore in the host membrane through which the viral genome
CC is translocated into the host cell cytoplasm (By similarity). After
CC genome has been released, the channel shrinks (By similarity).
CC {ECO:0000250|UniProtKB:P03300, ECO:0000250|UniProtKB:P12296}.
CC -!- FUNCTION: [Capsid protein VP0]: VP0 precursor is a component of
CC immature procapsids. {ECO:0000250|UniProtKB:P08617}.
CC -!- FUNCTION: [Protein 2A]: Involved in host translation shutoff by
CC inhibiting cap-dependent mRNA translation (By similarity). Nuclear
CC localization is required for this function (By similarity). The
CC resulting inhibition of cellular protein synthesis serves to ensure
CC maximal viral gene expression and to evade host immune response (By
CC similarity). {ECO:0000250|UniProtKB:Q66765}.
CC -!- FUNCTION: [Protein 2B]: Affects membrane integrity and causes an
CC increase in membrane permeability. {ECO:0000250}.
CC -!- FUNCTION: [Protein 2C]: Associates with and induces structural
CC rearrangements of intracellular membranes (By similarity). It displays
CC RNA-binding, nucleotide binding and NTPase activities (By similarity).
CC Interacts with IFIH1/MDA5 to inhibit the induction of the IFN-beta
CC signal pathway (By similarity). {ECO:0000250|UniProtKB:P03304,
CC ECO:0000250|UniProtKB:P03305, ECO:0000250|UniProtKB:P08545}.
CC -!- FUNCTION: [Protein 3A]: Serves as membrane anchor via its hydrophobic
CC domain. {ECO:0000250}.
CC -!- FUNCTION: [VPg]: Forms a primer, VPg-pU, which is utilized by the
CC polymerase for the initiation of RNA chains.
CC {ECO:0000250|UniProtKB:P03304}.
CC -!- FUNCTION: [Protease 3C]: Cysteine protease that generates mature viral
CC proteins from the precursor polyprotein (By similarity). In addition to
CC its proteolytic activity, it binds to viral RNA, and thus influences
CC viral genome replication. RNA and substrate cooperatively bind to the
CC protease. Cleaves host PABP1, this cleavage is important for viral
CC replication (By similarity). Cleaves host TANK and disrupts the TANK-
CC TBK1-IKKepsilon-IRF3 complex, thereby inhibiting the induction of the
CC IFN-beta signal pathway (By similarity). {ECO:0000250|UniProtKB:P03304,
CC ECO:0000250|UniProtKB:P12296}.
CC -!- FUNCTION: [RNA-directed RNA polymerase]: Replicates the genomic and
CC antigenomic RNAs by recognizing replications specific signals (By
CC similarity). Performs VPg uridylylation (By similarity).
CC {ECO:0000250|UniProtKB:P12296}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
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:0000305};
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:0000255|PROSITE-ProRule:PRU01222};
CC -!- SUBUNIT: [Protein 2A]: Interacts with host EIF4E (By similarity).
CC {ECO:0000250|UniProtKB:P03304, ECO:0000250|UniProtKB:Q66765}.
CC -!- SUBUNIT: [Protein 2C]: Interacts with host IFIH1/MDA5; this interaction
CC inhibits the induction of the IFN-beta signal pathway (By similarity).
CC {ECO:0000250|UniProtKB:P03304, ECO:0000250|UniProtKB:Q66765}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion
CC {ECO:0000250|UniProtKB:P12296}. Host cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion
CC {ECO:0000250|UniProtKB:P12296}. Host cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion
CC {ECO:0000250|UniProtKB:P12296}. Host cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Protein 2A]: Host nucleus, host nucleolus
CC {ECO:0000250|UniProtKB:Q66765}.
CC -!- SUBCELLULAR LOCATION: [Protein 2B]: Host cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q66765}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q66765}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q66765}. Note=Probably localizes to the surface
CC of intracellular membrane vesicles that are induced after virus
CC infection as the site for viral RNA replication. These vesicles are
CC probably autophagosome-like vesicles. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Protein 2C]: Host cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q66765}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q66765}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q66765}. Note=Probably localizes to the surface
CC of intracellular membrane vesicles that are induced after virus
CC infection as the site for viral RNA replication. These vesicles are
CC probably autophagosome-like vesicles. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Protein 3A]: Host cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:P03304}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes
CC to the surface of intracellular membrane vesicles that are induced
CC after virus infection as the site for viral RNA replication. These
CC vesicles are probably autophagosome-like vesicles.
CC {ECO:0000250|UniProtKB:P03304}.
CC -!- SUBCELLULAR LOCATION: [VPg]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Protease 3C]: Host cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host cytoplasmic
CC vesicle membrane {ECO:0000250|UniProtKB:Q66765}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:Q66765}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q66765}. Note=Probably localizes to the surface
CC of intracellular membrane vesicles that are induced after virus
CC infection as the site for viral RNA replication. These vesicles are
CC probably autophagosome-like vesicles. {ECO:0000305}.
CC -!- PTM: [Genome polyprotein]: Specific enzymatic cleavages by the viral
CC protease in vivo yield a variety of precursors and mature proteins (By
CC similarity). The polyprotein seems to be cotranslationally cleaved at
CC the 2A/2B junction by a ribosomal skip from one codon to the next
CC without formation of a peptide bond (By similarity). This process would
CC release the P1-2A peptide from the translational complex (By
CC similarity). {ECO:0000250|UniProtKB:P03304}.
CC -!- PTM: [Capsid protein VP0]: During virion maturation, immature virions
CC are rendered infectious following cleavage of VP0 into VP4 and VP2.
CC This maturation seems to be an autocatalytic event triggered by the
CC presence of RNA in the capsid and is followed by a conformational
CC change of the particle. {ECO:0000250|UniProtKB:P03300}.
CC -!- PTM: [Capsid protein VP4]: Myristoylation is required during RNA
CC encapsidation and formation of the mature virus particle.
CC {ECO:0000250|UniProtKB:Q66282}.
CC -!- PTM: [VPg]: Uridylylated by the polymerase and is covalently linked to
CC the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-
CC peptide primer for the polymerase. {ECO:0000250|UniProtKB:P12296}.
CC -!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
CC {ECO:0000305}.
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DR EMBL; FJ438902; ACL15185.1; -; Genomic_RNA.
DR RefSeq; YP_002956074.1; NC_012800.1.
DR SMR; B8XTP8; -.
DR GeneID; 7986820; -.
DR KEGG; vg:7986820; -.
DR Proteomes; UP000029753; Genome.
DR GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044196; C:host cell nucleolus; 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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
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:UniProtKB-EC.
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:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
DR GO; GO:0051259; P:protein complex 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:0006351; P:transcription, DNA-templated; IEA:InterPro.
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; cd00205; rhv_like; 2.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 2.60.120.20; -; 3.
DR Gene3D; 3.30.70.270; -; 2.
DR Gene3D; 4.10.90.10; -; 1.
DR InterPro; IPR037080; Capsid_VP4_sf_Picornavirus.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR044067; PCV_3C_PRO.
DR InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001676; Picornavirus_capsid.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
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; PF00548; Peptidase_C3; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF00073; Rhv; 2.
DR Pfam; PF00910; RNA_helicase; 1.
DR PRINTS; PR00918; CALICVIRUSNS.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51874; PCV_3C_PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS51218; SF3_HELICASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Capsid protein; Covalent protein-RNA linkage; Helicase;
KW Host cytoplasm; Host cytoplasmic vesicle; Host membrane; Host nucleus;
KW Host-virus interaction; Hydrolase; Ion channel; Ion transport; Lipoprotein;
KW Membrane; Myristate; Nucleotide-binding; Nucleotidyltransferase;
KW Phosphoprotein; Protease; Reference proteome; RNA-binding;
KW RNA-directed RNA polymerase; T=pseudo3 icosahedral capsid protein;
KW Thiol protease; Transferase; Transport; Viral attachment to host cell;
KW Viral ion channel; Viral RNA replication; Virion;
KW Virus entry into host cell.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000305"
FT CHAIN 2..2124
FT /note="Genome polyprotein"
FT /id="PRO_0000446193"
FT CHAIN 2..333
FT /note="Capsid protein VP0"
FT /id="PRO_0000446194"
FT CHAIN 2..68
FT /note="Capsid protein VP4"
FT /id="PRO_0000446195"
FT CHAIN 69..333
FT /note="Capsid protein VP2"
FT /id="PRO_0000446196"
FT CHAIN 334..568
FT /note="Capsid protein VP3"
FT /id="PRO_0000446197"
FT CHAIN 569..859
FT /note="Capsid protein VP1"
FT /id="PRO_0000446198"
FT CHAIN 860..889
FT /note="Protein 2A"
FT /id="PRO_0000446199"
FT CHAIN 890..1010
FT /note="Protein 2B"
FT /id="PRO_0000446200"
FT CHAIN 1011..1331
FT /note="Protein 2C"
FT /id="PRO_0000446201"
FT CHAIN 1332..1434
FT /note="Protein 3A"
FT /id="PRO_0000446202"
FT CHAIN 1435..1458
FT /note="VPg"
FT /id="PRO_0000446203"
FT CHAIN 1459..1661
FT /note="Protease 3C"
FT /id="PRO_0000446204"
FT CHAIN 1662..2123
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000446205"
FT DOMAIN 1102..1264
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1459..1648
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 1893..2011
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 873..880
FT /note="Host EIF4E binding"
FT /evidence="ECO:0000250|UniProtKB:Q66765"
FT REGION 1415..1446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1415..1437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1501
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1535
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1612
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1899
FT /note="For RdRp activity"
FT /evidence="ECO:0000250|UniProtKB:P12296"
FT ACT_SITE 1997
FT /note="For RdRp activity"
FT /evidence="ECO:0000250|UniProtKB:P12296"
FT BINDING 1130..1137
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT SITE 68..69
FT /note="Cleavage"
FT SITE 333..334
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 568..569
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 859..860
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 889..890
FT /note="Cleavage; by ribosomal skip"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1010..1011
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1331..1332
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1434..1435
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1458..1459
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1661..1662
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT MOD_RES 1442
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250|UniProtKB:Q66282"
SQ SEQUENCE 2124 AA; 235743 MW; 3CCC63E880276B6F CRC64;
MGANNSKESV SSNGNEGTIV NNFYSNQYYA SIDASAQGVG TSTTPENGNV SGFLGLAGSA
FNALSLLASP RTETGMMMED RVLSRTAGNT SVNSQAAEGV LQAYGTETDS NSPTSCGDDP
SKGTHATDRA FVIQLLPWKQ TTNSYFAQWV RLTQKLSNNL HGNVMAKNIK SHAFAKMGFE
VMLQANTSPF HNGILGLFLV PEFVRKGEIT DEWIDLTPTS SLVSNTELYN PQTYANFPFD
AKHSFDYSDI TPEQFMIFPH QLINPKDTNV ATVRVPYINI APTNDTTVHT VWTAVVMVLV
PLNFSSGASP TVSLTLTITP INSVFNGLHH TAQGPIPVRP FHNFQQFSTT VPLRTEPCYG
MTVTPPVDYM PLPITDLVEL AKVPSFVTVA NSDTTSERSF PYFSVSNTEQ GRNLFKSSVV
LSDLHYQHTL VANLARYFCN YRGSLQFDFI AATTAMTRGK LLISYTPPGA GEPQSIDQAM
MGTYAIWDLG LQSTFNFVVP FISASDFRFN TSSVSNALNS DGWITVWLMN PLTYPPSTPP
TQQILMLMSA GSDFSYRLPI SPGFAEGETS EHPMDNAECG KIDDKDAGMF SGHSVGLPTP
HTSTSFFYDR YRFVGIVKSV VNNTPKPVNI YDDTGKVKNL QQVFPTSDTL LPHSLMSLSP
CASVCGQPIS SFLFAQRANP KKTLKLRSGD EFLYRCCPFS YIKCDLEFTV VPPANSTRDY
IVHWYPPGAT LDAGEVAVGN TSGSNGFDDN GMNAGSSLFS YNPTFHARAP SKVSAVIPFC
LPVSLLPLYF DGFPDYSTTK GMYGCSPSFS FGTIYIESGL QETYSVYIRY KDFKGYAPRP
LIRTPHIRLS ERARYIMADS VLPRPLTRAE RDVARDLLLI AGDIESNPGP AFNPEYTAHG
PVTELIQLAR KPETVDNVNR LLTTLNTLMA KWNNLKDTVT DAVFLRDMVC LLVKLTSLMY
LVHGQGPGAY FAAASILLAD GITFFDWYEK IKIFMARKLR VSPPFFPAAQ GPDLRDFVTF
FNAARGAQWM IDSLKSLITC IKQWLELEEE NEAVQLEKML IDSPRHCKAI NDYNRGDSFQ
RPTNSFEFMD RLVECATKLG KVQIATYFRN FTTADSDTSR PEPVVVVLRG KPGVGKSAAA
TVMAAAVSKL LVGSQSVYTL SPDTEHMDGY HGQFVTLMDD LGQNPDGEDF RCFCQMVSCA
QYRPAMADLK DKGILFTSRL LIATTNLPDF NPVTISDPRA LDRRITFDIL VTPGSAATKN
GKLDLAAALK PDGPGEHPYT SDCPILHTTG LLLKNLRNNQ TMNLKDLVDM IVKRIKHKKE
VGNMLDSLVA QGPTMIVGYT KDDDGIAIVD CLEEWNKIKD KKKKQLALEM VAQELKDKHE
EHKGTIKLLK MFVTGLGVVA AVAGAYATMK YFTKDKPKEE EEEPEEKKEK KTEESKEAAG
PYNGPTKKEI KTLKLKAQSP LMDMEKKIAQ NVMPFQIFYN GKRYTQSCLA IGKRVILVNK
HAFESVEHKF VVDQKEYTLD QVTAISLDCG SGVTDVCAVC LPPGPDFKSI KKHFLPFNTT
MFPGTRLTIL SNDHYPMSRE GSFLRFEDEV PTNVGNMPFV MLYKSTSYFG MCGSVVCSRF
VDGGGIIGMH CAGGGGVSVG TRLTARMIES VFDYFYPPVA QGIIENTETG PRVHVPRTSK
LKRTNATYPA TEKYGPAALS RYDPRLNEGV NLDEVIFSKH TQNTLVEKGS TFRSALDMAA
EIYGEKFRGN DFSPLSVEDA ILGIPGLDRL DPNTASGLPY TKTRRQMIDF NTGQILDDTL
KCRLGQWLAG RPPQEVHYQT FLKDEIRPIE KVKAGKTRII DVPPLDHVIA FRMLFGRFIA
HYHLNFGFKT GSAIGCDPDV AWASFGFELS GFPYLYDFDY SNFDASHSTS IFEILEQKFF
SPELGFDPRC SLLLKSLAVS THCYENKRLQ IAGGLPSGTA GTSVLNTVIN NIIFHGALYH
TYTNFERDDI SMLAYGDDIV VASKFELDLV MVKAFMNRIG YKITPADKSD EFRPKCMDDI
CFLKRRFVKV AGVWAPVMET ENLEAMLSWY KPGTLNEKLQ SVSRLAHFSG RDVYDHLFKP
FIRDGFDVTP WKQLHLEWLN KLSA
