POLG_NVN68
ID POLG_NVN68 Reviewed; 1789 AA.
AC Q83883;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=Protein p48;
DE Contains:
DE RecName: Full=NTPase;
DE EC=3.6.1.15;
DE AltName: Full=p41;
DE Contains:
DE RecName: Full=Protein p22;
DE Contains:
DE RecName: Full=Viral genome-linked protein;
DE AltName: Full=VPG;
DE Contains:
DE RecName: Full=3C-like protease;
DE Short=3CLpro;
DE EC=3.4.22.66;
DE AltName: Full=Calicivirin;
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase;
DE Short=RdRp;
DE EC=2.7.7.48;
GN ORFNames=ORF1;
OS Norwalk virus (strain GI/Human/United States/Norwalk/1968)
OS (Hu/NV/NV/1968/US).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Caliciviridae; Norovirus.
OX NCBI_TaxID=524364;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 3-1789.
RX PubMed=8391187; DOI=10.1006/viro.1993.1345;
RA Jiang X., Wang M., Wang K., Estes M.K.;
RT "Sequence and genomic organization of Norwalk virus.";
RL Virology 195:51-61(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-3.
RX PubMed=8883366; DOI=10.1007/bf00284649;
RA Hardy M.E., Estes M.K.;
RT "Completion of the Norwalk virus genome sequence.";
RL Virus Genes 12:287-290(1996).
RN [3]
RP FUNCTION OF VPG.
RX PubMed=569187; DOI=10.1099/0022-1317-41-2-443;
RA Burroughs J.N., Brown F.;
RT "Presence of a covalently linked protein on calicivirus RNA.";
RL J. Gen. Virol. 41:443-446(1978).
RN [4]
RP FUNCTION OF NTPASE.
RX PubMed=11160659; DOI=10.1128/jvi.75.4.1611-1619.2001;
RA Pfister T., Wimmer E.;
RT "Polypeptide p41 of a Norwalk-like virus is a nucleic acid-independent
RT nucleoside triphosphatase.";
RL J. Virol. 75:1611-1619(2001).
RN [5]
RP MUTAGENESIS OF ASP-394; PHE-395; GLN-398; GLY-399; GLU-1154; ASP-1167 AND
RP GLU-1281.
RX PubMed=12367748; DOI=10.1016/s0168-1702(02)00114-4;
RA Hardy M.E., Crone T.J., Brower J.E., Ettayebi K.;
RT "Substrate specificity of the Norwalk virus 3C-like proteinase.";
RL Virus Res. 89:29-39(2002).
RN [6]
RP INTERACTION WITH HUMAN VAPA.
RX PubMed=14557663; DOI=10.1128/jvi.77.21.11790-11797.2003;
RA Ettayebi K., Hardy M.E.;
RT "Norwalk virus nonstructural protein p48 forms a complex with the SNARE
RT regulator VAP-A and prevents cell surface expression of vesicular
RT stomatitis virus G protein.";
RL J. Virol. 77:11790-11797(2003).
RN [7]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RX PubMed=17554035; DOI=10.1099/vir.0.82797-0;
RA Scheffler U., Rudolph W., Gebhardt J., Rohayem J.;
RT "Differential cleavage of the norovirus polyprotein precursor by two active
RT forms of the viral protease.";
RL J. Gen. Virol. 88:2013-2018(2007).
RN [8]
RP REVIEW.
RX PubMed=16168575; DOI=10.1016/j.femsle.2005.08.031;
RA Hardy M.E.;
RT "Norovirus protein structure and function.";
RL FEMS Microbiol. Lett. 253:1-8(2005).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1100-1281.
RX PubMed=16641296; DOI=10.1128/jvi.80.10.5050-5058.2006;
RA Zeitler C.E., Estes M.K., Venkataram Prasad B.V.;
RT "X-ray crystallographic structure of the Norwalk virus protease at 1.5-A
RT resolution.";
RL J. Virol. 80:5050-5058(2006).
CC -!- FUNCTION: Protein p48 may play a role in viral replication by
CC interacting with host VAPA, a vesicle-associated membrane protein that
CC plays a role in SNARE-mediated vesicle fusion. This interaction may
CC target replication complex to intracellular membranes.
CC -!- FUNCTION: NTPase presumably plays a role in replication. Despite having
CC similarities with helicases, does not seem to display any helicase
CC activity.
CC -!- FUNCTION: Protein P22 may play a role in targeting replication complex
CC to intracellular membranes.
CC -!- FUNCTION: Viral genome-linked protein is covalently linked to the 5'-
CC end of the positive-strand, negative-strand genomic RNAs and subgenomic
CC RNA. Acts as a genome-linked replication primer. May recruit ribosome
CC to viral RNA thereby promoting viral proteins translation.
CC -!- FUNCTION: 3C-like protease processes the polyprotein: 3CLpro-RdRp is
CC first released by autocleavage, then all other proteins are cleaved.
CC May cleave host polyadenylate-binding protein thereby inhibiting
CC cellular translation (By similarity). {ECO:0000250}.
CC -!- FUNCTION: RNA-directed RNA polymerase replicates genomic and
CC antigenomic RNA by recognizing replications specific signals.
CC Transcribes also a subgenomic mRNA by initiating RNA synthesis
CC internally on antigenomic RNA. This sgRNA codes for structural
CC proteins. Catalyzes the covalent attachment VPg with viral RNAs (By
CC similarity). {ECO:0000255|PROSITE-ProRule:PRU00539}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Endopeptidase with a preference for cleavage when the P1
CC position is occupied by Glu-|-Xaa and the P1' position is occupied by
CC Gly-|-Yaa.; EC=3.4.22.66; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00870};
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 -!- SUBUNIT: [Protein p48]: Interacts with human VAPA.
CC {ECO:0000269|PubMed:14557663}.
CC -!- SUBCELLULAR LOCATION: [Protein p48]: Host membrane {ECO:0000305};
CC Single-pass membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [NTPase]: Host membrane {ECO:0000305}; Single-
CC pass membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Protein p22]: Host membrane {ECO:0000305};
CC Single-pass membrane protein {ECO:0000305}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. 3CLpro
CC is first autocatalytically cleaved, then processes the whole
CC polyprotein. {ECO:0000255|PROSITE-ProRule:PRU00870,
CC ECO:0000269|PubMed:17554035}.
CC -!- PTM: VPg is uridylylated by the polymerase and is covalently attached
CC to the 5'-end of the polyadenylated genomic and subgenomic RNAs. This
CC uridylylated form acts as a nucleotide-peptide primer for the
CC polymerase (By similarity). {ECO:0000250}.
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DR EMBL; M87661; AAB50465.1; -; Genomic_RNA.
DR PIR; A53260; A53260.
DR PIR; C37471; C37471.
DR PIR; C53260; C53260.
DR PIR; D37471; D37471.
DR PIR; E37471; E37471.
DR RefSeq; NP_056820.1; NC_001959.2.
DR PDB; 2FYQ; X-ray; 1.50 A; A=1101-1281.
DR PDB; 2FYR; X-ray; 2.20 A; A=1101-1281.
DR PDB; 2LNC; NMR; -; A=1101-1281.
DR PDB; 3UR6; X-ray; 1.50 A; A/B=1101-1281.
DR PDB; 3UR9; X-ray; 1.65 A; A/B=1101-1281.
DR PDB; 4IMQ; X-ray; 1.50 A; A=1101-1281.
DR PDB; 4IMZ; X-ray; 1.70 A; A=1101-1281.
DR PDB; 4IN1; X-ray; 2.05 A; A=1101-1281.
DR PDB; 4IN2; X-ray; 2.40 A; A/B=1100-1281.
DR PDB; 4INH; X-ray; 1.70 A; A/B/C/D/E/F/G/H=1101-1281.
DR PDB; 4XBB; X-ray; 1.85 A; A=1101-1281.
DR PDB; 4XBC; X-ray; 1.60 A; A=1101-1281.
DR PDB; 4XBD; X-ray; 1.45 A; A/B=1101-1281.
DR PDB; 5DG6; X-ray; 2.35 A; A/B=1101-1281.
DR PDB; 5DGJ; X-ray; 1.00 A; A=1101-1281.
DR PDB; 5E0G; X-ray; 1.20 A; A=1101-1281.
DR PDB; 5E0H; X-ray; 1.95 A; A/B=1101-1281.
DR PDB; 5E0J; X-ray; 1.20 A; A=1101-1281.
DR PDB; 5T6D; X-ray; 2.10 A; A/B=1101-1281.
DR PDB; 5T6F; X-ray; 1.90 A; A/B=1101-1281.
DR PDB; 5T6G; X-ray; 2.45 A; A/B=1101-1281.
DR PDB; 5TG1; X-ray; 1.40 A; A=1101-1281.
DR PDB; 5TG2; X-ray; 1.75 A; A=1101-1281.
DR PDB; 5WEJ; X-ray; 1.95 A; A/B=1101-1281.
DR PDB; 6BIB; X-ray; 1.95 A; A/B=1101-1281.
DR PDB; 6BIC; X-ray; 2.25 A; A/B=1101-1281.
DR PDB; 6BID; X-ray; 1.15 A; A=1101-1281.
DR PDB; 6W5H; X-ray; 1.85 A; A/B/C/D=1101-1281.
DR PDB; 6W5J; X-ray; 1.85 A; A/B=1101-1281.
DR PDB; 6W5K; X-ray; 1.95 A; A/B/C/D=1101-1281.
DR PDB; 6W5L; X-ray; 2.10 A; A/B/C/D=1101-1281.
DR PDBsum; 2FYQ; -.
DR PDBsum; 2FYR; -.
DR PDBsum; 2LNC; -.
DR PDBsum; 3UR6; -.
DR PDBsum; 3UR9; -.
DR PDBsum; 4IMQ; -.
DR PDBsum; 4IMZ; -.
DR PDBsum; 4IN1; -.
DR PDBsum; 4IN2; -.
DR PDBsum; 4INH; -.
DR PDBsum; 4XBB; -.
DR PDBsum; 4XBC; -.
DR PDBsum; 4XBD; -.
DR PDBsum; 5DG6; -.
DR PDBsum; 5DGJ; -.
DR PDBsum; 5E0G; -.
DR PDBsum; 5E0H; -.
DR PDBsum; 5E0J; -.
DR PDBsum; 5T6D; -.
DR PDBsum; 5T6F; -.
DR PDBsum; 5T6G; -.
DR PDBsum; 5TG1; -.
DR PDBsum; 5TG2; -.
DR PDBsum; 5WEJ; -.
DR PDBsum; 6BIB; -.
DR PDBsum; 6BIC; -.
DR PDBsum; 6BID; -.
DR PDBsum; 6W5H; -.
DR PDBsum; 6W5J; -.
DR PDBsum; 6W5K; -.
DR PDBsum; 6W5L; -.
DR BMRB; Q83883; -.
DR SMR; Q83883; -.
DR BindingDB; Q83883; -.
DR MEROPS; C37.001; -.
DR PRIDE; Q83883; -.
DR GeneID; 1491970; -.
DR KEGG; vg:1491970; -.
DR BRENDA; 3.4.22.66; 8731.
DR EvolutionaryTrace; Q83883; -.
DR Proteomes; UP000000826; Genome.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; 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:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
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: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:0039694; P:viral RNA genome replication; IEA:InterPro.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 3.30.70.270; -; 2.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR InterPro; IPR001665; Norovirus_pept_C37.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR013614; Viral_PP_Calicivir_N.
DR Pfam; PF08405; Calici_PP_N; 1.
DR Pfam; PF05416; Peptidase_C37; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF00910; RNA_helicase; 1.
DR PRINTS; PR00917; SRSVCYSPTASE.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51537; NV_3CL_PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS51218; SF3_HELICASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Covalent protein-RNA linkage; Host membrane;
KW Host-virus interaction; Hydrolase; Membrane; Nucleotide-binding;
KW Nucleotidyltransferase; Phosphoprotein; Protease; Reference proteome;
KW RNA-directed RNA polymerase; Thiol protease; Transferase; Transmembrane;
KW Transmembrane helix; Viral RNA replication.
FT CHAIN 1..1789
FT /note="Genome polyprotein"
FT /id="PRO_0000341617"
FT CHAIN 1..398
FT /note="Protein p48"
FT /id="PRO_0000341618"
FT CHAIN 399..761
FT /note="NTPase"
FT /id="PRO_0000341619"
FT CHAIN 762..962
FT /note="Protein p22"
FT /id="PRO_0000341620"
FT CHAIN 963..1100
FT /note="Viral genome-linked protein"
FT /id="PRO_0000341621"
FT CHAIN 1101..1281
FT /note="3C-like protease"
FT /id="PRO_0000341622"
FT CHAIN 1282..1789
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000341623"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 870..890
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 532..697
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1101..1281
FT /note="Peptidase C37"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00870"
FT DOMAIN 1516..1637
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1130
FT /note="For 3CLpro activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00870"
FT ACT_SITE 1154
FT /note="For 3CLpro activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00870"
FT ACT_SITE 1239
FT /note="For 3CLpro activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00870"
FT BINDING 560..567
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT SITE 398..399
FT /note="Cleavage; by 3CLpro"
FT SITE 761..762
FT /note="Cleavage; by 3CLpro"
FT SITE 962..963
FT /note="Cleavage; by 3CLpro"
FT SITE 1100..1101
FT /note="Cleavage; by 3CLpro"
FT SITE 1281..1282
FT /note="Cleavage; by 3CLpro"
FT MOD_RES 992
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250"
FT MUTAGEN 394
FT /note="D->A,E,N: No effect on p48-p41 cleavage."
FT /evidence="ECO:0000269|PubMed:12367748"
FT MUTAGEN 395
FT /note="F->G: Complete loss of p48-p41 cleavage."
FT /evidence="ECO:0000269|PubMed:12367748"
FT MUTAGEN 395
FT /note="F->I,Y: No effect on p48-p41 cleavage."
FT /evidence="ECO:0000269|PubMed:12367748"
FT MUTAGEN 398
FT /note="Q->E,N: No effect on p48-p41 cleavage."
FT /evidence="ECO:0000269|PubMed:12367748"
FT MUTAGEN 398
FT /note="Q->G: Complete loss of p48-p41 cleavage."
FT /evidence="ECO:0000269|PubMed:12367748"
FT MUTAGEN 399
FT /note="G->A: No effect on p48-p41 cleavage."
FT /evidence="ECO:0000269|PubMed:12367748"
FT MUTAGEN 1154
FT /note="E->G: Complete loss of 3CLpro activity."
FT /evidence="ECO:0000269|PubMed:12367748"
FT MUTAGEN 1167
FT /note="D->G: No effect on 3CLpro activity."
FT /evidence="ECO:0000269|PubMed:12367748"
FT MUTAGEN 1281
FT /note="E->Q: No effect on 3CLpro activity."
FT /evidence="ECO:0000269|PubMed:12367748"
FT HELIX 1103..1106
FT /evidence="ECO:0007829|PDB:5DGJ"
FT STRAND 1109..1112
FT /evidence="ECO:0007829|PDB:5DGJ"
FT STRAND 1115..1128
FT /evidence="ECO:0007829|PDB:5DGJ"
FT HELIX 1129..1131
FT /evidence="ECO:0007829|PDB:5DGJ"
FT STRAND 1137..1139
FT /evidence="ECO:0007829|PDB:5DGJ"
FT HELIX 1144..1146
FT /evidence="ECO:0007829|PDB:5DGJ"
FT STRAND 1147..1152
FT /evidence="ECO:0007829|PDB:5DGJ"
FT STRAND 1155..1162
FT /evidence="ECO:0007829|PDB:5DGJ"
FT STRAND 1182..1188
FT /evidence="ECO:0007829|PDB:5DGJ"
FT STRAND 1190..1192
FT /evidence="ECO:0007829|PDB:2LNC"
FT STRAND 1194..1209
FT /evidence="ECO:0007829|PDB:5DGJ"
FT STRAND 1212..1221
FT /evidence="ECO:0007829|PDB:5DGJ"
FT HELIX 1223..1225
FT /evidence="ECO:0007829|PDB:5DGJ"
FT HELIX 1226..1229
FT /evidence="ECO:0007829|PDB:5TG1"
FT TURN 1232..1234
FT /evidence="ECO:0007829|PDB:5E0J"
FT HELIX 1236..1238
FT /evidence="ECO:0007829|PDB:6BID"
FT STRAND 1242..1247
FT /evidence="ECO:0007829|PDB:5DGJ"
FT STRAND 1250..1260
FT /evidence="ECO:0007829|PDB:5DGJ"
FT TURN 1262..1265
FT /evidence="ECO:0007829|PDB:5E0J"
FT STRAND 1266..1270
FT /evidence="ECO:0007829|PDB:5DGJ"
FT STRAND 1275..1278
FT /evidence="ECO:0007829|PDB:4IN2"
SQ SEQUENCE 1789 AA; 198694 MW; 6C84EF9EE62809B9 CRC64;
MMMASKDVVP TAASSENANN NSSIKSRLLA RLKGSGGATS PPNSIKITNQ DMALGLIGQV
PAPKATSVDV PKQQRDRPPR TVAEVQQNLR WTERPQDQNV KTWDELDHTT KQQILDEHAE
WFDAGGLGPS TLPTSHERYT HENDEGHQVK WSAREGVDLG ISGLTTVSGP EWNMCPLPPV
DQRSTTPATE PTIGDMIEFY EGHIYHYAIY IGQGKTVGVH SPQAAFSITR ITIQPISAWW
RVCYVPQPKQ RLTYDQLKEL ENEPWPYAAV TNNCFEFCCQ VMCLEDTWLQ RKLISSGRFY
HPTQDWSRDT PEFQQDSKLE MVRDAVLAAI NGLVSRPFKD LLGKLKPLNV LNLLSNCDWT
FMGVVEMVVL LLELFGIFWN PPDVSNFIAS LLPDFHLQGP EDLARDLVPI VLGGIGLAIG
FTRDKVSKMM KNAVDGLRAA TQLGQYGLEI FSLLKKYFFG GDQTEKTLKD IESAVIDMEV
LSSTSVTQLV RDKQSARAYM AILDNEEEKA RKLSVRNADP HVVSSTNALI SRISMARAAL
AKAQAEMTSR MRPVVIMMCG PPGIGKTKAA EHLAKRLANE IRPGGKVGLV PREAVDHWDG
YHGEEVMLWD DYGMTKIQED CNKLQAIADS APLTLNCDRI ENKGMQFVSD AIVITTNAPG
PAPVDFVNLG PVCRRVDFLV YCTAPEVEHT RKVSPGDTTA LKDCFKPDFS HLKMELAPQG
GFDNQGNTPF GKGVMKPTTI NRLLIQAVAL TMERQDEFQL QGPTYDFDTD RVAAFTRMAR
ANGLGLISMA SLGKKLRSVT TIEGLKNALS GYKISKCSIQ WQSRVYIIES DGASVQIKED
KQALTPLQQT INTASLAITR LKAARAVAYA SCFQSAITTI LQMAGSALVI NRAVKRMFGT
RTAAMALEGP GKEHNCRVHK AKEAGKGPIG HDDMVERFGL CETEEEESED QIQMVPSDAV
PEGKNKGKTK KGRGRKNNYN AFSRRGLSDE EYEEYKKIRE EKNGNYSIQE YLEDRQRYEE
ELAEVQAGGD GGIGETEMEI RHRVFYKSKS KKHQQEQRRQ LGLVTGSDIR KRKPIDWTPP
KNEWADDDRE VDYNEKINFE APPTLWSRVT KFGSGWGFWV SPTVFITTTH VVPTGVKEFF
GEPLSSIAIH QAGEFTQFRF SKKMRPDLTG MVLEEGCPEG TVCSVLIKRD SGELLPLAVR
MGAIASMRIQ GRLVHGQSGM LLTGANAKGM DLGTIPGDCG APYVHKRGND WVVCGVHAAA
TKSGNTVVCA VQAGEGETAL EGGDKGHYAG HEIVRYGSGP ALSTKTKFWR SSPEPLPPGV
YEPAYLGGKD PRVQNGPSLQ QVLRDQLKPF ADPRGRMPEP GLLEAAVETV TSMLEQTMDT
PSPWSYADAC QSLDKTTSSG YPHHKRKNDD WNGTTFVGEL GEQAAHANNM YENAKHMKPI
YTAALKDELV KPEKIYQKVK KRLLWGADLG TVVRAARAFG PFCDAIKSHV IKLPIKVGMN
TIEDGPLIYA EHAKYKNHFD ADYTAWDSTQ NRQIMTESFS IMSRLTASPE LAEVVAQDLL
APSEMDVGDY VIRVKEGLPS GFPCTSQVNS INHWIITLCA LSEATGLSPD VVQSMSYFSF
YGDDEIVSTD IDFDPARLTQ ILKEYGLKPT RPDKTEGPIQ VRKNVDGLVF LRRTISRDAA
GFQGRLDRAS IERQIFWTRG PNHSDPSETL VPHTQRKIQL ISLLGEASLH GEKFYRKISS
KVIHEIKTGG LEMYVPGWQA MFRWMRFHDL GLWTGDRDLL PEFVNDDGV
