POLG_SALVA
ID POLG_SALVA Reviewed; 2374 AA.
AC C5MSH2;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=Leader protein;
DE Short=L;
DE Contains:
DE RecName: Full=Capsid protein VP0;
DE Contains:
DE RecName: Full=Capsid protein VP3;
DE AltName: Full=P1C;
DE AltName: Full=Virion protein 3;
DE Contains:
DE RecName: Full=Capsid protein VP1;
DE AltName: Full=P1D;
DE AltName: Full=Virion protein 1;
DE Contains:
DE RecName: Full=Protein 2A;
DE Short=P2A;
DE Contains:
DE RecName: Full=Protein 2B;
DE Short=P2B;
DE Contains:
DE RecName: Full=Protein 2C;
DE Short=P2C;
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:P03300};
DE Contains:
DE RecName: Full=Protein 3A;
DE Short=P3A;
DE Contains:
DE RecName: Full=VPg;
DE Short=P3B;
DE AltName: Full=Protein 3B;
DE Contains:
DE RecName: Full=Protein 3CD;
DE EC=3.4.22.28;
DE Contains:
DE RecName: Full=Protease 3C {ECO:0000255|PROSITE-ProRule:PRU01222};
DE EC=3.4.22.28 {ECO:0000255|PROSITE-ProRule:PRU01222};
DE AltName: Full=Picornain 3C {ECO:0000255|PROSITE-ProRule:PRU01222};
DE Short=P3C {ECO:0000255|PROSITE-ProRule:PRU01222};
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 Salivirus A (isolate Human/Nigeria/NG-J1/2007) (SV-A).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Salivirus.
OX NCBI_TaxID=651733;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=19759142; DOI=10.1128/jvi.01241-09;
RA Li L., Victoria J., Kapoor A., Blinkova O., Wang C., Babrzadeh F.,
RA Mason C.J., Pandey P., Triki H., Bahri O., Oderinde B.S., Baba M.M.,
RA Bukbuk D.N., Besser J.M., Bartkus J.M., Delwart E.L.;
RT "A novel picornavirus associated with gastroenteritis.";
RL J. Virol. 83:12002-12006(2009).
CC -!- FUNCTION: [Leader protein]: Required for viral RNA replication and
CC viral RNA encapsidation (By similarity). Does not have any proteolytic
CC activity (By similarity). {ECO:0000250|UniProtKB:O91464}.
CC -!- FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo
CC T=3 symmetry with capsid proteins VP0 and VP3 (By similarity). Together
CC they form an icosahedral capsid composed of 60 copies of each VP0, VP1,
CC and VP3 (By similarity). All the three latter proteins contain a beta-
CC sheet structure called beta-barrel jelly roll (By similarity).
CC {ECO:0000250|UniProtKB:O91464}.
CC -!- FUNCTION: [Capsid protein VP0]: Forms an icosahedral capsid of pseudo
CC T=3 symmetry with capsid proteins VP1 and VP3 (By similarity). Together
CC they form an icosahedral capsid composed of 60 copies of each VP0, VP1,
CC and VP3 (By similarity). All the three latter proteins contain a beta-
CC sheet structure called beta-barrel jelly roll (By similarity).
CC {ECO:0000250|UniProtKB:O91464}.
CC -!- FUNCTION: [Capsid protein VP3]: Forms an icosahedral capsid of pseudo
CC T=3 symmetry with capsid proteins VP0 and VP1 (By similarity). Together
CC they form an icosahedral capsid composed of 60 copies of each VP0, VP1,
CC and VP3 (By similarity). All the three latter proteins contain a beta-
CC sheet structure called beta-barrel jelly roll (By similarity).
CC {ECO:0000250|UniProtKB:O91464}.
CC -!- FUNCTION: [Protein 2A]: Required for viral RNA replication (By
CC similarity). Does not have any proteolytic activity (By similarity).
CC {ECO:0000250|UniProtKB:O91464}.
CC -!- FUNCTION: [Protein 2B]: Affects membrane integrity and causes an
CC increase in membrane permeability. {ECO:0000250}.
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:0000250|UniProtKB:P03300}.
CC -!- FUNCTION: [Protein 3A]: Serves as membrane anchor via its hydrophobic
CC domain. Plays an essential role in viral RNA replication by recruiting
CC PI4KB at the viral replication sites, thereby allowing the formation of
CC rearranged membranous structures where viral replication takes place
CC (By similarity). {ECO:0000250|UniProtKB:O91464}.
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 (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=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 -!- 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:0000250|UniProtKB:P03300};
CC -!- SUBUNIT: [Capsid protein VP0]: Interacts with capsid protein VP1 (By
CC similarity). Interacts with capsid protein VP3 (By similarity).
CC {ECO:0000250|UniProtKB:O91464}.
CC -!- SUBUNIT: [Capsid protein VP1]: Interacts with capsid protein VP0 (By
CC similarity). Interacts with capsid protein VP3 (By similarity).
CC {ECO:0000250|UniProtKB:O91464}.
CC -!- SUBUNIT: [Capsid protein VP3]: Interacts with capsid protein VP0 (By
CC similarity). Interacts with capsid protein VP1 (By similarity).
CC {ECO:0000250|UniProtKB:O91464}.
CC -!- SUBUNIT: [Protein 2A]: Homodimer (By similarity). Interacts with
CC protein 2B (By similarity). Interacts with protein 2C (By similarity).
CC {ECO:0000250|UniProtKB:O91464}.
CC -!- SUBUNIT: [Protein 2B]: Homodimer. Interacts with host ABCD3 (By
CC similarity). Interacts with protein 2A (By similarity). Interacts with
CC host ACBD3 (By similarity). {ECO:0000250|UniProtKB:O91464}.
CC -!- SUBUNIT: [Protein 2C]: Homodimer. Interacts with host ABCD3 (By
CC similarity). Interacts with protein 2A (By similarity). Interacts with
CC protein 3A (By similarity). Interacts with protein 3C (By similarity).
CC Interacts with host ACBD3 (By similarity).
CC {ECO:0000250|UniProtKB:O91464}.
CC -!- SUBUNIT: [Protein 3A]: Homodimer (By similarity). Interacts with host
CC ABCD3 (via GOLD domain) and PI4KB; these interactions allow the
CC formation of a viral protein/ACBD3/PI4KB complex in order to synthesize
CC PI4P at the viral RNA replication sites (By similarity). Interacts with
CC protein 2C (By similarity). Interacts with protein 3C (By similarity).
CC Protein 3C: Interacts with protein 2A (By similarity). Protein 3C:
CC Interacts with protein 2C (By similarity).
CC {ECO:0000250|UniProtKB:O91464}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP0]: Virion
CC {ECO:0000250|UniProtKB:O91464}. Host cytoplasm
CC {ECO:0000250|UniProtKB:P12296}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion
CC {ECO:0000250|UniProtKB:O91464}. Host cytoplasm
CC {ECO:0000250|UniProtKB:P12296}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion
CC {ECO:0000250|UniProtKB:O91464}. Host cytoplasm
CC {ECO:0000250|UniProtKB:P12296}.
CC -!- SUBCELLULAR LOCATION: [Protein 2B]: Host cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:P03304}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P03304}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P03304}. 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:0000250|UniProtKB:P03304}.
CC -!- SUBCELLULAR LOCATION: [Protein 2C]: Host cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:P03304}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P03304}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P03304}. 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:0000250|UniProtKB:P03304}.
CC -!- SUBCELLULAR LOCATION: [Protein 3A]: Host cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:P03304}; Single-pass membrane protein
CC {ECO:0000255}. Host Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:O91464}; Single-pass membrane protein
CC {ECO:0000255}. Note=Probably localizes to intracellular membrane
CC vesicles that are induced after virus infection as the site for viral
CC RNA replication. {ECO:0000250|UniProtKB:P03304}.
CC -!- SUBCELLULAR LOCATION: [VPg]: Virion {ECO:0000250|UniProtKB:P03304}.
CC -!- SUBCELLULAR LOCATION: [Protease 3C]: Host cytoplasm
CC {ECO:0000250|UniProtKB:P03304}.
CC -!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host cytoplasmic
CC vesicle membrane {ECO:0000250|UniProtKB:P03304}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:P03304}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P03304}. 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:0000250|UniProtKB:P03304}.
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 leader protein-VP0 junction is cleaved by 3C
CC proteinase (By similarity). The VP1/2A junction is cleaved by the
CC protein 3CD in association with protein 2A (By similarity).
CC {ECO:0000250|UniProtKB:O91464, ECO:0000250|UniProtKB:P03300}.
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}.
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DR EMBL; GQ179640; ACS32214.2; -; Genomic_RNA.
DR RefSeq; YP_003038594.1; NC_012957.1.
DR SMR; C5MSH2; -.
DR DNASU; 11242466; -.
DR GeneID; 11242466; -.
DR KEGG; vg:11242466; -.
DR Proteomes; UP000029742; Genome.
DR GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0044385; C:integral to membrane of host cell; 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: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: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; 3.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 2.60.120.20; -; 3.
DR Gene3D; 3.30.70.270; -; 2.
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; 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; 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;
KW Eukaryotic host gene expression shutoff by virus;
KW Eukaryotic host translation shutoff by virus; Helicase; Host cytoplasm;
KW Host cytoplasmic vesicle; Host gene expression shutoff by virus;
KW Host Golgi apparatus; Host membrane; Host mRNA suppression by virus;
KW Host-virus interaction; Hydrolase;
KW Inhibition of host mRNA nuclear export by virus; Ion channel;
KW Ion transport; Lipoprotein; Membrane; Myristate; Nucleotide-binding;
KW Nucleotidyltransferase; Phosphoprotein; Protease; Reference proteome;
KW RNA-binding; RNA-directed RNA polymerase;
KW T=pseudo3 icosahedral capsid protein; Thiol protease; Transferase;
KW Transmembrane; Transmembrane helix; Transport;
KW Viral attachment to host cell; Viral ion channel; Viral RNA replication;
KW Virion; Virus entry into host cell.
FT CHAIN 1..2374
FT /note="Genome polyprotein"
FT /id="PRO_0000448019"
FT CHAIN 1..114
FT /note="Leader protein"
FT /id="PRO_0000448020"
FT CHAIN 115..482
FT /note="Capsid protein VP0"
FT /id="PRO_0000448021"
FT CHAIN 483..705
FT /note="Capsid protein VP3"
FT /id="PRO_0000448022"
FT CHAIN 706..955
FT /note="Capsid protein VP1"
FT /id="PRO_0000448023"
FT CHAIN 956..1100
FT /note="Protein 2A"
FT /id="PRO_0000448024"
FT CHAIN 1101..1253
FT /note="Protein 2B"
FT /id="PRO_0000448025"
FT CHAIN 1254..1599
FT /note="Protein 2C"
FT /id="PRO_0000448026"
FT CHAIN 1600..1676
FT /note="Protein 3A"
FT /id="PRO_0000448027"
FT CHAIN 1677..1705
FT /note="VPg"
FT /id="PRO_0000448028"
FT CHAIN 1706..2366
FT /note="Protein 3CD"
FT /id="PRO_0000448029"
FT CHAIN 1706..1900
FT /note="Protease 3C"
FT /id="PRO_0000448030"
FT CHAIN 1901..2366
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000448031"
FT TRANSMEM 1649..1669
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 1361..1525
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1700..1889
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 2126..2243
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 144..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1677..1699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1748
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1779
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1852
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 2132
FT /note="For RdRp activity"
FT /evidence="ECO:0000250|UniProtKB:P12296"
FT ACT_SITE 2229
FT /note="For RdRp activity"
FT /evidence="ECO:0000250|UniProtKB:P12296"
FT BINDING 1387..1394
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT SITE 114..115
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000305"
FT SITE 482..483
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 705..706
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 955..956
FT /note="Cleavage; by protein 3CD"
FT /evidence="ECO:0000250|UniProtKB:O91464"
FT SITE 1100..1101
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1253..1254
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1599..1600
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1676..1677
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1705..1706
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1900..1901
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT MOD_RES 1679
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT LIPID 115
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT LIPID 1600
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250|UniProtKB:C6KEF6"
SQ SEQUENCE 2374 AA; 255475 MW; DD94E33770F73453 CRC64;
MEGSNGFSSS LAGLSSSRSS LRLLTHFLSL PTLPVNIYLN ARRHSGWYRS PPTLPVNIYL
NEQFDNLCLA ALRYPGHKLY PSVHTLFPDV SPLKIPHSVP AFAHLVQRQG LRRQGNSITN
IYGNGNDVTT DVGANGMSLP IAVGDMPTAS TSEAPLGSNK GGSSTSPKST SNGNVVRGSR
YSKWWEPAAA RALDRALDHA VDATDAVAGA ASKGIKAGAA KLSNKLSGSQ TTALLALPGN
IAGGAPSATV NANNTSISSQ ALLPSVNPYP STPAVSLPNP DAPTQVGPAA DRQWLVDTLS
WSETIAPLTV FSGPKALTPG VYPPTIEPNT GVYPLPAALC VSHPESVFST AYNAHAYFNC
GFDVTVVVNA SQFHGGSLIV LAMAEGLGDI TPADSSTWFN FPHTIINLAN SNAATLKLPY
IGVTPNTSTE GLHNYWTILF APLTPLAVPT GSPTTVKVSL FVSPIDSAFY GLRFPVPFPA
PQHWKTRAVP GAGTYGSVVA GQEIPLVGYA PAAPPRDYLP GRVHNWLEYA ARHSWERNLT
WTSADEVGDQ LVSYPIQPEA LANTQTNTAF VLSLFSQWRG SLQISLIFTG PAQCYGRLLL
AYTPPSANPP TTIDEANNGT YDVWDVNGDS TYTFTIPFCS QAYWKTVDIG TSSGLVSNNG
YFTVFVMNPL VTPGPSPPSA TVAAFLHVAD DFDVRLPQCP ALGFQSGADG AEVQPAPTSD
LSDGNPTTDP APRDNFDYPH HPVDPSTDLA FYFSQYRWFG LNESLTPLDA TGGLFYHISL
NPINFQQSSL LSVLGAFTYV YANLSLNINV SAPSQPCTFY VFYAPPGASV PSVQTLAELS
FFTHTATPLN LAAPTNITVS IPYSSPQSVL CTSFGGFGLQ NGGDAGNLHS NTWGTLILYV
DLPQSDSVSV SAYISFRDFE AYVPRQTPGV GPVPTSTSIV RVARPTPKPR TARRQGGTLA
DLILSPESRC FIVAHTTAPF YSILLVNPDE EYAISMFSHG DESILQYSSR SGTRLTPTAP
AFFLCAAASV DTVLPYSISQ SHLWLTDLTG IPLRAVPPLT LFLSAGAALC AGAQTLIAVA
QGGSTPETPP TPNRALLRRQ GLGDLPDAAK GLSAALESVA RVAGDANIAT SSQAIATSIN
SLSNSIDGAT SFMQNFFSGL APRNPTSPLQ HLFAKLIKWV TKIIGSLIII CNNPTPSALI
GVSLMLCGDL AEDITEFFSN LGNPLAAVFY RCARALGLSP TPQSAAQAAG GRQGVRDYND
IMSALRNTDW FFEKIMTHIK NLLEWLGVLV KDDPRTKLNG QHEKILELYT DSVTASSTPP
SELSADAIRS NLDLAKQLLT LSHAANSVTH IQLCTRAITN YSTALSAISL VGTPGTRPEP
LVVYLYGPPG TGKSLLASLL ASTLAQALSG DPNNYYSPSS PDCKFYDGYS GQPVHYIDDI
GQDPDGADWA DFVNIVSSAP FIVPMADVND KGRFYTSRVV IVTSNFPGPN PRSARCVAAL
ERRLHIRLNV TARDGVAFSA AAALQPSNPP SATRYCKFAN PLTQFSMFNL AVDYKSVVLP
NTPLTCFDEL VDFVLSSLRD RASVNSLLSG MVRTDVTRQG GNADAPAPSA APLPSVIPSV
PSQDPFTRAV NENRPVSFLS KIWSWRAPIF AASSFLSLIA ATLTIVRCLR DLRSTQGAYS
GTPVPKPRKK DLPKQPVYSG PVRRQGFDPA VMKIMGNVDS FVTLSGTKPI WTMSCLWIGG
RNLIAPSHAF VSDEYEITHI RVGSRTLDVS RVTRVDDGEL SLLSVPDGPE HKSLIRYIRS
ASPKSGILAS KFSDTPVFVS FWNGKSHSTP LPGVVDEKDS FTYRCSSFQG LCGSPMIATD
PGGLGILGIH VAGVAGYNGF SARLTPERVQ AFLSHLATPQ SVLYFHPPMG PPAHVSRRSR
LHPIPPAFGA FPITKEPAAL SRKDPRLPEG TDLDAITLAK HDKGDIATPW PCMEEAADWY
FSQLPDNLPV LSQEDAIRGL DHMDAIDLSQ SPGYPWTTQG RSRRSLFDED GNPLPELQEA
IDSVWDGGSY IYQSFLKDEL RPTAKARAGK TRIVEAAPIQ AIVVGRRLLG SLINHLQGNP
LQHGSAVGCN PDIHWTQIFH SLTSFSNVWS IDYSCFDATI PSVLLSAIAS RIAARSDQPG
RVLDYLSYTT TSYHVYDSLW YTMIGGNPSG CVGTSILNTI ANNIAVISAM MYCNKFDPRD
PPVLYCYGDD LIWGSNQDFH PRELQAFYQK FTNFVVTPAD KASDFPDSSS IFDITFLKRY
FVPDDIHPHL IHPVMDEQTL TNSIMWLRGG EFEEVLRSLE TLAFHSGPKN YSAWCEKIKA
KIRENGCDAT FTPYSVLQRG WVSTCMTGPY PLTG
